|
Name |
Accession |
Description |
Interval |
E-value |
| Zn_serralysin |
NF035945 |
serralysin family metalloprotease; |
21-482 |
0e+00 |
|
serralysin family metalloprotease;
Pssm-ID: 468274 [Multi-domain] Cd Length: 457 Bit Score: 719.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 21 KANELQTQLQAYVPGKDPNIVVEhePS---KNAAKELIRGDYRWGHQGDdKSETFQLTYSFLESEPDNMPWHITGFSAFN 97
Cdd:NF035945 2 GYDDVNDLLHYHDRGNGLTINGK--PSytvDQAGDQITRGDATWNGKNV-FGKPANLTYSFLTSAPSSNPNGDTGFSAFN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 98 EEQRTAAKLSIQSWTDVANINFTETTDSDKAHITFGFFDASltgSYAFAYLPSPESKQSGTWYNLKSRTFSENDIGVNGY 177
Cdd:NF035945 79 AEQKAQAKLSLQSWSDVANITFTEVSAGQKANITFGNYSDS---GQAYAYLPGTSDVSGQSWYNYNSDYIRNLTPDLGNY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 178 GRQTFTHEIGHTLGLEHPAAYNASDKeRPTYKkSATYFEDSRAYTVMSYFGEKNTGQDFKGIYSSAPLLNDISAIQEVYG 257
Cdd:NF035945 156 GRQTLTHEIGHTLGLSHPGDYNAGEG-NPTYK-DATYAEDTRQYSVMSYWSESNTGQDFKGHYASAPLLDDIAAIQKLYG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 258 ANNTTRTDDTVYGFNSNTDRDFFTAKDENSKLLFTAWDAGGNDTFDFSGFTQDQRINLNEASFSDVGGLKGNVSIARGVT 337
Cdd:NF035945 234 ANMTTRTGDTVYGFNSNTDRDFYTATDSSDKLIFSVWDAGGNDTFDFSGYSQNQRINLNEGSFSDVGGLKGNVSIAAGVT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 338 IENAIGGSGNDILIGNDADNTLKGGAGDDIIYGGLGADQLWGGEGKDTFVYLSAKESPPLERDWIHDFVSGEDKIDVSLF 417
Cdd:NF035945 314 IENAIGGSGNDVLVGNDADNILKGGAGNDVIYGGGGADQLWGGAGKDIFVYGAVSDSTPSAPDWIMDFVSGIDKIDLSAF 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2447988261 418 DLGEAGKGGVKFVREFTGAVGEAVLRYDTVNKVNDFAINLGDKFSYdDFWVKIVGEPILESDFIL 482
Cdd:NF035945 394 NQGDGGGGFLHFVDAFSGKAGEALLSYDAQSNLSDLALNLGGHANP-DFLVKIVGQANQATDFIV 457
|
|
| Peptidase_M10_C |
pfam08548 |
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix ... |
258-481 |
3.13e-135 |
|
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: 389.04 E-value: 3.13e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 258 ANNTTRTDDTVYGFNSNTDRDFFTAKDENSKLLFTAWDAGGNDTFDFSGFTQDQRINLNEASFSDVGGLKGNVSIARGVT 337
Cdd:pfam08548 1 ANLTTRTGDTVYGFNSNTGRDFYTATDASSKLIFSVWDAGGNDTFDFSGYSQNQRINLNEGSFSDVGGLKGNVSIAHGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 338 IENAIGGSGNDILIGNDADNTLKGGAGDDIIYGGLGADQLWGGEGKDTFVYLSAKESPPLERDWIHDFVSGEDKIDVSLF 417
Cdd:pfam08548 81 IENAIGGSGNDVLIGNDADNILKGGAGNDILYGGGGADQLWGGAGNDIFVYASAKDSLTAAPDTIRDFVSGIDKIDLSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2447988261 418 DLGEAgkgGVKFVREFTGAVGEAVLRYDTVNKVNDFAINLGDKFSYDDFWVKIVGEPILESDFI 481
Cdd:pfam08548 161 NNNSD---GLQFVDRFSGKAGEALLRYNEVSNITNLAIDFSGQLSNNDFLVKIVGQALQTADFI 221
|
|
| ZnMc_serralysin_like |
cd04277 |
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ... |
73-257 |
5.91e-48 |
|
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: 163.36 E-value: 5.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 73 QLTYSFLESEPDNMPWH-----ITGFSAFNEEQRTAAKLSIQSWTDVANINFTETTDSDKAHITFGFFDASLTGSYAFAY 147
Cdd:cd04277 3 TLTYSFSNTGGPYSYGYgreedTTNTAALSAAQQAAARDALEAWEDVADIDFVEVSDNSGADIRFGNSSDPDGNTAGYAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 148 LPSPESKQSG---TWYNlksRTFSENDIGVNGYGRQTFTHEIGHTLGLEHPAAYNASDKERPTYKksatyfEDSRAYTVM 224
Cdd:cd04277 83 YPGSGSGTAYggdIWFN---SSYDTNSDSPGSYGYQTIIHEIGHALGLEHPGDYNGGDPVPPTYA------LDSREYTVM 153
|
170 180 190
....*....|....*....|....*....|...
gi 2447988261 225 SYFGEKNTGQDFKGIYSSAPLLNDISAIQEVYG 257
Cdd:cd04277 154 SYNSGYGNGASAGGGYPQTPMLLDIAALQYLYG 186
|
|
| ZnMc |
smart00235 |
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ... |
72-203 |
5.58e-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: 71.61 E-value: 5.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 72 FQLTYSFLESEpdnmpwhitgfsaFNEEQRTAAKLSIQSWTDVANINFTETTDSDKAHITFGffDASLTGSYAFAYLPSP 151
Cdd:smart00235 8 GTVPYVIDSSS-------------LSPEEREAIAKALAEWSDVTCIRFVERTGTADIYISFG--SGDSGCTLSHAGRPGG 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2447988261 152 ESKQS-GTWYnlksrtfsendigvngYGRQTFTHEIGHTLGLEHPAAYNASDK 203
Cdd:smart00235 73 DQHLSlGNGC----------------INTGVAAHELGHALGLYHEQSRSDRDN 109
|
|
| COG2931 |
COG2931 |
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ... |
247-387 |
1.00e-07 |
|
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442175 [Multi-domain] Cd Length: 252 Bit Score: 52.99 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 247 NDISAIQEVYGANNTTRTDDTVYGFNSNTDRDFFTAKDENSKLLFTAWDAGGNDTFDFSGFTQDQRINLNEASFSDVGGL 326
Cdd:COG2931 40 GGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGGGGGGDDTDGGGDGGDGGGGGTGDDTGDGGGGNDTLTGGD 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2447988261 327 kGNVSIARGVTIENAIGGSGNDILIGNDADNTLKGGAGDDIIYGGLGADQLWGGEGKDTFV 387
Cdd:COG2931 120 -GNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLYGGAGNDTLYGGAGNDTLDGGAGNDTLT 179
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Zn_serralysin |
NF035945 |
serralysin family metalloprotease; |
21-482 |
0e+00 |
|
serralysin family metalloprotease;
Pssm-ID: 468274 [Multi-domain] Cd Length: 457 Bit Score: 719.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 21 KANELQTQLQAYVPGKDPNIVVEhePS---KNAAKELIRGDYRWGHQGDdKSETFQLTYSFLESEPDNMPWHITGFSAFN 97
Cdd:NF035945 2 GYDDVNDLLHYHDRGNGLTINGK--PSytvDQAGDQITRGDATWNGKNV-FGKPANLTYSFLTSAPSSNPNGDTGFSAFN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 98 EEQRTAAKLSIQSWTDVANINFTETTDSDKAHITFGFFDASltgSYAFAYLPSPESKQSGTWYNLKSRTFSENDIGVNGY 177
Cdd:NF035945 79 AEQKAQAKLSLQSWSDVANITFTEVSAGQKANITFGNYSDS---GQAYAYLPGTSDVSGQSWYNYNSDYIRNLTPDLGNY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 178 GRQTFTHEIGHTLGLEHPAAYNASDKeRPTYKkSATYFEDSRAYTVMSYFGEKNTGQDFKGIYSSAPLLNDISAIQEVYG 257
Cdd:NF035945 156 GRQTLTHEIGHTLGLSHPGDYNAGEG-NPTYK-DATYAEDTRQYSVMSYWSESNTGQDFKGHYASAPLLDDIAAIQKLYG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 258 ANNTTRTDDTVYGFNSNTDRDFFTAKDENSKLLFTAWDAGGNDTFDFSGFTQDQRINLNEASFSDVGGLKGNVSIARGVT 337
Cdd:NF035945 234 ANMTTRTGDTVYGFNSNTDRDFYTATDSSDKLIFSVWDAGGNDTFDFSGYSQNQRINLNEGSFSDVGGLKGNVSIAAGVT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 338 IENAIGGSGNDILIGNDADNTLKGGAGDDIIYGGLGADQLWGGEGKDTFVYLSAKESPPLERDWIHDFVSGEDKIDVSLF 417
Cdd:NF035945 314 IENAIGGSGNDVLVGNDADNILKGGAGNDVIYGGGGADQLWGGAGKDIFVYGAVSDSTPSAPDWIMDFVSGIDKIDLSAF 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2447988261 418 DLGEAGKGGVKFVREFTGAVGEAVLRYDTVNKVNDFAINLGDKFSYdDFWVKIVGEPILESDFIL 482
Cdd:NF035945 394 NQGDGGGGFLHFVDAFSGKAGEALLSYDAQSNLSDLALNLGGHANP-DFLVKIVGQANQATDFIV 457
|
|
| Peptidase_M10_C |
pfam08548 |
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix ... |
258-481 |
3.13e-135 |
|
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: 389.04 E-value: 3.13e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 258 ANNTTRTDDTVYGFNSNTDRDFFTAKDENSKLLFTAWDAGGNDTFDFSGFTQDQRINLNEASFSDVGGLKGNVSIARGVT 337
Cdd:pfam08548 1 ANLTTRTGDTVYGFNSNTGRDFYTATDASSKLIFSVWDAGGNDTFDFSGYSQNQRINLNEGSFSDVGGLKGNVSIAHGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 338 IENAIGGSGNDILIGNDADNTLKGGAGDDIIYGGLGADQLWGGEGKDTFVYLSAKESPPLERDWIHDFVSGEDKIDVSLF 417
Cdd:pfam08548 81 IENAIGGSGNDVLIGNDADNILKGGAGNDILYGGGGADQLWGGAGNDIFVYASAKDSLTAAPDTIRDFVSGIDKIDLSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2447988261 418 DLGEAgkgGVKFVREFTGAVGEAVLRYDTVNKVNDFAINLGDKFSYDDFWVKIVGEPILESDFI 481
Cdd:pfam08548 161 NNNSD---GLQFVDRFSGKAGEALLRYNEVSNITNLAIDFSGQLSNNDFLVKIVGQALQTADFI 221
|
|
| ZnMc_serralysin_like |
cd04277 |
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ... |
73-257 |
5.91e-48 |
|
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: 163.36 E-value: 5.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 73 QLTYSFLESEPDNMPWH-----ITGFSAFNEEQRTAAKLSIQSWTDVANINFTETTDSDKAHITFGFFDASLTGSYAFAY 147
Cdd:cd04277 3 TLTYSFSNTGGPYSYGYgreedTTNTAALSAAQQAAARDALEAWEDVADIDFVEVSDNSGADIRFGNSSDPDGNTAGYAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 148 LPSPESKQSG---TWYNlksRTFSENDIGVNGYGRQTFTHEIGHTLGLEHPAAYNASDKERPTYKksatyfEDSRAYTVM 224
Cdd:cd04277 83 YPGSGSGTAYggdIWFN---SSYDTNSDSPGSYGYQTIIHEIGHALGLEHPGDYNGGDPVPPTYA------LDSREYTVM 153
|
170 180 190
....*....|....*....|....*....|...
gi 2447988261 225 SYFGEKNTGQDFKGIYSSAPLLNDISAIQEVYG 257
Cdd:cd04277 154 SYNSGYGNGASAGGGYPQTPMLLDIAALQYLYG 186
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
88-256 |
7.24e-20 |
|
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: 86.42 E-value: 7.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 88 WHITGFSAFNEEQRTAAKLSIQSWTDVANINFTETT-DSDKAHITFGFFDASLTGSY-AFAYLPS-PESKQSGTWYNLKS 164
Cdd:cd00203 11 DRDVEEENLSAQIQSLILIAMQIWRDYLNIRFVLVGvEIDKADIAILVTRQDFDGGTgGWAYLGRvCDSLRGVGVLQDNQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 165 RTfsendigvNGYGRQTFTHEIGHTLGLEHPAAYNASDKErPTYkKSATYFEDSRAYTVMSYFGEKntgqdFKGIYSSAP 244
Cdd:cd00203 91 SG--------TKEGAQTIAHELGHALGFYHDHDRKDRDDY-PTI-DDTLNAEDDDYYSVMSYTKGS-----FSDGQRKDF 155
|
170
....*....|..
gi 2447988261 245 LLNDISAIQEVY 256
Cdd:cd00203 156 SQCDIDQINKLY 167
|
|
| ZnMc_MMP_like |
cd04268 |
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ... |
94-256 |
4.98e-19 |
|
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: 84.09 E-value: 4.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 94 SAFNEEQRTAAKLSIQSWTDVANINFTETTDSDKAHITFGFFDASLTGSYAFAYLPSPESKQSGTWYnLKSRTFSENDIG 173
Cdd:cd04268 10 DSVPDKLRAAILDAIEAWNKAFAIGFKNANDVDPADIRYSVIRWIPYNDGTWSYGPSQVDPLTGEIL-LARVYLYSSFVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 174 VNG-YGRQTFTHEIGHTLGLEHPAAYNASDKErptykkSATYFEDSRAYTVMSYFGEKNTGQdFKGIYSSAPLLNDISAI 252
Cdd:cd04268 89 YSGaRLRNTAEHELGHALGLRHNFAASDRDDN------VDLLAEKGDTSSVMDYAPSNFSIQ-LGDGQKYTIGPYDIAAI 161
|
....
gi 2447988261 253 QEVY 256
Cdd:cd04268 162 KKLY 165
|
|
| ZnMc |
smart00235 |
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ... |
72-203 |
5.58e-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: 71.61 E-value: 5.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 72 FQLTYSFLESEpdnmpwhitgfsaFNEEQRTAAKLSIQSWTDVANINFTETTDSDKAHITFGffDASLTGSYAFAYLPSP 151
Cdd:smart00235 8 GTVPYVIDSSS-------------LSPEEREAIAKALAEWSDVTCIRFVERTGTADIYISFG--SGDSGCTLSHAGRPGG 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2447988261 152 ESKQS-GTWYnlksrtfsendigvngYGRQTFTHEIGHTLGLEHPAAYNASDK 203
Cdd:smart00235 73 DQHLSlGNGC----------------INTGVAAHELGHALGLYHEQSRSDRDN 109
|
|
| ZnMc_MMP |
cd04278 |
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ... |
68-216 |
2.60e-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: 64.53 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 68 KSETFQLTYSFLeSEPDNMPWhitgfsafnEEQRTAAKLSIQSWTDVANINFTETTDSDKAHITFGF----------FDA 137
Cdd:cd04278 1 KWSKTNLTYRIL-NYPPDLPR---------DDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFargnhgdgypFDG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 138 SlTGSYAFAYLPSPEskqSG--------TWynlksrTFSENDIGVNGYgrQTFTHEIGHTLGLEHpaaynASDKE---RP 206
Cdd:cd04278 71 P-GGTLAHAFFPGGI---GGdihfdddeQW------TLGSDSGGTDLF--SVAAHEIGHALGLGH-----SSDPDsimYP 133
|
170
....*....|
gi 2447988261 207 TYKKSATYFE 216
Cdd:cd04278 134 YYQGPVPKFK 143
|
|
| HemolysinCabind |
pfam00353 |
RTX calcium-binding nonapeptide repeat (4 copies); |
342-377 |
2.43e-08 |
|
RTX calcium-binding nonapeptide repeat (4 copies);
Pssm-ID: 459777 [Multi-domain] Cd Length: 36 Bit Score: 49.74 E-value: 2.43e-08
10 20 30
....*....|....*....|....*....|....*.
gi 2447988261 342 IGGSGNDILIGNDADNTLKGGAGDDIIYGGLGADQL 377
Cdd:pfam00353 1 YGGDGNDTLVGGAGNDTIYGGAGNDTLDGGAGNDTL 36
|
|
| COG2931 |
COG2931 |
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ... |
247-387 |
1.00e-07 |
|
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442175 [Multi-domain] Cd Length: 252 Bit Score: 52.99 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 247 NDISAIQEVYGANNTTRTDDTVYGFNSNTDRDFFTAKDENSKLLFTAWDAGGNDTFDFSGFTQDQRINLNEASFSDVGGL 326
Cdd:COG2931 40 GGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGGGGGGDDTDGGGDGGDGGGGGTGDDTGDGGGGNDTLTGGD 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2447988261 327 kGNVSIARGVTIENAIGGSGNDILIGNDADNTLKGGAGDDIIYGGLGADQLWGGEGKDTFV 387
Cdd:COG2931 120 -GNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLYGGAGNDTLYGGAGNDTLDGGAGNDTLT 179
|
|
| HemolysinCabind |
pfam00353 |
RTX calcium-binding nonapeptide repeat (4 copies); |
351-386 |
1.44e-07 |
|
RTX calcium-binding nonapeptide repeat (4 copies);
Pssm-ID: 459777 [Multi-domain] Cd Length: 36 Bit Score: 47.43 E-value: 1.44e-07
10 20 30
....*....|....*....|....*....|....*.
gi 2447988261 351 IGNDADNTLKGGAGDDIIYGGLGADQLWGGEGKDTF 386
Cdd:pfam00353 1 YGGDGNDTLVGGAGNDTIYGGAGNDTLDGGAGNDTL 36
|
|
| COG2931 |
COG2931 |
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ... |
247-387 |
1.95e-07 |
|
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442175 [Multi-domain] Cd Length: 252 Bit Score: 52.22 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 247 NDISAIQEVYGANNTTRTDDTVYGFNSNTDRDFFTAKDENSKLLFTAWDAGGNDTFDFSGFTQDQRINLNEASFSDVGGL 326
Cdd:COG2931 21 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGGGGGGDDTDGGGDGGDGGGGG 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2447988261 327 KGNVSIARGVTIENAIGGSGNDILIGNDADNTLKGGAGDDIIYGGLGADQLWGGEGKDTFV 387
Cdd:COG2931 101 TGDDTGDGGGGNDTLTGGDGNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLYGGAGNDTLY 161
|
|
| Peptidase_M10 |
pfam00413 |
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ... |
74-257 |
2.77e-07 |
|
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: 50.31 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 74 LTYSFLESEPDnMPWhitgfsafnEEQRTAAKLSIQSWTDVANINFTEtTDSDKAHITFGFFDASLTGSYAF-------- 145
Cdd:pfam00413 7 LTYRILNYTPD-LPR---------AEVRRAIRRAFKVWSEVTPLTFTE-VSTGEADIMIGFGRGDHGDGYPFdgpggvla 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 146 -AYLPSPEskQSG--------TWyNLKSRTFSENDIgvngygRQTFTHEIGHTLGLEHpaaynaSDKER----PTYkksa 212
Cdd:pfam00413 76 hAFFPGPG--LGGdihfdddeTW-TVGSDPPHGINL------FLVAAHEIGHALGLGH------SSDPGaimyPTY---- 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2447988261 213 tyfedsraytvmSYFGEKNTG--QDfkgiyssapllnDISAIQEVYG 257
Cdd:pfam00413 137 ------------SPLDSKKFRlsQD------------DIKGIQQLYG 159
|
|
| COG2931 |
COG2931 |
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ... |
238-387 |
1.57e-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: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 238 GIYSSAPLLNDISAIQEVYGANNTTRTDDTVYGFNSNTDRDFFTAKDENSKLLFTAWDAGGNDTFDFSGFTQDQRINLNE 317
Cdd:COG2931 3 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGGGG 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 318 ASFSDVGGLKGNVSIARGVTIENAIGGSGNDILIGNDADNTLKGGAGDDIIYGGLGADQLWGGEGKDTFV 387
Cdd:COG2931 83 GGDDTDGGGDGGDGGGGGTGDDTGDGGGGNDTLTGGDGNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLY 152
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
156-226 |
3.85e-05 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 44.33 E-value: 3.85e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2447988261 156 SGTWYNLKSRTFSENDIGVNGYGRQTFTHEIGHTLGLEHPAAYNASDKERPTYkksaTYFEDSRAYTVMSY 226
Cdd:pfam13688 115 SGSAGSVSTRVSGNNVVVSTATEWQVFAHEIGHNFGAVHDCDSSTSSQCCPPS----NSTCPAGGRYIMNP 181
|
|
| Reprolysin_4 |
pfam13583 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
78-229 |
4.47e-03 |
|
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: 404471 Cd Length: 203 Bit Score: 38.37 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 78 FLESEPDNMPWHITGFSAFNEEQRTaaklsIQSWTDvaninfteTTDSDKAHITFGFFDASLTGSYAFAYLPSPESKQsg 157
Cdd:pfam13583 58 YTDSSTDSFNADCSGGDLGNWRLAT-----LTSWRD--------SLNYDLAYLTLMTGPSGQNVGVAWVGALCSSARQ-- 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2447988261 158 twyNLKSRTFSENdigvnGYGRQTFTHEIGHTLGLEHPAAYNAsdkERPTYKksatyFEDSRAYTVMSYFGE 229
Cdd:pfam13583 123 ---NAKASGVARS-----RDEWDIFAHEIGHTFGAVHDCSSQG---EGLSSS-----TEDGSGQTIMSYAST 178
|
|
| ZnMc_MMP_like_1 |
cd04279 |
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ... |
83-194 |
5.77e-03 |
|
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: 37.44 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447988261 83 PDNMPWHITGFSAFNEE----QRTAAKLSIQSWTDVANINFTETTDSDK-AHITFGFFDASLTG-------SYAFAYLPS 150
Cdd:cd04279 1 KSPIRVYIDPTPAPPDSraqsWLQAVKQAAAEWENVGPLKFVYNPEEDNdADIVIFFDRPPPVGgaggglaRAGFPLISD 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2447988261 151 PESKQSGTWYNLKSRTFSENDIGVngygRQTFTHEIGHTLGLEH 194
Cdd:cd04279 81 GNRKLFNRTDINLGPGQPRGAENL----QAIALHELGHALGLWH 120
|
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