|
Name |
Accession |
Description |
Interval |
E-value |
| Zn_serralysin |
NF035945 |
serralysin family metalloprotease; |
24-482 |
0e+00 |
|
serralysin family metalloprotease;
Pssm-ID: 468274 [Multi-domain] Cd Length: 457 Bit Score: 710.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 24 SAYNQINSFSHQYDRGGNLTVNGKPSFSVDQAATQLLRDGAAYKDLN-GNGKIDLTYTFLTSASSStmYKHGISGFSQFS 102
Cdd:NF035945 1 SGYDDVNDLLHYHDRGNGLTINGKPSYTVDQAGDQITRGDATWNGKNvFGKPANLTYSFLTSAPSS--NPNGDTGFSAFN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 103 AQQKAQAVLAMQSWADVANVVFTEKASGGDAHMTFGNYSggqDGAAAFAYLPGTGAGyDGTSWYLINSSYTQNKNPDLNN 182
Cdd:NF035945 79 AEQKAQAKLSLQSWSDVANITFTEVSAGQKANITFGNYS---DSGQAYAYLPGTSDV-SGQSWYNYNSDYIRNLTPDLGN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 183 YGRQTLTHEIGHTLGLAHPGDYNAGEGNPSYKDASYGQDTRGYSVMSYWSESNTSQNFSKggveAYSSGPLMDDIAAIQK 262
Cdd:NF035945 155 YGRQTLTHEIGHTLGLSHPGDYNAGEGNPTYKDATYAEDTRQYSVMSYWSESNTGQDFKG----HYASAPLLDDIAAIQK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 263 LYGANYSTRAGDTTYGFNSNTGRDFYSASSSSDKLVFSVWDGGGNDTLDFSGFTQNQKINLNEASFSDVGGMVGNVSIAQ 342
Cdd:NF035945 231 LYGANMTTRTGDTVYGFNSNTDRDFYTATDSSDKLIFSVWDAGGNDTFDFSGYSQNQRINLNEGSFSDVGGLKGNVSIAA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 343 GVTVENAIGGSGNDLLIGNNAANVLKGGAGNDIIYGAGGADQLWGGSGSDTFVFAASTDSKPGAADQIMDFVSGLDKIDL 422
Cdd:NF035945 311 GVTIENAIGGSGNDVLVGNDADNILKGGAGNDVIYGGGGADQLWGGAGKDIFVYGAVSDSTPSAPDWIMDFVSGIDKIDL 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499373916 423 TGITKGAG----LHFVNAFTGAAGDAILT--TSGGVSTLSVDFSGHGVADFLVSTVGQAAV-SDIVA 482
Cdd:NF035945 391 SAFNQGDGgggfLHFVDAFSGKAGEALLSydAQSNLSDLALNLGGHANPDFLVKIVGQANQaTDFIV 457
|
|
| Peptidase_M10_C |
pfam08548 |
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix ... |
266-481 |
6.92e-107 |
|
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix metallopeptidases (MMPs). The peptidase unit is found at the N terminal while this domain at the C terminal forms a corkscrew and is thought to be important for secretion of the protein through the bacterial cell wall. This domain contains the calcium ion binding domain pfam00353.
Pssm-ID: 430067 [Multi-domain] Cd Length: 222 Bit Score: 317.01 E-value: 6.92e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 266 ANYSTRAGDTTYGFNSNTGRDFYSASSSSDKLVFSVWDGGGNDTLDFSGFTQNQKINLNEASFSDVGGMVGNVSIAQGVT 345
Cdd:pfam08548 1 ANLTTRTGDTVYGFNSNTGRDFYTATDASSKLIFSVWDAGGNDTFDFSGYSQNQRINLNEGSFSDVGGLKGNVSIAHGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 346 VENAIGGSGNDLLIGNNAANVLKGGAGNDIIYGAGGADQLWGGSGSDTFVFAASTDSKPGAADQIMDFVSGLDKIDLTGI 425
Cdd:pfam08548 81 IENAIGGSGNDVLIGNDADNILKGGAGNDILYGGGGADQLWGGAGNDIFVYASAKDSLTAAPDTIRDFVSGIDKIDLSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499373916 426 TKG-AGLHFVNAFTGAAGDAILT--TSGGVSTLSVDFSGH-GVADFLVSTVGQAAV-SDIV 481
Cdd:pfam08548 161 NNNsDGLQFVDRFSGKAGEALLRynEVSNITNLAIDFSGQlSNNDFLVKIVGQALQtADFI 221
|
|
| ZnMc_serralysin_like |
cd04277 |
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ... |
77-265 |
5.12e-45 |
|
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides.
Pssm-ID: 239804 [Multi-domain] Cd Length: 186 Bit Score: 155.65 E-value: 5.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 77 LTYTFLTSASSST---MYKHGISGFSQFSAQQKAQAVLAMQSWADVANVVFTEKASGGDAHMTFGNYSGGQDGAAAFAYL 153
Cdd:cd04277 4 LTYSFSNTGGPYSygyGREEDTTNTAALSAAQQAAARDALEAWEDVADIDFVEVSDNSGADIRFGNSSDPDGNTAGYAYY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 154 PGTGAG--YDGTSWYliNSSYTQNkNPDLNNYGRQTLTHEIGHTLGLAHPGDYNAGEGNPSykdaSYGQDTRGYSVMSYW 231
Cdd:cd04277 84 PGSGSGtaYGGDIWF--NSSYDTN-SDSPGSYGYQTIIHEIGHALGLEHPGDYNGGDPVPP----TYALDSREYTVMSYN 156
|
170 180 190
....*....|....*....|....*....|....
gi 499373916 232 SESNTSQNFSKGgveaYSSGPLMDDIAAIQKLYG 265
Cdd:cd04277 157 SGYGNGASAGGG----YPQTPMLLDIAALQYLYG 186
|
|
| ZnMc |
smart00235 |
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ... |
99-266 |
1.35e-15 |
|
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.
Pssm-ID: 214576 [Multi-domain] Cd Length: 139 Bit Score: 73.54 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 99 SQFSAQQKAQAVLAMQSWADVANVVFTEKASGGDAHMTFGNYSGGqdGAAAFAYLPGTGAGYDGTSWYlinssytqnknp 178
Cdd:smart00235 17 SSLSPEEREAIAKALAEWSDVTCIRFVERTGTADIYISFGSGDSG--CTLSHAGRPGGDQHLSLGNGC------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 179 dlnnYGRQTLTHEIGHTLGLAHPGDYNAGEG--NPSYKDasygQDTRGYSVMsywsesntsqnfskggveayssgplMDD 256
Cdd:smart00235 83 ----INTGVAAHELGHALGLYHEQSRSDRDNymYINYTN----IDTRNFDLS-------------------------EDD 129
|
170
....*....|
gi 499373916 257 IAAIQKLYGA 266
Cdd:smart00235 130 SLGIPYDYGS 139
|
|
| COG2931 |
COG2931 |
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ... |
255-461 |
1.63e-06 |
|
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442175 [Multi-domain] Cd Length: 252 Bit Score: 49.52 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 255 DDIAAIQKLYGANYSTRAGDTTYGFNSNTGRDFYSASSSSDKLVFSVWDGGGNDTLDFSGFTQNQKINLNEASFSDVGGm 334
Cdd:COG2931 40 GGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGGGGGGDDTDGGGDGGDGGGGGTGDDTGDGGGGNDTLTGG- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 335 VGNVSIAQGVTVENAIGGSGNDLLIGNNAANVLKGGAGNDIIYGAGGADQLWGGSGSDTFVFAASTDSKPGAADQIMDFV 414
Cdd:COG2931 119 DGNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLYGGAGNDTLYGGAGNDTLDGGAGNDTLTGGAGNDTLTGGAGNDTLDG 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499373916 415 SGLDKIDLTGITKGAGLHFVNAFTGAAGDAILTTSGGVSTLSVDFSG 461
Cdd:COG2931 199 GGGDDTLGGGGGDDGLDGGDGDDGLGGGGGDDTLGGGGGGDGGGGGG 245
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Zn_serralysin |
NF035945 |
serralysin family metalloprotease; |
24-482 |
0e+00 |
|
serralysin family metalloprotease;
Pssm-ID: 468274 [Multi-domain] Cd Length: 457 Bit Score: 710.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 24 SAYNQINSFSHQYDRGGNLTVNGKPSFSVDQAATQLLRDGAAYKDLN-GNGKIDLTYTFLTSASSStmYKHGISGFSQFS 102
Cdd:NF035945 1 SGYDDVNDLLHYHDRGNGLTINGKPSYTVDQAGDQITRGDATWNGKNvFGKPANLTYSFLTSAPSS--NPNGDTGFSAFN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 103 AQQKAQAVLAMQSWADVANVVFTEKASGGDAHMTFGNYSggqDGAAAFAYLPGTGAGyDGTSWYLINSSYTQNKNPDLNN 182
Cdd:NF035945 79 AEQKAQAKLSLQSWSDVANITFTEVSAGQKANITFGNYS---DSGQAYAYLPGTSDV-SGQSWYNYNSDYIRNLTPDLGN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 183 YGRQTLTHEIGHTLGLAHPGDYNAGEGNPSYKDASYGQDTRGYSVMSYWSESNTSQNFSKggveAYSSGPLMDDIAAIQK 262
Cdd:NF035945 155 YGRQTLTHEIGHTLGLSHPGDYNAGEGNPTYKDATYAEDTRQYSVMSYWSESNTGQDFKG----HYASAPLLDDIAAIQK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 263 LYGANYSTRAGDTTYGFNSNTGRDFYSASSSSDKLVFSVWDGGGNDTLDFSGFTQNQKINLNEASFSDVGGMVGNVSIAQ 342
Cdd:NF035945 231 LYGANMTTRTGDTVYGFNSNTDRDFYTATDSSDKLIFSVWDAGGNDTFDFSGYSQNQRINLNEGSFSDVGGLKGNVSIAA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 343 GVTVENAIGGSGNDLLIGNNAANVLKGGAGNDIIYGAGGADQLWGGSGSDTFVFAASTDSKPGAADQIMDFVSGLDKIDL 422
Cdd:NF035945 311 GVTIENAIGGSGNDVLVGNDADNILKGGAGNDVIYGGGGADQLWGGAGKDIFVYGAVSDSTPSAPDWIMDFVSGIDKIDL 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499373916 423 TGITKGAG----LHFVNAFTGAAGDAILT--TSGGVSTLSVDFSGHGVADFLVSTVGQAAV-SDIVA 482
Cdd:NF035945 391 SAFNQGDGgggfLHFVDAFSGKAGEALLSydAQSNLSDLALNLGGHANPDFLVKIVGQANQaTDFIV 457
|
|
| Peptidase_M10_C |
pfam08548 |
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix ... |
266-481 |
6.92e-107 |
|
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix metallopeptidases (MMPs). The peptidase unit is found at the N terminal while this domain at the C terminal forms a corkscrew and is thought to be important for secretion of the protein through the bacterial cell wall. This domain contains the calcium ion binding domain pfam00353.
Pssm-ID: 430067 [Multi-domain] Cd Length: 222 Bit Score: 317.01 E-value: 6.92e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 266 ANYSTRAGDTTYGFNSNTGRDFYSASSSSDKLVFSVWDGGGNDTLDFSGFTQNQKINLNEASFSDVGGMVGNVSIAQGVT 345
Cdd:pfam08548 1 ANLTTRTGDTVYGFNSNTGRDFYTATDASSKLIFSVWDAGGNDTFDFSGYSQNQRINLNEGSFSDVGGLKGNVSIAHGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 346 VENAIGGSGNDLLIGNNAANVLKGGAGNDIIYGAGGADQLWGGSGSDTFVFAASTDSKPGAADQIMDFVSGLDKIDLTGI 425
Cdd:pfam08548 81 IENAIGGSGNDVLIGNDADNILKGGAGNDILYGGGGADQLWGGAGNDIFVYASAKDSLTAAPDTIRDFVSGIDKIDLSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499373916 426 TKG-AGLHFVNAFTGAAGDAILT--TSGGVSTLSVDFSGH-GVADFLVSTVGQAAV-SDIV 481
Cdd:pfam08548 161 NNNsDGLQFVDRFSGKAGEALLRynEVSNITNLAIDFSGQlSNNDFLVKIVGQALQtADFI 221
|
|
| ZnMc_serralysin_like |
cd04277 |
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ... |
77-265 |
5.12e-45 |
|
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides.
Pssm-ID: 239804 [Multi-domain] Cd Length: 186 Bit Score: 155.65 E-value: 5.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 77 LTYTFLTSASSST---MYKHGISGFSQFSAQQKAQAVLAMQSWADVANVVFTEKASGGDAHMTFGNYSGGQDGAAAFAYL 153
Cdd:cd04277 4 LTYSFSNTGGPYSygyGREEDTTNTAALSAAQQAAARDALEAWEDVADIDFVEVSDNSGADIRFGNSSDPDGNTAGYAYY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 154 PGTGAG--YDGTSWYliNSSYTQNkNPDLNNYGRQTLTHEIGHTLGLAHPGDYNAGEGNPSykdaSYGQDTRGYSVMSYW 231
Cdd:cd04277 84 PGSGSGtaYGGDIWF--NSSYDTN-SDSPGSYGYQTIIHEIGHALGLEHPGDYNGGDPVPP----TYALDSREYTVMSYN 156
|
170 180 190
....*....|....*....|....*....|....
gi 499373916 232 SESNTSQNFSKGgveaYSSGPLMDDIAAIQKLYG 265
Cdd:cd04277 157 SGYGNGASAGGG----YPQTPMLLDIAALQYLYG 186
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
93-264 |
4.83e-32 |
|
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease.
Pssm-ID: 238124 [Multi-domain] Cd Length: 167 Bit Score: 120.32 E-value: 4.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 93 HGISGFSQFSAQQKAQAVLAMQSWADVANVVFTEKASGGDAH-MTFGNYSGGQDGA-AAFAYLPGTGAGYDGTSWYLINS 170
Cdd:cd00203 11 DRDVEEENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIDKAdIAILVTRQDFDGGtGGWAYLGRVCDSLRGVGVLQDNQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 171 SYtqnknpdlNNYGRQTLTHEIGHTLGLAHPGDYNAGEGNPSYKDASYGQDTRGYSVMSYWSESNTsqnfskggvEAYSS 250
Cdd:cd00203 91 SG--------TKEGAQTIAHELGHALGFYHDHDRKDRDDYPTIDDTLNAEDDDYYSVMSYTKGSFS---------DGQRK 153
|
170
....*....|....
gi 499373916 251 GPLMDDIAAIQKLY 264
Cdd:cd00203 154 DFSQCDIDQINKLY 167
|
|
| ZnMc_MMP_like |
cd04268 |
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ... |
101-264 |
3.29e-21 |
|
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.
Pssm-ID: 239796 [Multi-domain] Cd Length: 165 Bit Score: 90.25 E-value: 3.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 101 FSAQQKAQAVLAMQSWADVANVVFTEKASGGDAHMTFGNYSGGQDGAAAFAYLPGTGAGYDGTSWYLINSSYTQNKnPDL 180
Cdd:cd04268 12 VPDKLRAAILDAIEAWNKAFAIGFKNANDVDPADIRYSVIRWIPYNDGTWSYGPSQVDPLTGEILLARVYLYSSFV-EYS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 181 NNYGRQTLTHEIGHTLGLAHPGDYNAGEGNPSYkdasYGQDTRGYSVMSYWsesntSQNFSKGGVEAYSSGPLMDDIAAI 260
Cdd:cd04268 91 GARLRNTAEHELGHALGLRHNFAASDRDDNVDL----LAEKGDTSSVMDYA-----PSNFSIQLGDGQKYTIGPYDIAAI 161
|
....
gi 499373916 261 QKLY 264
Cdd:cd04268 162 KKLY 165
|
|
| ZnMc |
smart00235 |
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ... |
99-266 |
1.35e-15 |
|
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.
Pssm-ID: 214576 [Multi-domain] Cd Length: 139 Bit Score: 73.54 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 99 SQFSAQQKAQAVLAMQSWADVANVVFTEKASGGDAHMTFGNYSGGqdGAAAFAYLPGTGAGYDGTSWYlinssytqnknp 178
Cdd:smart00235 17 SSLSPEEREAIAKALAEWSDVTCIRFVERTGTADIYISFGSGDSG--CTLSHAGRPGGDQHLSLGNGC------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 179 dlnnYGRQTLTHEIGHTLGLAHPGDYNAGEG--NPSYKDasygQDTRGYSVMsywsesntsqnfskggveayssgplMDD 256
Cdd:smart00235 83 ----INTGVAAHELGHALGLYHEQSRSDRDNymYINYTN----IDTRNFDLS-------------------------EDD 129
|
170
....*....|
gi 499373916 257 IAAIQKLYGA 266
Cdd:smart00235 130 SLGIPYDYGS 139
|
|
| ZnMc_MMP |
cd04278 |
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ... |
112-265 |
1.10e-12 |
|
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).
Pssm-ID: 239805 [Multi-domain] Cd Length: 157 Bit Score: 65.69 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 112 AMQSWADVANVVFTEKASGGDAHMTFGNYSG---------GQDGAAAFAYLPGTGAG---YDGtswyliNSSYTQNKNPD 179
Cdd:cd04278 30 AFRVWSDVTPLTFREVTSGQEADIRISFARGnhgdgypfdGPGGTLAHAFFPGGIGGdihFDD------DEQWTLGSDSG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 180 LNNYgRQTLTHEIGHTLGLAHPGDYNagegnpsykdasygqdtrgySVMS-YWSESNTSQNFSKggveayssgplmDDIA 258
Cdd:cd04278 104 GTDL-FSVAAHEIGHALGLGHSSDPD--------------------SIMYpYYQGPVPKFKLSQ------------DDIR 150
|
....*..
gi 499373916 259 AIQKLYG 265
Cdd:cd04278 151 GIQALYG 157
|
|
| Peptidase_M10 |
pfam00413 |
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ... |
112-265 |
2.20e-09 |
|
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.
Pssm-ID: 425668 [Multi-domain] Cd Length: 159 Bit Score: 56.09 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 112 AMQSWADVANVVFTEkASGGDAHMTFGNYSG---------GQDGAAAFAYLPGTGAG----YDGTSWYLInssytQNKNP 178
Cdd:pfam00413 30 AFKVWSEVTPLTFTE-VSTGEADIMIGFGRGdhgdgypfdGPGGVLAHAFFPGPGLGgdihFDDDETWTV-----GSDPP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 179 DLNNYgRQTLTHEIGHTLGLAHPGDYNAGEgNPSYKdasyGQDTRGYSVmsywsesntSQnfskggveayssgplmDDIA 258
Cdd:pfam00413 104 HGINL-FLVAAHEIGHALGLGHSSDPGAIM-YPTYS----PLDSKKFRL---------SQ----------------DDIK 152
|
....*..
gi 499373916 259 AIQKLYG 265
Cdd:pfam00413 153 GIQQLYG 159
|
|
| COG2931 |
COG2931 |
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ... |
255-461 |
1.63e-06 |
|
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442175 [Multi-domain] Cd Length: 252 Bit Score: 49.52 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 255 DDIAAIQKLYGANYSTRAGDTTYGFNSNTGRDFYSASSSSDKLVFSVWDGGGNDTLDFSGFTQNQKINLNEASFSDVGGm 334
Cdd:COG2931 40 GGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGGGGGGDDTDGGGDGGDGGGGGTGDDTGDGGGGNDTLTGG- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 335 VGNVSIAQGVTVENAIGGSGNDLLIGNNAANVLKGGAGNDIIYGAGGADQLWGGSGSDTFVFAASTDSKPGAADQIMDFV 414
Cdd:COG2931 119 DGNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLYGGAGNDTLYGGAGNDTLDGGAGNDTLTGGAGNDTLTGGAGNDTLDG 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499373916 415 SGLDKIDLTGITKGAGLHFVNAFTGAAGDAILTTSGGVSTLSVDFSG 461
Cdd:COG2931 199 GGGDDTLGGGGGDDGLDGGDGDDGLGGGGGDDTLGGGGGGDGGGGGG 245
|
|
| ZnMc_MMP_like_1 |
cd04279 |
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ... |
94-200 |
2.00e-06 |
|
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.
Pssm-ID: 239806 [Multi-domain] Cd Length: 156 Bit Score: 47.45 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 94 GISGFSQFSAQQKAQAVL-AMQSWADVANVVFTEK-ASGGDAHM----TFGNYSGGQDGAAAFAYLPGTGAGYDGTSWYL 167
Cdd:cd04279 10 PTPAPPDSRAQSWLQAVKqAAAEWENVGPLKFVYNpEEDNDADIviffDRPPPVGGAGGGLARAGFPLISDGNRKLFNRT 89
|
90 100 110
....*....|....*....|....*....|....
gi 499373916 168 -INSSYTQNKNPDlnnYGRQTLTHEIGHTLGLAH 200
Cdd:cd04279 90 dINLGPGQPRGAE---NLQAIALHELGHALGLWH 120
|
|
| ZnMc_pappalysin_like |
cd04275 |
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ... |
130-226 |
4.87e-06 |
|
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma protein A (PAPP-A or pappalysin-1) cleaves insulin-like growth factor-binding proteins 4 and 5, thereby promoting cell growth by releasing bound growth factor. This model includes pappalysins and related metalloprotease domains from all three kingdoms of life. The three-dimensional structure of an archaeal representative, ulilysin, has been solved.
Pssm-ID: 239802 [Multi-domain] Cd Length: 225 Bit Score: 47.72 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 130 GGDAHMTFGNYSGGQDGAAAFAYLPGTGAG----YDGTSwylINSSYTQNKNPDLNNYGRqTLTHEIGHTLGLAH----- 200
Cdd:cd04275 83 GGYKYLNIYVANFLGGGLLGYATFPDSLVSlafiTDGVV---INPSSLPGGSAAPYNLGD-TATHEVGHWLGLYHtfqgg 158
|
90 100 110
....*....|....*....|....*....|.
gi 499373916 201 -----PGDYNAgeGNPSYKDASYGQDTRGYS 226
Cdd:cd04275 159 spcctTGDYVA--DTPAEASPSYGCPAGRDT 187
|
|
| HemolysinCabind |
pfam00353 |
RTX calcium-binding nonapeptide repeat (4 copies); |
359-394 |
1.47e-05 |
|
RTX calcium-binding nonapeptide repeat (4 copies);
Pssm-ID: 459777 [Multi-domain] Cd Length: 36 Bit Score: 41.65 E-value: 1.47e-05
10 20 30
....*....|....*....|....*....|....*.
gi 499373916 359 IGNNAANVLKGGAGNDIIYGAGGADQLWGGSGSDTF 394
Cdd:pfam00353 1 YGGDGNDTLVGGAGNDTIYGGAGNDTLDGGAGNDTL 36
|
|
| HemolysinCabind |
pfam00353 |
RTX calcium-binding nonapeptide repeat (4 copies); |
350-385 |
1.98e-05 |
|
RTX calcium-binding nonapeptide repeat (4 copies);
Pssm-ID: 459777 [Multi-domain] Cd Length: 36 Bit Score: 41.27 E-value: 1.98e-05
10 20 30
....*....|....*....|....*....|....*.
gi 499373916 350 IGGSGNDLLIGNNAANVLKGGAGNDIIYGAGGADQL 385
Cdd:pfam00353 1 YGGDGNDTLVGGAGNDTIYGGAGNDTLDGGAGNDTL 36
|
|
| COG2931 |
COG2931 |
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ... |
265-482 |
2.83e-05 |
|
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442175 [Multi-domain] Cd Length: 252 Bit Score: 45.67 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 265 GANYSTRAGDTTYGFNSNTGRDFYSASSSSDKLVFSVWDGGGNDTLDFSGFTQNQKINLNEASFSDVGGMVGNVSIAQGV 344
Cdd:COG2931 31 GGGGGGGGGGGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGGGGGGDDTDGGGDGGDGGGGGTGDDTGDGGG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 345 TVENAIGGSGNDLLIGNNAANVLKGGAGNDIIYGAGGADQLWGGSGSDTFVFAASTDSKPGAADQimDFVSGLDKIDLTG 424
Cdd:COG2931 111 GNDTLTGGDGNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLYGGAGNDTLYGGAGNDTLDGGAGN--DTLTGGAGNDTLT 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499373916 425 ITKGAGLHFVNAFTGAAGDAILTTSGGVSTLSVDFSGHGVADFLVSTVGQAAVSDIVA 482
Cdd:COG2931 189 GGAGNDTLDGGGGDDTLGGGGGDDGLDGGDGDDGLGGGGGDDTLGGGGGGDGGGGGGG 246
|
|
| ZnMc_MMP_like_2 |
cd04276 |
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ... |
185-265 |
4.43e-05 |
|
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase domains similar to matrix metalloproteinases and astacin.
Pssm-ID: 239803 Cd Length: 197 Bit Score: 44.24 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 185 RQTLTHEIGHTLGLAHpgdyN-AGEGNPSYKDASYGQDTRGY----SVMSYwSESNTSQNFSKGGvEAYSSGPLMDDIAA 259
Cdd:cd04276 117 RYLLAHEVGHTLGLRH----NfKASSDGSNEELEDPLGTKEKgatsSVMDY-PPPNVAAQGEDQG-DYYPPTIGPYDKWA 190
|
....*.
gi 499373916 260 IQKLYG 265
Cdd:cd04276 191 IEYGYT 196
|
|
| Reprolysin_2 |
pfam13574 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
135-241 |
4.58e-05 |
|
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.
Pssm-ID: 372637 Cd Length: 193 Bit Score: 44.16 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 135 MTFGNYSGGQDGAAAFAYLPGTGAGYDGTSWYLINSSYTQNKNPDLNNYgrQTLTHEIGHTLGLAH--PGDYNAGEGNPS 212
Cdd:pfam13574 77 VTMGTFSGGELGLAYVGQICQKGASSPKTNTGLSTTTNYGSFNYPTQEW--DVVAHEVGHNFGATHdcDGSQYASSGCER 154
|
90 100
....*....|....*....|....*....
gi 499373916 213 yKDASYGQDTRGYSVMSYWSESNTSQnFS 241
Cdd:pfam13574 155 -NAATSVCSANGSFIMNPASKSNNDL-FS 181
|
|
| COG2931 |
COG2931 |
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ... |
235-450 |
1.11e-04 |
|
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442175 [Multi-domain] Cd Length: 252 Bit Score: 43.74 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 235 NTSQNFSKGGVEAYSSGPLMDDIAAIQKLYGANYSTRAGDTTYGFNSNTGRDFYSASSSSDKLVFSVWDGGGNDTLDFSG 314
Cdd:COG2931 37 GGGGGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGGGGGGDDTDGGGDGGDGGGGGTGDDTGDGGGGNDTLT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 315 FTQNQKINLNEASFSDVGGMVGNVSIAQGVTVENAIGGSGNDLLIGNNAANVLKGGAGNDIIYGAGGADQLWGGSGSDTF 394
Cdd:COG2931 117 GGDGNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLYGGAGNDTLYGGAGNDTLDGGAGNDTLTGGAGNDTLTGGAGNDTL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499373916 395 VFAASTDSKPGAADQIMDFVSGLDKIDLTGITKGAGLHFVNAFTGAAGDAILTTSG 450
Cdd:COG2931 197 DGGGGDDTLGGGGGDDGLDGGDGDDGLGGGGGDDTLGGGGGGDGGGGGGGDDGLGG 252
|
|
| COG2931 |
COG2931 |
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ... |
244-395 |
4.76e-04 |
|
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442175 [Multi-domain] Cd Length: 252 Bit Score: 41.82 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 244 GVEAYSSGPLMDDIAAIQKLYGANYSTRAGDTTYGFNSNTGRDFYSASSSSDKLVFSVWDGGGNDTLDFSGFTQNQKINL 323
Cdd:COG2931 1 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499373916 324 NEASFSDVGGMVGNVSIAQGVTVENAIGGSGNDLLIGNNAANVLKGGAGNDIIYGAGGADQLWGGSGSDTFV 395
Cdd:COG2931 81 GGGGDDTDGGGDGGDGGGGGTGDDTGDGGGGNDTLTGGDGNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLY 152
|
|
| Peptidase_M43 |
pfam05572 |
Pregnancy-associated plasma protein-A; Pregnancy-associated plasma protein A (PAPP-A) is a ... |
147-210 |
4.17e-03 |
|
Pregnancy-associated plasma protein-A; Pregnancy-associated plasma protein A (PAPP-A) is a metallo-protease belonging to Merops family M43. It cleaves insulin-like growth factor (IGF) binding protein-4 (IGFBP-4), causing a dramatic reduction in its affinity for IGF-I and -II. Through this mechanism, PAPP-A is a regulator of IGF bioactivity in several systems, including the human ovary and the cardiovascular system.
Pssm-ID: 368506 Cd Length: 152 Bit Score: 37.98 E-value: 4.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499373916 147 AAAFAYLPGTGAGYDGTSWYLINSSYTQNKNPDLNNygRQTLTHEIGHTLGLAH--PGDYNAGEGN 210
Cdd:pfam05572 33 NSGVAWYPDSGMSADGTARVVFNGAYLAADPTSTNF--SSTLTHEFGHFLGLIHtfEGGCERGEGD 96
|
|
| ZnMc_salivary_gland_MPs |
cd04272 |
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
183-242 |
7.19e-03 |
|
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.
Pssm-ID: 239800 Cd Length: 220 Bit Score: 38.10 E-value: 7.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499373916 183 YGRQTLTHEIGHTLGLAHPGDYNAG--EGNPSYKDASYGQdtrGYsVMSYWSESNTSQNFSK 242
Cdd:cd04272 144 YGVYTMTHELAHLLGAPHDGSPPPSwvKGHPGSLDCPWDD---GY-IMSYVVNGERQYRFSQ 201
|
|
| ZnMc_MMP_like_3 |
cd04327 |
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ... |
95-200 |
7.24e-03 |
|
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.
Pssm-ID: 239819 [Multi-domain] Cd Length: 198 Bit Score: 37.74 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 95 ISGFSQFSAQQKAQAVLAMQSWADVANVVFTEKASG-GDAHMTFgnysggQDGAAAFAYLpGTGAGYDGTSWYLINSSYT 173
Cdd:cd04327 11 IAFLGGPDAFLKDKVRAAAREWLPYANLKFKFVTDAdADIRISF------TPGDGYWSYV-GTDALLIGADAPTMNLGWF 83
|
90 100
....*....|....*....|....*..
gi 499373916 174 QNKNPDLNnyGRQTLTHEIGHTLGLAH 200
Cdd:cd04327 84 TDDTPDPE--FSRVVLHEFGHALGFIH 108
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
151-243 |
9.42e-03 |
|
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.
Pssm-ID: 239795 Cd Length: 192 Bit Score: 37.40 E-value: 9.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499373916 151 AYLPGTGAGYDgtswyliNSSYTQNKNPDLNnyGRQTLTHEIGHTLGLAHPGDYNAGEGNPSykdasygqdtRGYSVMSY 230
Cdd:cd04267 109 AYVGSMCNPYS-------SVGVVEDTGFTLL--TALTMAHELGHNLGAEHDGGDELAFECDG----------GGNYIMAP 169
|
90
....*....|...
gi 499373916 231 WSESNTSQNFSKG 243
Cdd:cd04267 170 VDSGLNSYRFSQC 182
|
|
| |
