|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
218-425 |
1.95e-106 |
|
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: 326.12 E-value: 1.95e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 218 RFVETLVVADDKMAAF-HGAGLKRYLLTVMAAAAKAFKHPSIRNPVSLVVTRLVILGSGEEGPQVGPSAAQTLRSFCAWQ 296
Cdd:cd04273 1 RYVETLVVADSKMVEFhHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 297 RGLNTPEDSDPDHFDTAILFTRQDLCGV-STCDTLGMADVGTVCDPARSCAIVEDDGLQSAFTAAHELGHVFNMLHDNS- 374
Cdd:cd04273 81 KKLNPPNDSDPEHHDHAILLTRQDICRSnGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDg 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 998614223 375 KPCislnGPLSTSRHVMAPVMAHVDPEEPWSPCSARFITDFLDNGYGHCLL 425
Cdd:cd04273 161 NSC----GPEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
|
|
| ADAMTS_CR_2 |
pfam17771 |
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ... |
439-507 |
8.97e-23 |
|
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: 92.41 E-value: 8.97e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 439 PGKDYDADRQCQLTFGPDSRHCPQLP-PPCAALWCSghLNGHAMCQTKHSPWADGTPCGPAQACMGGRCL 507
Cdd:pfam17771 1 PGQLYSADEQCRLIFGPGSTFCPNGDeDVCSKLWCS--NPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
531-575 |
4.06e-11 |
|
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: 58.75 E-value: 4.06e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 998614223 531 DCSRTCGGGVQFSSRDCTRPVPRNGGKYCEGRRTRFRSCNTEDCP 575
Cdd:smart00209 9 PCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
|
|
| Pep_M12B_propep super family |
cl03265 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
60-181 |
2.00e-10 |
|
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.
The actual alignment was detected with superfamily member pfam01562:
Pssm-ID: 460254 Cd Length: 128 Bit Score: 59.25 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 60 EIVFPEKLNG-----SVLPGSGAPARLLCRLQAFGETLLLELEQDSGVQVEGLTVQYLGQAPELLGGAEPGT---YLTGT 131
Cdd:pfam01562 1 EVVIPVRLDPsrrrrSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTdhcYYQGH 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 998614223 132 INGDPESVASLHwDGGALLGVLQYRGAELHLQPLEGGTPNSAGGPgaHIL 181
Cdd:pfam01562 81 VEGHPDSSVALS-TCSGLRGFIRTENEEYLIEPLEKYSREEGGHP--HVV 127
|
|
| ADAMTS_CR_3 super family |
cl41950 |
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ... |
578-685 |
3.74e-08 |
|
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.
The actual alignment was detected with superfamily member pfam19236:
Pssm-ID: 437068 Cd Length: 115 Bit Score: 52.40 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 578 SALTFREEQCAaynhRTD--LFKSFPGPMDWVpRYTGVAPQDQ----CKLTCQAQALGYYYVLEPRVVDGTPCSPD---- 647
Cdd:pfam19236 1 TQLEFMSQQCA----RTDgqPLRSSPGGASFY-HWGAAVPHSQgdalCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpre 75
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 998614223 648 --SSSVCVQGRCIHAGCDRIIGSKKKFDKCMVCGGDGSGC 685
Cdd:pfam19236 76 dgTLSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
218-425 |
1.95e-106 |
|
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: 326.12 E-value: 1.95e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 218 RFVETLVVADDKMAAF-HGAGLKRYLLTVMAAAAKAFKHPSIRNPVSLVVTRLVILGSGEEGPQVGPSAAQTLRSFCAWQ 296
Cdd:cd04273 1 RYVETLVVADSKMVEFhHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 297 RGLNTPEDSDPDHFDTAILFTRQDLCGV-STCDTLGMADVGTVCDPARSCAIVEDDGLQSAFTAAHELGHVFNMLHDNS- 374
Cdd:cd04273 81 KKLNPPNDSDPEHHDHAILLTRQDICRSnGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDg 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 998614223 375 KPCislnGPLSTSRHVMAPVMAHVDPEEPWSPCSARFITDFLDNGYGHCLL 425
Cdd:cd04273 161 NSC----GPEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
|
|
| ADAMTS_CR_2 |
pfam17771 |
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ... |
439-507 |
8.97e-23 |
|
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: 92.41 E-value: 8.97e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 439 PGKDYDADRQCQLTFGPDSRHCPQLP-PPCAALWCSghLNGHAMCQTKHSPWADGTPCGPAQACMGGRCL 507
Cdd:pfam17771 1 PGQLYSADEQCRLIFGPGSTFCPNGDeDVCSKLWCS--NPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
|
|
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
218-428 |
1.42e-17 |
|
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: 81.96 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 218 RFVETLVVADDKMAAFHGAGL---KRYLLTVMAAAAKAFKHPSIRnpvslvvtrlVILGSGE---EGPQ--VGPSAAQTL 289
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTtvvRQRVFQVVNLVNSIYKELNIR----------VVLVGLEiwtDEDKidVSGDANDTL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 290 RSFCAW-QRGLNTPEDsdpdhFDTAILFTRQDLCGVSTcdtlGMADVGTVCDPARSCAIVED---DGLQSAFTAAHELGH 365
Cdd:pfam01421 71 RNFLKWrQEYLKKRKP-----HDVAQLLSGVEFGGTTV----GAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGH 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 998614223 366 VFNMLHDNSKP---CISLNGPlstsrhVMAPVMAHVDPEEpWSPCSARFITDFLDNGYGHCLLDKP 428
Cdd:pfam01421 142 NLGMQHDDFNGgckCPPGGGC------IMNPSAGSSFPRK-FSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
531-575 |
4.06e-11 |
|
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: 58.75 E-value: 4.06e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 998614223 531 DCSRTCGGGVQFSSRDCTRPVPRNGGKYCEGRRTRFRSCNTEDCP 575
Cdd:smart00209 9 PCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
60-181 |
2.00e-10 |
|
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: 59.25 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 60 EIVFPEKLNG-----SVLPGSGAPARLLCRLQAFGETLLLELEQDSGVQVEGLTVQYLGQAPELLGGAEPGT---YLTGT 131
Cdd:pfam01562 1 EVVIPVRLDPsrrrrSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTdhcYYQGH 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 998614223 132 INGDPESVASLHwDGGALLGVLQYRGAELHLQPLEGGTPNSAGGPgaHIL 181
Cdd:pfam01562 81 VEGHPDSSVALS-TCSGLRGFIRTENEEYLIEPLEKYSREEGGHP--HVV 127
|
|
| ADAMTS_CR_3 |
pfam19236 |
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ... |
578-685 |
3.74e-08 |
|
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.
Pssm-ID: 437068 Cd Length: 115 Bit Score: 52.40 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 578 SALTFREEQCAaynhRTD--LFKSFPGPMDWVpRYTGVAPQDQ----CKLTCQAQALGYYYVLEPRVVDGTPCSPD---- 647
Cdd:pfam19236 1 TQLEFMSQQCA----RTDgqPLRSSPGGASFY-HWGAAVPHSQgdalCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpre 75
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 998614223 648 --SSSVCVQGRCIHAGCDRIIGSKKKFDKCMVCGGDGSGC 685
Cdd:pfam19236 76 dgTLSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
438-509 |
1.51e-07 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 51.21 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 438 FPGKDYDADRQCQLTFGPDSR----HCPQL-----------------PPPCAA-------LWCSG--------------- 474
Cdd:smart00608 14 YNGRCPTRDNQCQALFGPGAKvapdSCYEElntkgdrfgncgrengtYIPCAPedvkcgkLQCTNvselpllgehatviy 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 998614223 475 -HLNGHaMCQTKHSP---------WADGTPCGPAQACMGGRCLHM 509
Cdd:smart00608 94 sNIGGL-VCWSLDYHlgtdpdigmVKDGTKCGPGKVCINGQCVDV 137
|
|
| TSP1_spondin |
pfam19028 |
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ... |
531-574 |
5.64e-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: 41.50 E-value: 5.64e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 998614223 531 DCSRTCGGGVQFSSRDCTRPvPRNGGKYCeGRRTRFRSCNTEDC 574
Cdd:pfam19028 11 ECSVTCGGGVQTRTRTVIVE-PQNGGRPC-PELLERRPCNLPPC 52
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
490-659 |
6.02e-05 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 43.50 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 490 ADGTPCGPAQA-CMGGRCLHMDQlQdfnipqaggwgpwgpwgdCSRTCGGGVQFSSRDCTRPVPRNGGK--YCEGRRTRF 566
Cdd:smart00608 1 QDGTPCDNGQGyCYNGRCPTRDN-Q------------------CQALFGPGAKVAPDSCYEELNTKGDRfgNCGRENGTY 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 567 RSCNTED-------CPTGSALT-FREEQCAAYNHRTDlfksfpgpmdwvprytgvapqdqckLTCqaQALGYYYVLEP-- 636
Cdd:smart00608 62 IPCAPEDvkcgklqCTNVSELPlLGEHATVIYSNIGG-------------------------LVC--WSLDYHLGTDPdi 114
|
170 180
....*....|....*....|....
gi 998614223 637 -RVVDGTPCSPDssSVCVQGRCIH 659
Cdd:smart00608 115 gMVKDGTKCGPG--KVCINGQCVD 136
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
218-425 |
1.95e-106 |
|
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: 326.12 E-value: 1.95e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 218 RFVETLVVADDKMAAF-HGAGLKRYLLTVMAAAAKAFKHPSIRNPVSLVVTRLVILGSGEEGPQVGPSAAQTLRSFCAWQ 296
Cdd:cd04273 1 RYVETLVVADSKMVEFhHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 297 RGLNTPEDSDPDHFDTAILFTRQDLCGV-STCDTLGMADVGTVCDPARSCAIVEDDGLQSAFTAAHELGHVFNMLHDNS- 374
Cdd:cd04273 81 KKLNPPNDSDPEHHDHAILLTRQDICRSnGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDg 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 998614223 375 KPCislnGPLSTSRHVMAPVMAHVDPEEPWSPCSARFITDFLDNGYGHCLL 425
Cdd:cd04273 161 NSC----GPEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
218-417 |
5.89e-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: 140.25 E-value: 5.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 218 RFVETLVVADDKM---AAFHGAGLKRYLLTVMAAAAKAFKHPSIRNPVSLVVTRLVILGSGEEGPQVGPSAAQTLRSFCA 294
Cdd:cd04267 1 REIELVVVADHRMvsyFNSDENILQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 295 WQRGlntpedsDPDHFDTAILFTRQDLCGvstCDTLGMADVGTVCDPARSCAIVEDDG--LQSAFTAAHELGHVFNMLHD 372
Cdd:cd04267 81 WRAE-------GPIRHDNAVLLTAQDFIE---GDILGLAYVGSMCNPYSSVGVVEDTGftLLTALTMAHELGHNLGAEHD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 998614223 373 nSKPCISLNGPlSTSRHVMAPVmahVDPEEP--WSPCSARFITDFLD 417
Cdd:cd04267 151 -GGDELAFECD-GGGNYIMAPV---DSGLNSyrFSQCSIGSIREFLD 192
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
218-426 |
4.27e-23 |
|
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: 97.69 E-value: 4.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 218 RFVETLVVADDKMAAFHGAGL---KRYLLTVMAAAAKAFKHPSIRnpVSLVvtrLVILGSGEEGPQVGPSAAQTLRSFCA 294
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLskvRQRVIEIVNIVDSIYRPLNIR--VVLV---GLEIWTDKDKISVSGDAGETLNRFLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 295 WQRglntpEDSDPDHF-DTAILFTRQDLCGvstcDTLGMADVGTVCDPARSCAIVEDDG---LQSAFTAAHELGHVFNML 370
Cdd:cd04269 76 WKR-----SNLLPRKPhDNAQLLTGRDFDG----NTVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHNLGME 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 998614223 371 HDNS------KPCIslngplstsrhvMAPVMahVDPEEPWSPCSARFITDFLDNGYGHCLLD 426
Cdd:cd04269 147 HDDGgctcgrSTCI------------MAPSP--SSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ADAMTS_CR_2 |
pfam17771 |
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ... |
439-507 |
8.97e-23 |
|
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: 92.41 E-value: 8.97e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 439 PGKDYDADRQCQLTFGPDSRHCPQLP-PPCAALWCSghLNGHAMCQTKHSPWADGTPCGPAQACMGGRCL 507
Cdd:pfam17771 1 PGQLYSADEQCRLIFGPGSTFCPNGDeDVCSKLWCS--NPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
|
|
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
218-428 |
1.42e-17 |
|
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: 81.96 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 218 RFVETLVVADDKMAAFHGAGL---KRYLLTVMAAAAKAFKHPSIRnpvslvvtrlVILGSGE---EGPQ--VGPSAAQTL 289
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTtvvRQRVFQVVNLVNSIYKELNIR----------VVLVGLEiwtDEDKidVSGDANDTL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 290 RSFCAW-QRGLNTPEDsdpdhFDTAILFTRQDLCGVSTcdtlGMADVGTVCDPARSCAIVED---DGLQSAFTAAHELGH 365
Cdd:pfam01421 71 RNFLKWrQEYLKKRKP-----HDVAQLLSGVEFGGTTV----GAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGH 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 998614223 366 VFNMLHDNSKP---CISLNGPlstsrhVMAPVMAHVDPEEpWSPCSARFITDFLDNGYGHCLLDKP 428
Cdd:pfam01421 142 NLGMQHDDFNGgckCPPGGGC------IMNPSAGSSFPRK-FSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
301-416 |
1.02e-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: 72.55 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 301 TPEDSDPDHFDTAILFTRQDLcgvsTCDTLGMADVGTVCDPARSCAIVEDDGL---QSAFTAAHELGHVFNMLHD----- 372
Cdd:cd00203 43 VLVGVEIDKADIAILVTRQDF----DGGTGGWAYLGRVCDSLRGVGVLQDNQSgtkEGAQTIAHELGHALGFYHDhdrkd 118
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 998614223 373 -NSKPCISLNGPLST--SRHVMAPVMAHVDPE--EPWSPCSARFITDFL 416
Cdd:cd00203 119 rDDYPTIDDTLNAEDddYYSVMSYTKGSFSDGqrKDFSQCDIDQINKLY 167
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
531-575 |
4.06e-11 |
|
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: 58.75 E-value: 4.06e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 998614223 531 DCSRTCGGGVQFSSRDCTRPVPRNGGKYCEGRRTRFRSCNTEDCP 575
Cdd:smart00209 9 PCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
|
|
| ZnMc_salivary_gland_MPs |
cd04272 |
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
219-416 |
5.24e-11 |
|
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.
Pssm-ID: 239800 Cd Length: 220 Bit Score: 63.14 E-value: 5.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 219 FVETLVVADdkmAAFHGAG-----LKRYLLTVMAAAAkaFKHPSIRNP-VSLVVTRLVILGSGEEGPQVGPS------AA 286
Cdd:cd04272 2 YPELFVVVD---YDHQSEFfsneqLIRYLAVMVNAAN--LRYRDLKSPrIRLLLVGITISKDPDFEPYIHPInygyidAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 287 QTLRSFCAWQRGLNTPEDSDpdhfdTAILFTRQDLC----GVSTCDTLGMADVGTVCDpARSCAIVEDDG--LQSAFTAA 360
Cdd:cd04272 77 ETLENFNEYVKKKRDYFNPD-----VVFLVTGLDMStysgGSLQTGTGGYAYVGGACT-ENRVAMGEDTPgsYYGVYTMT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 998614223 361 HELGHVFNMLHDNSKPCISLNGPLSTSR------HVMAPVMAHVDpEEPWSPCSARFITDFL 416
Cdd:cd04272 151 HELAHLLGAPHDGSPPPSWVKGHPGSLDcpwddgYIMSYVVNGER-QYRFSQCSQRQIRNVF 211
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
60-181 |
2.00e-10 |
|
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: 59.25 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 60 EIVFPEKLNG-----SVLPGSGAPARLLCRLQAFGETLLLELEQDSGVQVEGLTVQYLGQAPELLGGAEPGT---YLTGT 131
Cdd:pfam01562 1 EVVIPVRLDPsrrrrSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTdhcYYQGH 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 998614223 132 INGDPESVASLHwDGGALLGVLQYRGAELHLQPLEGGTPNSAGGPgaHIL 181
Cdd:pfam01562 81 VEGHPDSSVALS-TCSGLRGFIRTENEEYLIEPLEKYSREEGGHP--HVV 127
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
223-393 |
9.07e-10 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 58.97 E-value: 9.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 223 LVVADDK-MAAFHGAGLKRYLLTVMAAAAKAFKHPSirnPVSLVVTRLVILGSGEE---GPQVGPSAAQTLRSF--CAWQ 296
Cdd:pfam13688 8 LVAADCSyVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCPytpPACSTGDSSDRLSEFqdFSAW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 297 RGlntpEDSDpdhfDTAILFTrqdlcgVSTCDTLGMADVGTVCDPARSCAIVEDDG--------LQSAFTAAHELGHVFN 368
Cdd:pfam13688 85 RG----TQND----DLAYLFL------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSgnnvvvstATEWQVFAHEIGHNFG 150
|
170 180 190
....*....|....*....|....*....|....
gi 998614223 369 MLHDnskPCISLNG---PLSTS------RHVMAP 393
Cdd:pfam13688 151 AVHD---CDSSTSSqccPPSNStcpaggRYIMNP 181
|
|
| Reprolysin_3 |
pfam13582 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
240-372 |
1.45e-08 |
|
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: 53.53 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 240 RYLLTVMAAAAKAFKHPSirnPVSLVVTRLVILgSGEEGPQVGPSAAQTLRSFCAWQRglntpEDSDPDHFDTAILFTRQ 319
Cdd:pfam13582 1 ARIVSLVNRANTIYERDL---GIRLQLAAIIIT-TSADTPYTSSDALEILDELQEVND-----TRIGQYGYDLGHLFTGR 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 998614223 320 DLCGVstcdtLGMADVGTVCDPARSCAIVEDD---GLQSAFTAAHELGHVFNMLHD 372
Cdd:pfam13582 72 DGGGG-----GGIAYVGGVCNSGSKFGVNSGSgpvGDTGADTFAHEIGHNFGLNHT 122
|
|
| ADAMTS_CR_3 |
pfam19236 |
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ... |
578-685 |
3.74e-08 |
|
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.
Pssm-ID: 437068 Cd Length: 115 Bit Score: 52.40 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 578 SALTFREEQCAaynhRTD--LFKSFPGPMDWVpRYTGVAPQDQ----CKLTCQAQALGYYYVLEPRVVDGTPCSPD---- 647
Cdd:pfam19236 1 TQLEFMSQQCA----RTDgqPLRSSPGGASFY-HWGAAVPHSQgdalCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpre 75
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 998614223 648 --SSSVCVQGRCIHAGCDRIIGSKKKFDKCMVCGGDGSGC 685
Cdd:pfam19236 76 dgTLSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
438-509 |
1.51e-07 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 51.21 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 438 FPGKDYDADRQCQLTFGPDSR----HCPQL-----------------PPPCAA-------LWCSG--------------- 474
Cdd:smart00608 14 YNGRCPTRDNQCQALFGPGAKvapdSCYEElntkgdrfgncgrengtYIPCAPedvkcgkLQCTNvselpllgehatviy 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 998614223 475 -HLNGHaMCQTKHSP---------WADGTPCGPAQACMGGRCLHM 509
Cdd:smart00608 94 sNIGGL-VCWSLDYHlgtdpdigmVKDGTKCGPGKVCINGQCVDV 137
|
|
| TSP1_spondin |
pfam19028 |
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ... |
531-574 |
5.64e-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: 41.50 E-value: 5.64e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 998614223 531 DCSRTCGGGVQFSSRDCTRPvPRNGGKYCeGRRTRFRSCNTEDC 574
Cdd:pfam19028 11 ECSVTCGGGVQTRTRTVIVE-PQNGGRPC-PELLERRPCNLPPC 52
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
490-659 |
6.02e-05 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 43.50 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 490 ADGTPCGPAQA-CMGGRCLHMDQlQdfnipqaggwgpwgpwgdCSRTCGGGVQFSSRDCTRPVPRNGGK--YCEGRRTRF 566
Cdd:smart00608 1 QDGTPCDNGQGyCYNGRCPTRDN-Q------------------CQALFGPGAKVAPDSCYEELNTKGDRfgNCGRENGTY 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614223 567 RSCNTED-------CPTGSALT-FREEQCAAYNHRTDlfksfpgpmdwvprytgvapqdqckLTCqaQALGYYYVLEP-- 636
Cdd:smart00608 62 IPCAPEDvkcgklqCTNVSELPlLGEHATVIYSNIGG-------------------------LVC--WSLDYHLGTDPdi 114
|
170 180
....*....|....*....|....
gi 998614223 637 -RVVDGTPCSPDssSVCVQGRCIH 659
Cdd:smart00608 115 gMVKDGTKCGPG--KVCINGQCVD 136
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
531-574 |
2.50e-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: 36.66 E-value: 2.50e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 998614223 531 DCSRTCGGGVQFSSRDCTRPVPR--NGGKYCEG--RRTRFRSCNTEDC 574
Cdd:pfam19030 8 ECSVTCGGGVQTRLVQCVQKGGGsiVPDSECSAqkKPPETQSCNLKPC 55
|
|
| TSP_1 |
pfam00090 |
Thrombospondin type 1 domain; |
531-574 |
4.49e-03 |
|
Thrombospondin type 1 domain;
Pssm-ID: 459668 [Multi-domain] Cd Length: 49 Bit Score: 35.86 E-value: 4.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 998614223 531 DCSRTCGGGVQFSSRDCTRPVPrnGGKYCEGRRTRFRSCNTEDC 574
Cdd:pfam00090 8 PCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
|
|
| |
