Table S6. Homology detection & structure prediction by HMM-HMM comparison for the M60-like/PF13402 profile.
Query Q5E705_VIBF1/1109-1410/Q5E705 (seq=GSRQSAGVWI...FFGQLKLWAE Len=302 Neff=8.7 Nseqs=128)
Parameters score SS:yes search:local realign with MAP:no
No Hit Prob E-value P-value Score SS Cols Query HMM Template HMM
1 PTHR15730 EXPERIMENTAL AUTOIMM 100.0 0 0 389.4 14.2 282 3-302 546-843 (928)
2 PF03272 Enhancin: Viral enhan 100.0 2.2E-37 1.8E-42 307.8 25.8 281 1-302 27-331 (775)
3 pfam03272 Enhancin Viral enhan 100.0 1.3E-33 1.1E-38 277.7 22.4 287 1-302 27-330 (775)
4 pfam07828 PA-IL PA-IL-like pro 88.8 6.1 5E-05 32.0 6.6 85 4-88 14-120 (121)
5 3N2V_Entity_1 80.2 5.1 4.2E-05 34.4 3.3 90 141-230 21-117 (158)
6 3N2U_Entity_1 80.2 5.1 4.2E-05 34.4 3.3 90 141-230 21-117 (158)
7 1l7l_A PA-I galactophilic lect 78.6 3.8 3.1E-05 33.0 1.8 15 4-18 14-28 (121)
8 1qib_A Protein (gelatinase A); 78.3 3.9 3.2E-05 35.2 2.0 90 141-230 22-119 (161)
9 1i76_A MMP-8;, neutrophil coll 76.9 9.9 8.1E-05 33.3 4.0 86 141-230 26-122 (163)
10 1hv5_A Stromelysin 3; inhibiti 76.5 11 9.3E-05 32.5 4.3 90 141-230 26-123 (165)
11 PF12388 Peptidase_M57: Dual-a 75.6 11 9.3E-05 34.6 4.1 85 144-231 56-144 (211)
12 1y93_A Macrophage metalloelast 74.8 5.9 4.8E-05 34.1 2.2 90 141-230 22-118 (159)
13 d1i76a_ d.92.1.11 (A:) Neutrop 74.7 7.2 5.9E-05 33.9 2.7 90 141-230 26-122 (163)
14 1hy7_A Stromelysin-1, MMP-3; m 73.3 9.4 7.7E-05 33.5 3.0 90 141-230 27-123 (173)
15 d1l7la_ b.18.1.16 (A:) PA-IL, 73.1 18 0.00015 28.9 4.0 78 4-81 14-103 (121)
16 1mmq_A Matrilysin; metalloprot 72.3 9.9 8.1E-05 33.2 3.0 90 141-230 27-124 (170)
17 SUPFAM0037477 d.92.1 Metallopr 71.4 4.4 3.6E-05 32.1 0.6 9 224-232 117-125 (172)
18 d1hfca_ d.92.1.11 (A:) Fibrobl 71.0 16 0.00013 31.4 3.9 90 141-230 20-116 (157)
19 SUPFAM0042596 d.92.1 Metallopr 70.9 4.2 3.4E-05 31.5 0.4 8 224-231 111-118 (159)
20 SUPFAM0038581 d.92.1 Metallopr 70.2 4.6 3.7E-05 31.4 0.5 8 224-231 112-119 (160)
21 SUPFAM0036188 d.92.1 Metallopr 69.5 4.9 4E-05 31.5 0.5 9 224-232 117-125 (164)
22 PIRSF005785 Zn-prot_arch 68.9 4.5 3.7E-05 36.8 0.2 10 223-232 149-158 (204)
23 d1mmqa_ d.92.1.11 (A:) Matrily 68.5 13 0.00011 32.4 2.9 90 141-230 27-124 (166)
24 SUPFAM0035975 d.92.1 Metallopr 68.5 5.3 4.3E-05 31.5 0.5 9 224-232 116-124 (168)
25 d1kapp2 d.92.1.6 (P:1-246) Met 68.4 19 0.00016 34.0 4.1 88 143-230 90-180 (246)
26 SUPFAM0036877 d.92.1 Metallopr 68.1 5.3 4.3E-05 31.4 0.4 9 224-232 118-126 (169)
27 1cge_A Fibroblast collagenase; 67.8 19 0.00016 31.4 3.8 90 141-230 25-121 (168)
28 SUPFAM0041006 d.92.1 Metallopr 67.5 5.6 4.6E-05 31.3 0.4 9 224-232 118-126 (166)
29 pfam04228 Zn_peptidase Putativ 67.2 5.6 4.6E-05 37.9 0.4 12 222-233 172-183 (292)
30 SUPFAM0035790 d.92.1 Metallopr 66.8 4.9 4E-05 31.3 0.0 9 224-232 117-125 (165)
31 1bkcA00 3.40.390.10 65.6 6.6 5.4E-05 33.5 0.5 9 224-232 185-193 (255)
32 SUPFAM0043304 d.92.1 Metallopr 65.5 6.3 5.1E-05 31.1 0.4 9 224-232 121-129 (169)
33 SUPFAM0045657 d.92.1 Metallopr 64.4 5.4 4.4E-05 31.5 -0.2 9 224-232 117-125 (168)
34 SUPFAM0035666 d.92.1 Metallopr 64.2 6.9 5.6E-05 31.1 0.4 9 224-232 124-132 (174)
35 SUPFAM0039592 d.92.1 Metallopr 64.1 5.9 4.8E-05 30.6 -0.0 9 224-232 111-119 (158)
36 3KEC_Entity_1 63.7 18 0.00014 31.4 2.8 90 141-230 27-123 (167)
37 d1hv5a_ d.92.1.11 (A:) Stromel 63.4 34 0.00028 30.0 4.4 88 141-232 26-125 (162)
38 SUPFAM0040001 d.92.1 Metallopr 63.1 5.6 4.6E-05 34.0 -0.3 9 224-232 174-182 (246)
39 830c_A MMP-13, MMP-13; matrix 62.9 20 0.00016 31.3 3.0 92 141-232 27-125 (168)
40 SUPFAM0038130 d.92.1 Metallopr 62.9 5.9 4.8E-05 30.7 -0.2 8 224-231 115-122 (159)
41 d1hy7a_ d.92.1.11 (A:) Stromel 62.8 21 0.00017 31.1 3.0 90 141-230 27-123 (168)
42 SUPFAM0035598 d.92.1 Metallopr 62.5 8.6 7E-05 33.1 0.7 9 224-232 185-193 (255)
43 SUPFAM0038739 d.92.1 Metallopr 62.2 6.4 5.2E-05 30.8 -0.1 9 224-232 117-125 (162)
44 SUPFAM0040268 d.92.1 Metallopr 61.8 4.9 4E-05 30.0 -0.8 9 224-232 81-89 (132)
45 pfam12388 Peptidase_M57 Dual-a 61.7 28 0.00023 32.0 3.6 102 144-247 56-163 (211)
46 PF04228 Zn_peptidase: Putativ 61.5 8.6 7E-05 37.3 0.5 10 224-233 174-183 (292)
47 2ovx_A Matrix metalloproteinas 61.2 17 0.00014 31.2 2.2 90 141-230 24-121 (159)
48 2jsd_A Matrix metalloproteinas 59.5 59 0.00048 28.2 5.1 90 141-230 22-118 (160)
49 SUPFAM0040267 d.92.1 Metallopr 59.3 11 8.9E-05 31.1 0.7 9 224-232 140-148 (201)
50 d1rm8a_ d.92.1.11 (A:) Matrix 58.9 11 9.1E-05 32.6 0.7 9 222-230 119-127 (169)
51 SUPFAM0044993 d.92.1 Metallopr 57.2 13 0.00011 30.6 0.9 9 224-232 138-146 (198)
52 cd04271 ZnMc_ADAM_fungal Zinc- 57.0 8.1 6.6E-05 35.9 -0.4 9 224-232 149-157 (228)
53 cd04279 ZnMc_MMP_like_1 Zinc-d 56.8 43 0.00035 29.5 3.9 89 142-230 19-114 (156)
54 SUPFAM0038010 d.92.1 Metallopr 56.5 8.4 6.8E-05 32.8 -0.4 9 224-232 165-173 (242)
55 PIRSF020485 PA-IL 56.5 24 0.0002 29.7 2.2 15 4-18 16-30 (123)
56 1bud_A Protein (acutolysin A); 55.7 14 0.00012 33.3 0.9 9 224-232 137-145 (197)
57 SUPFAM0035195 d.92.1 Metallopr 55.5 15 0.00012 30.3 0.9 9 224-232 138-146 (200)
58 d1xuca1 d.92.1.11 (A:104-272) 55.3 14 0.00011 32.3 0.7 9 222-230 115-123 (169)
59 d1bswa_ d.92.1.9 (A:) Snake ve 55.3 15 0.00012 33.2 0.9 9 224-232 137-145 (197)
60 SUPFAM0042988 d.92.1 Metallopr 55.2 15 0.00012 30.1 0.8 9 224-232 139-147 (197)
61 1slm_A Stromelysin-1; hydrolas 55.1 33 0.00027 32.9 3.1 90 141-230 109-205 (255)
62 d1y93a1 d.92.1.11 (A:106-263) 54.8 15 0.00013 31.5 0.9 9 224-232 111-119 (158)
63 2w15_A Zinc metalloproteinase 54.7 15 0.00012 33.3 0.9 9 224-232 140-148 (202)
64 d1bqqm_ d.92.1.11 (M:) Membran 54.3 1.6E+02 0.0013 25.6 7.0 92 141-232 23-132 (174)
65 SUPFAM0045583 d.92.1 Metallopr 54.3 16 0.00013 30.2 0.8 9 224-232 139-147 (201)
66 pfam06262 DUF1025 Domain of un 54.2 16 0.00013 29.2 0.9 9 224-232 76-84 (96)
67 COG3824 Predicted Zn-dependent 53.9 14 0.00011 30.7 0.5 9 224-232 113-121 (136)
68 1c7k_A NCNP, zinc endoprotease 53.5 16 0.00013 31.0 0.8 7 224-230 81-87 (132)
69 d2ejqa1 d.92.1.17 (A:2-108) Un 52.7 17 0.00014 29.9 0.7 9 224-232 92-100 (107)
70 d2ovxa1 d.92.1.11 (A:110-443) 52.2 18 0.00015 31.2 0.9 9 224-232 115-123 (159)
71 1qua_A Acutolysin-C, hemorrhag 52.1 18 0.00015 32.7 0.9 9 224-232 139-147 (197)
72 cd04267 ZnMc_ADAM_like Zinc-de 51.9 16 0.00013 33.1 0.6 9 224-232 137-145 (192)
73 3b8z_A Protein adamts-5; alpha 51.7 18 0.00015 33.1 0.9 9 224-232 145-153 (217)
74 d1r55a_ d.92.1.9 (A:) ADAM33 { 51.6 18 0.00015 32.8 0.9 9 224-232 136-144 (203)
75 3ma2_D Matrix metalloproteinas 51.6 19 0.00015 31.6 0.9 9 224-232 126-134 (181)
76 d1qiba_ d.92.1.11 (A:) Gelatin 51.4 18 0.00015 31.2 0.8 7 224-230 113-119 (161)
77 SUPFAM0043540 d.92.1 Metallopr 50.5 9.9 8E-05 32.2 -0.9 7 224-230 171-177 (243)
78 PF07828 PA-IL: PA-IL-like pro 50.5 12 9.9E-05 30.0 -0.3 15 4-18 14-28 (121)
79 SUPFAM0041314 d.92.1 Metallopr 50.5 19 0.00016 29.6 0.9 9 224-232 140-148 (202)
80 2ejq_A Hypothetical protein TT 50.5 19 0.00015 30.7 0.7 9 224-232 93-101 (130)
81 1yp1_A FII; FII hydrolase; 1.9 50.1 20 0.00016 32.7 0.9 9 224-232 139-147 (202)
82 d1kufa_ d.92.1.9 (A:) Snake ve 50.1 20 0.00016 32.6 0.9 9 224-232 140-148 (201)
83 d1quaa_ d.92.1.9 (A:) Snake ve 50.1 20 0.00016 32.4 0.9 9 224-232 139-147 (197)
84 PF00413 Peptidase_M10: Matrix 50.0 17 0.00014 31.3 0.5 9 224-232 106-114 (152)
85 1kuf_A Atrolysin E, metallopro 49.8 20 0.00017 32.6 0.9 9 224-232 142-150 (203)
86 d1nd1a_ d.92.1.9 (A:) Snake ve 49.8 20 0.00017 32.6 0.9 9 224-232 140-148 (202)
87 PF01433 Peptidase_M1: Peptida 49.7 1.9E+02 0.0015 29.6 7.5 100 141-258 227-335 (391)
88 1rm8_A MMP-16, matrix metallop 49.3 20 0.00016 31.1 0.7 9 224-232 121-129 (169)
89 d1sata2 d.92.1.6 (A:4-246) Met 49.2 75 0.00061 30.2 4.4 86 143-230 80-177 (243)
90 d3b7sa3 d.92.1.13 (A:209-460) 48.8 2.1E+02 0.0017 27.2 7.3 114 121-259 6-121 (252)
91 COG1164 Oligoendopeptidase F [ 48.7 48 0.00039 36.1 3.4 82 129-233 312-393 (598)
92 3ba0_A Macrophage metalloelast 48.5 55 0.00044 33.1 3.6 90 141-230 21-117 (365)
93 1k7iA02 3.40.390.10 48.1 52 0.00042 27.5 3.0 88 143-230 64-157 (227)
94 cd04272 ZnMc_salivary_gland_MP 47.9 20 0.00016 33.3 0.5 9 224-232 149-157 (220)
95 COG3590 PepO Predicted metallo 47.7 22 0.00018 37.6 0.9 20 224-243 491-510 (654)
96 d1atla_ d.92.1.9 (A:) Snake ve 47.4 23 0.00019 32.1 0.9 9 224-232 138-146 (200)
97 2ddf_A ADAM 17; hydrolase; HET 47.0 24 0.00019 33.5 0.9 9 224-232 186-194 (257)
98 cd04273 ZnMc_ADAMTS_like Zinc- 47.0 23 0.00019 32.7 0.8 9 224-232 144-152 (207)
99 1atl_A Atrolysin C; metalloend 46.1 25 0.00021 32.0 0.9 9 224-232 140-148 (202)
100 COG1913 Predicted Zn-dependent 45.4 26 0.00021 31.3 0.9 10 223-232 127-136 (181)
No 1 
>template EXPERIMENTAL AUTOIMMUNE PROSTATITIS ANTIGEN 2-RELATED.
Probab=100.00 E-value=0 Score=389.42 Aligned_cols=282 Identities=21% Similarity=0.275 Sum_probs=0.0
Q ss_pred cccceEEECCCCEEEEEecC--CCCcEEEEEeecCCCcccccccccCCCCceEEEEecCCeEEEecCCCcEEEEEcCCCC
Q Q5E705_VIBF1/1 3 RQSAGVWIPAREVAYVHGLS--SDDTVMIAMADNLTGRVNHEMALNRPPRVSMSFNGVEASNGFKVPYGGSVYITLGSKE 80 (302)
Q Consensus 3 ~~~TG~y~~~Ge~i~V~~~~--~~~~~~v~i~~~~~~~~~~~~~~~r~~~~~~~~~L~~g~n~i~~p~GG~iyi~~~~~~ 80 (302)
|.|||+|++.++.+.|.++. ...++++||||| .|+++....+.|.|.+....-|+.....|++-+||++||.++.+.
T Consensus 546 W~STGLY~~~~q~~~v~~pe~Aasa~L~~qiGCh-tDdlt~A~kl~R~P~v~~~C~ld~~~~S~~ClWGGLlYiiVp~~~ 624 (928)
T PTHR15730 546 WMSTGLYLPGRQVIDVSLPESAASADLKVQIGCH-TDDLTRASKLFRGPLVINRCCLDKPTKSITCLWGGLLYIIVPQNS 624 (928)
T ss_pred eeecceeccCceeEEEEechhhhcCCceEEEeec-ccchhHHHHhhcCceeeeeeeeccccceeeeeecceeEEEeeccc
Q ss_pred c---eEEEEecceEECceeecCCCCHHHHHHHHHhCCCCEEEEEcCcEEEEEEHHHHhhhcccCHHHHHHHHHHHHHHHH
Q Q5E705_VIBF1/1 81 S---AQVSFGGSAIAAPMFMMTSATEGSWITTPEESDAPITEIVGKRFSYTTTTAGIKGHSEVDVLEMTKQFDLFTIGVN 157 (302)
Q Consensus 81 ~---v~v~i~~~~~~~P~f~~g~~t~~~w~~~l~~~~~p~~ei~~~~v~~t~p~~~~~~~~~~d~~~l~~~~d~ii~~~~ 157 (302)
+ |.++|.| ++++|+|++|+|+.+||++.+.++++||.|+.+|++++|+|+..++.+ +||..+++.||+||++..
T Consensus 625 ~lG~vp~t~~g-Av~AP~yklG~Ts~eeWk~~~~~~~gPWGELaTdNiILTvPt~nl~~L--~~PeplL~LWDemmqAva 701 (928)
T PTHR15730 625 KLGSVPVTVKG-AVRAPFYKLGETSKEEWKRRLLEYPGPWGELATDNIILTVPTANLRTL--ENPEPLLRLWDEMMQAVA 701 (928)
T ss_pred cccceeEEEee-ccccchhhcCCCcHHHHHHHHHhcCCCchhhhhcceeeeccchhhhhh--cCchHHHHHHHHHHHHHH
Q ss_pred HHhCCCCCCccccccccccccccchhhceeeeeccccceecCCcceeeecccccc---ceeccCCCcchhHHhhhhhccc
Q Q5E705_VIBF1/1 158 EFYGRDGVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHSGYPVMSTSFPRQK---SSLFKATDNWMLGHEIGHNQAA 234 (302)
Q Consensus 158 ~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~g~~~~~~~~~~~~---~~~~~~~~~WG~~HEiGH~~Q~ 234 (302)
+|.|.+..-.+|+ |+|+|+|++.||||+||||||+..+... ...+.+.|-||+.||+|||+|.
T Consensus 702 ~L~~~~fpl~~p~--------------RiVaDvQiS~GWmH~GYPImChlesv~eli~e~~ir~~G~WGp~HELG~NqQ~ 767 (928)
T PTHR15730 702 KLGGEPFPLRLPE--------------RIVADVQISVGWMHAGYPIMCHLESVQELINEKLIRTKGLWGPVHELGRNQQR 767 (928)
T ss_pred HhcCCCcccccch--------------heeeehhhccchhhccchHHHHHHHHHHHHhHHHHhhcCCcccccccCCcccc
Q ss_pred cccccCC-CccchhhHHHHHHHHHHhc-------cccchhhhHHHHHHhhccCcccccCCHHHHHHHHHHHHHhcC
Q Q5E705_VIBF1/1 235 NWLNVVG-AGETANNVLALYTQERNTG-------DMPRIKVSITNATEWANGDHPWADGTNADRLNFFGQLKLWAE 302 (302)
Q Consensus 235 ~~~~~~g-~~EvtnNi~sl~~q~~~~~-------~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~L~~f~QL~~~~G 302 (302)
..|.+++ +||.|||+++.|+.+...+ ..+....|..+++.|+..+.....++.|++|..|.||+++||
T Consensus 768 ~~WefpPHTTEAtCNLW~vYVHETVLGIPR~~A~~~L~pp~Re~r~~~yL~kG~~~~~Wn~WTALETYLQLqe~FG 843 (928)
T PTHR15730 768 QEWEFPPHTTEATCNLWCVYVHETVLGIPRSRANIALWPPVREKRVRIYLSKGPSVKHWNAWTALETYLQLQEAFG 843 (928)
T ss_pred ccccCCCCcchhhhhheeeeehhhhccCChhhhhhhcCchhHHHHHHHHhccCCchhhHHHHHHHHHHHHHHHhhc
No 2 
>PF03272 Enhancin: Viral enhancin protein; InterPro: Metalloproteases are the most diverse of the
four main types of protease, with more than 50 families identified to date. In these enzymes, a divalent cation,
usually zinc, activates the water molecule. The metal ion is held in place by amino acid ligands, usually
three in number. The known metal ligands are His, Glu, Asp or Lys and at least one other residue is required for
catalysis, which may play an electrophillic role. Of the known metalloproteases, around half contain an HEXXH
motif, which has been shown in crystallographic studies to form part of the metal-binding site . The HEXXH motif
is relatively common, but can be more stringently defined for metalloproteases as 'abXHEbbHbc', where 'a' is
most often valine or threonine and forms part of the S1' subsite in thermolysin and neprilysin, 'b' is an
uncharged residue, and 'c' a hydrophobic residue. Proline is never found in this site, possibly because it would break
the helical structure adopted by this motif in metalloproteases . Peptidases are grouped into clans and
families. Clans are groups of families for which there is evidence of common ancestry. Each clan is identified with
two letters, the first representing the catalytic type of the families included in the clan (with the letter
'P' being used for a clan containing families of more than one of the catalytic types serine, threonine and
cysteine). Some families cannot yet be assigned to clans, and when a formal assignment is required, such a family is
described as belonging to clan A-, C-, M-, S-, T- or U-, according to the catalytic type. Some clans are
divided into subclans because there is evidence of a very ancient divergence within the clan, for example MA(E), the
gluzincins, and MA(M), the metzincins. Families are grouped by their catalytic type, the first character
representing the catalytic type: A, aspartic; C, cysteine; G, glutamic acid; M, metallo; S, serine; T, threonine;
and U, unknown. The serine, threonine and cysteine peptidases utilise the amino acid as a nucleophile and form
an acyl intermediate - these peptidases can also readily act as transferases. In the case of aspartic, glutamic
and metallopeptidases, the nucleophile is an activated water molecule. This group of metallopeptidases
belong to the MEROPS peptidase family M60 (enhancin family, clan MA(E)). The active site residues for members of
this family and thermolysin, the type example for clan MA, occur in the motif HEXXH. The viral enhancin protein,
or enhancing factor, is involved in disruption of the peritrophic membrane and fusion of nucleocapsids with
mid-gut cells. ; GO: 0016032 viral reproduction
Probab=100.00 E-value=2.2e-37 Score=307.77 Aligned_cols=281 Identities=16% Similarity=0.127 Sum_probs=0.0
Q ss_pred CCcccceEEECCCCEEEEEe--cCCCCcEEEEEeecCCCcccccccccCCCCceEEEEecCCeEEEecCCCcEEEEEcCC
Q Q5E705_VIBF1/1 1 GSRQSAGVWIPAREVAYVHG--LSSDDTVMIAMADNLTGRVNHEMALNRPPRVSMSFNGVEASNGFKVPYGGSVYITLGS 78 (302)
Q Consensus 1 ~~~~~TG~y~~~Ge~i~V~~--~~~~~~~~v~i~~~~~~~~~~~~~~~r~~~~~~~~~L~~g~n~i~~p~GG~iyi~~~~ 78 (302)
|+|||.|++++||..|+|+. ++....+++++.+....++. ++.+..+.++++++.-...+|..+-
T Consensus 27 H~R~~lg~il~a~~~i~ir~~~~~~~~~~tlrlLNnd~~tE~-------------s~~~~~~~~~~~~~~~sVpFvd~~~ 93 (775)
T PF03272_consen 27 HDRQPLGYILPANTKIRIRQNNPNFVGPLTLRLLNNDRNTEK-------------SITVNNEWVTISVQHDSVPFVDTPY 93 (775)
T ss_pred cCCccCCEEECCCCEEEEEecCCCCCCCeEEEEecCCccceE-------------EEEecCccEEEEcccceEEEEeeee
Q ss_pred ---CCc---eEEEEecceEECceeecCCCCHHHHHHHHHhCCCCEEEEEcCcEEEEEEHHHHhhhc---ccCHHHHHHHH
Q Q5E705_VIBF1/1 79 ---KES---AQVSFGGSAIAAPMFMMTSATEGSWITTPEESDAPITEIVGKRFSYTTTTAGIKGHS---EVDVLEMTKQF 149 (302)
Q Consensus 79 ---~~~---v~v~i~~~~~~~P~f~~g~~t~~~w~~~l~~~~~p~~ei~~~~v~~t~p~~~~~~~~---~~d~~~l~~~~ 149 (302)
..+ |++.|.|...++|+|+.|.++ ++|++++++..+|+|.|+++++++++|..+.+.+. ..|+++|+++|
T Consensus 94 ~~~~~~~~~V~~~i~~~~~~LP~y~~g~~~-~~F~~~~~~~~~~fa~le~~~i~lLVP~~dk~~l~~~~~~~l~~L~~~Y 172 (775)
T PF03272_consen 94 GDNSDGEYEVEYEITGEHKPLPVYRKGQNE-SDFFSEWDDSDSPFAFLEGDRIQLLVPPADKNYLRNKDDTDLDELNDFY 172 (775)
T ss_pred cCCCCCcEEEEEEeCCCccccCEEEeCCCH-HHHHHhhhhcCCceEEEEcCeEEEEeCHhHHHHHhhhccCCHHHHHHHH
Q ss_pred HHHHHHHHHHhCCCCCCccccccccccccccchhhceeeeeccccceecCCcceeeeccccccceeccCCCcchhHHhhh
Q Q5E705_VIBF1/1 150 DLFTIGVNEFYGRDGVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHSGYPVMSTSFPRQKSSLFKATDNWMLGHEIG 229 (302)
Q Consensus 150 d~ii~~~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~g~~~~~~~~~~~~~~~~~~~~~WG~~HEiG 229 (302)
++|++.|++++||+.++..+.+.+..+.++ +++|..+.|+++|++++++.+.++.. .++.....+||+|||||
T Consensus 173 ~~Ii~~Yd~l~GL~~~~~~~~~~n~~~kyF------~KAD~~G~G~AYY~~~~~a~s~~s~~-~~L~~~~~nWg~LHEiG 245 (775)
T PF03272_consen 173 NEIISFYDDLTGLSDDPSMPVDSNFNRKYF------AKADKSGPGAAYYGSNWTANSSSSMS-FYLNPSPTNWGALHEIG 245 (775)
T ss_pred HHHHHHHHhhcccccCCcccccccccceeE------EecCCCCCCccccccceeecChHHHH-HHhCcCCccchhHhhhh
Q ss_pred hhcccccc-ccCCCccchhhHHHHHHHHHHhcc-----------ccchhhhHHHHHHhhccCcccccCCHHHHHHHHH-H
Q Q5E705_VIBF1/1 230 HNQAANWL-NVVGAGETANNVLALYTQERNTGD-----------MPRIKVSITNATEWANGDHPWADGTNADRLNFFG-Q 296 (302)
Q Consensus 230 H~~Q~~~~-~~~g~~EvtnNi~sl~~q~~~~~~-----------~~~~~~~~~~~~~~~~~~~~~~~~~~~~~L~~f~-Q 296 (302)
|.||.+++ ++..++||||||||+++|+.+.+. .-+.+.....+.+.+....++.+++.+.||.||+ +
T Consensus 246 H~yd~~F~~n~~~~~EVw~NI~~d~yQ~~~~~~~e~~~~~wly~~G~r~~ve~~i~~~~~~~~~~~~w~~~~kL~~~~~~ 325 (775)
T PF03272_consen 246 HGYDFGFTRNDPYLGEVWNNILADRYQYTYMNPDERQQLGWLYDNGKRERVERNINNLIDNNKPFDSWDLREKLIFFTWI 325 (775)
T ss_pred hhhcceeeecCCeeeeeehhhhHHHHHHHhcCHHHhhccchhhcCCCHHHHHHHHHHHhhcCCCcccccHHHHHHHHHHH
Q ss_pred HHHhcC
Q Q5E705_VIBF1/1 297 LKLWAE 302 (302)
Q Consensus 297 L~~~~G 302 (302)
|...+|
T Consensus 326 l~~~~G 331 (775)
T PF03272_consen 326 LNTKAG 331 (775)
T ss_pred HHHHHh
No 3 
>pfam03272 Enhancin Viral enhancin protein.
Probab=100.00 E-value=1.3e-33 Score=277.70 Aligned_cols=287 Identities=14% Similarity=0.055 Sum_probs=0.0
Q ss_pred CCcccceEEECCCCEEEEEe--cCCCCcEEEEEeecCCCcccccccccCCCCceEEEEecCCeEEEecCCCcEEEEEcCC
Q Q5E705_VIBF1/1 1 GSRQSAGVWIPAREVAYVHG--LSSDDTVMIAMADNLTGRVNHEMALNRPPRVSMSFNGVEASNGFKVPYGGSVYITLGS 78 (302)
Q Consensus 1 ~~~~~TG~y~~~Ge~i~V~~--~~~~~~~~v~i~~~~~~~~~~~~~~~r~~~~~~~~~L~~g~n~i~~p~GG~iyi~~~~ 78 (302)
|+|||.|++++||..|+|+. ++....+++++.+.....+.+......|..++.. ...+-.|.+|+||.. +.
T Consensus 27 H~R~plg~il~a~~~i~ir~~~~~~~~~~tlrlLNnn~~tE~si~v~~~w~~~~~~---~~sVpFvd~~~~~~~----~~ 99 (775)
T pfam03272 27 HYRQPLGYVLKAGSTIRLRTNNAAPVGPVTLRLLNNNRNTERSITVTNDWTTLTVE---HDSVPFVDTVVVDNR----DG 99 (775)
T ss_pred cCCcccCEEECCCCEEEEEeccCCCCCCeEEEEeeCCccceEEEEecCceEEEEec---cceEEEEeccccCCC----Cc
Q ss_pred CCceEEEEecceEECceeecCCCCHHHHHHHHHhCCCCEEEEEcCcEEEEEEHHHHhhhc---ccCHHHHHHHHHHHHHH
Q Q5E705_VIBF1/1 79 KESAQVSFGGSAIAAPMFMMTSATEGSWITTPEESDAPITEIVGKRFSYTTTTAGIKGHS---EVDVLEMTKQFDLFTIG 155 (302)
Q Consensus 79 ~~~v~v~i~~~~~~~P~f~~g~~t~~~w~~~l~~~~~p~~ei~~~~v~~t~p~~~~~~~~---~~d~~~l~~~~d~ii~~ 155 (302)
...|++.|.|...++|+|+.|.+. ++|++++++..+|+|.|++++|++++|..+...+. ..++++|.++|++|++.
T Consensus 100 ~~~ve~~i~g~~~~LP~y~~g~~~-~~f~~~~~~~~~~fa~ve~~~i~lLVP~~Dk~~l~~~~~~~i~~L~~fY~~I~~~ 178 (775)
T pfam03272 100 QYEVEYEIDGEHTPLPVYTFGQNE-QEFKSEWRDSNSSYAFVELKYIQLLVPPADKNALLNMNDDDLDELDDFYNSIVSF 178 (775)
T ss_pred cEEEEEEECCccccCCEEecCCCh-HHHHhhhhhcCCceEEEECCeEEEEeCcchHHHHhccccCCHHHHHHHHHHHHHH
Q ss_pred HHHHhCCCCCCccccccccccccccchhhceeeeeccccceecCCcceeeeccccccceeccCCCcchhHHhhhhhcccc
Q Q5E705_VIBF1/1 156 VNEFYGRDGVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHSGYPVMSTSFPRQKSSLFKATDNWMLGHEIGHNQAAN 235 (302)
Q Consensus 156 ~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~g~~~~~~~~~~~~~~~~~~~~~WG~~HEiGH~~Q~~ 235 (302)
|++++||+.+..++.+.+..+.++ +++|..++||++|++++++.+.++.. .|+.+...+||++|||||.||..
T Consensus 179 Yd~l~Gl~~~~~~~~~~n~~~kyF------~KAD~~G~G~AYY~~~w~a~s~~sl~-~yL~~s~~NW~~LHEIgH~Yd~~ 251 (775)
T pfam03272 179 YDDLTGLSFDPTAAVDINFNKKYF------AKADASGPGAAYYGPNWIAESSSSLG-FYLNPSPTNWGVLHEIGHAYDFY 251 (775)
T ss_pred HhhhhCCccCcccccccccccceE------EEecCCCCCcccccccceeccchhHH-HHhCCCCccchhhhhhhhhccee
Q ss_pred cc-ccCCCccchhhHHHHHHHHHHhcccc-----------chhhhHHHHHHhhccCcccccCCHHHHHHHHHHHHHhcC
Q Q5E705_VIBF1/1 236 WL-NVVGAGETANNVLALYTQERNTGDMP-----------RIKVSITNATEWANGDHPWADGTNADRLNFFGQLKLWAE 302 (302)
Q Consensus 236 ~~-~~~g~~EvtnNi~sl~~q~~~~~~~~-----------~~~~~~~~~~~~~~~~~~~~~~~~~~~L~~f~QL~~~~G 302 (302)
+. +-..+.|||||||+...|+.+.+.+. +.+.....+.+.+....++.+|+.+.||.+|-.|..-.|
T Consensus 252 F~~n~~~l~EVWnNil~d~yQy~~~~~~Erq~~~wiy~~G~r~~ve~~I~~~i~~~~~~~~w~~r~kL~~lt~l~~~~~ 330 (775)
T pfam03272 252 FTRNHTYLIEVWNNILADRYQYDWMTPAERQTDAWIYDNGRRDRVETNIIALIDTNKPFNSWSLRERLIFLTWLMNTKA 330 (775)
T ss_pred EecCCcchhHhhhhhhhHHHhHhhCChHHhhhhcceecCCchHHHHHHHHHHHhcCCCcccccHHHHHHHHHHHHHhhh
No 4
>pfam07828 PA-IL PA-IL-like protein. The members of this family are similar to the galactophilic lectin-1
expressed by P. aeruginosa ((PA-IL). Lectins recognising specific carbohydrates found on the surface of host cells are
known to be involved in the initiation of infections by this organism. The protein is thought to be organized
into an extensive network of beta-sheets, as is the case with many other lectins.
Probab=88.84 E-value=6.1 Score=31.96 Aligned_cols=85 Identities=7% Similarity=0.039 Sum_probs=0.0
Q ss_pred ccceEEECCCCEEEE------EecCCCCcEEEEEeecCCCcccccccc---cCCCCceEEEEecCCeEEEecC---CCcE
Q Q5E705_VIBF1/1 4 QSAGVWIPAREVAYV------HGLSSDDTVMIAMADNLTGRVNHEMAL---NRPPRVSMSFNGVEASNGFKVP---YGGS 71 (302)
Q Consensus 4 ~~TG~y~~~Ge~i~V------~~~~~~~~~~v~i~~~~~~~~~~~~~~---~r~~~~~~~~~L~~g~n~i~~p---~GG~ 71 (302)
|||||.+.+|+.|+| +-.....-+..--|.+....+...... =....-.+.|.+-.|+-.=++| .-|.
T Consensus 14 q~Tglilk~GDiIsIvA~GW~kyG~~~~~~aapqg~~p~~g~~~~~~~~~~LvaKIgnk~y~igNg~Lhktvpp~~vdGe 93 (121)
T pfam07828 14 KSTGIILKPGDTISIVAAGWAKYGPDNKEGAAGDGEHPDNGLICHDAFCAALVAKIANKGFAIGNGGLFKTVAPNNVDGA 93 (121)
T ss_pred CcceeEEcCCCEEEEeeechhhcCCCCCcccCCCCcCCCCCcccCcccchhhhhhhccccccccCceeeeecCCcccCce
Q ss_pred EEEEcCCCCc----------eEEEEec
Q Q5E705_VIBF1/1 72 VYITLGSKES----------AQVSFGG 88 (302)
Q Consensus 72 iyi~~~~~~~----------v~v~i~~ 88 (302)
|-+.+.+.+. |+|.|.+
T Consensus 94 lillf~D~pg~ygdNSgeF~V~V~ies 120 (121)
T pfam07828 94 IILIFNDVPGTFGDNSGEFQVEIGIDQ 120 (121)
T ss_pred EEEEEeCCCCcccCCCccEEEEEEEec
No 5
>3N2V_Entity_1
Probab=80.20 E-value=5.1 Score=34.36 Aligned_cols=90 Identities=11% Similarity=-0.278 Sum_probs=0.0
Q ss_pred CHHHHHHHHHHHHHHHHHHhCCCCCCccccccccccccccchhhceeeeeccccceecCCcceeeeccccccceeccCCC
Q Q5E705_VIBF1/1 141 DVLEMTKQFDLFTIGVNEFYGRDGVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHSGYPVMSTSFPRQKSSLFKATD 220 (302)
Q Consensus 141 d~~~l~~~~d~ii~~~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~g~~~~~~~~~~~~~~~~~~~~ 220 (302)
...+.-+...+.++...+.++++..............................+...++..+-.................
T Consensus 21 ~~~~~~~~i~~A~~~W~~~~~i~F~~~~~~~~~~~~~~~~~~~~~~~~~~~~~g~~~~~~~~~~~~~~~~~~~~~~~~~~ 100 (158)
T 3N2V_Entity_1 21 NREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTT 100 (158)
T ss_pred CHHHHHHHHHHHHHHHHhhcCeeEEEeccCCceEEEEEeecccCcccccccccceeeeccCCCCceeeeEEeecceeeee
Q ss_pred cch-------hHHhhhh
Q Q5E705_VIBF1/1 221 NWM-------LGHEIGH 230 (302)
Q Consensus 221 ~WG-------~~HEiGH 230 (302)
..+ +.|||||
T Consensus 101 ~~~~~~~~~v~~HEiGH 117 (158)
T 3N2V_Entity_1 101 HSGGTNLFLTAVHEIGH 117 (158)
T ss_pred ccCCccceeeehhhhcc
No 6
>3N2U_Entity_1
Probab=80.20 E-value=5.1 Score=34.36 Aligned_cols=90 Identities=11% Similarity=-0.278 Sum_probs=0.0
Q ss_pred CHHHHHHHHHHHHHHHHHHhCCCCCCccccccccccccccchhhceeeeeccccceecCCcceeeeccccccceeccCCC
Q Q5E705_VIBF1/1 141 DVLEMTKQFDLFTIGVNEFYGRDGVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHSGYPVMSTSFPRQKSSLFKATD 220 (302)
Q Consensus 141 d~~~l~~~~d~ii~~~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~g~~~~~~~~~~~~~~~~~~~~ 220 (302)
...+.-+...+.++...+.++++..............................+...++..+-.................
T Consensus 21 ~~~~~~~~i~~A~~~W~~~~~i~F~~~~~~~~~~~~~~~~~~~~~~~~~~~~~g~~~~~~~~~~~~~~~~~~~~~~~~~~ 100 (158)
T 3N2U_Entity_1 21 NREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTT 100 (158)
T ss_pred CHHHHHHHHHHHHHHHHhhcCeeEEEeccCCceEEEEEeecccCcccccccccceeeeccCCCCceeeeEEeecceeeee
Q ss_pred cch-------hHHhhhh
Q Q5E705_VIBF1/1 221 NWM-------LGHEIGH 230 (302)
Q Consensus 221 ~WG-------~~HEiGH 230 (302)
..+ +.|||||
T Consensus 101 ~~~~~~~~~v~~HEiGH 117 (158)
T 3N2U_Entity_1 101 HSGGTNLFLTAVHEIGH 117 (158)
T ss_pred ccCCccceeeehhhhcc
No 7 
>1l7l_A PA-I galactophilic lectin; agglutinin, single wavelength anomalous scattering phasing, structural
genomics, PSI; 1.50A {Pseudomonas aeruginosa} SCOP: b.18.1.16 PDB: 1oko _A* 1uoj _A 2vxj _A* 2wyf _A*
Probab=78.63 E-value=3.8 Score=33.02 Aligned_cols=15 Identities=13% Similarity=0.184 Sum_probs=0.0
Q ss_pred ccceEEECCCCEEEE
Q Q5E705_VIBF1/1 4 QSAGVWIPAREVAYV 18 (302)
Q Consensus 4 ~~TG~y~~~Ge~i~V 18 (302)
|||||.+.+|+.|+|
T Consensus 14 q~Tglilk~GDiIsI 28 (121)
T 1l7l_A 14 QVTSIIYNPGDVITI 28 (121)
T ss_dssp EEEEEEECTTCCEEE
T ss_pred CeeeEEecCCCEEEE
No 8
>1qib_A Protein (gelatinase A); inhibitor, matrixin, matrix metalloproteinase-2 (MMP-2), metzincin, hydrolase;
2.80A {Homo sapiens} SCOP: d.92.1.11 PDB: 1hov _A*
Probab=78.35 E-value=3.9 Score=35.24 Aligned_cols=90 Identities=10% Similarity=-0.239 Sum_probs=0.0
Q ss_pred CHHHHHHHHHHHHHHHHHHhCCCCCCccccccccccccccchhhceeeeeccccceecCCcceeeeccccccceeccCCC
Q Q5E705_VIBF1/1 141 DVLEMTKQFDLFTIGVNEFYGRDGVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHSGYPVMSTSFPRQKSSLFKATD 220 (302)
Q Consensus 141 d~~~l~~~~d~ii~~~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~g~~~~~~~~~~~~~~~~~~~~ 220 (302)
+..++-+...+.++...+.+++...................................+......................
T Consensus 22 ~~~~~~~ai~~A~~~W~~~~~i~F~~~~~~~ad~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~ 101 (161)
T 1qib_A 22 DPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWSL 101 (161)
T ss_dssp CHHHHHHHHHHHHHHHHTSSSCEEEECSSSCCSEEEEEECSCCSSSCCCCSSSSCCEEECCSCSTTTTCEEEETTSCEES
T ss_pred CHHHHHHHHHHHHHHHhcccCceEEEeccCCCcEEEeeccccccccccccCccccccccccCCCccccceeecccccccc
Q ss_pred cch--------hHHhhhh
Q Q5E705_VIBF1/1 221 NWM--------LGHEIGH 230 (302)
Q Consensus 221 ~WG--------~~HEiGH 230 (302)
.+. +.|||||
T Consensus 102 ~~~~~~~~~~v~~HEiGH 119 (161)
T 1qib_A 102 GKGVGYSLFLVAAHEFGH 119 (161)
T ss_dssp SSSSSEEHHHHHHHHHHH
T ss_pred ccccCcceeeeeeeehhh
No 9
>1i76_A MMP-8;, neutrophil collagenase; hydrolase, complex (metalloprotease/inhibitor); HET: BSI; 1.20A {Homo
sapiens} SCOP: d.92.1.11 PDB: 1i73 _A* 1jao _A* 1jap _A 1jaq _A* 1jj9 _A* 1mmb _A* 1zp5 _A* 1zs0 _A* 1zvx _A* 3dng _A*
3dpe _A* 3dpf _A* 1kbc _A* 1jan _A* 1bzs _A* 1mnc _A* 2oy2 _A 1a86 _A* 1jh1 _A* 1a85 _A ...
Probab=76.88 E-value=9.9 Score=33.27 Aligned_cols=86 Identities=12% Similarity=-0.072 Sum_probs=0.0
Q ss_pred CHHHHHHHHHHHHHHHHHHhCCCCCCccccccccccccccchhhceeeeeccccceecCCcceeeeccccccceeccCCC
Q Q5E705_VIBF1/1 141 DVLEMTKQFDLFTIGVNEFYGRDGVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHSGYPVMSTSFPRQKSSLFKATD 220 (302)
Q Consensus 141 d~~~l~~~~d~ii~~~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~g~~~~~~~~~~~~~~~~~~~~ 220 (302)
+..+.-+...+.++...+.+++...............+...............+...+. ..+.........++...
T Consensus 26 ~~~~~~~~i~~A~~~W~~v~~i~F~ev~~~~~di~i~~~~~~~~~~~~~~~~~~~~~~~----~~~~~~~~~~i~~~~~~ 101 (163)
T 1i76_A 26 SEAEVERAIKDAFELWSVASPLIFTRISQGEADINIAFYQRDHGDNSPFDGPNGILAHA----FQPGQGIGGDAHFDAEE 101 (163)
T ss_dssp CHHHHHHHHHHHHHHHHTTSSCEEEECSSSCCSEEEEEECSCCSSSCCCCSSSSCCEEE----CCSSSTTTTCEEEETTS
T ss_pred CHHHHHHHHHHHHHHHhCcCCcEEEEeccCCCcEEEEEeccccccccccCCcccceecc----cCCCCceeeEEecChHh
Q ss_pred cc-----------hhHHhhhh
Q Q5E705_VIBF1/1 221 NW-----------MLGHEIGH 230 (302)
Q Consensus 221 ~W-----------G~~HEiGH 230 (302)
.| -+.|||||
T Consensus 102 ~~~~~~~~~~~~~v~~HEIGH 122 (163)
T 1i76_A 102 TWTNTSANYNLFLVAAHEFGH 122 (163)
T ss_dssp CCBSSSSSCBHHHHHHHHHHH
T ss_pred ccccccccceeEEEeeehhcc
No 10
>1hv5_A Stromelysin 3; inhibition, phosphinic inhibitor, hydrolase; HET: CPS RXP; 2.60A {Mus musculus} SCOP:
d.92.1.11
Probab=76.47 E-value=11 Score=32.51 Aligned_cols=90 Identities=11% Similarity=-0.091 Sum_probs=0.0
Q ss_pred CHHHHHHHHHHHHHHHHHHhCCC--CCCccccccccccccccchhhceeeeeccccceecCCcceeeeccccccceeccC
Q Q5E705_VIBF1/1 141 DVLEMTKQFDLFTIGVNEFYGRD--GVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHSGYPVMSTSFPRQKSSLFKA 218 (302)
Q Consensus 141 d~~~l~~~~d~ii~~~~~l~Gl~--~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~g~~~~~~~~~~~~~~~~~~ 218 (302)
...+.-+.+.+.++..++.+++. +..............................+..+....................
T Consensus 26 ~~~~~~~~i~~A~~~W~~~~~i~F~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~ 105 (165)
T 1hv5_A 26 VREQVRQTVAEALQVWSEVTPLTFTEVHEGRADIMIDFARYWHGDNLPFDGPGGILAHAFFPKTHREGDVHFDYDETWTI 105 (165)
T ss_dssp CHHHHHHHHHHHHHHHHTTSSCEEEECSSSBCSEEEEEECSCSSSSCCCCSSSSCCEEEECCTTSSSEEEEEETTSCEES
T ss_pred CHHHHHHHHHHHHHHHhCcCCceEEEccCCCCCeEEEeeccccCCcccccccceeecccccCCCceeeeeeecccccccc
Q ss_pred CCcch------hHHhhhh
Q Q5E705_VIBF1/1 219 TDNWM------LGHEIGH 230 (302)
Q Consensus 219 ~~~WG------~~HEiGH 230 (302)
....+ +.|||||
T Consensus 106 ~~~~~~~~~~v~~HEiGH 123 (165)
T 1hv5_A 106 GDNQGTDLLQVAAHEFGH 123 (165)
T ss_dssp SCSSSEEHHHHHHHHHHH
T ss_pred ccccCcchhhhhhhhhhh
No 11
>PF12388 Peptidase_M57: Dual-action HEIGH metallo-peptidase
Probab=75.62 E-value=11 Score=34.62 Aligned_cols=85 Identities=14% Similarity=-0.095 Sum_probs=0.0
Q ss_pred HHHHHHHHHHHHHHHHhCCCCCCccccccccccccccchhhceeeeeccccceecCCcceeeeccccccceeccCCC---
Q Q5E705_VIBF1/1 144 EMTKQFDLFTIGVNEFYGRDGVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHSGYPVMSTSFPRQKSSLFKATD--- 220 (302)
Q Consensus 144 ~l~~~~d~ii~~~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~g~~~~~~~~~~~~~~~~~~~~--- 220 (302)
.+....++.|..++.+ |+.... +..-......................++.+.-..--+.+...... +.....+
T Consensus 56 ~~~~al~~Ai~~yN~l-~l~i~F-~~tfg~~~~~~di~v~~~~~~~~~g~ggsAgFP~s~G~P~~~I~I-~~~~~~~~~~ 132 (211)
T PF12388_consen 56 AWRTALDQAINNYNAL-NLSISF-RLTFGTNYQNADIVVYSDSSNNPSGVGGSAGFPTSNGNPYKSIQI-YGSNNYSVNV 132 (211)
T ss_pred HHHHHHHHHHHHHHhh-CcceEE-EEEeccCccccceEEEeccccCcCCcceeccCCccCCCCCceEEE-EecCCcchHH
Q ss_pred -cchhHHhhhhh
Q Q5E705_VIBF1/1 221 -NWMLGHEIGHN 231 (302)
Q Consensus 221 -~WG~~HEiGH~ 231 (302)
-+-+.|||||.
T Consensus 133 ~~~vi~HEIGH~ 144 (211)
T PF12388_consen 133 NAHVITHEIGHC 144 (211)
T ss_pred HHHHHHHHhhhh
No 12
>1y93_A Macrophage metalloelastase; matrix metalloproteinase, MMP12, complex (elastase-inhibitor),
acetohydroxamic acid, hydrolase; 1.03A {Homo sapiens} SCOP: d.92.1.11 PDB: 1rmz _A 1ycm _A* 1z3j _A* 2hu6 _A* 2oxu _A 2oxw _A
2oxz _A 1os9 _A 1os2 _A 3f17 _A* 3ehy _A* 3ehx _A* 3f15 _A* 3f16 _A* 3f18 _A* 3f19 _A* 3f1a _A* 3lka _A* 2wo9 _A* 2wo8 _A* ...
Probab=74.81 E-value=5.9 Score=34.08 Aligned_cols=90 Identities=11% Similarity=-0.278 Sum_probs=0.0
Q ss_pred CHHHHHHHHHHHHHHHHHHhCCCCCCccccccccccccccchhhceeeeeccccceecCCcceeeeccccccceeccCCC
Q Q5E705_VIBF1/1 141 DVLEMTKQFDLFTIGVNEFYGRDGVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHSGYPVMSTSFPRQKSSLFKATD 220 (302)
Q Consensus 141 d~~~l~~~~d~ii~~~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~g~~~~~~~~~~~~~~~~~~~~ 220 (302)
...+.-+...+.++...+.+++...............................+...++..+..................
T Consensus 22 ~~~~~~~~i~~Af~~W~~~~~i~f~~~~~~~~~~~i~~~~~~~~~~~~~~~~~g~~~~~~~~~~~~~~~~~~~~~~~~~~ 101 (159)
T 1y93_A 22 NREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTT 101 (159)
T ss_dssp CHHHHHHHHHHHHHHHHTTSSCEEEECSSSCCSEEEEEECSCCSSSCCCCSSSSCCEEECCSCSTTTTCEEEETTSCEES
T ss_pred CHHHHHHHHHHHHHHHHhhccceEEEeeccCcceEEEeeecccccccccCCCceeeeeccCCCCceeeeEeeccccccee
Q ss_pred cch-------hHHhhhh
Q Q5E705_VIBF1/1 221 NWM-------LGHEIGH 230 (302)
Q Consensus 221 ~WG-------~~HEiGH 230 (302)
..+ +.|||||
T Consensus 102 ~~~~~~~~~v~~HEiGH 118 (159)
T 1y93_A 102 HSGGTNLFLTAVHEIGH 118 (159)
T ss_dssp SSSSEEHHHHHHHHHHH
T ss_pred ccCCcchhhhhhhhhcc
No 13
>d1i76a_ d.92.1.11 (A:) Neutrophil collagenase (MMP-8) {Human (Homo sapiens) [TaxId: 9606]}
Probab=74.68 E-value=7.2 Score=33.86 Aligned_cols=90 Identities=10% Similarity=-0.222 Sum_probs=0.0
Q ss_pred CHHHHHHHHHHHHHHHHHHhCCCCCCccccccccccccccchhhceeeeeccccceecCCcceeeeccccccceeccCCC
Q Q5E705_VIBF1/1 141 DVLEMTKQFDLFTIGVNEFYGRDGVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHSGYPVMSTSFPRQKSSLFKATD 220 (302)
Q Consensus 141 d~~~l~~~~d~ii~~~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~g~~~~~~~~~~~~~~~~~~~~ 220 (302)
...+.-+...+.++...+.+++...............................+...+......................
T Consensus 26 ~~~~~~~~i~~Af~~ws~v~~i~F~ev~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~i~~~~~~~~~~ 105 (163)
T d1i76a_ 26 SEAEVERAIKDAFELWSVASPLIFTRISQGEADINIAFYQRDHGDNSPFDGPNGILAHAFQPGQGIGGDAHFDAEETWTN 105 (163)
T ss_dssp CHHHHHHHHHHHHHHHHTTSSCEEEECSSSCCSEEEEEECSCCSSSCCCCSSSSCCEEECCSSSTTTTCEEEETTSCCBS
T ss_pred CHHHHHHHHHHHHHHHhcccCceEEEecCCCcceEEEeeecccccccccCCcccceeeccCCCCceeeEEeecccccccc
Q ss_pred cch-------hHHhhhh
Q Q5E705_VIBF1/1 221 NWM-------LGHEIGH 230 (302)
Q Consensus 221 ~WG-------~~HEiGH 230 (302)
.++ ++|||||
T Consensus 106 ~~~~~~~~~v~~HEiGH 122 (163)
T d1i76a_ 106 TSANYNLFLVAAHEFGH 122 (163)
T ss_dssp SSSSCBHHHHHHHHHHH
T ss_pred ccccchheeehhhhhhh
No 14
>1hy7_A Stromelysin-1, MMP-3; mixed alpha beta structure, zinc protease, inhibited, hydrolase; HET: MBS; 1.50A
{Homo sapiens} SCOP: d.92.1.11 PDB: 1biw _A* 1bm6 _A* 1bqo _A* 1b3d _A* 1cqr _A 1d5j _A* 1d7x _A* 1d8f _A* 1d8m _A*
1g05 _A* 1g49 _A* 1c3i _A* 1sln _A* 1uea _A 2srt _A* 1ums _A* 1umt _A* 2d1o _A* 1ciz _A* 1caq _A* ...
Probab=73.26 E-value=9.4 Score=33.47 Aligned_cols=90 Identities=9% Similarity=-0.210 Sum_probs=0.0
Q ss_pred CHHHHHHHHHHHHHHHHHHhCCCCCCccccccccccccccchhhceeeeeccccceecC-------Ccceeeeccccccc
Q Q5E705_VIBF1/1 141 DVLEMTKQFDLFTIGVNEFYGRDGVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHS-------GYPVMSTSFPRQKS 213 (302)
Q Consensus 141 d~~~l~~~~d~ii~~~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~-------g~~~~~~~~~~~~~ 213 (302)
...+.-+...+.++..++++++...............................+...+. ...+....+.....
T Consensus 27 ~~~~~~~~i~~A~~~W~~~~~i~F~e~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~ 106 (173)
T 1hy7_A 27 PKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWTK 106 (173)
T ss_dssp CHHHHHHHHHHHHHHHHTTSSCEEEECSSSCCSEEEEEECSSCSSSCCCCSSSSCCEEECCSSSTTTTCEEEETTSCEES
T ss_pred CHHHHHHHHHHHHHHHhhhcCceEEEecCCCCcEEEEEeccccCccccccccccccccccccCCCccceeeecccccccc
Q ss_pred eeccCCCcchhHHhhhh
Q Q5E705_VIBF1/1 214 SLFKATDNWMLGHEIGH 230 (302)
Q Consensus 214 ~~~~~~~~WG~~HEiGH 230 (302)
......-.+-+.|||||
T Consensus 107 ~~~~~~~~~v~~HEiGH 123 (173)
T 1hy7_A 107 DTTGTNLFLVAAHEIGH 123 (173)
T ss_dssp SSSSEEHHHHHHHHHHH
T ss_pred cccccchhhhhhhhhcc
No 15
>d1l7la_ b.18.1.16 (A:) PA-IL, galactose-binding lectin 1 {Pseudomonas aeruginosa [TaxId: 287]}
Probab=73.12 E-value=18 Score=28.88 Aligned_cols=78 Identities=9% Similarity=-0.024 Sum_probs=0.0
Q ss_pred ccceEEECCCCEEEE----EecCCCCcEEEEEe--ecCCCcccccc----cccCCCCceEEEEecCCeEEEecC--CCcE
Q Q5E705_VIBF1/1 4 QSAGVWIPAREVAYV----HGLSSDDTVMIAMA--DNLTGRVNHEM----ALNRPPRVSMSFNGVEASNGFKVP--YGGS 71 (302)
Q Consensus 4 ~~TG~y~~~Ge~i~V----~~~~~~~~~~v~i~--~~~~~~~~~~~----~~~r~~~~~~~~~L~~g~n~i~~p--~GG~ 71 (302)
|+|||++.+|+.|+| .+.-...+----.+ .|....+.+.+ .+.--...+-+|++..|+-.-+.| .-|.
T Consensus 14 k~T~lI~~~GD~IsvvA~GW~~yG~~~~WgPqg~~~~P~~~l~~~d~~~~aLv~KIgn~~t~~i~~Gv~~~~~P~~V~G~ 93 (121)
T d1l7la_ 14 QVTSIIYNPGDVITIVAAGWASYGPTQKWGPQGDREHPDQGLICHDAFCGALVMKIGNSGTIPVNTGLFRWVAPNNVQGA 93 (121)
T ss_dssp EEEEEEECTTCCEEEEEEEEEESSSSSCBCTBCCTTSCCSSCSCTTSCTTBEEEEETTCCCEECTTEEEEECCCTTCCEE
T ss_pred ceeEEEecCCCEEEEeeechhhhCCcccccCCCCCCCCcccccccchhHHHHhhhhcccceEeccCcEEEEecCCccCce
Q ss_pred EEEEcCCCCc
Q Q5E705_VIBF1/1 72 VYITLGSKES 81 (302)
Q Consensus 72 iyi~~~~~~~ 81 (302)
|-+.+.+.+.
T Consensus 94 l~Ll~NDvPg 103 (121)
T d1l7la_ 94 ITLIYNDVPG 103 (121)
T ss_dssp EEEEECCCTT
T ss_pred EEEEEcCCCc
No 16
>1mmq_A Matrilysin; metalloprotease; HET: RRS; 1.90A {Homo sapiens} SCOP: d.92.1.11 PDB: 1mmp _A* 1mmr _A* 2ddy _A*
Probab=72.30 E-value=9.9 Score=33.19 Aligned_cols=90 Identities=10% Similarity=-0.186 Sum_probs=0.0
Q ss_pred CHHHHHHHHHHHHHHHHHHhCCCCCCccccccccccccccchhhceeeeeccccceecCCcceeeeccccccceeccCCC
Q Q5E705_VIBF1/1 141 DVLEMTKQFDLFTIGVNEFYGRDGVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHSGYPVMSTSFPRQKSSLFKATD 220 (302)
Q Consensus 141 d~~~l~~~~d~ii~~~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~g~~~~~~~~~~~~~~~~~~~~ 220 (302)
...+.-+...+.++...+.+++................................+..+......................
T Consensus 27 ~~~~~~~~i~~A~~~W~~v~~l~F~ev~~~~~di~i~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~ 106 (170)
T 1mmq_A 27 PHITVDRLVSKALNMWGKEIPLHFRKVVWGTADIMIGFARGAHGDSYPFDGPGNTLAHAFAPGTGLGGDAHFDEDERWTD 106 (170)
T ss_dssp CHHHHHHHHHHHHHHHHHHSSCEEEECSSSCCSEEEEEECSCCSSSCCCCSSSSCCEEECCSSSTTTTCEEEETTSCEES
T ss_pred CHHHHHHHHHHHHHHHhCccCceEEEeccCCCceEEEeeccCcccccccccccceeccccccccceeeeEEccccccccc
Q ss_pred c--------chhHHhhhh
Q Q5E705_VIBF1/1 221 N--------WMLGHEIGH 230 (302)
Q Consensus 221 ~--------WG~~HEiGH 230 (302)
. .-++|||||
T Consensus 107 ~~~~~~~~~~v~~HEiGH 124 (170)
T 1mmq_A 107 GSSLGINFLYAATHELGH 124 (170)
T ss_dssp SSSSSEEHHHHHHHHHHH
T ss_pred ccccccchhheeehhccc
No 17 
>SUPFAM template d.92.1 Metalloproteases ("zincins"), catalytic domain (55486) SCOP seed sequence: d1fbl_2.
Probab=71.43 E-value=4.4 Score=32.12 Aligned_cols=9 Identities=44% Similarity=0.829 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
..|||||..
T Consensus 117 ~~HE~GH~L 125 (172)
T SUPFAM0037477 117 AAHELGHAL 125 (172)
T ss_pred hhhhhhhhh
No 18
>d1hfca_ d.92.1.11 (A:) Fibroblast collagenase (MMP-1) {Human (Homo sapiens) [TaxId: 9606]}
Probab=70.95 E-value=16 Score=31.37 Aligned_cols=90 Identities=9% Similarity=-0.121 Sum_probs=0.0
Q ss_pred CHHHHHHHHHHHHHHHHHHhCCCCCCccccccccccccccchhhceeeeeccccceecC-------Ccceeeeccccccc
Q Q5E705_VIBF1/1 141 DVLEMTKQFDLFTIGVNEFYGRDGVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHS-------GYPVMSTSFPRQKS 213 (302)
Q Consensus 141 d~~~l~~~~d~ii~~~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~-------g~~~~~~~~~~~~~ 213 (302)
...+.-+.+.+.++...+.+++...............................+...+. +.-+....+.....
T Consensus 20 ~~~~~~~~i~~A~~~W~~~~~i~F~~v~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~i~~~~~~~~~~ 99 (157)
T d1hfca_ 20 PRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTN 99 (157)
T ss_dssp CHHHHHHHHHHHHHHHHTTSSCEEEECSSSCCSEEEEEECSSCSSSCCCCSSSSCCEEECCSSSTTTTCEEEETTSCCBS
T ss_pred CHHHHHHHHHHHHHHHHhhcCccEEEeccCCcccceeeeccccccccccCCCcceeEEeecCCCCeeeeEEecccccccc
Q ss_pred eeccCCCcchhHHhhhh
Q Q5E705_VIBF1/1 214 SLFKATDNWMLGHEIGH 230 (302)
Q Consensus 214 ~~~~~~~~WG~~HEiGH 230 (302)
.......-.-+.|||||
T Consensus 100 ~~~~~~~~~v~~HEiGH 116 (157)
T d1hfca_ 100 NFREYNLHRVAAHELGH 116 (157)
T ss_dssp SSSSCBHHHHHHHHHHH
T ss_pred ccccchhhhhHhhhhhh
No 19
>SUPFAM template d.92.1 Metalloproteases ("zincins"), catalytic domain (55486) SCOP seed sequence: d1q3aa_.
Probab=70.95 E-value=4.2 Score=31.55 Aligned_cols=8 Identities=50% Similarity=0.999 Sum_probs=0.0
Q ss_pred hHHhhhhh
Q Q5E705_VIBF1/1 224 LGHEIGHN 231 (302)
Q Consensus 224 ~~HEiGH~ 231 (302)
..|||||.
T Consensus 111 ~~HE~GH~ 118 (159)
T SUPFAM0042596 111 AAHELGHA 118 (159)
T ss_pred hhhhhhhh
No 20
>SUPFAM template d.92.1 Metalloproteases ("zincins"), catalytic domain (55486) SCOP seed sequence: d1hfs__.
Probab=70.22 E-value=4.6 Score=31.36 Aligned_cols=8 Identities=50% Similarity=0.999 Sum_probs=0.0
Q ss_pred hHHhhhhh
Q Q5E705_VIBF1/1 224 LGHEIGHN 231 (302)
Q Consensus 224 ~~HEiGH~ 231 (302)
..||+||.
T Consensus 112 ~~HE~GH~ 119 (160)
T SUPFAM0038581 112 AAHELGHA 119 (160)
T ss_pred hhhhhhhh
No 21
>SUPFAM template d.92.1 Metalloproteases ("zincins"), catalytic domain (55486) SCOP seed sequence: d1cxva_.
Probab=69.47 E-value=4.9 Score=31.51 Aligned_cols=9 Identities=44% Similarity=0.829 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
..||+||..
T Consensus 117 ~~HE~GH~L 125 (164)
T SUPFAM0036188 117 AAHELGHAL 125 (164)
T ss_pred hhhhhhhhc
No 22 
>PIRSF005785 Zn-prot_arch
Probab=68.91 E-value=4.5 Score=36.84 Aligned_cols=10 Identities=40% Similarity=0.521 Sum_probs=0.0
Q ss_pred hhHHhhhhhc
Q Q5E705_VIBF1/1 223 MLGHEIGHNQ 232 (302)
Q Consensus 223 G~~HEiGH~~ 232 (302)
+..||+||.+
T Consensus 149 Ev~HElGH~f 158 (204)
T PIRSF005785 149 EVLHELGHVF 158 (204)
T ss_pred hhhcchhhhc
No 23
>d1mmqa_ d.92.1.11 (A:) Matrilysin (MMP-7) {Human (Homo sapiens) [TaxId: 9606]}
Probab=68.51 E-value=13 Score=32.42 Aligned_cols=90 Identities=10% Similarity=-0.216 Sum_probs=0.0
Q ss_pred CHHHHHHHHHHHHHHHHHHhCCCCCCccccccccccccccchhhceeeeeccccceecCCcceeeeccccccceeccCCC
Q Q5E705_VIBF1/1 141 DVLEMTKQFDLFTIGVNEFYGRDGVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHSGYPVMSTSFPRQKSSLFKATD 220 (302)
Q Consensus 141 d~~~l~~~~d~ii~~~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~g~~~~~~~~~~~~~~~~~~~~ 220 (302)
...+.-+...+.++...+.+++...............................+..++..+.-.................
T Consensus 27 ~~~~~~~~i~~A~~~W~~v~~i~F~~v~~~~~di~i~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~i~~~~~~~~~~ 106 (166)
T d1mmqa_ 27 PHITVDRLVSKALNMWGKEIPLHFRKVVWGTADIMIGFARGAHGDSYPFDGPGNTLAHAFAPGTGLGGDAHFDEDERWTD 106 (166)
T ss_dssp CHHHHHHHHHHHHHHHHHHSSCEEEECSSSCCSEEEEEECSCCSSSCCCCSSSSCCEEECCSSSTTTTCEEEETTSCEES
T ss_pred CHHHHHHHHHHHHHHHhCcCCeeEEecccCCcceEEEEeccccCCcccccccceeeeeccCCCccccceEEecchhhhhc
Q ss_pred cch--------hHHhhhh
Q Q5E705_VIBF1/1 221 NWM--------LGHEIGH 230 (302)
Q Consensus 221 ~WG--------~~HEiGH 230 (302)
.+. +.|||||
T Consensus 107 ~~~~~~~~~~v~~HEiGH 124 (166)
T d1mmqa_ 107 GSSLGINFLYAATHELGH 124 (166)
T ss_dssp SSSSSEEHHHHHHHHHHH
T ss_pred cccccchhhhhhhhhhcc
No 24
>SUPFAM template d.92.1 Metalloproteases ("zincins"), catalytic domain (55486) SCOP seed sequence: d1cgla_.
Probab=68.50 E-value=5.3 Score=31.53 Aligned_cols=9 Identities=44% Similarity=0.829 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
..||+||..
T Consensus 116 ~~HE~GH~L 124 (168)
T SUPFAM0035975 116 AAHELGHAL 124 (168)
T ss_pred hhhhhhhhc
No 25
>d1kapp2 d.92.1.6 (P:1-246) Metalloprotease {Pseudomonas aeruginosa [TaxId: 287]}
Probab=68.42 E-value=19 Score=33.97 Aligned_cols=88 Identities=14% Similarity=-0.068 Sum_probs=0.0
Q ss_pred HHHHHHHHHHHHHHHHHhCCCCCCccccccccccccccchhhceeeeeccccceecCCcceeeeccccccceeccCCCcc
Q Q5E705_VIBF1/1 143 LEMTKQFDLFTIGVNEFYGRDGVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHSGYPVMSTSFPRQKSSLFKATDNW 222 (302)
Q Consensus 143 ~~l~~~~d~ii~~~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~g~~~~~~~~~~~~~~~~~~~~~W 222 (302)
.+-.+...+.++...+++++.........................+...........+..+....+...........++.
T Consensus 90 ~~q~~~vr~A~~~ws~va~i~F~ev~~~~~adI~~~~~~~~~~~~~~a~~~~~~~~~~~~~~~~~~~~~~~~~~~~~g~~ 169 (246)
T d1kapp2 90 AQQQAQAKLSLQSWSDVTNIHFVDAGQGDQGDLTFGNFSSSVGGAAFAFLPDVPDALKGQSWYLINSSYSANVNPANGNY 169 (246)
T ss_dssp HHHHHHHHHHHHHHHTTBSEEEEEEEESSCSSEEEEEECSCCSSSEEECCTTSCTTTTTEEEEECSSSCCTTTSCCTTSH
T ss_pred HHHHHHHHHHHHHHHHhhCcceeeccCCCceEEEEEEeCCCCCCeeEeccCCCCcccccccccccccccccccCcccchh
Q ss_pred h---hHHhhhh
Q Q5E705_VIBF1/1 223 M---LGHEIGH 230 (302)
Q Consensus 223 G---~~HEiGH 230 (302)
+ ++|||||
T Consensus 170 ~~~t~lHEIGH 180 (246)
T d1kapp2 170 GRQTLTHEIGH 180 (246)
T ss_dssp HHHHHHHHHHH
T ss_pred HHHHHHHHHHH
No 26
>SUPFAM template d.92.1 Metalloproteases ("zincins"), catalytic domain (55486) SCOP seed sequence: d1eaka2.
Probab=68.11 E-value=5.3 Score=31.41 Aligned_cols=9 Identities=44% Similarity=0.829 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
..|||||..
T Consensus 118 ~~HE~GH~L 126 (169)
T SUPFAM0036877 118 AAHELGHAL 126 (169)
T ss_pred hhhhhhhhh
No 27
>1cge_A Fibroblast collagenase; hydrolase (metalloprotease); 1.90A {Homo sapiens} SCOP: d.92.1.11 PDB: 2j0t _A
1ayk _A 1hfc _A* 2ayk _A 2tcl _A* 3ayk _A* 4ayk _A* 1cgl _A* 1cgf _A 966c _A*
Probab=67.83 E-value=19 Score=31.44 Aligned_cols=90 Identities=8% Similarity=-0.156 Sum_probs=0.0
Q ss_pred CHHHHHHHHHHHHHHHHHHhCCCCCCccccccccccccccchhhceeeeeccccceecCCc-------ceeeeccccccc
Q Q5E705_VIBF1/1 141 DVLEMTKQFDLFTIGVNEFYGRDGVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHSGY-------PVMSTSFPRQKS 213 (302)
Q Consensus 141 d~~~l~~~~d~ii~~~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~g~-------~~~~~~~~~~~~ 213 (302)
+..+..+...+.++...+.+++...............................+..++..+ -+....+.....
T Consensus 25 ~~~~~~~ai~~A~~~W~~~~~i~F~~v~~~~~di~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~ 104 (168)
T 1cge_A 25 PRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTN 104 (168)
T ss_dssp CHHHHHHHHHHHHHHHHTTSSCEEEECSSSCCSEEEEEECSCCSSSSCCCSSSSCCEEECCSSSTTTTCEEEETTSCCBS
T ss_pred CHHHHHHHHHHHHHHHHhhcCeeEEEccCCCCceEEEeecccccccccccccccceeeeeCCCCceeeeEEeeccccccc
Q ss_pred eeccCCCcchhHHhhhh
Q Q5E705_VIBF1/1 214 SLFKATDNWMLGHEIGH 230 (302)
Q Consensus 214 ~~~~~~~~WG~~HEiGH 230 (302)
.........-+.|||||
T Consensus 105 ~~~~~~~~~v~~HEiGH 121 (168)
T 1cge_A 105 NFREYNLHRVAAHELGH 121 (168)
T ss_dssp SSSSCBHHHHHHHHHHH
T ss_pred ccchhHHHHHHHHHhhh
No 28
>SUPFAM template d.92.1 Metalloproteases ("zincins"), catalytic domain (55486) SCOP seed sequence: d1mmq__.
Probab=67.51 E-value=5.6 Score=31.27 Aligned_cols=9 Identities=44% Similarity=0.829 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
..||+||..
T Consensus 118 ~~HE~GH~L 126 (166)
T SUPFAM0041006 118 AAHELGHAL 126 (166)
T ss_pred hhhhhhhhc
No 29
>pfam04228 Zn_peptidase Putative neutral zinc metallopeptidase. Members of this family have a predicted zinc
binding motif characteristic of neutral zinc metallopeptidases (Prosite:PDOC00129).
Probab=67.23 E-value=5.6 Score=37.94 Aligned_cols=12 Identities=33% Similarity=0.938 Sum_probs=0.0
Q ss_pred chhHHhhhhhcc
Q Q5E705_VIBF1/1 222 WMLGHEIGHNQA 233 (302)
Q Consensus 222 WG~~HEiGH~~Q 233 (302)
+.+.||+|||-|
T Consensus 172 YViAHEvGHHVQ 183 (292)
T pfam04228 172 YVIAHEVGHHVQ 183 (292)
T ss_pred HHHHhhhhhHHH
No 30
>SUPFAM template d.92.1 Metalloproteases ("zincins"), catalytic domain (55486) SCOP seed sequence: d1bzsa_.
Probab=66.81 E-value=4.9 Score=31.35 Aligned_cols=9 Identities=44% Similarity=0.829 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
..||+||..
T Consensus 117 ~~HE~GH~L 125 (165)
T SUPFAM0035790 117 AAHELGHAL 125 (165)
T ss_pred eehhhhhhc
No 31
>1bkcA00 3.40.390.10
Probab=65.58 E-value=6.6 Score=33.49 Aligned_cols=9 Identities=56% Similarity=1.091 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
+.||+||++
T Consensus 185 ~AHE~GH~l 193 (255)
T 1bkcA00 185 VAHELGHNL 193 (255)
T ss_pred hhhhhhhhc
No 32
>SUPFAM template d.92.1 Metalloproteases ("zincins"), catalytic domain (55486) SCOP seed sequence: d1rm8a_.
Probab=65.54 E-value=6.3 Score=31.13 Aligned_cols=9 Identities=44% Similarity=0.829 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
..||+||..
T Consensus 121 ~~HE~GH~L 129 (169)
T SUPFAM0043304 121 AAHELGHAL 129 (169)
T ss_pred hhhhhhhhh
No 33
>SUPFAM template d.92.1 Metalloproteases ("zincins"), catalytic domain (55486) SCOP seed sequence: d830ca_.
Probab=64.42 E-value=5.4 Score=31.45 Aligned_cols=9 Identities=44% Similarity=0.829 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
..||+||..
T Consensus 117 ~~HE~GH~L 125 (168)
T SUPFAM0045657 117 AAHELGHAL 125 (168)
T ss_pred eeehhhhhc
No 34
>SUPFAM template d.92.1 Metalloproteases ("zincins"), catalytic domain (55486) SCOP seed sequence: d1bqqm_.
Probab=64.18 E-value=6.9 Score=31.07 Aligned_cols=9 Identities=44% Similarity=0.829 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
..||+||..
T Consensus 124 ~~HElGH~L 132 (174)
T SUPFAM0035666 124 AAHELGHAL 132 (174)
T ss_pred hhhhhhhhh
No 35
>SUPFAM template d.92.1 Metalloproteases ("zincins"), catalytic domain (55486) SCOP seed sequence: d1jk3a_.
Probab=64.14 E-value=5.9 Score=30.64 Aligned_cols=9 Identities=44% Similarity=0.829 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
..|||||..
T Consensus 111 ~~HE~GH~L 119 (158)
T SUPFAM0039592 111 AAHELGHAL 119 (158)
T ss_pred eehhhhhhc
No 36
>3KEC_Entity_1
Probab=63.67 E-value=18 Score=31.44 Aligned_cols=90 Identities=14% Similarity=-0.151 Sum_probs=0.0
Q ss_pred CHHHHHHHHHHHHHHHHHHhCCCCCCccccccccccccccchhhceeeeeccccceecC-------Ccceeeeccccccc
Q Q5E705_VIBF1/1 141 DVLEMTKQFDLFTIGVNEFYGRDGVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHS-------GYPVMSTSFPRQKS 213 (302)
Q Consensus 141 d~~~l~~~~d~ii~~~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~-------g~~~~~~~~~~~~~ 213 (302)
+..+.-+...+.++...+.+++...............................+...+. +..+....+.....
T Consensus 27 ~~~~~~~~i~~Af~~W~~~~~~~f~~v~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~i~~~~~~~~~~ 106 (167)
T 3KEC_Entity_1 27 THSEVEKAFKKAFKVWSDVTPLNFTRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTS 106 (167)
T ss_pred CHHHHHHHHHHHHHHHHhhcCeeEEEecCCCCceEEEEeeccccccccccCcccccccccCCCCcccceEeccccccccc
Q ss_pred eeccCCCcchhHHhhhh
Q Q5E705_VIBF1/1 214 SLFKATDNWMLGHEIGH 230 (302)
Q Consensus 214 ~~~~~~~~WG~~HEiGH 230 (302)
.......-+-+.|||||
T Consensus 107 ~~~~~~~~~v~~HEiGH 123 (167)
T 3KEC_Entity_1 107 SSKGYNLFLVAAHEFGH 123 (167)
T ss_pred cCCCceeEEEeeeeccc
No 37
>d1hv5a_ d.92.1.11 (A:) Stromelysin-3 (MMP-11) {Mouse (Mus musculus) [TaxId: 10090]}
Probab=63.45 E-value=34 Score=29.96 Aligned_cols=88 Identities=13% Similarity=-0.053 Sum_probs=0.0
Q ss_pred CHHHHHHHHHHHHHHHHHHhCCCCCCccccccccccccccchhhceeeeeccccceecCCcceeeeccccccceeccCCC
Q Q5E705_VIBF1/1 141 DVLEMTKQFDLFTIGVNEFYGRDGVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHSGYPVMSTSFPRQKSSLFKATD 220 (302)
Q Consensus 141 d~~~l~~~~d~ii~~~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~g~~~~~~~~~~~~~~~~~~~~ 220 (302)
...+.-+...+.++...+.+++...............+..............++..+++ ..+..........+...
T Consensus 26 ~~~~~~~~i~~A~~~W~~v~~i~F~ev~~~~~di~i~~~~~~~~~~~~~~~~~~~~~~~----~~~~~~~~~~i~~~~~~ 101 (162)
T d1hv5a_ 26 VREQVRQTVAEALQVWSEVTPLTFTEVHEGRADIMIDFARYWHGDNLPFDGPGGILAHA----FFPKTHREGDVHFDYDE 101 (162)
T ss_dssp CHHHHHHHHHHHHHHHHTTSSCEEEECSSSBCSEEEEEECSCSSSSCCCCSSSSCCEEE----ECCTTSSSEEEEEETTS
T ss_pred CHHHHHHHHHHHHHHHhccCCceEEEeecCCCceEEEEeccccCCcccccCCCceeeee----ecCCCccccceeecchh
Q ss_pred cc------------hhHHhhhhhc
Q Q5E705_VIBF1/1 221 NW------------MLGHEIGHNQ 232 (302)
Q Consensus 221 ~W------------G~~HEiGH~~ 232 (302)
.| -+.|||||..
T Consensus 102 ~~~~~~~~g~~~~~v~~HEiGHaL 125 (162)
T d1hv5a_ 102 TWTIGDNQGTDLLQVAAHEFGHVL 125 (162)
T ss_dssp CEESSCSSSEEHHHHHHHHHHHHT
T ss_pred ccccccccCcchhhhhhhhhhhhc
No 38
>SUPFAM template d.92.1 Metalloproteases ("zincins"), catalytic domain (55486) SCOP seed sequence: d1kapp2.
Probab=63.10 E-value=5.6 Score=33.98 Aligned_cols=9 Identities=44% Similarity=0.977 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
+.|||||+.
T Consensus 174 ~~HE~GH~L 182 (246)
T SUPFAM0040001 174 IAHELGHAL 182 (246)
T ss_pred eeeehhhhh
No 39
>830c_A MMP-13, MMP-13; matrix metalloprotease; HET: RS1; 1.60A {Homo sapiens} SCOP: d.92.1.11 PDB: 456c _A*
1you _A* 1eub _A* 1xuc _A* 1xud _A* 1xur _A* 3elm _A* 3i7g _A* 3i7i _A* 2ow9 _A* 2ozr _A* 2d1n _A* 1fls _A* 1fm1 _A* 1ztq _A*
2e2d _A 2pjt _A* 1cxv _A*
Probab=62.92 E-value=20 Score=31.32 Aligned_cols=92 Identities=14% Similarity=-0.150 Sum_probs=0.0
Q ss_pred CHHHHHHHHHHHHHHHHHHhCCCCCCccccccccccccccchhhceeeeeccccceecC-------Ccceeeeccccccc
Q Q5E705_VIBF1/1 141 DVLEMTKQFDLFTIGVNEFYGRDGVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHS-------GYPVMSTSFPRQKS 213 (302)
Q Consensus 141 d~~~l~~~~d~ii~~~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~-------g~~~~~~~~~~~~~ 213 (302)
+..+.-+...+.++..++..++......................-........+...+. +..+....+.....
T Consensus 27 ~~~~~~~~i~~Af~~W~~~~~~~f~~v~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~i~~~~~~~~~~ 106 (168)
T 830c_A 27 THSEVEKAFKKAFKVWSDVTPLNFTRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTS 106 (168)
T ss_dssp CHHHHHHHHHHHHHHHHTTSSCEEEEESSSCCSEEEEEECSSCSSSCCCCSSSSCCEEECCSSSTTTTCEEEETTSCEES
T ss_pred CHHHHHHHHHHHHHHHHcccCceEEEeccCCCceEEEeeeccccccccccCcccceeeccCCCCcccceEeccccccccc
Q ss_pred eeccCCCcchhHHhhhhhc
Q Q5E705_VIBF1/1 214 SLFKATDNWMLGHEIGHNQ 232 (302)
Q Consensus 214 ~~~~~~~~WG~~HEiGH~~ 232 (302)
.......-.-+.|||||..
T Consensus 107 ~~~~~~~~~v~~HEiGHaL 125 (168)
T 830c_A 107 SSKGYNLFLVAAHEFGHSL 125 (168)
T ss_dssp SSSSEEHHHHHHHHHHHHT
T ss_pred cCCCceeEEEeeeeccccc
No 40
>SUPFAM template d.92.1 Metalloproteases ("zincins"), catalytic domain (55486) SCOP seed sequence: d1gkda_.
Probab=62.90 E-value=5.9 Score=30.72 Aligned_cols=8 Identities=50% Similarity=0.999 Sum_probs=0.0
Q ss_pred hHHhhhhh
Q Q5E705_VIBF1/1 224 LGHEIGHN 231 (302)
Q Consensus 224 ~~HEiGH~ 231 (302)
..|||||.
T Consensus 115 ~~HE~GH~ 122 (159)
T SUPFAM0038130 115 AAHELGHA 122 (159)
T ss_pred eeehhhhh
No 41
>d1hy7a_ d.92.1.11 (A:) Stromelysin-1 (MMP-3) {Human (Homo sapiens), fibroblast [TaxId: 9606]}
Probab=62.78 E-value=21 Score=31.09 Aligned_cols=90 Identities=9% Similarity=-0.210 Sum_probs=0.0
Q ss_pred CHHHHHHHHHHHHHHHHHHhCCCCCCccccccccccccccchhhceeeeeccccceecC-------Ccceeeeccccccc
Q Q5E705_VIBF1/1 141 DVLEMTKQFDLFTIGVNEFYGRDGVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHS-------GYPVMSTSFPRQKS 213 (302)
Q Consensus 141 d~~~l~~~~d~ii~~~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~-------g~~~~~~~~~~~~~ 213 (302)
...+.-+...+.++...+.+++...............................+...+. ...+..........
T Consensus 27 ~~~~~~~~i~~A~~~W~~~~~i~F~e~~~~~~d~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~ 106 (168)
T d1hy7a_ 27 PKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWTK 106 (168)
T ss_dssp CHHHHHHHHHHHHHHHHTTSSCEEEECSSSCCSEEEEEECSSCSSSCCCCSSSSCCEEECCSSSTTTTCEEEETTSCEES
T ss_pred CHHHHHHHHHHHHHHHHhhcCceeEeccCCcCceEEEeeccccccccccccccccccccccCCCCeeeeEeecccccccc
Q ss_pred eeccCCCcchhHHhhhh
Q Q5E705_VIBF1/1 214 SLFKATDNWMLGHEIGH 230 (302)
Q Consensus 214 ~~~~~~~~WG~~HEiGH 230 (302)
.......-+-+.|||||
T Consensus 107 ~~~~~~~~~v~~HEiGH 123 (168)
T d1hy7a_ 107 DTTGTNLFLVAAHEIGH 123 (168)
T ss_dssp SSSSEEHHHHHHHHHHH
T ss_pred ccccccceeeeHhhhcc
No 42
>SUPFAM template d.92.1 Metalloproteases ("zincins"), catalytic domain (55486) SCOP seed sequence: d1bkca_.
Probab=62.53 E-value=8.6 Score=33.13 Aligned_cols=9 Identities=56% Similarity=0.981 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
+.||+||+.
T Consensus 185 ~aHE~GH~l 193 (255)
T SUPFAM0035598 185 AAHELGHNL 193 (255)
T ss_pred HhhhhHHHh
No 43
>SUPFAM template d.92.1 Metalloproteases ("zincins"), catalytic domain (55486) SCOP seed sequence: d1hv5a_.
Probab=62.17 E-value=6.4 Score=30.78 Aligned_cols=9 Identities=44% Similarity=0.829 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
..||+||..
T Consensus 117 ~~HE~GH~L 125 (162)
T SUPFAM0038739 117 AAHELGHAL 125 (162)
T ss_pred eeehhhhhh
No 44
>SUPFAM template d.92.1 Metalloproteases ("zincins"), catalytic domain (55486) SCOP seed sequence: d1kuh__.
Probab=61.82 E-value=4.9 Score=30.02 Aligned_cols=9 Identities=44% Similarity=0.829 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
..||+||..
T Consensus 81 ~~HE~GH~L 89 (132)
T SUPFAM0040268 81 AAHELGHAL 89 (132)
T ss_pred eeeeccccc
No 45
>pfam12388 Peptidase_M57 Dual-action HEIGH metallo-peptidase. The catalytic triad for this family of proteases is
HE-H-H, which in many members is in the sequence motif HEIGH.
Probab=61.74 E-value=28 Score=31.97 Aligned_cols=102 Identities=15% Similarity=0.133 Sum_probs=0.0
Q ss_pred HHHHHHHHHHHHHHHHhCCCCCCccc--cccccccccccchhhceeeeecccccee-cCCcceeeeccccccceeccCCC
Q Q5E705_VIBF1/1 144 EMTKQFDLFTIGVNEFYGRDGVSGAH--KMFTDSAPELEYQNMRLVDDIQISIGSA-HSGYPVMSTSFPRQKSSLFKATD 220 (302)
Q Consensus 144 ~l~~~~d~ii~~~~~l~Gl~~~~~~~--~~~~~~~~~~~~~~~~~~~~~~~~~~~~-~~g~~~~~~~~~~~~~~~~~~~~ 220 (302)
.+....++.|..||.| |+....... .+...-..........--...-+.+|+. ..|.|-....-.....+......
T Consensus 56 ~~~~al~~AI~~yN~l-~l~l~F~~t~gtn~~~~di~v~~~~~~~~~g~ggsAGFP~s~G~P~~~V~i~~~~~~~~~~~~ 134 (211)
T pfam12388 56 KGQTALDDAVNNYNNL-GLDISFRLTFGTNYQNADMVVYDNSVNNPSGSGGSAGFPDSNGDPAKFVQIYDLENGSTNVNE 134 (211)
T ss_pred HHHHHHHHHHHHHhhc-CceEEEEEEeccCCCCCcEEEEeccccCCCCceeeccCCCCCCCCCceEEEeccCCCCcchhh
Q ss_pred cchhHHhhhhhcccccccc---CCCccchh
Q Q5E705_VIBF1/1 221 NWMLGHEIGHNQAANWLNV---VGAGETAN 247 (302)
Q Consensus 221 ~WG~~HEiGH~~Q~~~~~~---~g~~Evtn 247 (302)
. -+.|||||..=.+.-.| .++|...|
T Consensus 135 ~-vi~HEiGHciGfRHTD~fnRsSCG~~~n 163 (211)
T pfam12388 135 H-VITHEIGHSIGFRHTDYFDRSSCGQGGN 163 (211)
T ss_pred h-hhhhhhhceeccccccccCccccccCCC
No 46
>PF04228 Zn_peptidase: Putative neutral zinc metallopeptidase; InterPro: Members of this family of
bacterial proteins are described as hypothetical proteins or zinc metallopeptidases. The majority have a HExxH
zinc-binding motif characteristic of neutral zinc metallopeptidases, however there is no evidence to support
their function as metallopeptidases.
Probab=61.50 E-value=8.6 Score=37.28 Aligned_cols=10 Identities=50% Similarity=0.850 Sum_probs=0.0
Q ss_pred hHHhhhhhcc
Q Q5E705_VIBF1/1 224 LGHEIGHNQA 233 (302)
Q Consensus 224 ~~HEiGH~~Q 233 (302)
+.||+||+-|
T Consensus 174 lAHEyGHHVQ 183 (292)
T PF04228_consen 174 LAHEYGHHVQ 183 (292)
T ss_pred HHHHHHHHHH
No 47
>2ovx_A Matrix metalloproteinase-9 (EC 3.4.24.35) (MMP- 9) (92 kDa type IV collagenase) (92...; hydrolase,
S1-prime pocket; HET: 4MR; 2.00A {Homo sapiens} SCOP: d.92.1.11 PDB: 2ovz _A* 2ow0 _A* 2ow1 _A* 2ow2 _A* 1gkd _A* 1gkc _A*
Probab=61.17 E-value=17 Score=31.24 Aligned_cols=90 Identities=8% Similarity=-0.285 Sum_probs=0.0
Q ss_pred CHHHHHHHHHHHHHHHHHHhCCCCCCccccccccccccccchhhceeeeeccccceecCCcceeeeccccccceeccCCC
Q Q5E705_VIBF1/1 141 DVLEMTKQFDLFTIGVNEFYGRDGVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHSGYPVMSTSFPRQKSSLFKATD 220 (302)
Q Consensus 141 d~~~l~~~~d~ii~~~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~g~~~~~~~~~~~~~~~~~~~~ 220 (302)
...+.-+...+.++...+..++..........................................................
T Consensus 24 ~~~~~~~~i~~A~~~W~~~~~i~F~~v~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~ 103 (159)
T 2ovx_A 24 PRAVIDDAFARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELWSL 103 (159)
T ss_dssp CHHHHHHHHHHHHHHHHTSSSCEEEECSSTTSSEEEEEECSSCSSSCCCCSSSSCCEEECCSSSTTTTCEEEETTSCEEC
T ss_pred CHHHHHHHHHHHHHHHHhhcCceEEEeccCCCCEEEEeeeeccCCCccccccccccccccccccccccceeeccchhccc
Q ss_pred cc--------hhHHhhhh
Q Q5E705_VIBF1/1 221 NW--------MLGHEIGH 230 (302)
Q Consensus 221 ~W--------G~~HEiGH 230 (302)
.+ .+.|||||
T Consensus 104 ~~~~~~~~~~v~~HEiGH 121 (159)
T 2ovx_A 104 GKGQGYSLFLVAAHQFGH 121 (159)
T ss_dssp SSSSSEEHHHHHHHHHHH
T ss_pred CCccccceeEEeeeeccc
No 48
>2jsd_A Matrix metalloproteinase-20; MMP-NNGH, structural genomics, structural proteomics in europe, spine,
spine-2, spine2-complexes, hydrolase; HET: NGH; NMR {Homo sapiens}
Probab=59.46 E-value=59 Score=28.21 Aligned_cols=90 Identities=11% Similarity=0.048 Sum_probs=0.0
Q ss_pred CHHHHHHHHHHHHHHHHHHhCCC--CCCccccccccccccccchhhceeeeeccccceecCCcceeeeccccccceeccC
Q Q5E705_VIBF1/1 141 DVLEMTKQFDLFTIGVNEFYGRD--GVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHSGYPVMSTSFPRQKSSLFKA 218 (302)
Q Consensus 141 d~~~l~~~~d~ii~~~~~l~Gl~--~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~g~~~~~~~~~~~~~~~~~~ 218 (302)
+..+.-+...+.++..++..++. +..............................+..+....................
T Consensus 22 ~~~~~~~~i~~A~~~W~~~~~i~F~ev~~~~~~i~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~ 101 (160)
T 2jsd_A 22 SSVEVDKAVEMALQAWSSAVPLSFVRINSGEADIMISFENGDHGDSYPFDGPRGTLAHAFAPGEGLGGDTHFDNAEKWTM 101 (160)
T ss_dssp CHHHHHHHHHHHHHHHHHHSSCEEEECSSSCCSEEEEEECSCSSSSSCCCSSSSCSEEECCSSSSSTTCEEEETTSCEES
T ss_pred CHHHHHHHHHHHHHHHhcCCCceEEEEcCCCCCeEEEeeeccCCCcccccccccceeccccCCCcccceeeecccccccc
Q ss_pred CCcc-----hhHHhhhh
Q Q5E705_VIBF1/1 219 TDNW-----MLGHEIGH 230 (302)
Q Consensus 219 ~~~W-----G~~HEiGH 230 (302)
...+ -+.|||||
T Consensus 102 ~~~~~~~~~v~~HEiGH 118 (160)
T 2jsd_A 102 GTNGFNLFTVAAHEFGH 118 (160)
T ss_dssp SSSSEEHHHHHHHHHHH
T ss_pred ccCCceeEEEeeeeccc
No 49
>SUPFAM template d.92.1 Metalloproteases ("zincins"), catalytic domain (55486) SCOP seed sequence: d1kufa_.
Probab=59.27 E-value=11 Score=31.06 Aligned_cols=9 Identities=56% Similarity=0.981 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
..|||||+.
T Consensus 140 ~~HE~GH~L 148 (201)
T SUPFAM0040267 140 AAHELGHNL 148 (201)
T ss_pred HHHHhHHHh
No 50
>d1rm8a_ d.92.1.11 (A:) Matrix metalloproteinase-16 (MMP-16) {Human (Homo sapiens) [TaxId: 9606]}
Probab=58.93 E-value=11 Score=32.60 Aligned_cols=9 Identities=44% Similarity=0.793 Sum_probs=0.0
Q ss_pred chhHHhhhh
Q Q5E705_VIBF1/1 222 WMLGHEIGH 230 (302)
Q Consensus 222 WG~~HEiGH 230 (302)
+.++|||||
T Consensus 119 ~v~~HEiGH 127 (169)
T d1rm8a_ 119 LVAVHELGH 127 (169)
T ss_dssp HHHHHHHHH
T ss_pred hhhhhhhhh
No 51
>SUPFAM template d.92.1 Metalloproteases ("zincins"), catalytic domain (55486) SCOP seed sequence: d1wnia_.
Probab=57.23 E-value=13 Score=30.55 Aligned_cols=9 Identities=67% Similarity=1.173 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
..|||||+.
T Consensus 138 ~~HelGH~l 146 (198)
T SUPFAM0044993 138 LAHELGHNL 146 (198)
T ss_pred HHHHHHHHc
No 52
>cd04271 ZnMc_ADAM_fungal Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A
Disintegrin And Metalloprotease) family of metalloproteases are integral membrane proteases acting on a variety
of extracellular targets. They are involved in shedding soluble peptides or proteins from the cell surface. This
subfamily contains fungal ADAMs, whose precise function has yet to be determined.
Probab=56.95 E-value=8.1 Score=35.94 Aligned_cols=9 Identities=56% Similarity=0.984 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
++||+||++
T Consensus 149 ~AHEiGHnf 157 (228)
T cd04271 149 FAHEIGHTF 157 (228)
T ss_pred eeehhhccc
No 53
>cd04279 ZnMc_MMP_like_1 Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal,
and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.
Probab=56.81 E-value=43 Score=29.48 Aligned_cols=89 Identities=6% Similarity=-0.163 Sum_probs=0.0
Q ss_pred HHHHHHHHHHHHHHHHHHhCCCCCCccccccccccccccchhhceeeeeccccceecCCcceeeeccccccceeccCCCc
Q Q5E705_VIBF1/1 142 VLEMTKQFDLFTIGVNEFYGRDGVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHSGYPVMSTSFPRQKSSLFKATDN 221 (302)
Q Consensus 142 ~~~l~~~~d~ii~~~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~g~~~~~~~~~~~~~~~~~~~~~ 221 (302)
.....+...+.+..-.+...|.......................+...-...+...+.......................
T Consensus 19 ~~~~~~Ai~~Af~~Ws~v~~l~fve~~~~~~~adI~I~f~~~~~~dg~gg~lA~a~~p~~~~~~~~~~~~~~~~~~~~~~ 98 (156)
T cd04279 19 AQSWLQAVKQAAAEWENVGPLKFVYNPEEDNDADIVIFFDRPPPVGGAGGGLARAGFPLISDGNRKLFNRTDINLGPGQP 98 (156)
T ss_pred HHHHHHHHHHHHHHHhccCCceEEEecCCCCCCCEEEEecCCCCCCCCCCcceEecCCCCCCCCccccceeeeeecccCC
Q ss_pred -------chhHHhhhh
Q Q5E705_VIBF1/1 222 -------WMLGHEIGH 230 (302)
Q Consensus 222 -------WG~~HEiGH 230 (302)
+...|||||
T Consensus 99 ~~~~~l~~vA~HEiGH 114 (156)
T cd04279 99 RGAENLQAIALHELGH 114 (156)
T ss_pred ccchhHHHHHHHHhcc
No 54
>SUPFAM template d.92.1 Metalloproteases ("zincins"), catalytic domain (55486) SCOP seed sequence: d1g9ka2.
Probab=56.55 E-value=8.4 Score=32.78 Aligned_cols=9 Identities=44% Similarity=0.829 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
+.|||||..
T Consensus 165 ~~HE~GH~L 173 (242)
T SUPFAM0038010 165 AAHELGHAL 173 (242)
T ss_pred eeeehhhhh
No 55
>PIRSF020485 PA-IL
Probab=56.50 E-value=24 Score=29.71 Aligned_cols=15 Identities=13% Similarity=0.209 Sum_probs=0.0
Q ss_pred ccceEEECCCCEEEE
Q Q5E705_VIBF1/1 4 QSAGVWIPAREVAYV 18 (302)
Q Consensus 4 ~~TG~y~~~Ge~i~V 18 (302)
|+|||.+.+|++|+|
T Consensus 16 ~~T~lI~~~GD~I~~ 30 (123)
T PIRSF020485 16 KVTSLILKQGDVISV 30 (123)
T ss_pred ceeEEEEcCCCEEEE
No 56
>1bud_A Protein (acutolysin A); metalloproteinase, snake venom, MMP, toxin; 1.90A {Deinagkistrodon acutus} SCOP:
d.92.1.9 PDB: 1bsw _A
Probab=55.73 E-value=14 Score=33.28 Aligned_cols=9 Identities=56% Similarity=0.936 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
+.|||||++
T Consensus 137 iAHElGH~l 145 (197)
T 1bud_A 137 LAHEMAHNL 145 (197)
T ss_dssp HHHHHHHHT
T ss_pred hHHHhhcee
No 57
>SUPFAM template d.92.1 Metalloproteases ("zincins"), catalytic domain (55486) SCOP seed sequence: d1atla_.
Probab=55.49 E-value=15 Score=30.34 Aligned_cols=9 Identities=67% Similarity=1.173 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
..|||||+.
T Consensus 138 ~~HelGH~L 146 (200)
T SUPFAM0035195 138 LAHELGHNL 146 (200)
T ss_pred HHHHHHHHc
No 58
>d1xuca1 d.92.1.11 (A:104-272) Collagenase-3 (MMP-13) {Human (Homo sapiens) [TaxId: 9606]}
Probab=55.31 E-value=14 Score=32.27 Aligned_cols=9 Identities=44% Similarity=0.866 Sum_probs=0.0
Q ss_pred chhHHhhhh
Q Q5E705_VIBF1/1 222 WMLGHEIGH 230 (302)
Q Consensus 222 WG~~HEiGH 230 (302)
+-+.|||||
T Consensus 115 ~v~~HEiGH 123 (169)
T d1xuca1 115 LVAAHEFGH 123 (169)
T ss_dssp HHHHHHHHH
T ss_pred eehhhhhcc
No 59
>d1bswa_ d.92.1.9 (A:) Snake venom metalloprotease {Five-pace snake (Agkistrodon acutus), acutolysin A [TaxId:
36307]}
Probab=55.26 E-value=15 Score=33.17 Aligned_cols=9 Identities=56% Similarity=0.936 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
+.||+||++
T Consensus 137 ~AHElGH~l 145 (197)
T d1bswa_ 137 LAHEMAHNL 145 (197)
T ss_dssp HHHHHHHHT
T ss_pred HHHHHHhhc
No 60
>SUPFAM template d.92.1 Metalloproteases ("zincins"), catalytic domain (55486) SCOP seed sequence: d1quaa_.
Probab=55.24 E-value=15 Score=30.14 Aligned_cols=9 Identities=56% Similarity=0.981 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
..||+||+.
T Consensus 139 ~~He~GH~L 147 (197)
T SUPFAM0042988 139 AAHELGHNL 147 (197)
T ss_pred HHHHHHHHh
No 61
>1slm_A Stromelysin-1; hydrolase, metalloprotease, fibroblast, collagen degradation; 1.90A {Homo sapiens} SCOP:
a.20.1.2 d.92.1.11
Probab=55.08 E-value=33 Score=32.88 Aligned_cols=90 Identities=10% Similarity=-0.189 Sum_probs=0.0
Q ss_pred CHHHHHHHHHHHHHHHHHHhCCCCCCccccccccccccccchhhceeeeeccccceecCCcc-------eeeeccccccc
Q Q5E705_VIBF1/1 141 DVLEMTKQFDLFTIGVNEFYGRDGVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHSGYP-------VMSTSFPRQKS 213 (302)
Q Consensus 141 d~~~l~~~~d~ii~~~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~g~~-------~~~~~~~~~~~ 213 (302)
...++-+...+.++...+++.+...........+...+..........-...++..+|+.++ +-+-.+..+..
T Consensus 109 ~~~~vr~~i~~Af~~Ws~v~~l~F~Ev~~~~aDI~I~f~~~~h~~~~~fdg~~g~la~a~~p~~~~~g~i~fd~~e~w~~ 188 (255)
T 1slm_A 109 PKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWTK 188 (255)
T ss_dssp CHHHHHHHHHHHHHHHHTTSSCEEEECSSSCCSEEEEEECSCCSSSCCCCSSSSBCEEECCSSSTTTTCEEEETTSCEES
T ss_pred CHHHHHHHHHHHhhhhhcccceEEEEecCCCCCEEEEEeccCCCccccccCCCCcceeeecccCCccceEEecccccccc
Q ss_pred eeccCCCcchhHHhhhh
Q Q5E705_VIBF1/1 214 SLFKATDNWMLGHEIGH 230 (302)
Q Consensus 214 ~~~~~~~~WG~~HEiGH 230 (302)
.....+--+-..|||||
T Consensus 189 ~~~~~~l~~va~HEIGH 205 (255)
T 1slm_A 189 DTTGTNLFLVAAHEIGH 205 (255)
T ss_dssp SSSSEEHHHHHHHHHHH
T ss_pred cccccchhhhhhhhhcc
No 62
>d1y93a1 d.92.1.11 (A:106-263) Macrophage elastase (MMP-12) {Human (Homo sapiens) [TaxId: 9606]}
Probab=54.79 E-value=15 Score=31.52 Aligned_cols=9 Identities=56% Similarity=0.778 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
++|||||..
T Consensus 111 ~~HEiGHaL 119 (158)
T d1y93a1 111 AVHEIGHSL 119 (158)
T ss_dssp HHHHHHHHT
T ss_pred hhhhhhhhc
No 63
>2w15_A Zinc metalloproteinase BAP1; hydrolase inhibitor complex, metal-binding, zinc-depending, metalloprotease,
metalloproteinase/inhibitor complex; HET: WR2; 1.05A {Bothrops asper} PDB: 2w12 _A* 2w13 _A* 2w14 _A* 1nd1 _A
3gbo _A
Probab=54.65 E-value=15 Score=33.32 Aligned_cols=9 Identities=56% Similarity=1.128 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
++|||||++
T Consensus 140 ~AHElGH~l 148 (202)
T 2w15_A 140 MAHELGHNL 148 (202)
T ss_dssp HHHHHHHHT
T ss_pred HHHHHHHhc
No 64
>d1bqqm_ d.92.1.11 (M:) Membrane-type matrix metalloproteinase (CDMT1-MMP) {Human (Homo sapiens) [TaxId: 9606]}
Probab=54.33 E-value=1.6e+02 Score=25.60 Aligned_cols=92 Identities=4% Similarity=-0.087 Sum_probs=0.0
Q ss_pred CHHHHHHHHHHHHHHHHHHhCCCCCCccccccccccccccchhhceeeeeccccceecCCcceeeecccc----------
Q Q5E705_VIBF1/1 141 DVLEMTKQFDLFTIGVNEFYGRDGVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHSGYPVMSTSFPR---------- 210 (302)
Q Consensus 141 d~~~l~~~~d~ii~~~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~g~~~~~~~~~~---------- 210 (302)
...+.-+...+.+....+..++.......................................+........
T Consensus 23 ~~~~~~~~i~~A~~~W~~~~~i~f~~~~~~~~~~~~~~~~~i~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~ 102 (174)
T d1bqqm_ 23 GEYATYEAIRKAFRVWESATPLRFREVPYAYIREGHEKQADIMIFFAEGFHGDSTPFDGEGGFLAHAYFPGPNIGGDTHF 102 (174)
T ss_dssp CHHHHHHHHHHHHHHHHHHSSCEEECCSCCSSCTTSSSCCSSEEEEECSCSSSSCCCCSSSSEEEEECCSCSTTTTCEEE
T ss_pred CHHHHHHHHHHHHHHHHHhcCcceeeecccccccccccccceEEEeccccCCCcccccCCCcceeeeccCCCCccceeee
Q ss_pred -ccceeccCCCc-------chhHHhhhhhc
Q Q5E705_VIBF1/1 211 -QKSSLFKATDN-------WMLGHEIGHNQ 232 (302)
Q Consensus 211 -~~~~~~~~~~~-------WG~~HEiGH~~ 232 (302)
........... +-+.|||||..
T Consensus 103 ~~~~~~~~~~~~~~~~~~~~v~~HEiGHaL 132 (174)
T d1bqqm_ 103 DSAEPWTVRNEDLNGNDIFLVAVHELGHAL 132 (174)
T ss_dssp ETTSCCBSTTSCCSSCBHHHHHHHHHHHTT
T ss_pred cccccccccccCCcchhhhhhhhccccccc
No 65
>SUPFAM template d.92.1 Metalloproteases ("zincins"), catalytic domain (55486) SCOP seed sequence: d4aig__.
Probab=54.26 E-value=16 Score=30.23 Aligned_cols=9 Identities=67% Similarity=1.173 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
..|||||+.
T Consensus 139 ~~HelGH~L 147 (201)
T SUPFAM0045583 139 LAHELGHNL 147 (201)
T ss_pred HHHHHHHHh
No 66
>pfam06262 DUF1025 Domain of unknown function (DUF1025). Family of bacterial protein with undetermined function.
Probab=54.20 E-value=16 Score=29.23 Aligned_cols=9 Identities=56% Similarity=0.818 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
..|||||++
T Consensus 76 viHEiaHhf 84 (96)
T pfam06262 76 VIHEIGHHF 84 (96)
T ss_pred HHHHHHHHc
No 67 
>COG3824 Predicted Zn-dependent protease [General function prediction only]
Probab=53.89 E-value=14 Score=30.72 Aligned_cols=9 Identities=67% Similarity=0.900 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
..|||||++
T Consensus 113 liHEIgHhF 121 (136)
T COG3824 113 LIHEIGHHF 121 (136)
T ss_pred hhhhhhhhc
No 68
>1c7k_A NCNP, zinc endoprotease; alpha and beta protein, metalloproteinase, hydrolase; 1.00A {Streptomyces
caespitosus} SCOP: d.92.1.1 PDB: 1kuh _A
Probab=53.52 E-value=16 Score=30.95 Aligned_cols=7 Identities=57% Similarity=0.990 Sum_probs=0.0
Q ss_pred hHHhhhh
Q Q5E705_VIBF1/1 224 LGHEIGH 230 (302)
Q Consensus 224 ~~HEiGH 230 (302)
..|||||
T Consensus 81 a~HEiGH 87 (132)
T 1c7k_A 81 TAHETGH 87 (132)
T ss_dssp HHHHHHH
T ss_pred HHHHHhh
No 69
>d2ejqa1 d.92.1.17 (A:2-108) Uncharacterized protein TTHA0227 {Thermus thermophilus [TaxId: 274]}
Probab=52.75 E-value=17 Score=29.87 Aligned_cols=9 Identities=33% Similarity=0.571 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
++|||||++
T Consensus 92 vvHEigHhf 100 (107)
T d2ejqa1 92 MLHELRHHL 100 (107)
T ss_dssp HHHHHHHHH
T ss_pred HHHHHHHHH
No 70
>d2ovxa1 d.92.1.11 (A:110-443) Gelatinase B (MMP-9) {Human (Homo sapiens) [TaxId: 9606]}
Probab=52.17 E-value=18 Score=31.23 Aligned_cols=9 Identities=33% Similarity=0.693 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
+.|||||..
T Consensus 115 ~~HElGHaL 123 (159)
T d2ovxa1 115 AAHQFGHAL 123 (159)
T ss_dssp HHHHHHHHT
T ss_pred ehhhhcccc
No 71
>1qua_A Acutolysin-C, hemorrhagin III; metalloprotease, hemorrhagic toxin, snake venom proteinase; 2.20A
{Deinagkistrodon acutus} SCOP: d.92.1.9
Probab=52.07 E-value=18 Score=32.70 Aligned_cols=9 Identities=56% Similarity=1.128 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
+.||+||++
T Consensus 139 iAHElGH~l 147 (197)
T 1qua_A 139 MAHELGHNL 147 (197)
T ss_dssp HHHHHHHHT
T ss_pred HHHHHHhhc
No 72
>cd04267 ZnMc_ADAM_like Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The
adamalysin_like or ADAM family of metalloproteases contains proteolytic domains from snake venoms, proteases from the
mammalian reproductive tract, and the tumor necrosis factor alpha convertase, TACE. ADAMs (A Disintegrin And
Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.
Probab=51.87 E-value=16 Score=33.08 Aligned_cols=9 Identities=56% Similarity=1.128 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
+.|||||+.
T Consensus 137 ~AHElGH~l 145 (192)
T cd04267 137 MAHELGHNL 145 (192)
T ss_pred hhhhhhhhc
No 73
>3b8z_A Protein adamts-5; alpha/beta, hydrolase; HET: 294; 1.40A {Homo sapiens} PDB: 3hyg _A* 3hy9 _A* 3hy7 _A*
3ljt _A*
Probab=51.66 E-value=18 Score=33.14 Aligned_cols=9 Identities=56% Similarity=0.885 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
+.||+||++
T Consensus 145 ~AHElGH~l 153 (217)
T 3b8z_A 145 VAHEIGHLL 153 (217)
T ss_dssp HHHHHHHHT
T ss_pred HHHHHhhcc
No 74
>d1r55a_ d.92.1.9 (A:) ADAM33 {Human (Homo sapiens) [TaxId: 9606]}
Probab=51.63 E-value=18 Score=32.84 Aligned_cols=9 Identities=56% Similarity=1.066 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
+.|||||++
T Consensus 136 ~AHElGH~l 144 (203)
T d1r55a_ 136 MAHEIGHSL 144 (203)
T ss_dssp HHHHHHHHT
T ss_pred HHHHHHHhc
No 75
>3ma2_D Matrix metalloproteinase-14; protein - protein complex, cleavage on PAIR of basic residue disulfide bond,
membrane, metal-binding; 2.05A {Homo sapiens} PDB: 1bqq _M 1buv _M
Probab=51.56 E-value=19 Score=31.59 Aligned_cols=9 Identities=44% Similarity=0.689 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
+.|||||..
T Consensus 126 ~~HEiGHaL 134 (181)
T 3ma2_D 126 AVHELGHAL 134 (181)
T ss_dssp HHHHHHHHT
T ss_pred HHhhhcccc
No 76
>d1qiba_ d.92.1.11 (A:) Gelatinase A {Human (Homo sapiens) [TaxId: 9606]}
Probab=51.41 E-value=18 Score=31.21 Aligned_cols=7 Identities=57% Similarity=1.070 Sum_probs=0.0
Q ss_pred hHHhhhh
Q Q5E705_VIBF1/1 224 LGHEIGH 230 (302)
Q Consensus 224 ~~HEiGH 230 (302)
+.|||||
T Consensus 113 ~~HEiGH 119 (161)
T d1qiba_ 113 AAHEFGH 119 (161)
T ss_dssp HHHHHHH
T ss_pred eeecccc
No 77
>SUPFAM template d.92.1 Metalloproteases ("zincins"), catalytic domain (55486) SCOP seed sequence: d1sat_2.
Probab=50.55 E-value=9.9 Score=32.24 Aligned_cols=7 Identities=57% Similarity=0.918 Sum_probs=0.0
Q ss_pred hHHhhhh
Q Q5E705_VIBF1/1 224 LGHEIGH 230 (302)
Q Consensus 224 ~~HEiGH 230 (302)
+.|||||
T Consensus 171 ~~HE~GH 177 (243)
T SUPFAM0043540 171 AIHELGH 177 (243)
T ss_pred eeeecch
No 78
>PF07828 PA-IL: PA-IL-like protein; InterPro: The members of this family are similar to the
galactophilic lectin-1 expressed by P. aeruginosa ((PA-IL, Q05097 from SWISSPROT). Lectins recognising specific
carbohydrates found on the surface of host cells are known to be involved in the initiation of infections by this
organism. The protein is thought to be organised into an extensive network of beta-sheets, as is the case with
many other lectins . ; PDB: 1uoj _D 2vxj _P 1oko _C 1l7l _A.
Probab=50.53 E-value=12 Score=29.96 Aligned_cols=15 Identities=20% Similarity=0.346 Sum_probs=0.0
Q ss_pred ccceEEECCCCEEEE
Q Q5E705_VIBF1/1 4 QSAGVWIPAREVAYV 18 (302)
Q Consensus 4 ~~TG~y~~~Ge~i~V 18 (302)
|+|||.+.+|+.|+|
T Consensus 14 k~T~lI~~~GD~Isv 28 (121)
T PF07828_consen 14 KVTGLILKQGDVISV 28 (121)
T ss_dssp -B-S-------BB--
T ss_pred ceeEEEecCCCEEEE
No 79
>SUPFAM template d.92.1 Metalloproteases ("zincins"), catalytic domain (55486) SCOP seed sequence: d1nd1a_.
Probab=50.49 E-value=19 Score=29.65 Aligned_cols=9 Identities=56% Similarity=0.981 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
..||+||+.
T Consensus 140 ~aHelGH~L 148 (202)
T SUPFAM0041314 140 AAHELGHNL 148 (202)
T ss_pred HHHHHHHHc
No 80
>2ejq_A Hypothetical protein TTHA0227; NPPSFA, national project on protein structural and functional analyses;
2.08A {Thermus thermophilus} SCOP: d.92.1.17
Probab=50.45 E-value=19 Score=30.68 Aligned_cols=9 Identities=33% Similarity=0.571 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
++|||||++
T Consensus 93 lvHEigHHf 101 (130)
T 2ejq_A 93 MLHELRHHL 101 (130)
T ss_dssp HHHHHHHHH
T ss_pred HHHHHHHHH
No 81
>1yp1_A FII; FII hydrolase; 1.90A {Deinagkistrodon acutus}
Probab=50.10 E-value=20 Score=32.68 Aligned_cols=9 Identities=56% Similarity=1.128 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
+.||+||++
T Consensus 139 iAHElGH~l 147 (202)
T 1yp1_A 139 MAHELGHNL 147 (202)
T ss_dssp HHHHHHHHT
T ss_pred HHHHHHhhc
No 82
>d1kufa_ d.92.1.9 (A:) Snake venom metalloprotease {Taiwan habu (Trimeresurus mucrosquamatus), atrolysin E
[TaxId: 103944]}
Probab=50.06 E-value=20 Score=32.56 Aligned_cols=9 Identities=56% Similarity=1.069 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
+.||+||++
T Consensus 140 ~AHElGH~l 148 (201)
T d1kufa_ 140 MTHELGHNL 148 (201)
T ss_dssp HHHHHHHHT
T ss_pred HHHHHHHhc
No 83
>d1quaa_ d.92.1.9 (A:) Snake venom metalloprotease {Chinese five-pace snake (Agkistrodon acutus), acutolysin C
[TaxId: 36307]}
Probab=50.06 E-value=20 Score=32.41 Aligned_cols=9 Identities=56% Similarity=1.128 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
+.||+||++
T Consensus 139 ~AHElGH~l 147 (197)
T d1quaa_ 139 MAHELGHNL 147 (197)
T ss_dssp HHHHHHHHT
T ss_pred HHHHHHhhc
No 84
>PF00413 Peptidase_M10: Matrixin This Prosite motif covers only the active site.; InterPro:
Metalloproteases are the most diverse of the four main types of protease, with more than 50 families identified to
date. In these enzymes, a divalent cation, usually zinc, activates the water molecule. The metal ion is held in
place by amino acid ligands, usually three in number. The known metal ligands are His, Glu, Asp or Lys and at
least one other residue is required for catalysis, which may play an electrophillic role. Of the known
metalloproteases, around half contain an HEXXH motif, which has been shown in crystallographic studies to form part of the
metal-binding site . The HEXXH motif is relatively common, but can be more stringently defined for
metalloproteases as 'abXHEbbHbc', where 'a' is most often valine or threonine and forms part of the S1' subsite in
thermolysin and neprilysin, 'b' is an uncharged residue, and 'c' a hydrophobic residue. Proline is never found in this
site, possibly because it would break the helical structure adopted by this motif in metalloproteases .
Peptidases are grouped into clans and families. Clans are groups of families for which there is evidence of common
ancestry. Each clan is identified with two letters, the first representing the catalytic type of the families
included in the clan (with the letter 'P' being used for a clan containing families of more than one of the
catalytic types serine, threonine and cysteine). Some families cannot yet be assigned to clans, and when a formal
assignment is required, such a family is described as belonging to clan A-, C-, M-, S-, T- or U-, according to
the catalytic type. Some clans are divided into subclans because there is evidence of a very ancient divergence
within the clan, for example MA(E), the gluzincins, and MA(M), the metzincins. Families are grouped by their
catalytic type, the first character representing the catalytic type: A, aspartic; C, cysteine; G, glutamic
acid; M, metallo; S, serine; T, threonine; and U, unknown. The serine, threonine and cysteine peptidases utilise
the amino acid as a nucleophile and form an acyl intermediate - these peptidases can also readily act as
transferases. In the case of aspartic, glutamic and metallopeptidases, the nucleophile is an activated water molecule.
This group of metallopeptidases belong to the MEROPS peptidase families: Family M10 (clan MA(M)),
subfamily M10A - matrixin Family M12 (clan MA(M)), subfamily M12B - adamalysin The protein fold of the peptidase
domain for members of this family resembles that of thermolysin, the type example for clan MA. Sequences having
this domain are extracellular metalloproteases, such as collagenase and stromelysin, which degrade the
extracellular matrix, are known as matrixins. They are zinc-dependent, calcium-activated proteases synthesised as
inactive precursors (zymogens), which are proteolytically cleaved to yield the active enzyme , . All matrixins and
related proteins possess 2 domains: an N-terminal domain, and a zinc-binding active site domain. The N-terminal
domain peptide, cleaved during the activation step, includes a conserved PRCGVPDV octapeptide, known as the
cysteine switch, whose Cys residue chelates the active site zinc atom, rendering the enzyme inactive. The active
enzyme degrades components of the extracellular matrix, playing a role in the initial steps of tissue
remodelling during morphogenesis, wound healing, angiogenesis and tumour invasion , . ; GO: 0004222 metalloendopeptidase
activity, 0006508 proteolysis, 0005578 proteinaceous extracellular matrix; PDB: 1hv5 _B 1rm8 _A 1bqq _M 1buv _M
1go7 _P 1go8 _P 1k7i _A 3hda _P 1k7q _A 3hbv _P ....
Probab=50.05 E-value=17 Score=31.29 Aligned_cols=9 Identities=56% Similarity=0.689 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
+.|||||..
T Consensus 106 ~~HEiGHaL 114 (152)
T PF00413_consen 106 AIHEIGHAL 114 (152)
T ss_dssp HHHH-----
T ss_pred chhhhcccc
No 85
>1kuf_A Atrolysin E, metalloproteinase; alpha/beta protein, hydrolase; 1.35A {Protobothrops mucrosquamatus} SCOP:
d.92.1.9 PDB: 1kui _A 1kuk _A 1kug _A 1wni _A
Probab=49.83 E-value=20 Score=32.56 Aligned_cols=9 Identities=56% Similarity=1.069 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
+.||+||++
T Consensus 142 ~AHElGH~l 150 (203)
T 1kuf_A 142 MTHELGHNL 150 (203)
T ss_dssp HHHHHHHHT
T ss_pred HHHHHhhhc
No 86
>d1nd1a_ d.92.1.9 (A:) Snake venom metalloprotease {Terciopelo (Bothrops asper), bap1 [TaxId: 8722]}
Probab=49.82 E-value=20 Score=32.58 Aligned_cols=9 Identities=56% Similarity=1.128 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
+.||+||++
T Consensus 140 ~AHElGH~l 148 (202)
T d1nd1a_ 140 MAHELGHNL 148 (202)
T ss_dssp HHHHHHHHT
T ss_pred HHHHHHhhc
No 87
>PF01433 Peptidase_M1: Peptidase family M1 This is family M1 in the peptidase classification. ; InterPro: Metalloproteases are the most diverse of the four main types of protease, with more than 50 families
identified to date. In these enzymes, a divalent cation, usually zinc, activates the water molecule. The metal ion
is held in place by amino acid ligands, usually three in number. The known metal ligands are His, Glu, Asp or
Lys and at least one other residue is required for catalysis, which may play an electrophillic role. Of the
known metalloproteases, around half contain an HEXXH motif, which has been shown in crystallographic studies to
form part of the metal-binding site . The HEXXH motif is relatively common, but can be more stringently defined
for metalloproteases as 'abXHEbbHbc', where 'a' is most often valine or threonine and forms part of the S1'
subsite in thermolysin and neprilysin, 'b' is an uncharged residue, and 'c' a hydrophobic residue. Proline is never
found in this site, possibly because it would break the helical structure adopted by this motif in
metalloproteases . Peptidases are grouped into clans and families. Clans are groups of families for which there is
evidence of common ancestry. Each clan is identified with two letters, the first representing the catalytic type of
the families included in the clan (with the letter 'P' being used for a clan containing families of more than
one of the catalytic types serine, threonine and cysteine). Some families cannot yet be assigned to clans, and
when a formal assignment is required, such a family is described as belonging to clan A-, C-, M-, S-, T- or U-,
according to the catalytic type. Some clans are divided into subclans because there is evidence of a very
ancient divergence within the clan, for example MA(E), the gluzincins, and MA(M), the metzincins. Families are
grouped by their catalytic type, the first character representing the catalytic type: A, aspartic; C, cysteine; G,
glutamic acid; M, metallo; S, serine; T, threonine; and U, unknown. The serine, threonine and cysteine
peptidases utilise the amino acid as a nucleophile and form an acyl intermediate - these peptidases can also readily
act as transferases. In the case of aspartic, glutamic and metallopeptidases, the nucleophile is an activated
water molecule. This group of metallopeptidases belong to the MEROPS peptidase family M1 (clan MA(E)), the
type example being aminopeptidase N from Homo sapiens. The protein fold of the peptidase domain for members of
this family resembles that of thermolysin, the type example for clan MA. Membrane alanine aminopeptidase
(3.4.11.2 from EC) is part of the HEXXH^+E group; it consists entirely of aminopeptidases, spread across a wide
variety of species . Functional studies show that CD13/APN catalyzes the removal of single amino acids from the amino
terminus of small peptides and probably plays a role in their final digestion; one family member
(leukotriene-A4 hydrolase) is known to hydrolyse the epoxide leukotriene-A4 to form an inflammatory mediator . This
hydrolase has been shown to have aminopeptidase activity , and the zinc ligands of the M1 family were identified by
site-directed mutagenesis on this enzyme CD13 participates in trimming peptides bound to MHC class II molecules
and cleaves MIP-1 chemokine, which alters target cell specificity from basophils to eosinophils . CD13 acts as
a receptor for specific strains of RNA viruses (coronaviruses) which cause a relatively large percentage of
upper respiratory trace infections. CD molecules are leucocyte antigens on cell surfaces. CD antigens
nomenclature is updated at Protein Reviews On The Web (http://mpr.nci.nih.gov/prow/). ; GO: 0008237 metallopeptidase
activity, 0008270 zinc ion binding; PDB: 1z1w _A 1z5h _A 2gtq _A 3b3b _A 3b2x _A 2dq6 _A 2hpo _A 2dqm _A 2hpt _A 3b34 _A
....
Probab=49.71 E-value=1.9e+02 Score=29.64 Aligned_cols=100 Identities=11% Similarity=-0.025 Sum_probs=0.0
Q ss_pred CHHHHHHHHHHHHHHHHHHhCCCCCCccccccccccccccchhhceeeeeccccceecCCcceeeeccccccceeccCCC
Q Q5E705_VIBF1/1 141 DVLEMTKQFDLFTIGVNEFYGRDGVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHSGYPVMSTSFPRQKSSLFKATD 220 (302)
Q Consensus 141 d~~~l~~~~d~ii~~~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~g~~~~~~~~~~~~~~~~~~~~ 220 (302)
.....++.-.++++.+.++.|++.... +..++.-+.+..+.|....-+..... ....-....
T Consensus 227 ~~~~~l~~~~~~l~~~~~~~g~pyP~~---------------~~~~v~~p~~~~~~me~~g~i~~~~~---~~l~~~~~~ 288 (391)
T PF01433_consen 227 QAERALDVAKDALDYFEEYFGIPYPFP---------------KLDIVAVPDFPFGGMENWGLITYSEN---FLLYDPDST 288 (391)
T ss_dssp GHHHHHHHHHHHHHHHHHH-----SSS---------------EEEEEEEST-----B--T-TEEEEGG---GTS--TTTT
T ss_pred HHHHHHHHHHHHHHHHHHhcCCCCCCc---------------cCCEEEecCcCcchhccceEEEEecc---ccccCCccc
Q ss_pred cc--------hhHHhhhhhccccccccCCCccch-hhHHHHHHHHHH
Q Q5E705_VIBF1/1 221 NW--------MLGHEIGHNQAANWLNVVGAGETA-NNVLALYTQERN 258 (302)
Q Consensus 221 ~W--------G~~HEiGH~~Q~~~~~~~g~~Evt-nNi~sl~~q~~~ 258 (302)
.+ .+.||++|.-=.+..+-..+.+.| +.=|+.|....+
T Consensus 289 ~~~~~~~~~~~iaHElaHqWfG~~Vt~~~w~~~WL~Eg~a~y~~~~~ 335 (391)
T PF01433_consen 289 DDSQKQRIARVIAHELAHQWFGNLVTPDWWKDLWLNEGFATYLEYLY 335 (391)
T ss_dssp THHHHHHHHHHHHHCCHGCT----SEESSGGGHHHHHHHHHHHHHHH
T ss_pred cccchhhhhhHHHHHHHHHHhhcEecccccCCEeHHHHHHHHHHHHH
No 88
>1rm8_A MMP-16, matrix metalloproteinase-16, MT3-MMP; membrane type - matrix metalloproteinase, batimastat,
hydroxamate inhibitor, protease, hydrolase; HET: BAT; 1.80A {Homo sapiens} SCOP: d.92.1.11
Probab=49.27 E-value=20 Score=31.06 Aligned_cols=9 Identities=44% Similarity=0.689 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
+.|||||..
T Consensus 121 ~~HEiGHaL 129 (169)
T 1rm8_A 121 AVHELGHAL 129 (169)
T ss_dssp HHHHHHHHH
T ss_pred hhhhhhhhc
No 89
>d1sata2 d.92.1.6 (A:4-246) Metalloprotease {Serratia marcescens [TaxId: 615]}
Probab=49.22 E-value=75 Score=30.22 Aligned_cols=86 Identities=13% Similarity=-0.051 Sum_probs=0.0
Q ss_pred HHHHHHHHHHHHHHHHHhCCCCCCccccccccccccccchhhceeeeeccccceecCCcceeeeccccccceeccCCCcc
Q Q5E705_VIBF1/1 143 LEMTKQFDLFTIGVNEFYGRDGVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHSGYPVMSTSFPRQKSSLFKATDNW 222 (302)
Q Consensus 143 ~~l~~~~d~ii~~~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~g~~~~~~~~~~~~~~~~~~~~~W 222 (302)
.+-.+...++++...+++++................+..............+....... ..................|
T Consensus 80 ~~q~~~~r~a~~~Ws~vani~F~ev~~~~~adi~~~~~~~~~~~~~~~~~~a~a~~p~~--~~~~~~~~~~~~~~~~~~~ 157 (243)
T d1sata2 80 AEQQQQAKLSLQSWADVANITFTEVAAGQKANITFGNYSQDRPGHYDYGTQAYAFLPNT--IWQGQDLGGQTWYNVNQSN 157 (243)
T ss_dssp HHHHHHHHHHHHHHHHHBSEEEEECCTTSCCSEEEEEECEEETTEECCSCCEEECCTTC--EETTEECTTEEEEETTSHH
T ss_pred HHHHHHHHHHHHHHHhhcCcEEEEecCCCceEEEEEeccCCCCCCCCCCcceeeecCCC--cccCccccccccccccccc
Q ss_pred ------------hhHHhhhh
Q Q5E705_VIBF1/1 223 ------------MLGHEIGH 230 (302)
Q Consensus 223 ------------G~~HEiGH 230 (302)
-++|||||
T Consensus 158 ~~~~~~g~~~~~t~lHEIGH 177 (243)
T d1sata2 158 VKHPATEDYGRQTFTHEIGH 177 (243)
T ss_dssp HHCTTTCHHHHHHHHHHHHH
T ss_pred ccCCcccchHHHHHHHHHHH
No 90
>d3b7sa3 d.92.1.13 (A:209-460) Leukotriene A4 hydrolase catalytic domain {Human (Homo sapiens) [TaxId: 9606]}
Probab=48.82 E-value=2.1e+02 Score=27.15 Aligned_cols=114 Identities=11% Similarity=0.048 Sum_probs=0.0
Q ss_pred EcCcEEEEEEHHHHhhhcccCHHHHHHHHHHHHHHHHHHhCCCCCCccccccccccccccchhhceeee-eccccceecC
Q Q5E705_VIBF1/1 121 VGKRFSYTTTTAGIKGHSEVDVLEMTKQFDLFTIGVNEFYGRDGVSGAHKMFTDSAPELEYQNMRLVDD-IQISIGSAHS 199 (302)
Q Consensus 121 ~~~~v~~t~p~~~~~~~~~~d~~~l~~~~d~ii~~~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~-~~~~~~~~~~ 199 (302)
+|.++.+-.+.+.+ ......++.--++++.+.++.| ..+..+..++.- +.+..+.|-.
T Consensus 6 ~g~~vrv~~~p~~~-----~~~~~~l~~~~~~l~~~e~~~g----------------~YP~~k~d~v~~~~~~~~ggmE~ 64 (252)
T d3b7sa3 6 IGPRTLVWSEKEQV-----EKSAYEFSETESMLKIAEDLGG----------------PYVWGQYDLLVLPPSFPYGGMEN 64 (252)
T ss_dssp EETTEEEEECGGGH-----HHHHHHTTTHHHHHHHHHHHHC----------------CCCSSCCEEEECCTTCSSSEECC
T ss_pred cCCceEEEEccchH-----HHHHHHHHHHHHHHHHHHHhCC----------------CCCchhcCEEEeCCCcccccccc
Q ss_pred CcceeeeccccccceeccCCCcchhHHhhhhhccccccccCCCccch-hhHHHHHHHHHHh
Q Q5E705_VIBF1/1 200 GYPVMSTSFPRQKSSLFKATDNWMLGHEIGHNQAANWLNVVGAGETA-NNVLALYTQERNT 259 (302)
Q Consensus 200 g~~~~~~~~~~~~~~~~~~~~~WG~~HEiGH~~Q~~~~~~~g~~Evt-nNi~sl~~q~~~~ 259 (302)
..-+............+. ..+.||++|.-=.+..+...+.+.| |.=|+.|+...+.
T Consensus 65 ~~l~~~~~~~~~~~~~~~----~~iaHE~aHqWfG~~Vt~~~w~~~WL~EG~a~y~~~~~~ 121 (252)
T d3b7sa3 65 PCLTFVTPTLLAGDKSLS----NVIAHQISHSWTGNLVTNKTWDHFWLNEGHTVYLERHIC 121 (252)
T ss_dssp TTEEEECGGGCCSSSTTT----HHHHHHHHTTTBTTTEEESSGGGHHHHHHHHHHHHHHHH
T ss_pred ceeeeecchhccccchHH----HHHHHHHHHHHHhhhceeccccchHhhccHHHHHHHHhh
No 91
>COG1164 Oligoendopeptidase F [Amino acid transport and metabolism]
Probab=48.72 E-value=48 Score=36.10 Aligned_cols=82 Identities=12% Similarity=-0.072 Sum_probs=0.0
Q ss_pred EEHHHHhhhcccCHHHHHHHHHHHHHHHHHHhCCCCCCccccccccccccccchhhceeeeeccccceecCCcceeeecc
Q Q5E705_VIBF1/1 129 TTTAGIKGHSEVDVLEMTKQFDLFTIGVNEFYGRDGVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHSGYPVMSTSF 208 (302)
Q Consensus 129 ~p~~~~~~~~~~d~~~l~~~~d~ii~~~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~g~~~~~~~~ 208 (302)
++.++.++.+-.....|-..|.+++....+- +...-.+++-++ +|||+++.+.. ...
T Consensus 312 ~s~~ea~~~v~~~l~~lg~ey~~~~~~a~~~-~WiD~~~~~gKr--------------------sGaYs~~~~~~--~~p 368 (598)
T COG1164 312 YSYEEAKELVLKALAPLGPEYAKIARRAFDE-RWIDVYPRKGKR--------------------SGAYSIGFYKG--DHP 368 (598)
T ss_pred ccHHHHHHHHHHHHHhhCHHHHHHHHHHHHc-CCcccccCCCCC--------------------CCcccCCCCCC--CCc
Q ss_pred ccccceeccCCCcchhHHhhhhhcc
Q Q5E705_VIBF1/1 209 PRQKSSLFKATDNWMLGHEIGHNQA 233 (302)
Q Consensus 209 ~~~~~~~~~~~~~WG~~HEiGH~~Q 233 (302)
..-+.|.-...+-=.+.||+||.++
T Consensus 369 ~IlmN~~gt~~dV~TLaHElGHs~H 393 (598)
T COG1164 369 FILMNYDGTLRDVFTLAHELGHSVH 393 (598)
T ss_pred eEEecCCCchhhhhHHhhhhhHHHH
No 92
>3ba0_A Macrophage metalloelastase; FULL-length MMP-12, hemopexin domain, catalytic domain, domain interaction.,
calcium, extracellular matrix; 3.00A {Homo sapiens} PDB: 2jxy _A
Probab=48.54 E-value=55 Score=33.14 Aligned_cols=90 Identities=10% Similarity=-0.274 Sum_probs=0.0
Q ss_pred CHHHHHHHHHHHHHHHHHHhCCCCCCccccccccccccccchhhceeeeeccccceecCCcc-------eeeeccccccc
Q Q5E705_VIBF1/1 141 DVLEMTKQFDLFTIGVNEFYGRDGVSGAHKMFTDSAPELEYQNMRLVDDIQISIGSAHSGYP-------VMSTSFPRQKS 213 (302)
Q Consensus 141 d~~~l~~~~d~ii~~~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~g~~-------~~~~~~~~~~~ 213 (302)
...+.-+...+.++...+.++|...........++-.+..........-...++..+++-.+ +....+.....
T Consensus 21 ~~~~~~~~i~~Af~~Ws~v~~l~F~ev~~~~adi~I~f~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~i~~~~~~~~~~ 100 (365)
T 3ba0_A 21 NREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTT 100 (365)
T ss_dssp CSHHHHHHHHHHHHHHHTTSSCCEEECSSSCCSEEEEEECSSCSSSSCCCSSSSCCEEECCSCSSSSSCEEEETTSCEES
T ss_pred CHHHHHHHHHHHHHHHhcccCcEEEEeCCCCccEEEEEecCcCCCCcccCCCcceEeccccCCCceeeeEEecccccccc
Q ss_pred eeccCCCcchhHHhhhh
Q Q5E705_VIBF1/1 214 SLFKATDNWMLGHEIGH 230 (302)
Q Consensus 214 ~~~~~~~~WG~~HEiGH 230 (302)
..-....-.-+.|||||
T Consensus 101 ~~~~~~~~~v~~HEiGH 117 (365)
T 3ba0_A 101 HSGGTNLFLTAVHEIGH 117 (365)
T ss_dssp SSSSEESSHHHHHHHHH
T ss_pred CCCCceeEEEeeehhhh
No 93
>1k7iA02 3.40.390.10
Probab=48.08 E-value=52 Score=27.45 Aligned_cols=88 Identities=9% Similarity=-0.078 Sum_probs=0.0
Q ss_pred HHHHHHHHHHHHHHHHHhCCCCCCccccccccccccccchhhce------eeeeccccceecCCcceeeeccccccceec
Q Q5E705_VIBF1/1 143 LEMTKQFDLFTIGVNEFYGRDGVSGAHKMFTDSAPELEYQNMRL------VDDIQISIGSAHSGYPVMSTSFPRQKSSLF 216 (302)
Q Consensus 143 ~~l~~~~d~ii~~~~~l~Gl~~~~~~~~~~~~~~~~~~~~~~~~------~~~~~~~~~~~~~g~~~~~~~~~~~~~~~~ 216 (302)
.+.-+.....++...+++.|........................ .+...........+................
T Consensus 64 ~~~~~~~~~al~~w~~v~~l~F~~~~~~~~~~~~~~~~~~~~~~~~~~~~~a~A~~P~~~~~~~~~~~~~~~~~~~~~~~ 143 (227)
T 1k7iA02 64 AEVKEAIKLALQVWSDVANLTFTEVSDGSDANITFGFYSLGDPGDLPGGTLAHAYLPGSGGIGGDAHFDIDEDWTLNPDL 143 (227)
T ss_pred hHHHHHHHHHHHhhhhhccceEEEecCCCcceEEEEeeccccccCCCcceeEEEEcCCCcccccceeecccccccccccc
Q ss_pred cCCCcchhHHhhhh
Q Q5E705_VIBF1/1 217 KATDNWMLGHEIGH 230 (302)
Q Consensus 217 ~~~~~WG~~HEiGH 230 (302)
......-..||+||
T Consensus 144 ~~~~~~~~~HE~GH 157 (227)
T 1k7iA02 144 GNYLFLVAAHEIGH 157 (227)
T ss_pred cceeeeeeeeecch
No 94
>cd04272 ZnMc_salivary_gland_MPs Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by
the salivary glands of arthropods.
Probab=47.87 E-value=20 Score=33.34 Aligned_cols=9 Identities=33% Similarity=0.593 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
+.||+||+.
T Consensus 149 ~AHElGHnL 157 (220)
T cd04272 149 MTHELAHLL 157 (220)
T ss_pred hhhhhhhhc
No 95
>COG3590 PepO Predicted metalloendopeptidase [Posttranslational modification, protein turnover, chaperones]
Probab=47.69 E-value=22 Score=37.62 Aligned_cols=20 Identities=40% Similarity=0.654 Sum_probs=0.0
Q ss_pred hHHhhhhhccccccccCCCc
Q Q5E705_VIBF1/1 224 LGHEIGHNQAANWLNVVGAG 243 (302)
Q Consensus 224 ~~HEiGH~~Q~~~~~~~g~~ 243 (302)
+.|||||+++..--.+.+.|
T Consensus 491 IgHEI~HgFDdqGakfD~~G 510 (654)
T COG3590 491 IGHEIGHGFDDQGAKFDGDG 510 (654)
T ss_pred ehhhhcccccCCccccCCCC
No 96
>d1atla_ d.92.1.9 (A:) Snake venom metalloprotease {Western diamonback rattlesnake (Crotalus atrox), atrolysin C
[TaxId: 8730]}
Probab=47.36 E-value=23 Score=32.12 Aligned_cols=9 Identities=56% Similarity=1.128 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
+.||+||++
T Consensus 138 ~AHElGH~l 146 (200)
T d1atla_ 138 MAHELGHNL 146 (200)
T ss_dssp HHHHHHHHT
T ss_pred HHHHHHhhc
No 97
>2ddf_A ADAM 17; hydrolase; HET: INN CIT; 1.70A {Homo sapiens} PDB: 2fv5 _A* 3l0v _A* 3kme _A* 3l0t _A* 3kmc _A*
3ewj _A* 3edz _A* 3e8r _A* 2fv9 _A* 1zxc _A* 2oi0 _A* 3b92 _A* 2a8h _A* 1bkc _A* 3cki _A 1bkc _I* 1bkc _E*
Probab=47.05 E-value=24 Score=33.49 Aligned_cols=9 Identities=56% Similarity=0.881 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
+.|||||++
T Consensus 186 ~AHElGH~l 194 (257)
T 2ddf_A 186 TTHELGHNF 194 (257)
T ss_dssp HHHHHHHHT
T ss_pred HHHHhHHhc
No 98
>cd04273 ZnMc_ADAMTS_like Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And
Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This
particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with
thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are
inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis,
development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various
components of the extracellular matrix.
Probab=47.03 E-value=23 Score=32.69 Aligned_cols=9 Identities=44% Similarity=0.907 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
+.||+||+.
T Consensus 144 ~AHElGHnL 152 (207)
T cd04273 144 IAHELGHVL 152 (207)
T ss_pred HHHHHHhhc
No 99
>1atl_A Atrolysin C; metalloendopeptidase; HET: MTJ; 1.80A {Crotalus atrox} SCOP: d.92.1.9 PDB: 1htd _A 1dth _A*
2aig _P* 3aig _A* 4aig _A* 1iag _A
Probab=46.09 E-value=25 Score=31.98 Aligned_cols=9 Identities=56% Similarity=1.128 Sum_probs=0.0
Q ss_pred hHHhhhhhc
Q Q5E705_VIBF1/1 224 LGHEIGHNQ 232 (302)
Q Consensus 224 ~~HEiGH~~ 232 (302)
+.||+||++
T Consensus 140 ~AHElGH~l 148 (202)
T 1atl_A 140 MAHELGHNL 148 (202)
T ss_dssp HHHHHHHHT
T ss_pred HHHHHHHhc
No 100
>COG1913 Predicted Zn-dependent proteases [General function prediction only]
Probab=45.40 E-value=26 Score=31.33 Aligned_cols=10 Identities=40% Similarity=0.527 Sum_probs=0.0
Q ss_pred hhHHhhhhhc
Q Q5E705_VIBF1/1 223 MLGHEIGHNQ 232 (302)
Q Consensus 223 G~~HEiGH~~ 232 (302)
+..||+||.+
T Consensus 127 Ev~HElGH~~ 136 (181)
T COG1913 127 EVLHELGHLL 136 (181)
T ss_pred HHHHHhhhhc
Done!
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