|
Name |
Accession |
Description |
Interval |
E-value |
| Zn_serralysin |
NF035945 |
serralysin family metalloprotease; |
42-438 |
1.29e-148 |
|
serralysin family metalloprotease;
Pssm-ID: 468274 [Multi-domain] Cd Length: 457 Bit Score: 430.55 E-value: 1.29e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 42 QSWKENTIHNKNTNLTYSFSRaytlWDYDRTFQQNAYISLFNPAQIHQAKIAMQSWADVANISFTEASADSSANILFLNF 121
Cdd:NF035945 41 ATWNGKNVFGKPANLTYSFLT----SAPSSNPNGDTGFSAFNAEQKAQAKLSLQSWSDVANITFTEVSAGQKANITFGNY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 122 QRpsNVAGYAYYPNPGSFS-PIW--INYSFSDNQHPSRLNDGGGVLTHEIGHALGLGH------SHAPHGY--------T 184
Cdd:NF035945 117 SD--SGQAYAYLPGTSDVSgQSWynYNSDYIRNLTPDLGNYGRQTLTHEIGHTLGLSHpgdynaGEGNPTYkdatyaedT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 185 QQMSVMSYLSEQGSGANYGQHYLSTPQMYDIAAIQYLYGANLHTRTGDTVYGFNSTSYRDHFTATHASDALIFCVWDAGG 264
Cdd:NF035945 195 RQYSVMSYWSESNTGQDFKGHYASAPLLDDIAAIQKLYGANMTTRTGDTVYGFNSNTDRDFYTATDSSDKLIFSVWDAGG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 265 NDTFDFSGYKQNQMINLNELCFSDVGGLKGNVSIAADVTIENAIGGSGHDDIIGNHTNNILTGN---------GGSDQLW 335
Cdd:NF035945 275 NDTFDFSGYSQNQRINLNEGSFSDVGGLKGNVSIAAGVTIENAIGGSGNDVLVGNDADNILKGGagndviyggGGADQLW 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 336 GNGGNNTFRYASARDSMTTSPDTIHDFKSGRDKIDLS---QLMPSTDRVIFVDrlSFNGQT-EMGQQYNEVADITYLMID 411
Cdd:NF035945 355 GGAGKDIFVYGAVSDSTPSAPDWIMDFVSGIDKIDLSafnQGDGGGGFLHFVD--AFSGKAgEALLSYDAQSNLSDLALN 432
|
410 420
....*....|....*....|....*..
gi 488138322 412 FDAQVSEcDMMIKFTGRhHFTANDFIL 438
Cdd:NF035945 433 LGGHANP-DFLVKIVGQ-ANQATDFIV 457
|
|
| Peptidase_M10_C |
pfam08548 |
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix ... |
224-437 |
3.30e-130 |
|
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: 374.79 E-value: 3.30e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 224 ANLHTRTGDTVYGFNSTSYRDHFTATHASDALIFCVWDAGGNDTFDFSGYKQNQMINLNELCFSDVGGLKGNVSIAADVT 303
Cdd:pfam08548 1 ANLTTRTGDTVYGFNSNTGRDFYTATDASSKLIFSVWDAGGNDTFDFSGYSQNQRINLNEGSFSDVGGLKGNVSIAHGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 304 IENAIGGSGHDDIIGNHTNN---------ILTGNGGSDQLWGNGGNNTFRYASARDSMTTSPDTIHDFKSGRDKIDLSQL 374
Cdd:pfam08548 81 IENAIGGSGNDVLIGNDADNilkggagndILYGGGGADQLWGGAGNDIFVYASAKDSLTAAPDTIRDFVSGIDKIDLSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488138322 375 MPSTDRVIFVDRLSfNGQTEMGQQYNEVADITYLMIDFDAQVSECDMMIKFTGRHHFTANDFI 437
Cdd:pfam08548 161 NNNSDGLQFVDRFS-GKAGEALLRYNEVSNITNLAIDFSGQLSNNDFLVKIVGQALQTADFIV 222
|
|
| ZnMc_serralysin_like |
cd04277 |
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ... |
53-223 |
7.78e-50 |
|
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: 167.59 E-value: 7.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 53 NTNLTYSFSRAYTLWDYDRTF-QQNAYISLFNPAQIHQAKIAMQSWADVANISFTEASADSSANILFLNFQRP-SNVAGY 130
Cdd:cd04277 1 DTTLTYSFSNTGGPYSYGYGReEDTTNTAALSAAQQAAARDALEAWEDVADIDFVEVSDNSGADIRFGNSSDPdGNTAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 131 AYYPNPGSFSP----IWINYSFSDNQHpSRLNDGGGVLTHEIGHALGLGHSHAPHGY----------TQQMSVMSYLSEQ 196
Cdd:cd04277 81 AYYPGSGSGTAyggdIWFNSSYDTNSD-SPGSYGYQTIIHEIGHALGLEHPGDYNGGdpvpptyaldSREYTVMSYNSGY 159
|
170 180
....*....|....*....|....*..
gi 488138322 197 GSGANYGQHYLSTPQMYDIAAIQYLYG 223
Cdd:cd04277 160 GNGASAGGGYPQTPMLLDIAALQYLYG 186
|
|
| ZnMc |
smart00235 |
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ... |
80-224 |
3.65e-13 |
|
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: 66.61 E-value: 3.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 80 SLFNPAQIHQAKIAMQSWADVANISFTEASADSSANILFLNFQRpSNVAGYAYYPNPGsfspIWINYSFSDnqhpsrlnD 159
Cdd:smart00235 17 SSLSPEEREAIAKALAEWSDVTCIRFVERTGTADIYISFGSGDS-GCTLSHAGRPGGD----QHLSLGNGC--------I 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488138322 160 GGGVLTHEIGHALGLGHSHAPHGYTQQMSVMSylseqgsgANYGQHYLSTPQmYDIAAIQYLYGA 224
Cdd:smart00235 84 NTGVAAHELGHALGLYHEQSRSDRDNYMYINY--------TNIDTRNFDLSE-DDSLGIPYDYGS 139
|
|
| COG2931 |
COG2931 |
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ... |
213-353 |
2.89e-03 |
|
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442175 [Multi-domain] Cd Length: 252 Bit Score: 39.12 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 213 YDIAAIQYLYGANLHTRTGDTVYGFNSTSYRDHFTATHASDALIFCVWDAGGNDTFDFSGYKQNQMINLNELcFSDVGGL 292
Cdd:COG2931 40 GGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGGGGGGDDTDGGGDGGDGGGGGTGDDTGDGGGG-NDTLTGG 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488138322 293 KGNVSIAADVTIENAIGGSGHDDIIGNHTNNILTGNGGSDQLWGNGGNNTFRYASARDSMT 353
Cdd:COG2931 119 DGNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLYGGAGNDTLYGGAGNDTLDGGAGNDTLT 179
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Zn_serralysin |
NF035945 |
serralysin family metalloprotease; |
42-438 |
1.29e-148 |
|
serralysin family metalloprotease;
Pssm-ID: 468274 [Multi-domain] Cd Length: 457 Bit Score: 430.55 E-value: 1.29e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 42 QSWKENTIHNKNTNLTYSFSRaytlWDYDRTFQQNAYISLFNPAQIHQAKIAMQSWADVANISFTEASADSSANILFLNF 121
Cdd:NF035945 41 ATWNGKNVFGKPANLTYSFLT----SAPSSNPNGDTGFSAFNAEQKAQAKLSLQSWSDVANITFTEVSAGQKANITFGNY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 122 QRpsNVAGYAYYPNPGSFS-PIW--INYSFSDNQHPSRLNDGGGVLTHEIGHALGLGH------SHAPHGY--------T 184
Cdd:NF035945 117 SD--SGQAYAYLPGTSDVSgQSWynYNSDYIRNLTPDLGNYGRQTLTHEIGHTLGLSHpgdynaGEGNPTYkdatyaedT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 185 QQMSVMSYLSEQGSGANYGQHYLSTPQMYDIAAIQYLYGANLHTRTGDTVYGFNSTSYRDHFTATHASDALIFCVWDAGG 264
Cdd:NF035945 195 RQYSVMSYWSESNTGQDFKGHYASAPLLDDIAAIQKLYGANMTTRTGDTVYGFNSNTDRDFYTATDSSDKLIFSVWDAGG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 265 NDTFDFSGYKQNQMINLNELCFSDVGGLKGNVSIAADVTIENAIGGSGHDDIIGNHTNNILTGN---------GGSDQLW 335
Cdd:NF035945 275 NDTFDFSGYSQNQRINLNEGSFSDVGGLKGNVSIAAGVTIENAIGGSGNDVLVGNDADNILKGGagndviyggGGADQLW 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 336 GNGGNNTFRYASARDSMTTSPDTIHDFKSGRDKIDLS---QLMPSTDRVIFVDrlSFNGQT-EMGQQYNEVADITYLMID 411
Cdd:NF035945 355 GGAGKDIFVYGAVSDSTPSAPDWIMDFVSGIDKIDLSafnQGDGGGGFLHFVD--AFSGKAgEALLSYDAQSNLSDLALN 432
|
410 420
....*....|....*....|....*..
gi 488138322 412 FDAQVSEcDMMIKFTGRhHFTANDFIL 438
Cdd:NF035945 433 LGGHANP-DFLVKIVGQ-ANQATDFIV 457
|
|
| Peptidase_M10_C |
pfam08548 |
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix ... |
224-437 |
3.30e-130 |
|
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: 374.79 E-value: 3.30e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 224 ANLHTRTGDTVYGFNSTSYRDHFTATHASDALIFCVWDAGGNDTFDFSGYKQNQMINLNELCFSDVGGLKGNVSIAADVT 303
Cdd:pfam08548 1 ANLTTRTGDTVYGFNSNTGRDFYTATDASSKLIFSVWDAGGNDTFDFSGYSQNQRINLNEGSFSDVGGLKGNVSIAHGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 304 IENAIGGSGHDDIIGNHTNN---------ILTGNGGSDQLWGNGGNNTFRYASARDSMTTSPDTIHDFKSGRDKIDLSQL 374
Cdd:pfam08548 81 IENAIGGSGNDVLIGNDADNilkggagndILYGGGGADQLWGGAGNDIFVYASAKDSLTAAPDTIRDFVSGIDKIDLSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488138322 375 MPSTDRVIFVDRLSfNGQTEMGQQYNEVADITYLMIDFDAQVSECDMMIKFTGRHHFTANDFI 437
Cdd:pfam08548 161 NNNSDGLQFVDRFS-GKAGEALLRYNEVSNITNLAIDFSGQLSNNDFLVKIVGQALQTADFIV 222
|
|
| ZnMc_serralysin_like |
cd04277 |
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ... |
53-223 |
7.78e-50 |
|
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: 167.59 E-value: 7.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 53 NTNLTYSFSRAYTLWDYDRTF-QQNAYISLFNPAQIHQAKIAMQSWADVANISFTEASADSSANILFLNFQRP-SNVAGY 130
Cdd:cd04277 1 DTTLTYSFSNTGGPYSYGYGReEDTTNTAALSAAQQAAARDALEAWEDVADIDFVEVSDNSGADIRFGNSSDPdGNTAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 131 AYYPNPGSFSP----IWINYSFSDNQHpSRLNDGGGVLTHEIGHALGLGHSHAPHGY----------TQQMSVMSYLSEQ 196
Cdd:cd04277 81 AYYPGSGSGTAyggdIWFNSSYDTNSD-SPGSYGYQTIIHEIGHALGLEHPGDYNGGdpvpptyaldSREYTVMSYNSGY 159
|
170 180
....*....|....*....|....*..
gi 488138322 197 GSGANYGQHYLSTPQMYDIAAIQYLYG 223
Cdd:cd04277 160 GNGASAGGGYPQTPMLLDIAALQYLYG 186
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
64-222 |
3.80e-14 |
|
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: 70.24 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 64 YTLWDYDRTFQQNAYislfnPAQIH-QAKIAMQSWADVANISFTEASAD-SSANILFLNFQ--RPSNVAGYAYYPN--PG 137
Cdd:cd00203 5 YVVVADDRDVEEENL-----SAQIQsLILIAMQIWRDYLNIRFVLVGVEiDKADIAILVTRqdFDGGTGGWAYLGRvcDS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 138 SFSPIWINysfsdnQHPSRLNDGGGVLTHEIGHALGLGHSH--------------APHGYTQQMSVMSYLSEQGSGAnYG 203
Cdd:cd00203 80 LRGVGVLQ------DNQSGTKEGAQTIAHELGHALGFYHDHdrkdrddyptiddtLNAEDDDYYSVMSYTKGSFSDG-QR 152
|
170
....*....|....*....
gi 488138322 204 QHYLStpqmYDIAAIQYLY 222
Cdd:cd00203 153 KDFSQ----CDIDQINKLY 167
|
|
| ZnMc_MMP_like |
cd04268 |
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ... |
78-222 |
4.00e-14 |
|
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: 69.83 E-value: 4.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 78 YISLFNPAQIHQA-KIAMQSWADVANISFTEASADSSANILFLNFQR-PSNVAGYAYYP---NPGSFsPIWINYSFSDNQ 152
Cdd:cd04268 7 YIDDSVPDKLRAAiLDAIEAWNKAFAIGFKNANDVDPADIRYSVIRWiPYNDGTWSYGPsqvDPLTG-EILLARVYLYSS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 153 HPSRLNDGG-GVLTHEIGHALGLGHSHA----------PHGYTQQMSVMSYLSEQGSgANYGQHYLSTPQMYDIAAIQYL 221
Cdd:cd04268 86 FVEYSGARLrNTAEHELGHALGLRHNFAasdrddnvdlLAEKGDTSSVMDYAPSNFS-IQLGDGQKYTIGPYDIAAIKKL 164
|
.
gi 488138322 222 Y 222
Cdd:cd04268 165 Y 165
|
|
| ZnMc_MMP |
cd04278 |
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ... |
54-223 |
5.33e-14 |
|
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: 69.16 E-value: 5.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 54 TNLTY---SFSRAYTLWDYDRTFQQnayislfnpaqihqakiAMQSWADVANISFTEASADSSANILFlNFQR------- 123
Cdd:cd04278 5 TNLTYrilNYPPDLPRDDVRRAIAR-----------------AFRVWSDVTPLTFREVTSGQEADIRI-SFARgnhgdgy 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 124 ----PSNVAGYAYYPNP--GSFSpiwinysFSDNQHPSRLNDGGG-----VLTHEIGHALGLGHSHAPHgytqqmSVMsY 192
Cdd:cd04278 67 pfdgPGGTLAHAFFPGGigGDIH-------FDDDEQWTLGSDSGGtdlfsVAAHEIGHALGLGHSSDPD------SIM-Y 132
|
170 180 190
....*....|....*....|....*....|.
gi 488138322 193 LSEQGSGANYGQHYlstpqmYDIAAIQYLYG 223
Cdd:cd04278 133 PYYQGPVPKFKLSQ------DDIRGIQALYG 157
|
|
| ZnMc |
smart00235 |
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ... |
80-224 |
3.65e-13 |
|
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: 66.61 E-value: 3.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 80 SLFNPAQIHQAKIAMQSWADVANISFTEASADSSANILFLNFQRpSNVAGYAYYPNPGsfspIWINYSFSDnqhpsrlnD 159
Cdd:smart00235 17 SSLSPEEREAIAKALAEWSDVTCIRFVERTGTADIYISFGSGDS-GCTLSHAGRPGGD----QHLSLGNGC--------I 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488138322 160 GGGVLTHEIGHALGLGHSHAPHGYTQQMSVMSylseqgsgANYGQHYLSTPQmYDIAAIQYLYGA 224
Cdd:smart00235 84 NTGVAAHELGHALGLYHEQSRSDRDNYMYINY--------TNIDTRNFDLSE-DDSLGIPYDYGS 139
|
|
| Peptidase_M10 |
pfam00413 |
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ... |
52-223 |
1.51e-12 |
|
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: 65.33 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 52 KNTNLTYSFSraytlwdydrtfqqnAYISLFNPAQIHQA-KIAMQSWADVANISFTEASaDSSANIL----------FLN 120
Cdd:pfam00413 3 RKKNLTYRIL---------------NYTPDLPRAEVRRAiRRAFKVWSEVTPLTFTEVS-TGEADIMigfgrgdhgdGYP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 121 FQRPSNVAGYAYYPNPGSFSPIwinySFSDNQHPSRLNDGGG------VLTHEIGHALGLGHSHAPHgytqqmSVM-SYL 193
Cdd:pfam00413 67 FDGPGGVLAHAFFPGPGLGGDI----HFDDDETWTVGSDPPHginlflVAAHEIGHALGLGHSSDPG------AIMyPTY 136
|
170 180 190
....*....|....*....|....*....|
gi 488138322 194 SEQGSGANygqhylsTPQMYDIAAIQYLYG 223
Cdd:pfam00413 137 SPLDSKKF-------RLSQDDIKGIQQLYG 159
|
|
| ZnMc_MMP_like_1 |
cd04279 |
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ... |
93-223 |
4.03e-09 |
|
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: 55.16 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 93 AMQSWADVANISF---TEASADSSANILFLNFQRPSNVAGY-AYYPNPGSFSPIWINYSF----SDNQHPSRLNDGGGVL 164
Cdd:cd04279 29 AAAEWENVGPLKFvynPEEDNDADIVIFFDRPPPVGGAGGGlARAGFPLISDGNRKLFNRtdinLGPGQPRGAENLQAIA 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 488138322 165 THEIGHALGLGHSHAphgytqQMSVMSYLSEqgsgaNYGQHYLSTPQMYDIAAIQYLYG 223
Cdd:cd04279 109 LHELGHALGLWHHSD------RPEDAMYPSQ-----GQGPDGNPTLSARDVATLKRLYG 156
|
|
| ZnMc_MMP_like_2 |
cd04276 |
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ... |
163-223 |
7.77e-06 |
|
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: 46.55 E-value: 7.77e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488138322 163 VLTHEIGHALGLGH-----SHAPHGYTQQM----------SVMSYLSEQGS--GANYGQHYLSTPQMYDIAAIQYLYG 223
Cdd:cd04276 119 LLAHEVGHTLGLRHnfkasSDGSNEELEDPlgtkekgatsSVMDYPPPNVAaqGEDQGDYYPPTIGPYDKWAIEYGYT 196
|
|
| HemolysinCabind |
pfam00353 |
RTX calcium-binding nonapeptide repeat (4 copies); |
308-343 |
1.60e-04 |
|
RTX calcium-binding nonapeptide repeat (4 copies);
Pssm-ID: 459777 [Multi-domain] Cd Length: 36 Bit Score: 38.96 E-value: 1.60e-04
10 20 30
....*....|....*....|....*....|....*.
gi 488138322 308 IGGSGHDDIIGNHTNNILTGNGGSDQLWGNGGNNTF 343
Cdd:pfam00353 1 YGGDGNDTLVGGAGNDTIYGGAGNDTLDGGAGNDTL 36
|
|
| ZnMc_pappalysin_like |
cd04275 |
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ... |
115-178 |
1.94e-04 |
|
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: 42.71 E-value: 1.94e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488138322 115 NILFLNFqRPSNVAGYAYYPNP-GSFSPIW----INYSF--SDNQHPsrlNDGGGVLTHEIGHALGLGHSH 178
Cdd:cd04275 89 NIYVANF-LGGGLLGYATFPDSlVSLAFITdgvvINPSSlpGGSAAP---YNLGDTATHEVGHWLGLYHTF 155
|
|
| DUF4953 |
pfam16313 |
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic ... |
163-223 |
3.81e-04 |
|
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic met-zincin mmotif HExxHxxGxxH, the extended zinc-binding domain of metallopeptidases.
Pssm-ID: 435269 Cd Length: 319 Bit Score: 42.24 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 163 VLTHEIGHALGLGH----SHA-PH------GYTQQM----SVMSYL--------SEQGSGANygqhyLSTPQM--YDIAA 217
Cdd:pfam16313 16 VSAHEVGHTLGLRHnfaaSSAyPVdslrdkSFTRKYgttpSIMDYArfnyvaqpEDQIDLSG-----LYPPGIgpYDKWA 90
|
....*.
gi 488138322 218 IQYLYG 223
Cdd:pfam16313 91 IEWGYR 96
|
|
| COG2931 |
COG2931 |
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ... |
213-353 |
2.89e-03 |
|
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442175 [Multi-domain] Cd Length: 252 Bit Score: 39.12 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 213 YDIAAIQYLYGANLHTRTGDTVYGFNSTSYRDHFTATHASDALIFCVWDAGGNDTFDFSGYKQNQMINLNELcFSDVGGL 292
Cdd:COG2931 40 GGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGGGGGGDDTDGGGDGGDGGGGGTGDDTGDGGGG-NDTLTGG 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488138322 293 KGNVSIAADVTIENAIGGSGHDDIIGNHTNNILTGNGGSDQLWGNGGNNTFRYASARDSMT 353
Cdd:COG2931 119 DGNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLYGGAGNDTLYGGAGNDTLDGGAGNDTLT 179
|
|
| Peptidase_M57 |
pfam12388 |
Dual-action HEIGH metallo-peptidase; The catalytic triad for this family of proteases is ... |
124-218 |
7.08e-03 |
|
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.
Pssm-ID: 432518 Cd Length: 212 Bit Score: 37.88 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 124 PSNVAGYAYYP---NPGSFSPI---WINYSFSDNQHpsrlndgggVLTHEIGHALGLGHSHAphgYTQQMSVMSYLSE-- 195
Cdd:pfam12388 100 PSGTGGSAGFPsggLPYGTIQIgtgLQSYSTDVNEH---------VITHELGHSIGFRHSDY---YNRSISCGSGGNEgt 167
|
90 100
....*....|....*....|...
gi 488138322 196 QGSGANygqHYLSTPQMYDIAAI 218
Cdd:pfam12388 168 AGVGAI---LIPGTPTTATGGSI 187
|
|
| COG2931 |
COG2931 |
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ... |
214-353 |
8.12e-03 |
|
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442175 [Multi-domain] Cd Length: 252 Bit Score: 37.96 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 214 DIAAIQYLYGANLHTRTGDTVYGFNSTSYRDHFTATHASDALIFCVWDAGGNDTFDFSGYKQNQMINLNELCFSDVGGLK 293
Cdd:COG2931 13 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGGGGGGDDTDGGGD 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138322 294 GNVSIAADVTIENAIGGSGHDDIIGNHTNNILTGNGGSDQLWGNGGNNTFRYASARDSMT 353
Cdd:COG2931 93 GGDGGGGGTGDDTGDGGGGNDTLTGGDGNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLY 152
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