|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
223-431 |
1.62e-113 |
|
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: 356.93 E-value: 1.62e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 223 KWVETLVVADSKMVEYHGQPQVESYVLTIMNMVAGLYHDPSIGNPIHITVVRLIILEDEEKDLKITHHADDTLKNFCRWQ 302
Cdd:cd04273 1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 303 KNVNMKGDDHPQHHDTAILLTRKDLCaTMNHPCETLGLSHVAGLCHPQLSCSVSEDTGLPLAFTVAHELGHSFGIQHDGT 382
Cdd:cd04273 81 KKLNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2008101618 383 GNDCESIGKRPFIMSPQLLYDRGiPLTWSRCSREYITRFLDRGWGLCLD 431
Cdd:cd04273 160 GNSCGPEGKDGHIMSPTLGANTG-PFTWSKCSRRYLTSFLDTGDGNCLL 207
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
34-174 |
4.99e-37 |
|
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: 135.90 E-value: 4.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 34 DIVHPVRVDAGgsflsyelwpRVLRKRDVSAAQASSAFYQLQYQGRELLFNLTTNPYLLAPGFVSEIRRRSNLSNVHIQT 113
Cdd:pfam01562 1 EVVIPVRLDPS----------RRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPV 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2008101618 114 SVPTCHLLGDVQDpeLEGGFAAISACDGLRGVFQLSNEDYFIEPLdEVPAQPGHAQPHMVY 174
Cdd:pfam01562 71 QTDHCYYQGHVEG--HPDSSVALSTCSGLRGFIRTENEEYLIEPL-EKYSREEGGHPHVVY 128
|
|
| ADAMTS_spacer1 |
pfam05986 |
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ... |
681-790 |
2.04e-32 |
|
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like proteins. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase) and is a subfamily of the metalloprotease family, sharing a high degree of sequence similarity and conserved domain organization among its members. Members of the ADAM-TS family have been implicated in a range of diseases. ADAM-TS-like proteins lack a metalloprotease domain. They resides in the ECM and have regulatory roles. Examples of ADAM-TS-like proteins are papilin and punctin.
:
Pssm-ID: 461796 Cd Length: 115 Bit Score: 122.30 E-value: 2.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 681 TVSRTFKEAEGMGYVDVGLIPAGAREILIEEVAEAANFLALRSeDPDKYFLNGGWTIQ-WNGDYQVAGTTFTYTRKGN-W 758
Cdd:pfam05986 1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPaL 79
|
90 100 110
....*....|....*....|....*....|....*
gi 2008101618 759 ETLTSPGPTTEPVWIQLLFQ---ERNPGVHYKYTI 790
Cdd:pfam05986 80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFI 114
|
|
| ADAMTS_CR_2 |
pfam17771 |
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ... |
446-510 |
1.44e-24 |
|
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: 98.19 E-value: 1.44e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2008101618 446 PGVLYDVNHQCRLQYGPSSAYCEDV-DNVCYTLWCSVGT--TCHSKMDAAVDGTSCGKNKWCLNGECV 510
Cdd:pfam17771 1 PGQLYSADEQCRLIFGPGSTFCPNGdEDVCSKLWCSNPGgsTCTTKNLPAADGTPCGNKKWCLNGKCV 68
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
523-575 |
3.92e-14 |
|
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: 68.00 E-value: 3.92e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2008101618 523 WSGWSAWSVCSRSCGVGVRSSERQCTQPVPKNKGKYCVGERKRYRLCNLQACP 575
Cdd:smart00209 1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1482-1537 |
6.37e-14 |
|
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: 67.48 E-value: 6.37e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2008101618 1482 WVVGPWGQCSAPCGGGVQRRLVKCVNTqTGLAEEDSDLCSHEAWPESSRPCATEDC 1537
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQK-GGGSIVPDSECSAQKKPPETQSCNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
805-859 |
8.88e-14 |
|
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: 67.09 E-value: 8.88e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2008101618 805 WHYGPWSKCPVTCGTGVQRQSLYCMEKQAGIVDEGH-CDHLSRPRDRKRkCNEEPC 859
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSeCSAQKKPPETQS-CNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1375-1430 |
6.99e-12 |
|
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: 61.70 E-value: 6.99e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2008101618 1375 WRAGNWSKCSRNCGGGSATRDVQCVDTRDLRPLRPFHCqPGPTKPPTRQLCGTQPC 1430
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSEC-SAQKKPPETQSCNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
926-974 |
5.28e-11 |
|
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: 59.39 E-value: 5.28e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2008101618 926 WGVGNWSQCSVTCGAGIRQRSVLCI---NNTGVP---CDGAERPITETFCFLQPC 974
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVqkgGGSIVPdseCSAQKKPPETQSCNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1324-1372 |
4.41e-10 |
|
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: 56.69 E-value: 4.41e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2008101618 1324 WQVGNWSQCSTTCGLGAIWRLVRCSSG------NDEDCTLSSRPQPARHCHLRPC 1372
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKgggsivPDSECSAQKKPPETQSCNLKPC 55
|
|
| ADAMTS_CR_3 super family |
cl41950 |
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ... |
581-679 |
3.49e-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: 53.17 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 581 FRHTQCSQFDSMLYK-----GKLHKW---VPVLNDENPCELHCRPFNYSNREKLRDAVMDGTPCYQGRISRD----ICID 648
Cdd:pfam19236 5 FMSQQCARTDGQPLRsspggASFYHWgaaVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDgtlsLCVL 84
|
90 100 110
....*....|....*....|....*....|.
gi 2008101618 649 GICKKVGCDFELDSGAEEDRCGVCRGDGSTC 679
Cdd:pfam19236 85 GSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
|
|
| TSP1_ADAMTS super family |
cl40597 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1433-1479 |
4.75e-08 |
|
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.
The actual alignment was detected with superfamily member pfam19030:
Pssm-ID: 465950 [Multi-domain] Cd Length: 55 Bit Score: 50.91 E-value: 4.75e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2008101618 1433 WYTSSWRECSEACGGGEQQRLVTCPEPG--------LCEESLRPNNTRPCNTHPC 1479
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKGggsivpdsECSAQKKPPETQSCNLKPC 55
|
|
| TSP1_ADAMTS super family |
cl40597 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
863-916 |
9.53e-08 |
|
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.
The actual alignment was detected with superfamily member pfam19030:
Pssm-ID: 465950 [Multi-domain] Cd Length: 55 Bit Score: 50.14 E-value: 9.53e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2008101618 863 WWVGDWQPCSRSCGpGGFFRRAVFCTRSVGLDEQRalePSACGHLPRPLAEIPC 916
Cdd:pfam19030 1 WVAGPWGECSVTCG-GGVQTRLVQCVQKGGGSIVP---DSECSAQKKPPETQSC 50
|
|
| PHA03247 super family |
cl33720 |
large tegument protein UL36; Provisional |
1003-1312 |
1.47e-07 |
|
large tegument protein UL36; Provisional
The actual alignment was detected with superfamily member PHA03247:
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 56.87 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 1003 PHQPVPRPS----------PASSPKPVSISNAIDEEDPELDPPGPvfvddfyydynfinfhedlsygsfeeshsdlvdig 1072
Cdd:PHA03247 2570 PPRPAPRPSepavtsrarrPDAPPQSARPRAPVDDRGDPRGPAPP----------------------------------- 2614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 1073 gqTVPPhirPTEPPSDSPvPTAGAPGAEEEGiQGSWSPSPllseashsPPVLLENTPVNPLANFLTEEESPIGAPELGLP 1152
Cdd:PHA03247 2615 --SPLP---PDTHAPDPP-PPSPSPAANEPD-PHPPPTVP--------PPERPRDDPAPGRVSRPRRARRLGRAAQASSP 2679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 1153 SVSW-PPASVD--GMVTSVA----PGNPDELLVREDTQSQPSTPWSDRNKLSKDGNPLGPTSPALPKSPF----PTQPSS 1221
Cdd:PHA03247 2680 PQRPrRRAARPtvGSLTSLAdpppPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAtpggPARPAR 2759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 1222 PSNSTTQASLSPDAVEVS------TGWNVALDPVLEADLKPVHAPTDPGLLDQIQTPHTEGTQSP-GLLPRPAQETQTNS 1294
Cdd:PHA03247 2760 PPTTAGPPAPAPPAAPAAgpprrlTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPaGPLPPPTSAQPTAP 2839
|
330
....*....|....*...
gi 2008101618 1295 SKDPAvqPLQPSLVEDGA 1312
Cdd:PHA03247 2840 PPPPG--PPPPSLPLGGS 2855
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
223-431 |
1.62e-113 |
|
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: 356.93 E-value: 1.62e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 223 KWVETLVVADSKMVEYHGQPQVESYVLTIMNMVAGLYHDPSIGNPIHITVVRLIILEDEEKDLKITHHADDTLKNFCRWQ 302
Cdd:cd04273 1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 303 KNVNMKGDDHPQHHDTAILLTRKDLCaTMNHPCETLGLSHVAGLCHPQLSCSVSEDTGLPLAFTVAHELGHSFGIQHDGT 382
Cdd:cd04273 81 KKLNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2008101618 383 GNDCESIGKRPFIMSPQLLYDRGiPLTWSRCSREYITRFLDRGWGLCLD 431
Cdd:cd04273 160 GNSCGPEGKDGHIMSPTLGANTG-PFTWSKCSRRYLTSFLDTGDGNCLL 207
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
34-174 |
4.99e-37 |
|
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: 135.90 E-value: 4.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 34 DIVHPVRVDAGgsflsyelwpRVLRKRDVSAAQASSAFYQLQYQGRELLFNLTTNPYLLAPGFVSEIRRRSNLSNVHIQT 113
Cdd:pfam01562 1 EVVIPVRLDPS----------RRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPV 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2008101618 114 SVPTCHLLGDVQDpeLEGGFAAISACDGLRGVFQLSNEDYFIEPLdEVPAQPGHAQPHMVY 174
Cdd:pfam01562 71 QTDHCYYQGHVEG--HPDSSVALSTCSGLRGFIRTENEEYLIEPL-EKYSREEGGHPHVVY 128
|
|
| ADAMTS_spacer1 |
pfam05986 |
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ... |
681-790 |
2.04e-32 |
|
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like proteins. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase) and is a subfamily of the metalloprotease family, sharing a high degree of sequence similarity and conserved domain organization among its members. Members of the ADAM-TS family have been implicated in a range of diseases. ADAM-TS-like proteins lack a metalloprotease domain. They resides in the ECM and have regulatory roles. Examples of ADAM-TS-like proteins are papilin and punctin.
Pssm-ID: 461796 Cd Length: 115 Bit Score: 122.30 E-value: 2.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 681 TVSRTFKEAEGMGYVDVGLIPAGAREILIEEVAEAANFLALRSeDPDKYFLNGGWTIQ-WNGDYQVAGTTFTYTRKGN-W 758
Cdd:pfam05986 1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPaL 79
|
90 100 110
....*....|....*....|....*....|....*
gi 2008101618 759 ETLTSPGPTTEPVWIQLLFQ---ERNPGVHYKYTI 790
Cdd:pfam05986 80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFI 114
|
|
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
223-434 |
2.98e-31 |
|
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: 122.02 E-value: 2.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 223 KWVETLVVADSKMVEYHGQPQ--VESYVLTIMNMVAGLYhdpsigNPIHITVVrLIILE---DEEKdLKITHHADDTLKN 297
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTtvVRQRVFQVVNLVNSIY------KELNIRVV-LVGLEiwtDEDK-IDVSGDANDTLRN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 298 FCRWQKNVNMKgddhPQHHDTAILLTRKDLCATmnhpceTLGLSHVAGLCHPQLSCSVSED---TGLPLAFTVAHELGHS 374
Cdd:pfam01421 73 FLKWRQEYLKK----RKPHDVAQLLSGVEFGGT------TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHN 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 375 FGIQHDGTGNDCESIGKRPFIMSPQLLYDrgIPLTWSRCSREYITRFLDRGWGLCLDDRP 434
Cdd:pfam01421 143 LGMQHDDFNGGCKCPPGGGCIMNPSAGSS--FPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ADAMTS_CR_2 |
pfam17771 |
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ... |
446-510 |
1.44e-24 |
|
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: 98.19 E-value: 1.44e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2008101618 446 PGVLYDVNHQCRLQYGPSSAYCEDV-DNVCYTLWCSVGT--TCHSKMDAAVDGTSCGKNKWCLNGECV 510
Cdd:pfam17771 1 PGQLYSADEQCRLIFGPGSTFCPNGdEDVCSKLWCSNPGgsTCTTKNLPAADGTPCGNKKWCLNGKCV 68
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
523-575 |
3.92e-14 |
|
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: 68.00 E-value: 3.92e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2008101618 523 WSGWSAWSVCSRSCGVGVRSSERQCTQPVPKNKGKYCVGERKRYRLCNLQACP 575
Cdd:smart00209 1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1482-1537 |
6.37e-14 |
|
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: 67.48 E-value: 6.37e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2008101618 1482 WVVGPWGQCSAPCGGGVQRRLVKCVNTqTGLAEEDSDLCSHEAWPESSRPCATEDC 1537
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQK-GGGSIVPDSECSAQKKPPETQSCNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
805-859 |
8.88e-14 |
|
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: 67.09 E-value: 8.88e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2008101618 805 WHYGPWSKCPVTCGTGVQRQSLYCMEKQAGIVDEGH-CDHLSRPRDRKRkCNEEPC 859
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSeCSAQKKPPETQS-CNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1375-1430 |
6.99e-12 |
|
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: 61.70 E-value: 6.99e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2008101618 1375 WRAGNWSKCSRNCGGGSATRDVQCVDTRDLRPLRPFHCqPGPTKPPTRQLCGTQPC 1430
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSEC-SAQKKPPETQSCNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
926-974 |
5.28e-11 |
|
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: 59.39 E-value: 5.28e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2008101618 926 WGVGNWSQCSVTCGAGIRQRSVLCI---NNTGVP---CDGAERPITETFCFLQPC 974
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVqkgGGSIVPdseCSAQKKPPETQSCNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1324-1372 |
4.41e-10 |
|
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: 56.69 E-value: 4.41e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2008101618 1324 WQVGNWSQCSTTCGLGAIWRLVRCSSG------NDEDCTLSSRPQPARHCHLRPC 1372
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKgggsivPDSECSAQKKPPETQSCNLKPC 55
|
|
| ADAMTS_CR_3 |
pfam19236 |
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ... |
581-679 |
3.49e-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: 53.17 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 581 FRHTQCSQFDSMLYK-----GKLHKW---VPVLNDENPCELHCRPFNYSNREKLRDAVMDGTPCYQGRISRD----ICID 648
Cdd:pfam19236 5 FMSQQCARTDGQPLRsspggASFYHWgaaVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDgtlsLCVL 84
|
90 100 110
....*....|....*....|....*....|.
gi 2008101618 649 GICKKVGCDFELDSGAEEDRCGVCRGDGSTC 679
Cdd:pfam19236 85 GSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1433-1479 |
4.75e-08 |
|
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: 50.91 E-value: 4.75e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2008101618 1433 WYTSSWRECSEACGGGEQQRLVTCPEPG--------LCEESLRPNNTRPCNTHPC 1479
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKGggsivpdsECSAQKKPPETQSCNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
863-916 |
9.53e-08 |
|
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: 50.14 E-value: 9.53e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2008101618 863 WWVGDWQPCSRSCGpGGFFRRAVFCTRSVGLDEQRalePSACGHLPRPLAEIPC 916
Cdd:pfam19030 1 WVAGPWGECSVTCG-GGVQTRLVQCVQKGGGSIVP---DSECSAQKKPPETQSC 50
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1003-1312 |
1.47e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 56.87 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 1003 PHQPVPRPS----------PASSPKPVSISNAIDEEDPELDPPGPvfvddfyydynfinfhedlsygsfeeshsdlvdig 1072
Cdd:PHA03247 2570 PPRPAPRPSepavtsrarrPDAPPQSARPRAPVDDRGDPRGPAPP----------------------------------- 2614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 1073 gqTVPPhirPTEPPSDSPvPTAGAPGAEEEGiQGSWSPSPllseashsPPVLLENTPVNPLANFLTEEESPIGAPELGLP 1152
Cdd:PHA03247 2615 --SPLP---PDTHAPDPP-PPSPSPAANEPD-PHPPPTVP--------PPERPRDDPAPGRVSRPRRARRLGRAAQASSP 2679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 1153 SVSW-PPASVD--GMVTSVA----PGNPDELLVREDTQSQPSTPWSDRNKLSKDGNPLGPTSPALPKSPF----PTQPSS 1221
Cdd:PHA03247 2680 PQRPrRRAARPtvGSLTSLAdpppPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAtpggPARPAR 2759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 1222 PSNSTTQASLSPDAVEVS------TGWNVALDPVLEADLKPVHAPTDPGLLDQIQTPHTEGTQSP-GLLPRPAQETQTNS 1294
Cdd:PHA03247 2760 PPTTAGPPAPAPPAAPAAgpprrlTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPaGPLPPPTSAQPTAP 2839
|
330
....*....|....*...
gi 2008101618 1295 SKDPAvqPLQPSLVEDGA 1312
Cdd:PHA03247 2840 PPPPG--PPPPSLPLGGS 2855
|
|
| TSP1_spondin |
pfam19028 |
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ... |
524-574 |
6.06e-06 |
|
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: 44.96 E-value: 6.06e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2008101618 524 SGWSAWSVCSRSCGVGVRSSERQCTQPvPKNKGKYCVGERKRyRLCNLQAC 574
Cdd:pfam19028 4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELLER-RPCNLPPC 52
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
805-860 |
6.24e-06 |
|
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: 44.89 E-value: 6.24e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2008101618 805 WHYGPWSKCPVTCGTGVQRQSLYCmEKQAGIVDEGHCDHlsrPRDRKRKCNEEPCP 860
Cdd:smart00209 2 SEWSEWSPCSVTCGGGVQTRTRSC-CSPPPQNGGGPCTG---EDVETRACNEQPCP 53
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
924-974 |
1.08e-05 |
|
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: 44.11 E-value: 1.08e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2008101618 924 SSWGvgNWSQCSVTCGAGIRQRSVLCINNT----GVPCDGAERpiTETFCFLQPC 974
Cdd:smart00209 2 SEWS--EWSPCSVTCGGGVQTRTRSCCSPPpqngGGPCTGEDV--ETRACNEQPC 52
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
1479-1538 |
5.31e-05 |
|
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: 42.19 E-value: 5.31e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 1479 CTQWvvGPWGQCSAPCGGGVQRRLVKCVNtqtGLAEEDSDLCSHEAwpESSRPCATEDCE 1538
Cdd:smart00209 1 WSEW--SEWSPCSVTCGGGVQTRTRSCCS---PPPQNGGGPCTGED--VETRACNEQPCP 53
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
1435-1479 |
4.77e-03 |
|
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: 36.80 E-value: 4.77e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2008101618 1435 TSSWRECSEACGGGEQQRLVTC--PEPGLCEESLRPNN--TRPCNTHPC 1479
Cdd:smart00209 4 WSEWSPCSVTCGGGVQTRTRSCcsPPPQNGGGPCTGEDveTRACNEQPC 52
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
1378-1430 |
5.16e-03 |
|
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: 36.80 E-value: 5.16e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2008101618 1378 GNWSKCSRNCGGGSATRDVQCVDtrdlrPLRPFHCQPGPTKPPTRQLCGTQPC 1430
Cdd:smart00209 5 SEWSPCSVTCGGGVQTRTRSCCS-----PPPQNGGGPCTGEDVETRACNEQPC 52
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
223-431 |
1.62e-113 |
|
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: 356.93 E-value: 1.62e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 223 KWVETLVVADSKMVEYHGQPQVESYVLTIMNMVAGLYHDPSIGNPIHITVVRLIILEDEEKDLKITHHADDTLKNFCRWQ 302
Cdd:cd04273 1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 303 KNVNMKGDDHPQHHDTAILLTRKDLCaTMNHPCETLGLSHVAGLCHPQLSCSVSEDTGLPLAFTVAHELGHSFGIQHDGT 382
Cdd:cd04273 81 KKLNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2008101618 383 GNDCESIGKRPFIMSPQLLYDRGiPLTWSRCSREYITRFLDRGWGLCLD 431
Cdd:cd04273 160 GNSCGPEGKDGHIMSPTLGANTG-PFTWSKCSRRYLTSFLDTGDGNCLL 207
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
34-174 |
4.99e-37 |
|
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: 135.90 E-value: 4.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 34 DIVHPVRVDAGgsflsyelwpRVLRKRDVSAAQASSAFYQLQYQGRELLFNLTTNPYLLAPGFVSEIRRRSNLSNVHIQT 113
Cdd:pfam01562 1 EVVIPVRLDPS----------RRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPV 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2008101618 114 SVPTCHLLGDVQDpeLEGGFAAISACDGLRGVFQLSNEDYFIEPLdEVPAQPGHAQPHMVY 174
Cdd:pfam01562 71 QTDHCYYQGHVEG--HPDSSVALSTCSGLRGFIRTENEEYLIEPL-EKYSREEGGHPHVVY 128
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
225-423 |
4.68e-36 |
|
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: 135.63 E-value: 4.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 225 VETLVVADSKMVEYHgQPQVES---YVLTIMNMVAGLYHDPSIGNPIHITVVRLIILEDEEKDLKITHHADDTLKNFCRW 301
Cdd:cd04267 3 IELVVVADHRMVSYF-NSDENIlqaYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSFW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 302 QKNVnmkgddhPQHHDTAILLTRKDLCAtmnhpCETLGLSHVAGLCHPQLSCSVSEDTGLPL--AFTVAHELGHSFGIQH 379
Cdd:cd04267 82 RAEG-------PIRHDNAVLLTAQDFIE-----GDILGLAYVGSMCNPYSSVGVVEDTGFTLltALTMAHELGHNLGAEH 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2008101618 380 DGTGNDCESIGKRP-FIMSPQLlyDRGIPLTWSRCSREYITRFLD 423
Cdd:cd04267 150 DGGDELAFECDGGGnYIMAPVD--SGLNSYRFSQCSIGSIREFLD 192
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
223-430 |
6.48e-34 |
|
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: 129.66 E-value: 6.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 223 KWVETLVVADSKMVEYHGQ--PQVESYVLTIMNMVAGLYHdpsignPIHITVVrLIILE---DEEKdLKITHHADDTLKN 297
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSnlSKVRQRVIEIVNIVDSIYR------PLNIRVV-LVGLEiwtDKDK-ISVSGDAGETLNR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 298 FCRWQKNVNmkgdDHPQHHDTAILLTRKDLCATmnhpceTLGLSHVAGLCHPQLSCSVSEDTG---LPLAFTVAHELGHS 374
Cdd:cd04269 73 FLDWKRSNL----LPRKPHDNAQLLTGRDFDGN------TVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHN 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2008101618 375 FGIQHDGTGNDCESigkRPFIMSPQLLYdrgIPLTWSRCSREYITRFLDRGWGLCL 430
Cdd:cd04269 143 LGMEHDDGGCTCGR---STCIMAPSPSS---LTDAFSNCSYEDYQKFLSRGGGQCL 192
|
|
| ADAMTS_spacer1 |
pfam05986 |
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ... |
681-790 |
2.04e-32 |
|
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like proteins. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase) and is a subfamily of the metalloprotease family, sharing a high degree of sequence similarity and conserved domain organization among its members. Members of the ADAM-TS family have been implicated in a range of diseases. ADAM-TS-like proteins lack a metalloprotease domain. They resides in the ECM and have regulatory roles. Examples of ADAM-TS-like proteins are papilin and punctin.
Pssm-ID: 461796 Cd Length: 115 Bit Score: 122.30 E-value: 2.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 681 TVSRTFKEAEGMGYVDVGLIPAGAREILIEEVAEAANFLALRSeDPDKYFLNGGWTIQ-WNGDYQVAGTTFTYTRKGN-W 758
Cdd:pfam05986 1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPaL 79
|
90 100 110
....*....|....*....|....*....|....*
gi 2008101618 759 ETLTSPGPTTEPVWIQLLFQ---ERNPGVHYKYTI 790
Cdd:pfam05986 80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFI 114
|
|
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
223-434 |
2.98e-31 |
|
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: 122.02 E-value: 2.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 223 KWVETLVVADSKMVEYHGQPQ--VESYVLTIMNMVAGLYhdpsigNPIHITVVrLIILE---DEEKdLKITHHADDTLKN 297
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTtvVRQRVFQVVNLVNSIY------KELNIRVV-LVGLEiwtDEDK-IDVSGDANDTLRN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 298 FCRWQKNVNMKgddhPQHHDTAILLTRKDLCATmnhpceTLGLSHVAGLCHPQLSCSVSED---TGLPLAFTVAHELGHS 374
Cdd:pfam01421 73 FLKWRQEYLKK----RKPHDVAQLLSGVEFGGT------TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHN 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 375 FGIQHDGTGNDCESIGKRPFIMSPQLLYDrgIPLTWSRCSREYITRFLDRGWGLCLDDRP 434
Cdd:pfam01421 143 LGMQHDDFNGGCKCPPGGGCIMNPSAGSS--FPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ADAMTS_CR_2 |
pfam17771 |
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ... |
446-510 |
1.44e-24 |
|
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: 98.19 E-value: 1.44e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2008101618 446 PGVLYDVNHQCRLQYGPSSAYCEDV-DNVCYTLWCSVGT--TCHSKMDAAVDGTSCGKNKWCLNGECV 510
Cdd:pfam17771 1 PGQLYSADEQCRLIFGPGSTFCPNGdEDVCSKLWCSNPGgsTCTTKNLPAADGTPCGNKKWCLNGKCV 68
|
|
| ZnMc_salivary_gland_MPs |
cd04272 |
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
225-430 |
6.62e-19 |
|
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.
Pssm-ID: 239800 Cd Length: 220 Bit Score: 87.41 E-value: 6.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 225 VETLVVADSKMVEYHGQ-PQVESYVLTIMNMVAGLYHDpsIGNP-IHITVVRLIILEDEEKDLKITHHADD------TLK 296
Cdd:cd04272 3 PELFVVVDYDHQSEFFSnEQLIRYLAVMVNAANLRYRD--LKSPrIRLLLVGITISKDPDFEPYIHPINYGyidaaeTLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 297 NFcrwqkNVNMKGDDHPQHHDTAILLTRKDLCATMNHPCET--LGLSHVAGLCHpQLSCSVSEDTGLPL--AFTVAHELG 372
Cdd:cd04272 81 NF-----NEYVKKKRDYFNPDVVFLVTGLDMSTYSGGSLQTgtGGYAYVGGACT-ENRVAMGEDTPGSYygVYTMTHELA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 373 HSFGIQHDGTGnDCESIGKRP----------FIMSpqllYDRGIP--LTWSRCSREYITRFLDRGWGLCL 430
Cdd:cd04272 155 HLLGAPHDGSP-PPSWVKGHPgsldcpwddgYIMS----YVVNGErqYRFSQCSQRQIRNVFRRLGASCL 219
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
313-422 |
9.00e-15 |
|
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: 73.71 E-value: 9.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 313 PQHHDTAILLTRKDlcatmnHPCETLGLSHVAGLCHPQLSCSVSEDTGLP---LAFTVAHELGHSFGIQHDGTGNDCESI 389
Cdd:cd00203 49 IDKADIAILVTRQD------FDGGTGGWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAHELGHALGFYHDHDRKDRDDY 122
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2008101618 390 GKRP-----------FIMSPQLL-YDRGIPLTWSRCSREYITRFL 422
Cdd:cd00203 123 PTIDdtlnaedddyySVMSYTKGsFSDGQRKDFSQCDIDQINKLY 167
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
523-575 |
3.92e-14 |
|
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: 68.00 E-value: 3.92e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2008101618 523 WSGWSAWSVCSRSCGVGVRSSERQCTQPVPKNKGKYCVGERKRYRLCNLQACP 575
Cdd:smart00209 1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1482-1537 |
6.37e-14 |
|
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: 67.48 E-value: 6.37e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2008101618 1482 WVVGPWGQCSAPCGGGVQRRLVKCVNTqTGLAEEDSDLCSHEAWPESSRPCATEDC 1537
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQK-GGGSIVPDSECSAQKKPPETQSCNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
805-859 |
8.88e-14 |
|
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: 67.09 E-value: 8.88e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2008101618 805 WHYGPWSKCPVTCGTGVQRQSLYCMEKQAGIVDEGH-CDHLSRPRDRKRkCNEEPC 859
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSeCSAQKKPPETQS-CNLKPC 55
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
221-399 |
6.12e-13 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 68.98 E-value: 6.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 221 KEKWVETLVVADSKMVEYHGQPQVESYVLTIMNMVAGLYHDPSignPIHITVVRLIILEDEEKDLKI---THHADDTLKN 297
Cdd:pfam13688 1 STRTVALLVAADCSYVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCPYTPPacsTGDSSDRLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 298 FCRWQKNvnmkgdDHPQHHDTAILLTRKDlcatmnhpCETLGLSHVAGLCHPQLSCSVSEDTGLP--------LAFTVAH 369
Cdd:pfam13688 78 FQDFSAW------RGTQNDDLAYLFLMTN--------CSGGGLAWLGQLCNSGSAGSVSTRVSGNnvvvstatEWQVFAH 143
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2008101618 370 ELGHSFGIQHDGT----------GNDCESIGKRpFIMSPQ 399
Cdd:pfam13688 144 EIGHNFGAVHDCDsstssqccppSNSTCPAGGR-YIMNPS 182
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1375-1430 |
6.99e-12 |
|
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: 61.70 E-value: 6.99e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2008101618 1375 WRAGNWSKCSRNCGGGSATRDVQCVDTRDLRPLRPFHCqPGPTKPPTRQLCGTQPC 1430
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSEC-SAQKKPPETQSCNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
926-974 |
5.28e-11 |
|
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: 59.39 E-value: 5.28e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2008101618 926 WGVGNWSQCSVTCGAGIRQRSVLCI---NNTGVP---CDGAERPITETFCFLQPC 974
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVqkgGGSIVPdseCSAQKKPPETQSCNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1324-1372 |
4.41e-10 |
|
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: 56.69 E-value: 4.41e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2008101618 1324 WQVGNWSQCSTTCGLGAIWRLVRCSSG------NDEDCTLSSRPQPARHCHLRPC 1372
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKgggsivPDSECSAQKKPPETQSCNLKPC 55
|
|
| ADAMTS_CR_3 |
pfam19236 |
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ... |
581-679 |
3.49e-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: 53.17 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 581 FRHTQCSQFDSMLYK-----GKLHKW---VPVLNDENPCELHCRPFNYSNREKLRDAVMDGTPCYQGRISRD----ICID 648
Cdd:pfam19236 5 FMSQQCARTDGQPLRsspggASFYHWgaaVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDgtlsLCVL 84
|
90 100 110
....*....|....*....|....*....|.
gi 2008101618 649 GICKKVGCDFELDSGAEEDRCGVCRGDGSTC 679
Cdd:pfam19236 85 GSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1433-1479 |
4.75e-08 |
|
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: 50.91 E-value: 4.75e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2008101618 1433 WYTSSWRECSEACGGGEQQRLVTCPEPG--------LCEESLRPNNTRPCNTHPC 1479
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKGggsivpdsECSAQKKPPETQSCNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
863-916 |
9.53e-08 |
|
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: 50.14 E-value: 9.53e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2008101618 863 WWVGDWQPCSRSCGpGGFFRRAVFCTRSVGLDEQRalePSACGHLPRPLAEIPC 916
Cdd:pfam19030 1 WVAGPWGECSVTCG-GGVQTRLVQCVQKGGGSIVP---DSECSAQKKPPETQSC 50
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1003-1312 |
1.47e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 56.87 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 1003 PHQPVPRPS----------PASSPKPVSISNAIDEEDPELDPPGPvfvddfyydynfinfhedlsygsfeeshsdlvdig 1072
Cdd:PHA03247 2570 PPRPAPRPSepavtsrarrPDAPPQSARPRAPVDDRGDPRGPAPP----------------------------------- 2614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 1073 gqTVPPhirPTEPPSDSPvPTAGAPGAEEEGiQGSWSPSPllseashsPPVLLENTPVNPLANFLTEEESPIGAPELGLP 1152
Cdd:PHA03247 2615 --SPLP---PDTHAPDPP-PPSPSPAANEPD-PHPPPTVP--------PPERPRDDPAPGRVSRPRRARRLGRAAQASSP 2679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 1153 SVSW-PPASVD--GMVTSVA----PGNPDELLVREDTQSQPSTPWSDRNKLSKDGNPLGPTSPALPKSPF----PTQPSS 1221
Cdd:PHA03247 2680 PQRPrRRAARPtvGSLTSLAdpppPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAtpggPARPAR 2759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 1222 PSNSTTQASLSPDAVEVS------TGWNVALDPVLEADLKPVHAPTDPGLLDQIQTPHTEGTQSP-GLLPRPAQETQTNS 1294
Cdd:PHA03247 2760 PPTTAGPPAPAPPAAPAAgpprrlTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPaGPLPPPTSAQPTAP 2839
|
330
....*....|....*...
gi 2008101618 1295 SKDPAvqPLQPSLVEDGA 1312
Cdd:PHA03247 2840 PPPPG--PPPPSLPLGGS 2855
|
|
| TSP1_spondin |
pfam19028 |
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ... |
524-574 |
6.06e-06 |
|
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: 44.96 E-value: 6.06e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2008101618 524 SGWSAWSVCSRSCGVGVRSSERQCTQPvPKNKGKYCVGERKRyRLCNLQAC 574
Cdd:pfam19028 4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELLER-RPCNLPPC 52
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
805-860 |
6.24e-06 |
|
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: 44.89 E-value: 6.24e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2008101618 805 WHYGPWSKCPVTCGTGVQRQSLYCmEKQAGIVDEGHCDHlsrPRDRKRKCNEEPCP 860
Cdd:smart00209 2 SEWSEWSPCSVTCGGGVQTRTRSC-CSPPPQNGGGPCTG---EDVETRACNEQPCP 53
|
|
| TSP_1 |
pfam00090 |
Thrombospondin type 1 domain; |
524-574 |
6.27e-06 |
|
Thrombospondin type 1 domain;
Pssm-ID: 459668 [Multi-domain] Cd Length: 49 Bit Score: 44.72 E-value: 6.27e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2008101618 524 SGWSAWSVCSRSCGVGVRSSERQCTQPVPknKGKYCVGERKRYRLCNLQAC 574
Cdd:pfam00090 1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
924-974 |
1.08e-05 |
|
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: 44.11 E-value: 1.08e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2008101618 924 SSWGvgNWSQCSVTCGAGIRQRSVLCINNT----GVPCDGAERpiTETFCFLQPC 974
Cdd:smart00209 2 SEWS--EWSPCSVTCGGGVQTRTRSCCSPPpqngGGPCTGEDV--ETRACNEQPC 52
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1064-1375 |
1.09e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 50.71 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 1064 SHSDLVDIGGQTVPPHIRPTEPPSDSPVPTAGAPGaeeegiqGSWSPSPLLSEASHSPPV-----LLENTPVNPLANFLT 1138
Cdd:PHA03247 2694 SLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAA-------RQASPALPAAPAPPAVPAgpatpGGPARPARPPTTAGP 2766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 1139 EEESPIGAPELGLP-SVSWPPASVDGMVTSVAPGNPDEllvrEDTQSQPSTPWSDRNKLSKDGNPLGPTSPALPKSPFPT 1217
Cdd:PHA03247 2767 PAPAPPAAPAAGPPrRLTRPAVASLSESRESLPSPWDP----ADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPP 2842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 1218 QPSSPSNSTTQASLSPdavevstGWNVALDPVLEADLKPVHAPTDPGLLDQIQTPHTEGTQS-------PGLLPRPAQET 1290
Cdd:PHA03247 2843 PGPPPPSLPLGGSVAP-------GGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESfalppdqPERPPQPQAPP 2915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 1291 QTNSSKDPAVQPL-QPSLVEDGAP-------TDLLPAKNASWQVGNWSQCSTTCGLGAIWRLvRCSSGNDEDCTLSSRPQ 1362
Cdd:PHA03247 2916 PPQPQPQPPPPPQpQPPPPPPPRPqpplaptTDPAGAGEPSGAVPQPWLGALVPGRVAVPRF-RVPQPAPSREAPASSTP 2994
|
330
....*....|...
gi 2008101618 1363 PARHCHLRPCAAW 1375
Cdd:PHA03247 2995 PLTGHSLSRVSSW 3007
|
|
| Reprolysin_2 |
pfam13574 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
337-419 |
1.41e-05 |
|
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.
Pssm-ID: 372637 Cd Length: 193 Bit Score: 47.62 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 337 TLGLSHVAGLCHPQLSCsVSEDTGLPLAFT-------------VAHELGHSFGIQHDGTG--NDCESI----------GK 391
Cdd:pfam13574 86 ELGLAYVGQICQKGASS-PKTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDCDGsqYASSGCernaatsvcsAN 164
|
90 100
....*....|....*....|....*...
gi 2008101618 392 RPFIMSPQllYDRGIPLtWSRCSREYIT 419
Cdd:pfam13574 165 GSFIMNPA--SKSNNDL-FSPCSISLIC 189
|
|
| Reprolysin_3 |
pfam13582 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
268-380 |
2.55e-05 |
|
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.
Pssm-ID: 463926 [Multi-domain] Cd Length: 122 Bit Score: 45.05 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 268 IHITVVRLIILED-EEKDLKIThhADDTLKNFCRWqknvNMKGDDHPQHhDTAILLTRKDlcatmnhPCETLGLSHVAGL 346
Cdd:pfam13582 20 IRLQLAAIIITTSaDTPYTSSD--ALEILDELQEV----NDTRIGQYGY-DLGHLFTGRD-------GGGGGGIAYVGGV 85
|
90 100 110
....*....|....*....|....*....|....*..
gi 2008101618 347 CHPQLSCSVSED---TGLPLAFTVAHELGHSFGIQHD 380
Cdd:pfam13582 86 CNSGSKFGVNSGsgpVGDTGADTFAHEIGHNFGLNHT 122
|
|
| ZnMc_TACE_like |
cd04270 |
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ... |
228-436 |
4.27e-05 |
|
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: 46.98 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 228 LVVADSKMVEYHGQPQVESYVLTIMNMVAG---LYHDPSIGNP----IHITVVRLIIL-EDEEKDLKITHHAddtlKNFC 299
Cdd:cd04270 6 LLVADHRFYKYMGRGEEETTINYLISHIDRvddIYRNTDWDGGgfkgIGFQIKRIRIHtTPDEVDPGNKFYN----KSFP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 300 RWQKNVNMKGDDHPQHHD---TAILLTRKDLcaTMNhpceTLGLSHVA--------GLCHPQLSCSVSED----TGLPLA 364
Cdd:cd04270 82 NWGVEKFLVKLLLEQFSDdvcLAHLFTYRDF--DMG----TLGLAYVGsprdnsagGICEKAYYYSNGKKkylnTGLTTT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 365 F-------------TVAHELGHSFGIQHDGTGNDC---ESIGKRpFIMSPQLLY-DRGIPLTWSRCSREYITRFLDRGWG 427
Cdd:cd04270 156 VnygkrvptkesdlVTAHELGHNFGSPHDPDIAECapgESQGGN-YIMYARATSgDKENNKKFSPCSKKSISKVLEVKSN 234
|
....*....
gi 2008101618 428 LCLDDRPSK 436
Cdd:cd04270 235 SCFVERSQS 243
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
1479-1538 |
5.31e-05 |
|
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: 42.19 E-value: 5.31e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 1479 CTQWvvGPWGQCSAPCGGGVQRRLVKCVNtqtGLAEEDSDLCSHEAwpESSRPCATEDCE 1538
Cdd:smart00209 1 WSEW--SEWSPCSVTCGGGVQTRTRSCCS---PPPQNGGGPCTGED--VETRACNEQPCP 53
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1074-1322 |
9.28e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.16 E-value: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 1074 QTVPPH---IRPTEP--------PSDSPVPTAG-APGAEEEGIQGSWSPSPLLSEASHSPPVLLENTPvnplANFLTEEE 1141
Cdd:PHA03247 2566 RSVPPPrpaPRPSEPavtsrarrPDAPPQSARPrAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSP----AANEPDPH 2641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 1142 SPIGAPELGLPSVSWPPASVDGMVTSVAPGNPdellvredtqSQPSTPwsdrnklskdgnPLGPTSPALPKS-------- 1213
Cdd:PHA03247 2642 PPPTVPPPERPRDDPAPGRVSRPRRARRLGRA----------AQASSP------------PQRPRRRAARPTvgsltsla 2699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 1214 ---PFPTQPSSPSNSTTQASLSPDAVEVSTGWNVALdPVLEADLKPVHAPTDPGLLDQIQTPHTEGTQSPGLLPRPAQET 1290
Cdd:PHA03247 2700 dppPPPPTPEPAPHALVSATPLPPGPAAARQASPAL-PAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAG 2778
|
250 260 270
....*....|....*....|....*....|..
gi 2008101618 1291 QTNSSKDPAVQPLQPSLVEDGAPTDLLPAKNA 1322
Cdd:PHA03247 2779 PPRRLTRPAVASLSESRESLPSPWDPADPPAA 2810
|
|
| PTZ00441 |
PTZ00441 |
sporozoite surface protein 2 (SSP2); Provisional |
931-1230 |
1.21e-03 |
|
sporozoite surface protein 2 (SSP2); Provisional
Pssm-ID: 240420 [Multi-domain] Cd Length: 576 Bit Score: 43.41 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 931 WSQCSVTCGAGIRQRSvlcinntgvpcdgaeRPITETFCflqpcqystyivdtgasgsgssSPELFNEVDFDPHQPVPRP 1010
Cdd:PTZ00441 246 WTPCSVTCGKGTHSRS---------------RPILHEGC----------------------TTHMVEECEEEECPVEPEP 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 1011 SPASSPKPVSisnaideedPELDPPGPvfVDDfyyDYNFINFHEDLSYGSFEESHS--------------DLVDIGGQTV 1076
Cdd:PTZ00441 289 LPVPAPVPPT---------PEDDNPRP--TDD---EFAVPNFNEGLDVPDNPQDPVpppnegkdgnpneeNLFPPGDDEV 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 1077 PPHirPTEPPSDSPVPTAGAPGAEEEGIQGSWSPSPLLSEASHSPPV-----LLENTPVNP---LANFLTEEESP----I 1144
Cdd:PTZ00441 355 PDE--SNVPPNPPNVPGGSNSEFSSDVENPPNPPNPDIPEQEPNIPEdsnkeVPEDVPMEPeddRDNNFNEPKKPenkgD 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008101618 1145 GAPELGLPSVSWPPASVDGMVTSVAPGNPDEllvREDTQSQP-STPWSDRNKLSKDGNplgptspaLPKSPFPTQPSSPS 1223
Cdd:PTZ00441 433 GQNEPVIPKPLDNERDQSNKNKQVNPGNRHN---SEDRYTRPhGRNNENRNYNNKNSD--------IPKHPERSEHEQPE 501
|
....*..
gi 2008101618 1224 NSTTQAS 1230
Cdd:PTZ00441 502 DKKKKSS 508
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
526-574 |
1.48e-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: 38.20 E-value: 1.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2008101618 526 WSA--WSVCSRSCGVGVRSSERQCTQPVPK--NKGKYCVGERK--RYRLCNLQAC 574
Cdd:pfam19030 1 WVAgpWGECSVTCGGGVQTRLVQCVQKGGGsiVPDSECSAQKKppETQSCNLKPC 55
|
|
| TSP_1 |
pfam00090 |
Thrombospondin type 1 domain; |
931-974 |
1.56e-03 |
|
Thrombospondin type 1 domain;
Pssm-ID: 459668 [Multi-domain] Cd Length: 49 Bit Score: 37.78 E-value: 1.56e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2008101618 931 WSQCSVTCGAGIRQRSVLCINNT--GVPCDGaerPITET-FCFLQPC 974
Cdd:pfam00090 6 WSPCSVTCGKGIQVRQRTCKSPFpgGEPCTG---DDIETqACKMDKC 49
|
|
| TSP1_spondin |
pfam19028 |
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ... |
1432-1479 |
3.77e-03 |
|
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: 36.87 E-value: 3.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2008101618 1432 PWytSSWRECSEACGGGEQQR---LVTCPEPG--LCEESLRpnnTRPCNTHPC 1479
Cdd:pfam19028 5 EW--SEWSECSVTCGGGVQTRtrtVIVEPQNGgrPCPELLE---RRPCNLPPC 52
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
1435-1479 |
4.77e-03 |
|
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: 36.80 E-value: 4.77e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2008101618 1435 TSSWRECSEACGGGEQQRLVTC--PEPGLCEESLRPNN--TRPCNTHPC 1479
Cdd:smart00209 4 WSEWSPCSVTCGGGVQTRTRSCcsPPPQNGGGPCTGEDveTRACNEQPC 52
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
1378-1430 |
5.16e-03 |
|
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: 36.80 E-value: 5.16e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2008101618 1378 GNWSKCSRNCGGGSATRDVQCVDtrdlrPLRPFHCQPGPTKPPTRQLCGTQPC 1430
Cdd:smart00209 5 SEWSPCSVTCGGGVQTRTRSCCS-----PPPQNGGGPCTGEDVETRACNEQPC 52
|
|
| TSP_1 |
pfam00090 |
Thrombospondin type 1 domain; |
1432-1479 |
6.02e-03 |
|
Thrombospondin type 1 domain;
Pssm-ID: 459668 [Multi-domain] Cd Length: 49 Bit Score: 36.24 E-value: 6.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2008101618 1432 PWytSSWRECSEACGGGEQQRLVTC----PEPGLCEESLRPnnTRPCNTHPC 1479
Cdd:pfam00090 2 PW--SPWSPCSVTCGKGIQVRQRTCkspfPGGEPCTGDDIE--TQACKMDKC 49
|
|
| TSP1_CCN |
pfam19035 |
CCN3 Nov like TSP1 domain; This entry represents a sub-type of TSP1 domains found in ... |
1325-1372 |
6.42e-03 |
|
CCN3 Nov like TSP1 domain; This entry represents a sub-type of TSP1 domains found in matricellular CCN proteins that have an alternative disulphide binding pattern compared to the canonical TSP1 domains.
Pssm-ID: 465952 Cd Length: 44 Bit Score: 36.16 E-value: 6.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2008101618 1325 QVGNWSQCSTTCGLGAIwrlVRCSSGNDEdCTLSsrpQPARHCHLRPC 1372
Cdd:pfam19035 4 QSTEWSPCSKTCGMGVS---TRVSNDNAE-CKLV---TETRLCQLRPC 44
|
|
| |
