|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
250-465 |
3.93e-112 |
|
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.
:
Pssm-ID: 239801 Cd Length: 207 Bit Score: 334.21 E-value: 3.93e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 250 RFVETLVVADKMMVGYHGRKDIEHYILSVMNIVAKLYRDSSLGNVVNIIVARLIVLTEDQPNLEINHHADKSLDSFCKWQ 329
Cdd:cd04273 1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 330 KSILSHQsdgntipENGIAHHDNAVLITRYDICTYkNKPCGTLGLASVAGMCEPERSCSINEDIGLGSAFTIAHEIGHNF 409
Cdd:cd04273 81 KKLNPPN-------DSDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217354288 410 GMNHDGIGNSCGTKGhEAAKLMAAHITANTNPFSWSACSRDYITSFLDSGRGTCLD 465
Cdd:cd04273 153 GMPHDGDGNSCGPEG-KDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
43-191 |
2.11e-44 |
|
Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.
:
Pssm-ID: 460254 Cd Length: 128 Bit Score: 154.39 E-value: 2.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 43 QLTIPIRVDqngaflsftvkndkHSRRRRSMDpiDPQQAVSKLFFKLSAYGKHFHLNLTLNTDFVSKHFTVEYWGKDGPQ 122
Cdd:pfam01562 1 EVVIPVRLD--------------PSRRRRSLA--SESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTG 64
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217354288 123 WKHDFL--DNCHYTGYLQDQRSTTkVALSNCVGLHGVIATEDEEYFIEPLKNTTEDskhfsyENGHPHVIY 191
Cdd:pfam01562 65 VESPPVqtDHCYYQGHVEGHPDSS-VALSTCSGLRGFIRTENEEYLIEPLEKYSRE------EGGHPHVVY 128
|
|
| ADAMTS_CR_2 |
pfam17771 |
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ... |
480-548 |
4.14e-21 |
|
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (pfam08516). Members of the ADAM-TS family have been implicated in a range of diseases. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity.
:
Pssm-ID: 465496 Cd Length: 68 Bit Score: 87.02 E-value: 4.14e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217354288 480 PGQVYDADEQCRFQYGATSRQCKYGE--VCRELWC-LSKSNRCVTNSIPAAEGTLCqtgnIEKGWCYQGDCV 548
Cdd:pfam17771 1 PGQLYSADEQCRLIFGPGSTFCPNGDedVCSKLWCsNPGGSTCTTKNLPAADGTPC----GNKKWCLNGKCV 68
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
561-611 |
5.75e-15 |
|
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
:
Pssm-ID: 214559 [Multi-domain] Cd Length: 53 Bit Score: 69.15 E-value: 5.75e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2217354288 561 WGPWSLWGECSRTCGGGVSSSLRHCDSPAPSGGGKYCLGERKRYRSCNTDV 611
Cdd:smart00209 1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQP 51
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
250-465 |
3.93e-112 |
|
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.
Pssm-ID: 239801 Cd Length: 207 Bit Score: 334.21 E-value: 3.93e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 250 RFVETLVVADKMMVGYHGRKDIEHYILSVMNIVAKLYRDSSLGNVVNIIVARLIVLTEDQPNLEINHHADKSLDSFCKWQ 329
Cdd:cd04273 1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 330 KSILSHQsdgntipENGIAHHDNAVLITRYDICTYkNKPCGTLGLASVAGMCEPERSCSINEDIGLGSAFTIAHEIGHNF 409
Cdd:cd04273 81 KKLNPPN-------DSDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217354288 410 GMNHDGIGNSCGTKGhEAAKLMAAHITANTNPFSWSACSRDYITSFLDSGRGTCLD 465
Cdd:cd04273 153 GMPHDGDGNSCGPEG-KDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
43-191 |
2.11e-44 |
|
Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.
Pssm-ID: 460254 Cd Length: 128 Bit Score: 154.39 E-value: 2.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 43 QLTIPIRVDqngaflsftvkndkHSRRRRSMDpiDPQQAVSKLFFKLSAYGKHFHLNLTLNTDFVSKHFTVEYWGKDGPQ 122
Cdd:pfam01562 1 EVVIPVRLD--------------PSRRRRSLA--SESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTG 64
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217354288 123 WKHDFL--DNCHYTGYLQDQRSTTkVALSNCVGLHGVIATEDEEYFIEPLKNTTEDskhfsyENGHPHVIY 191
Cdd:pfam01562 65 VESPPVqtDHCYYQGHVEGHPDSS-VALSTCSGLRGFIRTENEEYLIEPLEKYSRE------EGGHPHVVY 128
|
|
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
250-468 |
2.03e-30 |
|
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.
Pssm-ID: 426256 [Multi-domain] Cd Length: 200 Bit Score: 118.17 E-value: 2.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 250 RFVETLVVADKMMVGYHGRkDIEH---YILSVMNIVAKLYRDSslgNVVNIIVARLIVLTEDQpnLEINHHADKSLDSFC 326
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGS-DTTVvrqRVFQVVNLVNSIYKEL---NIRVVLVGLEIWTDEDK--IDVSGDANDTLRNFL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 327 KWQKSILSHQSDgntipengiahHDNAVLITrydictYKNKPCGTLGLASVAGMCEPERSCSINEDIG---LGSAFTIAH 403
Cdd:pfam01421 75 KWRQEYLKKRKP-----------HDVAQLLS------GVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSknlESFAVTMAH 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217354288 404 EIGHNFGMNHDGIGN--SCGTKGheaAKLMAAHITAnTNPFSWSACSRDYITSFLDSGRGTCLDNEP 468
Cdd:pfam01421 138 ELGHNLGMQHDDFNGgcKCPPGG---GCIMNPSAGS-SFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ADAMTS_CR_2 |
pfam17771 |
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ... |
480-548 |
4.14e-21 |
|
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (pfam08516). Members of the ADAM-TS family have been implicated in a range of diseases. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity.
Pssm-ID: 465496 Cd Length: 68 Bit Score: 87.02 E-value: 4.14e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217354288 480 PGQVYDADEQCRFQYGATSRQCKYGE--VCRELWC-LSKSNRCVTNSIPAAEGTLCqtgnIEKGWCYQGDCV 548
Cdd:pfam17771 1 PGQLYSADEQCRLIFGPGSTFCPNGDedVCSKLWCsNPGGSTCTTKNLPAADGTPC----GNKKWCLNGKCV 68
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
561-611 |
5.75e-15 |
|
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
Pssm-ID: 214559 [Multi-domain] Cd Length: 53 Bit Score: 69.15 E-value: 5.75e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2217354288 561 WGPWSLWGECSRTCGGGVSSSLRHCDSPAPSGGGKYCLGERKRYRSCNTDV 611
Cdd:smart00209 1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQP 51
|
|
| TSP_1 |
pfam00090 |
Thrombospondin type 1 domain; |
562-608 |
2.53e-07 |
|
Thrombospondin type 1 domain;
Pssm-ID: 459668 [Multi-domain] Cd Length: 49 Bit Score: 47.41 E-value: 2.53e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2217354288 562 GPWSLWGECSRTCGGGVSSSLRHCDSPAPsgGGKYCLGERKRYRSCN 608
Cdd:pfam00090 1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACK 45
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
250-465 |
3.93e-112 |
|
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.
Pssm-ID: 239801 Cd Length: 207 Bit Score: 334.21 E-value: 3.93e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 250 RFVETLVVADKMMVGYHGRKDIEHYILSVMNIVAKLYRDSSLGNVVNIIVARLIVLTEDQPNLEINHHADKSLDSFCKWQ 329
Cdd:cd04273 1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 330 KSILSHQsdgntipENGIAHHDNAVLITRYDICTYkNKPCGTLGLASVAGMCEPERSCSINEDIGLGSAFTIAHEIGHNF 409
Cdd:cd04273 81 KKLNPPN-------DSDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217354288 410 GMNHDGIGNSCGTKGhEAAKLMAAHITANTNPFSWSACSRDYITSFLDSGRGTCLD 465
Cdd:cd04273 153 GMPHDGDGNSCGPEG-KDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
43-191 |
2.11e-44 |
|
Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.
Pssm-ID: 460254 Cd Length: 128 Bit Score: 154.39 E-value: 2.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 43 QLTIPIRVDqngaflsftvkndkHSRRRRSMDpiDPQQAVSKLFFKLSAYGKHFHLNLTLNTDFVSKHFTVEYWGKDGPQ 122
Cdd:pfam01562 1 EVVIPVRLD--------------PSRRRRSLA--SESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTG 64
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217354288 123 WKHDFL--DNCHYTGYLQDQRSTTkVALSNCVGLHGVIATEDEEYFIEPLKNTTEDskhfsyENGHPHVIY 191
Cdd:pfam01562 65 VESPPVqtDHCYYQGHVEGHPDSS-VALSTCSGLRGFIRTENEEYLIEPLEKYSRE------EGGHPHVVY 128
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
250-457 |
6.86e-38 |
|
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: 138.71 E-value: 6.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 250 RFVETLVVADKMMVGYHGRK--DIEHYILSVMNIVAKLYRDSSLGNVVNIIVARLIVLTEDQPNLEINHHADKSLDSFCK 327
Cdd:cd04267 1 REIELVVVADHRMVSYFNSDenILQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 328 WQKSilshqsdgntipenGIAHHDNAVLITRYDICTyknkpCGTLGLASVAGMCEPERSCSINEDIG--LGSAFTIAHEI 405
Cdd:cd04267 81 WRAE--------------GPIRHDNAVLLTAQDFIE-----GDILGLAYVGSMCNPYSSVGVVEDTGftLLTALTMAHEL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2217354288 406 GHNFGMNHDGIGNSCGTKGHEAAKLMaAHITANTNPFSWSACSRDYITSFLD 457
Cdd:cd04267 142 GHNLGAEHDGGDELAFECDGGGNYIM-APVDSGLNSYRFSQCSIGSIREFLD 192
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
250-466 |
2.70e-35 |
|
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.
Pssm-ID: 239797 [Multi-domain] Cd Length: 194 Bit Score: 131.58 E-value: 2.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 250 RFVETLVVADKMMVGYHGRKD--IEHYILSVMNIVAKLYRDsslgnvVNIIVA--RLIVLTEDQPnLEINHHADKSLDSF 325
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLskVRQRVIEIVNIVDSIYRP------LNIRVVlvGLEIWTDKDK-ISVSGDAGETLNRF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 326 CKWQKSILSHQsdgntIPengiahHDNAVLITrydictYKNKPCGTLGLASVAGMCEPERSCSINEDIG---LGSAFTIA 402
Cdd:cd04269 74 LDWKRSNLLPR-----KP------HDNAQLLT------GRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMA 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217354288 403 HEIGHNFGMNHDGIGNSCGTKGHeaakLMAAHITanTNPFSWSACSRDYITSFLDSGRGTCLDN 466
Cdd:cd04269 137 HELGHNLGMEHDDGGCTCGRSTC----IMAPSPS--SLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
250-468 |
2.03e-30 |
|
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.
Pssm-ID: 426256 [Multi-domain] Cd Length: 200 Bit Score: 118.17 E-value: 2.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 250 RFVETLVVADKMMVGYHGRkDIEH---YILSVMNIVAKLYRDSslgNVVNIIVARLIVLTEDQpnLEINHHADKSLDSFC 326
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGS-DTTVvrqRVFQVVNLVNSIYKEL---NIRVVLVGLEIWTDEDK--IDVSGDANDTLRNFL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 327 KWQKSILSHQSDgntipengiahHDNAVLITrydictYKNKPCGTLGLASVAGMCEPERSCSINEDIG---LGSAFTIAH 403
Cdd:pfam01421 75 KWRQEYLKKRKP-----------HDVAQLLS------GVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSknlESFAVTMAH 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217354288 404 EIGHNFGMNHDGIGN--SCGTKGheaAKLMAAHITAnTNPFSWSACSRDYITSFLDSGRGTCLDNEP 468
Cdd:pfam01421 138 ELGHNLGMQHDDFNGgcKCPPGG---GCIMNPSAGS-SFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ADAMTS_CR_2 |
pfam17771 |
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ... |
480-548 |
4.14e-21 |
|
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (pfam08516). Members of the ADAM-TS family have been implicated in a range of diseases. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity.
Pssm-ID: 465496 Cd Length: 68 Bit Score: 87.02 E-value: 4.14e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217354288 480 PGQVYDADEQCRFQYGATSRQCKYGE--VCRELWC-LSKSNRCVTNSIPAAEGTLCqtgnIEKGWCYQGDCV 548
Cdd:pfam17771 1 PGQLYSADEQCRLIFGPGSTFCPNGDedVCSKLWCsNPGGSTCTTKNLPAADGTPC----GNKKWCLNGKCV 68
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
561-611 |
5.75e-15 |
|
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
Pssm-ID: 214559 [Multi-domain] Cd Length: 53 Bit Score: 69.15 E-value: 5.75e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2217354288 561 WGPWSLWGECSRTCGGGVSSSLRHCDSPAPSGGGKYCLGERKRYRSCNTDV 611
Cdd:smart00209 1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQP 51
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
346-456 |
1.62e-12 |
|
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: 66.01 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 346 GIAHHDNAVLITRYDictyknKPCGTLGLASVAGMCEPERSCSINEDIGLGS---AFTIAHEIGHNFGMNHDGIGNSCGT 422
Cdd:cd00203 48 EIDKADIAILVTRQD------FDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTkegAQTIAHELGHALGFYHDHDRKDRDD 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2217354288 423 KGHEAAK----------LMAAHITANT--NPFSWSACSRDYITSFL 456
Cdd:cd00203 122 YPTIDDTlnaedddyysVMSYTKGSFSdgQRKDFSQCDIDQINKLY 167
|
|
| ZnMc_salivary_gland_MPs |
cd04272 |
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
251-464 |
7.33e-12 |
|
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.
Pssm-ID: 239800 Cd Length: 220 Bit Score: 65.07 E-value: 7.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 251 FVETLVVADKMMVGYHGR-KDIEHYILSVMNIVAKLYRDSSLGNVVniivarlIVLTedqpNLEINHHADKSLDSFCKWQ 329
Cdd:cd04272 2 YPELFVVVDYDHQSEFFSnEQLIRYLAVMVNAANLRYRDLKSPRIR-------LLLV----GITISKDPDFEPYIHPINY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 330 KSILSHQS--DGNT--IPENGIAHHDNAVLITRYDICTYKNKPC--GTLGLASVAGMCEpERSCSINEDIGlGS---AFT 400
Cdd:cd04272 71 GYIDAAETleNFNEyvKKKRDYFNPDVVFLVTGLDMSTYSGGSLqtGTGGYAYVGGACT-ENRVAMGEDTP-GSyygVYT 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217354288 401 IAHEIGHNFGMNHDGIGNSCGTKGHEAAK--------LMAAHITAnTNPFSWSACSRDYITSFLDSGRGTCL 464
Cdd:cd04272 149 MTHELAHLLGAPHDGSPPPSWVKGHPGSLdcpwddgyIMSYVVNG-ERQYRFSQCSQRQIRNVFRRLGASCL 219
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
255-443 |
1.45e-10 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 60.90 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 255 LVVADKMMVGYHGRKDIEHYILSVMNIVAKL-YRDSSlgnvVNIIVARLIVLTEDQPNleiNHHADKSLDSfckwqKSIL 333
Cdd:pfam13688 8 LVAADCSYVAAFGGDAAQANIINMVNTASNVyERDFN----ISLGLVNLTISDSTCPY---TPPACSTGDS-----SDRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 334 SHQSDGNTIpeNGIAHHDNAVLITrydictykNKPCGTLGLASVAGMCEPERSCSINEDIGLGS--------AFTIAHEI 405
Cdd:pfam13688 76 SEFQDFSAW--RGTQNDDLAYLFL--------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSGNNvvvstateWQVFAHEI 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2217354288 406 GHNFGMNHD-----GIGNSCGTKGHEAAK---LMAAHITANTNPFS 443
Cdd:pfam13688 146 GHNFGAVHDcdsstSSQCCPPSNSTCPAGgryIMNPSSSPNSTDFS 191
|
|
| Reprolysin_3 |
pfam13582 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
274-414 |
6.00e-09 |
|
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: 463926 [Multi-domain] Cd Length: 122 Bit Score: 54.30 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 274 YILSVMNIVAKLY-RDSSLG-NVVNIIvarlIVLTEDQPNLEINhhADKSLDSFCKWQksilSHQSDGNTIpengiahhD 351
Cdd:pfam13582 2 RIVSLVNRANTIYeRDLGIRlQLAAII----ITTSADTPYTSSD--ALEILDELQEVN----DTRIGQYGY--------D 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217354288 352 NAVLITRYDictyknkPCGTLGLASVAGMCEPERSCSINEDI---GLGSAFTIAHEIGHNFGMNHD 414
Cdd:pfam13582 64 LGHLFTGRD-------GGGGGGIAYVGGVCNSGSKFGVNSGSgpvGDTGADTFAHEIGHNFGLNHT 122
|
|
| ZnMc_TACE_like |
cd04270 |
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ... |
255-463 |
8.39e-08 |
|
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha converting enzyme, releases soluble TNF-alpha from transmembrane pro-TNF-alpha.
Pssm-ID: 239798 [Multi-domain] Cd Length: 244 Bit Score: 53.53 E-value: 8.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 255 LVVADKMMVGYHGRKDIE---HYILSVMNIVAKLYRDSSLGNV----VNIIVARLIVLTEDQPNLEINHHADKSLDSF-- 325
Cdd:cd04270 6 LLVADHRFYKYMGRGEEEttiNYLISHIDRVDDIYRNTDWDGGgfkgIGFQIKRIRIHTTPDEVDPGNKFYNKSFPNWgv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 326 CKWQKSILSHQsdgntipengiaHHDNAVLITRYdicTYKNKPCGTLGLASVA--------GMCEPE------RSCSINe 391
Cdd:cd04270 86 EKFLVKLLLEQ------------FSDDVCLAHLF---TYRDFDMGTLGLAYVGsprdnsagGICEKAyyysngKKKYLN- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 392 dIGLGSAF-------------TIAHEIGHNFGMNHDGIGNSCGTKGHEAAK-LMAAHIT----ANTNPFswSACSRDYIT 453
Cdd:cd04270 150 -TGLTTTVnygkrvptkesdlVTAHELGHNFGSPHDPDIAECAPGESQGGNyIMYARATsgdkENNKKF--SPCSKKSIS 226
|
250
....*....|
gi 2217354288 454 SFLDSGRGTC 463
Cdd:cd04270 227 KVLEVKSNSC 236
|
|
| TSP_1 |
pfam00090 |
Thrombospondin type 1 domain; |
562-608 |
2.53e-07 |
|
Thrombospondin type 1 domain;
Pssm-ID: 459668 [Multi-domain] Cd Length: 49 Bit Score: 47.41 E-value: 2.53e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2217354288 562 GPWSLWGECSRTCGGGVSSSLRHCDSPAPsgGGKYCLGERKRYRSCN 608
Cdd:pfam00090 1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACK 45
|
|
| Reprolysin_2 |
pfam13574 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
275-456 |
2.93e-06 |
|
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: 48.39 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 275 ILSVMNIVAKLYRDSSLG-NVVNIIVARLIVLTE--DQPNLEINHHADKS--LDSFCKWQksilshqsdgntipenGIAH 349
Cdd:pfam13574 7 LVNVVNRVNQIYEPDDINiNGGLVNPGEIPATTSasDSGNNYCNSPTTIVrrLNFLSQWR----------------GEQD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 350 HDNAVLITRYDiCTyknkpCGTLGLASVAGMCEPERSCS-----INEDIGLGSAFT-------IAHEIGHNFGMNHD-GI 416
Cdd:pfam13574 71 YCLAHLVTMGT-FS-----GGELGLAYVGQICQKGASSPktntgLSTTTNYGSFNYptqewdvVAHEVGHNFGATHDcDG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2217354288 417 GNSCGTKGHEAAK----------LMAAhiTANTNPFSWSACSRDYITSFL 456
Cdd:pfam13574 145 SQYASSGCERNAAtsvcsangsfIMNP--ASKSNNDLFSPCSISLICDVL 192
|
|
| TSP1_spondin |
pfam19028 |
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ... |
562-610 |
2.44e-05 |
|
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.
Pssm-ID: 465948 Cd Length: 52 Bit Score: 41.88 E-value: 2.44e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2217354288 562 GPWSLWGECSRTCGGGVSSSLRHCDSPaPSGGGKYCLGERKRyRSCNTD 610
Cdd:pfam19028 4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELLER-RPCNLP 50
|
|
| Reprolysin_4 |
pfam13583 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
250-422 |
2.78e-04 |
|
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: 42.61 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 250 RFVETLVVADKMMVGYHGRKD-IEHYILSVMNIVAKLYrdsslGNVVNIivaRLIVLTEDQPNleinhHADKSLDSFCKW 328
Cdd:pfam13583 3 RVYRVAVATDCTYSASFGSVDeLRANINATVTTANEVY-----GRDFNV---SLALISDRDVI-----YTDSSTDSFNAD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 329 QKSILSHQSDGNTIPEN-GIAHHDNAVLITRYDICTYKNkpcgtlGLASVAGMCEPERSCSinedigLGSAF-------- 399
Cdd:pfam13583 70 CSGGDLGNWRLATLTSWrDSLNYDLAYLTLMTGPSGQNV------GVAWVGALCSSARQNA------KASGVarsrdewd 137
|
170 180
....*....|....*....|...
gi 2217354288 400 TIAHEIGHNFGMNHDGIGNSCGT 422
Cdd:pfam13583 138 IFAHEIGHTFGAVHDCSSQGEGL 160
|
|
| ZnMc_ADAM_fungal |
cd04271 |
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ... |
256-464 |
8.40e-04 |
|
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.
Pssm-ID: 239799 [Multi-domain] Cd Length: 228 Bit Score: 41.25 E-value: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 256 VVAD-KMMVGYHGRKDIEHYILSVMNIVAKLYRDS---SLGnVVNIIVARL---IVLTEDQP-NLEINHHADKS--LDSF 325
Cdd:cd04271 7 VAADcSYTKSFGSVEEARRNILNNVNSASQLYESSfniSLG-LRNLTISDAscpSTAVDSAPwNLPCNSRIDIDdrLSIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 326 CKWQksilSHQSDgntipengiahhDNAVLITRYDICtyknkPCG-TLGLASVAGMCEPERSCSINEDIG--LGSAFT-- 400
Cdd:cd04271 86 SQWR----GQQPD------------DGNAFWTLMTAC-----PSGsEVGVAWLGQLCRTGASDQGNETVAgtNVVVRTsn 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217354288 401 ----IAHEIGHNFGMNHDGIGNSCGTKGHEAAK---LMAAHITAN----TNPFS------WSACSRDYITSFL--DSGRG 461
Cdd:cd04271 145 ewqvFAHEIGHTFGAVHDCTSGTCSDGSVGSQQccpLSTSTCDANgqyiMNPSSssgiteFSPCTIGNICSLLgrNPVRT 224
|
...
gi 2217354288 462 TCL 464
Cdd:cd04271 225 SCL 227
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
567-608 |
2.59e-03 |
|
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.
Pssm-ID: 465950 [Multi-domain] Cd Length: 55 Bit Score: 36.28 E-value: 2.59e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217354288 567 WGECSRTCGGGVSSSLRHCDSPAPSG--GGKYCLGERK--RYRSCN 608
Cdd:pfam19030 6 WGECSVTCGGGVQTRLVQCVQKGGGSivPDSECSAQKKppETQSCN 51
|
|
| |
