|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
226-434 |
1.81e-111 |
|
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: 351.16 E-value: 1.81e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 226 KWVETLVVADSKMVEYHGQPQVESYVLTIMNMVAGLFHDPSIGNPIHISIVRLIILEDEEKDLKITHHAEETLKNFCRWQ 305
Cdd:cd04273 1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 306 KNINIKGDDHPQHHDTAILLTRKDLCaSMNQPCETLGLSHVSGLCHPQLSCSVSEDTGMPLAFTVAHELGHSFGIQHDGT 385
Cdd:cd04273 81 KKLNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568960639 386 GNDCESIGKRPFIMSPQLLYDRGiPLTWSRCSREYITRFLDRGWGLCLD 434
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 |
4.28e-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: 136.29 E-value: 4.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 34 DIVHPVRVDAGgsflsyelwpRVLRKRDVSTTQASSAFYQLQYQGRELLFNLTTNPYLMAPGFVSEIRRHSTLGHAHIQT 113
Cdd:pfam01562 1 EVVIPVRLDPS----------RRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPV 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568960639 114 SVPTCHLLGDVQDpeLEGGFAAISACDGLRGVFQLSNEDYFIEPLDGvSAQPGHAQPHVVY 174
Cdd:pfam01562 71 QTDHCYYQGHVEG--HPDSSVALSTCSGLRGFIRTENEEYLIEPLEK-YSREEGGHPHVVY 128
|
|
| ADAMTS_spacer1 |
pfam05986 |
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ... |
684-793 |
3.60e-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: 121.53 E-value: 3.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 684 TVSRTFKETEGQGYVDIGLIPAGAREILIEEVAEAANFLALRSeDPDKYFLNGGWTIQ-WNGDYRVAGTTFTYARKGN-W 761
Cdd:pfam05986 1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPaL 79
|
90 100 110
....*....|....*....|....*....|....*
gi 568960639 762 ENLTSPGPTSEPVWIQLLFQ---EKNPGVHYQYTI 793
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 ... |
449-513 |
2.60e-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: 97.42 E-value: 2.60e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568960639 449 PGVLYDVNHQCRLQYGSHSAYCEDM-DDVCHTLWCSVGT--TCHSKLDAAVDGTSCGKNKWCLKGECV 513
Cdd:pfam17771 1 PGQLYSADEQCRLIFGPGSTFCPNGdEDVCSKLWCSNPGgsTCTTKNLPAADGTPCGNKKWCLNGKCV 68
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
526-578 |
5.11e-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: 67.61 E-value: 5.11e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 568960639 526 WSGWSAWSDCSRSCGVGVRSSERQCTQPVPKNRGKYCVGERKRSQLCNLPACP 578
Cdd:smart00209 1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1485-1540 |
7.25e-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: 7.25e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568960639 1485 WVVGPWGQCSAPCGGGVQRRLVRCVNTqTGLAEEDSDLCSHEAWPESSRPCATEDC 1540
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQK-GGGSIVPDSECSAQKKPPETQSCNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
808-862 |
2.21e-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: 63.24 E-value: 2.21e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568960639 808 WHYGPWSKCTVTCGTGVQRQSLYCM-ERQAGVVAEEYCNTLNRPDERQRkCSEEPC 862
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVqKGGGSIVPDSECSAQKKPPETQS-CNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1378-1433 |
5.35e-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: 5.35e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568960639 1378 WRTGNWSKCSRNCGGGSSTRDVQCVDTRDLRPLRPFHCqPGPTKPPNRQLCGTQPC 1433
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSEC-SAQKKPPETQSCNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
929-977 |
2.41e-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: 57.46 E-value: 2.41e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 568960639 929 WGVGNWSQCSVTCGAGIRQRSVLCI---NNTDVP---CDEAERPITETFCFLQPC 977
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVqkgGGSIVPdseCSAQKKPPETQSCNLKPC 55
|
|
| PHA03247 super family |
cl33720 |
large tegument protein UL36; Provisional |
1058-1344 |
2.49e-10 |
|
large tegument protein UL36; Provisional
The actual alignment was detected with superfamily member PHA03247:
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 65.73 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1058 SYGSFEEPHPDlvdnggwTAPPHIRPTESPSDTPVPTAGALGAEAEDiQGSWSPSPLLSEASYSPPGLEQTSINPLANFL 1137
Cdd:PHA03247 2694 SLTSLADPPPP-------PPTPEPAPHALVSATPLPPGPAAARQASP-ALPAAPAPPAVPAGPATPGGPARPARPPTTAG 2765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1138 TEEDTPMGAPELGFP-SLPWPPASVDDMMTPVGPGNPDellvKEDEQSPPSTPWSDRNKLSTDGNPLGHTSPALPQSPIP 1216
Cdd:PHA03247 2766 PPAPAPPAAPAAGPPrRLTRPAVASLSESRESLPSPWD----PADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPP 2841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1217 TQPSPPSISPTQASPSP--DVVEVSTGWNAAWDPVleadlKPGHVPTD-LRSPGPSGQPQtPNLEGTQSPGLLPTPARET 1293
Cdd:PHA03247 2842 PPGPPPPSLPLGGSVAPggDVRRRPPSRSPAAKPA-----APARPPVRrLARPAVSRSTE-SFALPPDQPERPPQPQAPP 2915
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 568960639 1294 QTNSSKDPEVQPL-QPSLEEDGDPADPLPARNASWQVGNWSQCSTTCGLGAI 1344
Cdd:PHA03247 2916 PPQPQPQPPPPPQpQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGAL 2967
|
|
| ADAMTS_CR_3 super family |
cl41950 |
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ... |
584-682 |
8.01e-10 |
|
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: 57.80 E-value: 8.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 584 FRHTQCSQFDGMLYK-----GKLHKW---VPVPNDDNPCELHCRPSNSSNTEKLRDAVVDGTPCYQSRISRD----ICLN 651
Cdd:pfam19236 5 FMSQQCARTDGQPLRsspggASFYHWgaaVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDgtlsLCVL 84
|
90 100 110
....*....|....*....|....*....|.
gi 568960639 652 GICKNVGCDFVIDSGAEEDRCGVCRGDGSTC 682
Cdd:pfam19236 85 GSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1327-1375 |
1.26e-09 |
|
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: 55.54 E-value: 1.26e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 568960639 1327 WQVGNWSQCSTTCGLGAIWRLVSCSSG------NDEDCTLASRPQPARHCHLRPC 1375
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKgggsivPDSECSAQKKPPETQSCNLKPC 55
|
|
| TSP1_ADAMTS super family |
cl40597 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
866-922 |
7.70e-09 |
|
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: 53.23 E-value: 7.70e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568960639 866 WWAGEWQPCSRSCGPeGLSRRAVFCIRSMGLDEQRAlelSACEHLPRPLAETPCNRH 922
Cdd:pfam19030 1 WVAGPWGECSVTCGG-GVQTRLVQCVQKGGGSIVPD---SECSAQKKPPETQSCNLK 53
|
|
| TSP1_ADAMTS super family |
cl40597 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1436-1482 |
1.34e-07 |
|
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: 49.76 E-value: 1.34e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 568960639 1436 WYTSSWRECSEACGGGEQQRLVTCPEPG--------LCEESLRPNNSRPCNTHPC 1482
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKGggsivpdsECSAQKKPPETQSCNLKPC 55
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
226-434 |
1.81e-111 |
|
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: 351.16 E-value: 1.81e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 226 KWVETLVVADSKMVEYHGQPQVESYVLTIMNMVAGLFHDPSIGNPIHISIVRLIILEDEEKDLKITHHAEETLKNFCRWQ 305
Cdd:cd04273 1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 306 KNINIKGDDHPQHHDTAILLTRKDLCaSMNQPCETLGLSHVSGLCHPQLSCSVSEDTGMPLAFTVAHELGHSFGIQHDGT 385
Cdd:cd04273 81 KKLNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568960639 386 GNDCESIGKRPFIMSPQLLYDRGiPLTWSRCSREYITRFLDRGWGLCLD 434
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 |
4.28e-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: 136.29 E-value: 4.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 34 DIVHPVRVDAGgsflsyelwpRVLRKRDVSTTQASSAFYQLQYQGRELLFNLTTNPYLMAPGFVSEIRRHSTLGHAHIQT 113
Cdd:pfam01562 1 EVVIPVRLDPS----------RRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPV 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568960639 114 SVPTCHLLGDVQDpeLEGGFAAISACDGLRGVFQLSNEDYFIEPLDGvSAQPGHAQPHVVY 174
Cdd:pfam01562 71 QTDHCYYQGHVEG--HPDSSVALSTCSGLRGFIRTENEEYLIEPLEK-YSREEGGHPHVVY 128
|
|
| ADAMTS_spacer1 |
pfam05986 |
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ... |
684-793 |
3.60e-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: 121.53 E-value: 3.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 684 TVSRTFKETEGQGYVDIGLIPAGAREILIEEVAEAANFLALRSeDPDKYFLNGGWTIQ-WNGDYRVAGTTFTYARKGN-W 761
Cdd:pfam05986 1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPaL 79
|
90 100 110
....*....|....*....|....*....|....*
gi 568960639 762 ENLTSPGPTSEPVWIQLLFQ---EKNPGVHYQYTI 793
Cdd:pfam05986 80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFI 114
|
|
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
226-437 |
4.11e-30 |
|
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.
Pssm-ID: 426256 [Multi-domain] Cd Length: 200 Bit Score: 118.94 E-value: 4.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 226 KWVETLVVADSKMVEYHGQPQ--VESYVLTIMNMVAglfhdpSIGNPIHISIVrLIILE---DEEKdLKITHHAEETLKN 300
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTtvVRQRVFQVVNLVN------SIYKELNIRVV-LVGLEiwtDEDK-IDVSGDANDTLRN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 301 FCRWQKNiNIKgddHPQHHDTAILLTRKDLCASmnqpceTLGLSHVSGLCHPQLSCSVSED---TGMPLAFTVAHELGHS 377
Cdd:pfam01421 73 FLKWRQE-YLK---KRKPHDVAQLLSGVEFGGT------TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHN 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 378 FGIQHDGTGNDCESIGKRPFIMSPQLLYDrgIPLTWSRCSREYITRFLDRGWGLCLDDRP 437
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 ... |
449-513 |
2.60e-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: 97.42 E-value: 2.60e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568960639 449 PGVLYDVNHQCRLQYGSHSAYCEDM-DDVCHTLWCSVGT--TCHSKLDAAVDGTSCGKNKWCLKGECV 513
Cdd:pfam17771 1 PGQLYSADEQCRLIFGPGSTFCPNGdEDVCSKLWCSNPGgsTCTTKNLPAADGTPCGNKKWCLNGKCV 68
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
526-578 |
5.11e-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: 67.61 E-value: 5.11e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 568960639 526 WSGWSAWSDCSRSCGVGVRSSERQCTQPVPKNRGKYCVGERKRSQLCNLPACP 578
Cdd:smart00209 1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1485-1540 |
7.25e-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: 7.25e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568960639 1485 WVVGPWGQCSAPCGGGVQRRLVRCVNTqTGLAEEDSDLCSHEAWPESSRPCATEDC 1540
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQK-GGGSIVPDSECSAQKKPPETQSCNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
808-862 |
2.21e-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: 63.24 E-value: 2.21e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568960639 808 WHYGPWSKCTVTCGTGVQRQSLYCM-ERQAGVVAEEYCNTLNRPDERQRkCSEEPC 862
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVqKGGGSIVPDSECSAQKKPPETQS-CNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1378-1433 |
5.35e-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: 5.35e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568960639 1378 WRTGNWSKCSRNCGGGSSTRDVQCVDTRDLRPLRPFHCqPGPTKPPNRQLCGTQPC 1433
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSEC-SAQKKPPETQSCNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
929-977 |
2.41e-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: 57.46 E-value: 2.41e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 568960639 929 WGVGNWSQCSVTCGAGIRQRSVLCI---NNTDVP---CDEAERPITETFCFLQPC 977
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVqkgGGSIVPdseCSAQKKPPETQSCNLKPC 55
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1058-1344 |
2.49e-10 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 65.73 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1058 SYGSFEEPHPDlvdnggwTAPPHIRPTESPSDTPVPTAGALGAEAEDiQGSWSPSPLLSEASYSPPGLEQTSINPLANFL 1137
Cdd:PHA03247 2694 SLTSLADPPPP-------PPTPEPAPHALVSATPLPPGPAAARQASP-ALPAAPAPPAVPAGPATPGGPARPARPPTTAG 2765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1138 TEEDTPMGAPELGFP-SLPWPPASVDDMMTPVGPGNPDellvKEDEQSPPSTPWSDRNKLSTDGNPLGHTSPALPQSPIP 1216
Cdd:PHA03247 2766 PPAPAPPAAPAAGPPrRLTRPAVASLSESRESLPSPWD----PADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPP 2841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1217 TQPSPPSISPTQASPSP--DVVEVSTGWNAAWDPVleadlKPGHVPTD-LRSPGPSGQPQtPNLEGTQSPGLLPTPARET 1293
Cdd:PHA03247 2842 PPGPPPPSLPLGGSVAPggDVRRRPPSRSPAAKPA-----APARPPVRrLARPAVSRSTE-SFALPPDQPERPPQPQAPP 2915
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 568960639 1294 QTNSSKDPEVQPL-QPSLEEDGDPADPLPARNASWQVGNWSQCSTTCGLGAI 1344
Cdd:PHA03247 2916 PPQPQPQPPPPPQpQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGAL 2967
|
|
| ADAMTS_CR_3 |
pfam19236 |
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ... |
584-682 |
8.01e-10 |
|
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: 57.80 E-value: 8.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 584 FRHTQCSQFDGMLYK-----GKLHKW---VPVPNDDNPCELHCRPSNSSNTEKLRDAVVDGTPCYQSRISRD----ICLN 651
Cdd:pfam19236 5 FMSQQCARTDGQPLRsspggASFYHWgaaVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDgtlsLCVL 84
|
90 100 110
....*....|....*....|....*....|.
gi 568960639 652 GICKNVGCDFVIDSGAEEDRCGVCRGDGSTC 682
Cdd:pfam19236 85 GSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1327-1375 |
1.26e-09 |
|
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: 55.54 E-value: 1.26e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 568960639 1327 WQVGNWSQCSTTCGLGAIWRLVSCSSG------NDEDCTLASRPQPARHCHLRPC 1375
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKgggsivPDSECSAQKKPPETQSCNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
866-922 |
7.70e-09 |
|
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: 53.23 E-value: 7.70e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568960639 866 WWAGEWQPCSRSCGPeGLSRRAVFCIRSMGLDEQRAlelSACEHLPRPLAETPCNRH 922
Cdd:pfam19030 1 WVAGPWGECSVTCGG-GVQTRLVQCVQKGGGSIVPD---SECSAQKKPPETQSCNLK 53
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1436-1482 |
1.34e-07 |
|
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: 49.76 E-value: 1.34e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 568960639 1436 WYTSSWRECSEACGGGEQQRLVTCPEPG--------LCEESLRPNNSRPCNTHPC 1482
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKGggsivpdsECSAQKKPPETQSCNLKPC 55
|
|
| TSP_1 |
pfam00090 |
Thrombospondin type 1 domain; |
527-577 |
2.83e-07 |
|
Thrombospondin type 1 domain;
Pssm-ID: 459668 [Multi-domain] Cd Length: 49 Bit Score: 48.57 E-value: 2.83e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568960639 527 SGWSAWSDCSRSCGVGVRSSERQCTQPVPKnrGKYCVGERKRSQLCNLPAC 577
Cdd:pfam00090 1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPG--GEPCTGDDIETQACKMDKC 49
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1076-1321 |
5.62e-07 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 54.77 E-value: 5.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1076 TAPPHIR---PTESPSDTPVPTAGALgAEAEDIQGSWSPSPLLSEASYSPPGLEQTSINPLAnfLTEEdtpmgAPELGFP 1152
Cdd:pfam03154 169 TQPPVLQaqsGAASPPSPPPPGTTQA-ATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHT--LIQQ-----TPTLHPQ 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1153 SLPWPPASVDDMMTPVGPgnpdellvkeDEQSPPSTPwsdRNKLSTDGNPLGH---TSPALPQSPIPTQP--SPPSISPT 1227
Cdd:pfam03154 241 RLPSPHPPLQPMTQPPPP----------SQVSPQPLP---QPSLHGQMPPMPHslqTGPSHMQHPVPPQPfpLTPQSSQS 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1228 QASPSPDVVEVSTGWNAAWDPVLEADLKPGHVPTD------------LRSPGPSGQPQTPNLEGTQSPGLLPTPAR-ETQ 1294
Cdd:pfam03154 308 QVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREqplppaplsmphIKPPPTTPIPQLPNPQSHKHPPHLSGPSPfQMN 387
|
250 260
....*....|....*....|....*...
gi 568960639 1295 TNSSKDPEVQPLQpSLEEDGDP-ADPLP 1321
Cdd:pfam03154 388 SNLPPPPALKPLS-SLSTHHPPsAHPPP 414
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
808-863 |
1.93e-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: 43.34 E-value: 1.93e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568960639 808 WHYGPWSKCTVTCGTGVQRQSLYCmERQAGVVAEEYCNTlnrPDERQRKCSEEPCP 863
Cdd:smart00209 2 SEWSEWSPCSVTCGGGVQTRTRSC-CSPPPQNGGGPCTG---EDVETRACNEQPCP 53
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
1482-1541 |
8.19e-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: 41.80 E-value: 8.19e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1482 CTQWvvGPWGQCSAPCGGGVQRRLVRCVNtqtGLAEEDSDLCSHEAwpESSRPCATEDCE 1541
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. |
927-977 |
1.07e-04 |
|
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: 41.42 E-value: 1.07e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 568960639 927 STWGvgNWSQCSVTCGAGIRQRSVLCINNTDVPCDEA-ERPITET-FCFLQPC 977
Cdd:smart00209 2 SEWS--EWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPcTGEDVETrACNEQPC 52
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
1378-1433 |
4.87e-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: 4.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568960639 1378 WRTGNWSKCSRNCGGGSSTRDVQCVDtrdlrPLRPFHCQPGPTKPPNRQLCGTQPC 1433
Cdd:smart00209 2 SEWSEWSPCSVTCGGGVQTRTRSCCS-----PPPQNGGGPCTGEDVETRACNEQPC 52
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
226-434 |
1.81e-111 |
|
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: 351.16 E-value: 1.81e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 226 KWVETLVVADSKMVEYHGQPQVESYVLTIMNMVAGLFHDPSIGNPIHISIVRLIILEDEEKDLKITHHAEETLKNFCRWQ 305
Cdd:cd04273 1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 306 KNINIKGDDHPQHHDTAILLTRKDLCaSMNQPCETLGLSHVSGLCHPQLSCSVSEDTGMPLAFTVAHELGHSFGIQHDGT 385
Cdd:cd04273 81 KKLNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568960639 386 GNDCESIGKRPFIMSPQLLYDRGiPLTWSRCSREYITRFLDRGWGLCLD 434
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 |
4.28e-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: 136.29 E-value: 4.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 34 DIVHPVRVDAGgsflsyelwpRVLRKRDVSTTQASSAFYQLQYQGRELLFNLTTNPYLMAPGFVSEIRRHSTLGHAHIQT 113
Cdd:pfam01562 1 EVVIPVRLDPS----------RRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPV 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568960639 114 SVPTCHLLGDVQDpeLEGGFAAISACDGLRGVFQLSNEDYFIEPLDGvSAQPGHAQPHVVY 174
Cdd:pfam01562 71 QTDHCYYQGHVEG--HPDSSVALSTCSGLRGFIRTENEEYLIEPLEK-YSREEGGHPHVVY 128
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
228-426 |
1.63e-35 |
|
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: 134.08 E-value: 1.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 228 VETLVVADSKMVEYHgQPQVES---YVLTIMNMVAGLFHDPSIGNPIHISIVRLIILEDEEKDLKITHHAEETLKNFCRW 304
Cdd:cd04267 3 IELVVVADHRMVSYF-NSDENIlqaYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSFW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 305 QKninikgdDHPQHHDTAILLTRKDLCAsmnqpCETLGLSHVSGLCHPQLSCSVSEDTGMPL--AFTVAHELGHSFGIQH 382
Cdd:cd04267 82 RA-------EGPIRHDNAVLLTAQDFIE-----GDILGLAYVGSMCNPYSSVGVVEDTGFTLltALTMAHELGHNLGAEH 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568960639 383 DGTGNDCESIGKRP-FIMSPQLlyDRGIPLTWSRCSREYITRFLD 426
Cdd:cd04267 150 DGGDELAFECDGGGnYIMAPVD--SGLNSYRFSQCSIGSIREFLD 192
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
226-433 |
1.45e-32 |
|
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: 125.81 E-value: 1.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 226 KWVETLVVADSKMVEYHGQ--PQVESYVLTIMNMVAGLFHdpSIGnpIHISIVRLIILEDEEKdLKITHHAEETLKNFCR 303
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSnlSKVRQRVIEIVNIVDSIYR--PLN--IRVVLVGLEIWTDKDK-ISVSGDAGETLNRFLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 304 W-QKNINikgddHPQHHDTAILLTRKDLCAsmnqpcETLGLSHVSGLCHPQLSCSVSEDTGMPL---AFTVAHELGHSFG 379
Cdd:cd04269 76 WkRSNLL-----PRKPHDNAQLLTGRDFDG------NTVGLAYVGGMCSPKYSGGVVQDHSRNLllfAVTMAHELGHNLG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568960639 380 IQHDGTGNDCESigkRPFIMSPQLLYdrgIPLTWSRCSREYITRFLDRGWGLCL 433
Cdd:cd04269 145 MEHDDGGCTCGR---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 ... |
684-793 |
3.60e-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: 121.53 E-value: 3.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 684 TVSRTFKETEGQGYVDIGLIPAGAREILIEEVAEAANFLALRSeDPDKYFLNGGWTIQ-WNGDYRVAGTTFTYARKGN-W 761
Cdd:pfam05986 1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPaL 79
|
90 100 110
....*....|....*....|....*....|....*
gi 568960639 762 ENLTSPGPTSEPVWIQLLFQ---EKNPGVHYQYTI 793
Cdd:pfam05986 80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFI 114
|
|
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
226-437 |
4.11e-30 |
|
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.
Pssm-ID: 426256 [Multi-domain] Cd Length: 200 Bit Score: 118.94 E-value: 4.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 226 KWVETLVVADSKMVEYHGQPQ--VESYVLTIMNMVAglfhdpSIGNPIHISIVrLIILE---DEEKdLKITHHAEETLKN 300
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTtvVRQRVFQVVNLVN------SIYKELNIRVV-LVGLEiwtDEDK-IDVSGDANDTLRN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 301 FCRWQKNiNIKgddHPQHHDTAILLTRKDLCASmnqpceTLGLSHVSGLCHPQLSCSVSED---TGMPLAFTVAHELGHS 377
Cdd:pfam01421 73 FLKWRQE-YLK---KRKPHDVAQLLSGVEFGGT------TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHN 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 378 FGIQHDGTGNDCESIGKRPFIMSPQLLYDrgIPLTWSRCSREYITRFLDRGWGLCLDDRP 437
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 ... |
449-513 |
2.60e-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: 97.42 E-value: 2.60e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568960639 449 PGVLYDVNHQCRLQYGSHSAYCEDM-DDVCHTLWCSVGT--TCHSKLDAAVDGTSCGKNKWCLKGECV 513
Cdd:pfam17771 1 PGQLYSADEQCRLIFGPGSTFCPNGdEDVCSKLWCSNPGgsTCTTKNLPAADGTPCGNKKWCLNGKCV 68
|
|
| ZnMc_salivary_gland_MPs |
cd04272 |
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
228-433 |
2.11e-19 |
|
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.
Pssm-ID: 239800 Cd Length: 220 Bit Score: 88.56 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 228 VETLVVADSKMVEYHGQ-PQVESYVLTIMNMVAGLFHDpsIGNP-IHISIVRLIILEDEEKDLKITHH------AEETLK 299
Cdd:cd04272 3 PELFVVVDYDHQSEFFSnEQLIRYLAVMVNAANLRYRD--LKSPrIRLLLVGITISKDPDFEPYIHPInygyidAAETLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 300 NFcrwqkNINIKGDDHPQHHDTAILLTRKDLCASMNQPCET--LGLSHVSGLCHpQLSCSVSEDTGMPL--AFTVAHELG 375
Cdd:cd04272 81 NF-----NEYVKKKRDYFNPDVVFLVTGLDMSTYSGGSLQTgtGGYAYVGGACT-ENRVAMGEDTPGSYygVYTMTHELA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 376 HSFGIQHDGTGnDCESIGKRP----------FIMSpqllYDRGIP--LTWSRCSREYITRFLDRGWGLCL 433
Cdd:cd04272 155 HLLGAPHDGSP-PPSWVKGHPgsldcpwddgYIMS----YVVNGErqYRFSQCSQRQIRNVFRRLGASCL 219
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
316-425 |
2.45e-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: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 316 PQHHDTAILLTRKDLcasmnqPCETLGLSHVSGLCHPQLSCSVSEDTGMP---LAFTVAHELGHSFGIQHDGTGNDCESI 392
Cdd:cd00203 49 IDKADIAILVTRQDF------DGGTGGWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAHELGHALGFYHDHDRKDRDDY 122
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 568960639 393 GKRP-----------FIMSPQLL-YDRGIPLTWSRCSREYITRFL 425
Cdd:cd00203 123 PTIDdtlnaedddyySVMSYTKGsFSDGQRKDFSQCDIDQINKLY 167
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
526-578 |
5.11e-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: 67.61 E-value: 5.11e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 568960639 526 WSGWSAWSDCSRSCGVGVRSSERQCTQPVPKNRGKYCVGERKRSQLCNLPACP 578
Cdd:smart00209 1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1485-1540 |
7.25e-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: 7.25e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568960639 1485 WVVGPWGQCSAPCGGGVQRRLVRCVNTqTGLAEEDSDLCSHEAWPESSRPCATEDC 1540
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQK-GGGSIVPDSECSAQKKPPETQSCNLKPC 55
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
224-402 |
5.47e-13 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 69.37 E-value: 5.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 224 KEKWVETLVVADSKMVEYHGQPQVESYVLTIMNMVAGLFHDPSignPIHISIVRLIILEDEEKDlkiTHHAEETLKNFCR 303
Cdd:pfam13688 1 STRTVALLVAADCSYVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCPY---TPPACSTGDSSDR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 304 WQKNINIKGDDHPQHHDTAILLTrkdlcasmNQPCETLGLSHVSGLCHPQLSCSVSEDTGMP--------LAFTVAHELG 375
Cdd:pfam13688 75 LSEFQDFSAWRGTQNDDLAYLFL--------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSGNnvvvstatEWQVFAHEIG 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 568960639 376 HSFGIQHDGT----------GNDCESIGKRpFIMSPQ 402
Cdd:pfam13688 147 HNFGAVHDCDsstssqccppSNSTCPAGGR-YIMNPS 182
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
808-862 |
2.21e-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: 63.24 E-value: 2.21e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568960639 808 WHYGPWSKCTVTCGTGVQRQSLYCM-ERQAGVVAEEYCNTLNRPDERQRkCSEEPC 862
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVqKGGGSIVPDSECSAQKKPPETQS-CNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1378-1433 |
5.35e-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: 5.35e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568960639 1378 WRTGNWSKCSRNCGGGSSTRDVQCVDTRDLRPLRPFHCqPGPTKPPNRQLCGTQPC 1433
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSEC-SAQKKPPETQSCNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
929-977 |
2.41e-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: 57.46 E-value: 2.41e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 568960639 929 WGVGNWSQCSVTCGAGIRQRSVLCI---NNTDVP---CDEAERPITETFCFLQPC 977
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVqkgGGSIVPdseCSAQKKPPETQSCNLKPC 55
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1058-1344 |
2.49e-10 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 65.73 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1058 SYGSFEEPHPDlvdnggwTAPPHIRPTESPSDTPVPTAGALGAEAEDiQGSWSPSPLLSEASYSPPGLEQTSINPLANFL 1137
Cdd:PHA03247 2694 SLTSLADPPPP-------PPTPEPAPHALVSATPLPPGPAAARQASP-ALPAAPAPPAVPAGPATPGGPARPARPPTTAG 2765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1138 TEEDTPMGAPELGFP-SLPWPPASVDDMMTPVGPGNPDellvKEDEQSPPSTPWSDRNKLSTDGNPLGHTSPALPQSPIP 1216
Cdd:PHA03247 2766 PPAPAPPAAPAAGPPrRLTRPAVASLSESRESLPSPWD----PADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPP 2841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1217 TQPSPPSISPTQASPSP--DVVEVSTGWNAAWDPVleadlKPGHVPTD-LRSPGPSGQPQtPNLEGTQSPGLLPTPARET 1293
Cdd:PHA03247 2842 PPGPPPPSLPLGGSVAPggDVRRRPPSRSPAAKPA-----APARPPVRrLARPAVSRSTE-SFALPPDQPERPPQPQAPP 2915
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 568960639 1294 QTNSSKDPEVQPL-QPSLEEDGDPADPLPARNASWQVGNWSQCSTTCGLGAI 1344
Cdd:PHA03247 2916 PPQPQPQPPPPPQpQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGAL 2967
|
|
| ADAMTS_CR_3 |
pfam19236 |
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ... |
584-682 |
8.01e-10 |
|
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: 57.80 E-value: 8.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 584 FRHTQCSQFDGMLYK-----GKLHKW---VPVPNDDNPCELHCRPSNSSNTEKLRDAVVDGTPCYQSRISRD----ICLN 651
Cdd:pfam19236 5 FMSQQCARTDGQPLRsspggASFYHWgaaVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDgtlsLCVL 84
|
90 100 110
....*....|....*....|....*....|.
gi 568960639 652 GICKNVGCDFVIDSGAEEDRCGVCRGDGSTC 682
Cdd:pfam19236 85 GSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1327-1375 |
1.26e-09 |
|
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: 55.54 E-value: 1.26e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 568960639 1327 WQVGNWSQCSTTCGLGAIWRLVSCSSG------NDEDCTLASRPQPARHCHLRPC 1375
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKgggsivPDSECSAQKKPPETQSCNLKPC 55
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1077-1327 |
2.54e-09 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 62.65 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1077 APPHIRPTESPSDTPVPTAGALGAEAEDIQGSWSPSPLLSEASYSPPGLeqtsiNPLANFLTEEDTPMGAPELGFPSLPW 1156
Cdd:PHA03247 2770 APPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAAL-----PPAASPAGPLPPPTSAQPTAPPPPPG 2844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1157 PPASVDDMMTPVGPGNPdeLLVKEDEQSPPSTPWSDRN-----------KLSTDGNPLGHTSPA-LPQSPIPTQPSPPSI 1224
Cdd:PHA03247 2845 PPPPSLPLGGSVAPGGD--VRRRPPSRSPAAKPAAPARppvrrlarpavSRSTESFALPPDQPErPPQPQAPPPPQPQPQ 2922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1225 SPTQASPSPdvvevstgwnaAWDPVLEADLKPGHVPTDLRSPGPSGQPQTPNLeGTQSPGLLPTPARETQTNSSKDPEVQ 1304
Cdd:PHA03247 2923 PPPPPQPQP-----------PPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWL-GALVPGRVAVPRFRVPQPAPSREAPA 2990
|
250 260
....*....|....*....|...
gi 568960639 1305 PLQPSLEEDGDPadplpaRNASW 1327
Cdd:PHA03247 2991 SSTPPLTGHSLS------RVSSW 3007
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
866-922 |
7.70e-09 |
|
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: 53.23 E-value: 7.70e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568960639 866 WWAGEWQPCSRSCGPeGLSRRAVFCIRSMGLDEQRAlelSACEHLPRPLAETPCNRH 922
Cdd:pfam19030 1 WVAGPWGECSVTCGG-GVQTRLVQCVQKGGGSIVPD---SECSAQKKPPETQSCNLK 53
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1065-1326 |
1.02e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 60.72 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1065 PHPDLVDNGGWTAPPHIRPTESPSDTPVPTAGALGAEAEDIQGSWSPSPLLSEASYSPPGLEQTSINPLANFLTEEDTPM 1144
Cdd:PHA03247 2601 PVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPP 2680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1145 GAPELgfPSLPWPPASVDDMMTPVGPGNPDEllvkedeqsPPSTPWSDRNKLSTDGNPLGHTSPALPQSPIP-------- 1216
Cdd:PHA03247 2681 QRPRR--RAARPTVGSLTSLADPPPPPPTPE---------PAPHALVSATPLPPGPAAARQASPALPAAPAPpavpagpa 2749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1217 -----TQPSPPSISPTQASPSPDVVEVSTGWNAAWDPV---LEADLKPGHVPTDLRSPGPSGQPQTPNLEGTQSP-GLLP 1287
Cdd:PHA03247 2750 tpggpARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAvasLSESRESLPSPWDPADPPAAVLAPAAALPPAASPaGPLP 2829
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568960639 1288 TPARETQTNSSKDPEvqPLQPSLEEDGD--PADPLPARNAS 1326
Cdd:PHA03247 2830 PPTSAQPTAPPPPPG--PPPPSLPLGGSvaPGGDVRRRPPS 2868
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1436-1482 |
1.34e-07 |
|
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: 49.76 E-value: 1.34e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 568960639 1436 WYTSSWRECSEACGGGEQQRLVTCPEPG--------LCEESLRPNNSRPCNTHPC 1482
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKGggsivpdsECSAQKKPPETQSCNLKPC 55
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1077-1322 |
1.48e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 56.87 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1077 APPHIRPTE--SPS-DTPVPTAGALGAEAEDIQGSWS-PSP-LLSEASYSPP----------GLEQtsinplanfLTEED 1141
Cdd:PHA03247 2477 APVYRRPAEarFPFaAGAAPDPGGGGPPDPDAPPAPSrLAPaILPDEPVGEPvhprmltwirGLEE---------LASDD 2547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1142 TpmGAPELGFPSLPWPPASVDDMMTPVGPGNPDELLVKEDEQSPPSTPWSDRNKlsTDGNPLGhtSPALPQSPIPTQPSP 1221
Cdd:PHA03247 2548 A--GDPPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPR--APVDDRG--DPRGPAPPSPLPPDT 2621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1222 PSISPTQASPSPDVVEVSTGWNAAWDPVLEADLKPG----HVPTDLRSPGPSGQPQTPnLEGTQSPGLLPTPARETQTNS 1297
Cdd:PHA03247 2622 HAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPApgrvSRPRRARRLGRAAQASSP-PQRPRRRAARPTVGSLTSLAD 2700
|
250 260
....*....|....*....|....*.
gi 568960639 1298 SKDPEVQPL-QPSLEEDGDPADPLPA 1322
Cdd:PHA03247 2701 PPPPPPTPEpAPHALVSATPLPPGPA 2726
|
|
| TSP_1 |
pfam00090 |
Thrombospondin type 1 domain; |
527-577 |
2.83e-07 |
|
Thrombospondin type 1 domain;
Pssm-ID: 459668 [Multi-domain] Cd Length: 49 Bit Score: 48.57 E-value: 2.83e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568960639 527 SGWSAWSDCSRSCGVGVRSSERQCTQPVPKnrGKYCVGERKRSQLCNLPAC 577
Cdd:pfam00090 1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPG--GEPCTGDDIETQACKMDKC 49
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1076-1321 |
5.62e-07 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 54.77 E-value: 5.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1076 TAPPHIR---PTESPSDTPVPTAGALgAEAEDIQGSWSPSPLLSEASYSPPGLEQTSINPLAnfLTEEdtpmgAPELGFP 1152
Cdd:pfam03154 169 TQPPVLQaqsGAASPPSPPPPGTTQA-ATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHT--LIQQ-----TPTLHPQ 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1153 SLPWPPASVDDMMTPVGPgnpdellvkeDEQSPPSTPwsdRNKLSTDGNPLGH---TSPALPQSPIPTQP--SPPSISPT 1227
Cdd:pfam03154 241 RLPSPHPPLQPMTQPPPP----------SQVSPQPLP---QPSLHGQMPPMPHslqTGPSHMQHPVPPQPfpLTPQSSQS 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1228 QASPSPDVVEVSTGWNAAWDPVLEADLKPGHVPTD------------LRSPGPSGQPQTPNLEGTQSPGLLPTPAR-ETQ 1294
Cdd:pfam03154 308 QVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREqplppaplsmphIKPPPTTPIPQLPNPQSHKHPPHLSGPSPfQMN 387
|
250 260
....*....|....*....|....*...
gi 568960639 1295 TNSSKDPEVQPLQpSLEEDGDP-ADPLP 1321
Cdd:pfam03154 388 SNLPPPPALKPLS-SLSTHHPPsAHPPP 414
|
|
| TSP1_spondin |
pfam19028 |
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ... |
527-577 |
1.26e-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: 46.89 E-value: 1.26e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568960639 527 SGWSAWSDCSRSCGVGVRSSERQCTQPvPKNRGKYCvGERKRSQLCNLPAC 577
Cdd:pfam19028 4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPC-PELLERRPCNLPPC 52
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1065-1319 |
1.37e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 53.40 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1065 PHPDLVDNGGWTAPPHIRP--TESPSDTPVPTAGALG----AEAEDIQGSWSPSPLLSE--ASYSPPGLEQTSINPLANF 1136
Cdd:PHA03247 2806 DPPAAVLAPAAALPPAASPagPLPPPTSAQPTAPPPPpgppPPSLPLGGSVAPGGDVRRrpPSRSPAAKPAAPARPPVRR 2885
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1137 L-----TEEDTPMGAPELGFPSLPWPPAsvddmmtPVGPGNPDELLVKEDEQSPPSTPWSDRNKLSTDGNP--------- 1202
Cdd:PHA03247 2886 LarpavSRSTESFALPPDQPERPPQPQA-------PPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPagagepsga 2958
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1203 -----LGHTSPALPQSPIPTQPSPPSISPTQASPSPDVVEVSTGWNAAWDPVLEADLKPGHVPTDLRS---PGPSGQPQT 1274
Cdd:PHA03247 2959 vpqpwLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSLKQtlwPPDDTEDSD 3038
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 568960639 1275 PNLEGTQSPGLLPTPARETQTNSSKDPEVQPLQPSLEEDGDPADP 1319
Cdd:PHA03247 3039 ADSLFDSDSERSDLEALDPLPPEPHDPFAHEPDPATPEAGARESP 3083
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
1076-1322 |
4.75e-06 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 51.08 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1076 TAPphIRPTES-----PSDTPVPTAGALGAEAEDI-QGSWSPSPLLSEASYSPPGLEQTSINPLANFLTEED-TPMGAPe 1148
Cdd:PLN03209 310 TAP--LTPMEEllakiPSQRVPPKESDAADGPKPVpTKPVTPEAPSPPIEEEPPQPKAVVPRPLSPYTAYEDlKPPTSP- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1149 lgfpsLPWPPASVDDMMTPVgpgnpdELLVKEDEQSPPSTPWSDRNKLSTDGNPL-----GHTSPAL-------PQSPIP 1216
Cdd:PLN03209 387 -----IPTPPSSSPASSKSV------DAVAKPAEPDVVPSPGSASNVPEVEPAQVeakktRPLSPYAryedlkpPTSPSP 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1217 TQPS---PPSISPTQASPSPDVVEVSTGWNAAWDP----------VLEADLKPGHVPTDLrSPGPSGQPQTPNLEGTQSP 1283
Cdd:PLN03209 456 TAPTgvsPSVSSTSSVPAVPDTAPATAATDAAAPPpanmrplspyAVYDDLKPPTSPSPA-APVGKVAPSSTNEVVKVGN 534
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568960639 1284 GLLPTPARETQTNssKDPEVQPLQP--SLEEDGDPADPLPA 1322
Cdd:PLN03209 535 SAPPTALADEQHH--AQPKPRPLSPytMYEDLKPPTSPTPS 573
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1006-1291 |
1.02e-05 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 50.54 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1006 PNQLAPRPSPASSPKPVSISNAIDEEELdPPGPvfvddfyydynfinfhEDLSYGSFEEPHPdlvdngGWTAPPHIRPTE 1085
Cdd:pfam03154 248 PLQPMTQPPPPSQVSPQPLPQPSLHGQM-PPMP----------------HSLQTGPSHMQHP------VPPQPFPLTPQS 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1086 SPSDTPVPTAGALGAEAEdiQGSWSPSPLLSEASYSPPgLEQ-----------------TSINPLANFLTEEDTP--MGA 1146
Cdd:pfam03154 305 SQSQVPPGPSPAAPGQSQ--QRIHTPPSQSQLQSQQPP-REQplppaplsmphikppptTPIPQLPNPQSHKHPPhlSGP 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1147 PELGFPS-LPWPPA-----SVDDMMTPVGPGNPDELLVKEDE-QSPPSTP--WSDRNKLSTDGN---PLGHTSPALPQSP 1214
Cdd:pfam03154 382 SPFQMNSnLPPPPAlkplsSLSTHHPPSAHPPPLQLMPQSQQlPPPPAQPpvLTQSQSLPPPAAshpPTSGLHQVPSQSP 461
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568960639 1215 IPTQPSPPSISPTQASPSPDVVEVSTGWNAAWDPVLEADLKPGHVPTDLRSPGPSGQPQTPNLEGTQSPGLLPTPAR 1291
Cdd:pfam03154 462 FPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPR 538
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
808-863 |
1.93e-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: 43.34 E-value: 1.93e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568960639 808 WHYGPWSKCTVTCGTGVQRQSLYCmERQAGVVAEEYCNTlnrPDERQRKCSEEPCP 863
Cdd:smart00209 2 SEWSEWSPCSVTCGGGVQTRTRSC-CSPPPQNGGGPCTG---EDVETRACNEQPCP 53
|
|
| Reprolysin_2 |
pfam13574 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
340-422 |
2.12e-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: 47.24 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 340 TLGLSHVSGLCHPQLSCsVSEDTGMPLAFT-------------VAHELGHSFGIQHDGTG--NDCESI----------GK 394
Cdd:pfam13574 86 ELGLAYVGQICQKGASS-PKTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDCDGsqYASSGCernaatsvcsAN 164
|
90 100
....*....|....*....|....*...
gi 568960639 395 RPFIMSPQllYDRGIPLtWSRCSREYIT 422
Cdd:pfam13574 165 GSFIMNPA--SKSNNDL-FSPCSISLIC 189
|
|
| ZnMc_TACE_like |
cd04270 |
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ... |
231-439 |
2.29e-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: 47.75 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 231 LVVADSKMVEYHGQPQVESYVLTIMNMVAGL--------FHDPSIGNpIHISIVRLIIL-EDEEKDLKITHHaeetlkNF 301
Cdd:cd04270 6 LLVADHRFYKYMGRGEEETTINYLISHIDRVddiyrntdWDGGGFKG-IGFQIKRIRIHtTPDEVDPGNKFY------NK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 302 C-------RWQKNINIKgddhpQHHD---TAILLTRKDLcaSMNqpceTLGLSHVS--------GLCHPQLSCSV----S 359
Cdd:cd04270 79 SfpnwgveKFLVKLLLE-----QFSDdvcLAHLFTYRDF--DMG----TLGLAYVGsprdnsagGICEKAYYYSNgkkkY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 360 EDTGMPLAF-------------TVAHELGHSFGIQHDGTGNDC---ESIGKRpFIMSPQLLY-DRGIPLTWSRCSREYIT 422
Cdd:cd04270 148 LNTGLTTTVnygkrvptkesdlVTAHELGHNFGSPHDPDIAECapgESQGGN-YIMYARATSgDKENNKKFSPCSKKSIS 226
|
250
....*....|....*..
gi 568960639 423 RFLDRGWGLCLDDRPSK 439
Cdd:cd04270 227 KVLEVKSNSCFVERSQS 243
|
|
| Reprolysin_3 |
pfam13582 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
271-383 |
3.28e-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: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 271 IHISIVRLIILED-EEKDLKIThhAEETLKNFCRWQKNiNIKGDDHPQHHdtaiLLTRKDlcasmnqPCETLGLSHVSGL 349
Cdd:pfam13582 20 IRLQLAAIIITTSaDTPYTSSD--ALEILDELQEVNDT-RIGQYGYDLGH----LFTGRD-------GGGGGGIAYVGGV 85
|
90 100 110
....*....|....*....|....*....|....*..
gi 568960639 350 CHPQLSCSVSEDTGMP---LAFTVAHELGHSFGIQHD 383
Cdd:pfam13582 86 CNSGSKFGVNSGSGPVgdtGADTFAHEIGHNFGLNHT 122
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
1482-1541 |
8.19e-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: 41.80 E-value: 8.19e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1482 CTQWvvGPWGQCSAPCGGGVQRRLVRCVNtqtGLAEEDSDLCSHEAwpESSRPCATEDCE 1541
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. |
927-977 |
1.07e-04 |
|
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: 41.42 E-value: 1.07e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 568960639 927 STWGvgNWSQCSVTCGAGIRQRSVLCINNTDVPCDEA-ERPITET-FCFLQPC 977
Cdd:smart00209 2 SEWS--EWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPcTGEDVETrACNEQPC 52
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
529-577 |
1.88e-04 |
|
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: 40.90 E-value: 1.88e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 568960639 529 WSA--WSDCSRSCGVGVRSSERQCTQPVPK--NRGKYCVGERK--RSQLCNLPAC 577
Cdd:pfam19030 1 WVAgpWGECSVTCGGGVQTRLVQCVQKGGGsiVPDSECSAQKKppETQSCNLKPC 55
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1067-1319 |
2.10e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.47 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1067 PDLVDNGGWTAPPHIRPTESPSDTPVPTAGALGAEAEDiqGSWSPSplLSEASYSPPGLEQTSINPLANFLTEEDTPMGA 1146
Cdd:PHA03247 258 PPVVGEGADRAPETARGATGPPPPPEAAAPNGAAAPPD--GVWGAA--LAGAPLALPAPPDPPPPAPAGDAEEEDDEDGA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1147 PElgfpslpwppasvddMMTPVGPGNPDELLVKEDEQSPPSTPWSDRNKLSTdgnplGHTSPalPQSPIPT---QPSPPS 1223
Cdd:PHA03247 334 ME---------------VVSPLPRPRQHYPLGFPKRRRPTWTPPSSLEDLSA-----GRHHP--KRASLPTrkrRSARHA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1224 ISPTQASPSPDVVEVSTGWNAAWDPVLEADLKPGHVPTDLRSPGPSGQPQTPNLEGTQSPGLLPTPARETQTNSSKDPEV 1303
Cdd:PHA03247 392 ATPFARGPGGDDQTRPAAPVPASVPTPAPTPVPASAPPPPATPLPSAEPGSDDGPAPPPERQPPAPATEPAPDDPDDATR 471
|
250
....*....|....*.
gi 568960639 1304 QPLQpSLEEDGDPADP 1319
Cdd:PHA03247 472 KALD-ALRERRPPEPP 486
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1178-1395 |
5.91e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.78 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1178 VKEDEQSPPSTPW--SDRNKLSTD--GNPLGHTSPALPQSPIPTQPSPPSISPTQASPSPDvvevSTGWNAAWDPVLEAD 1253
Cdd:PHA03307 64 RFEPPTGPPPGPGteAPANESRSTptWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPA----SPPPSPAPDLSEMLR 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1254 LKPGHVPTDLRSPGPSGQPQTPNLEGTQSPG----LLPTPARETQTNSSKDPEVQPLQPSLEEDGDPA------------ 1317
Cdd:PHA03307 140 PVGSPGPPPAASPPAAGASPAAVASDAASSRqaalPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPrrsspisasass 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568960639 1318 -DPLPARNASWQVGNWSQCSTTcglgaiWRLVSCSSGNDEDCTLaSRPQPARhchlRPCAAWRTGNWSKCSRNCGGGSS 1395
Cdd:PHA03307 220 pAPAPGRSAADDAGASSSDSSS------SESSGCGWGPENECPL-PRPAPIT----LPTRIWEASGWNGPSSRPGPASS 287
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1065-1236 |
7.09e-04 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 44.37 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1065 PHPDLVDNGGWTAPPHI---RPTESPSDTPVPTA-GALGAEAEDIQGSWSPSPL--------LSEASYSPPGLEQTSINP 1132
Cdd:pfam03154 362 PIPQLPNPQSHKHPPHLsgpSPFQMNSNLPPPPAlKPLSSLSTHHPPSAHPPPLqlmpqsqqLPPPPAQPPVLTQSQSLP 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960639 1133 L--ANFLTEEDTPMGAPELGFPSLPWPPASVDDMMTPVGP---GNPDELLVKEDEQSPPSTPWSDRNKLSTDGNPLGHTS 1207
Cdd:pfam03154 442 PpaASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPptsTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKE 521
|
170 180
....*....|....*....|....*....
gi 568960639 1208 PALPQSPIPTQPSPPSISPtqaSPSPDVV 1236
Cdd:pfam03154 522 EALDEAEEPESPPPPPRSP---SPEPTVV 547
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
1378-1433 |
4.87e-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: 4.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568960639 1378 WRTGNWSKCSRNCGGGSSTRDVQCVDtrdlrPLRPFHCQPGPTKPPNRQLCGTQPC 1433
Cdd:smart00209 2 SEWSEWSPCSVTCGGGVQTRTRSCCS-----PPPQNGGGPCTGEDVETRACNEQPC 52
|
|
| TSP_1 |
pfam00090 |
Thrombospondin type 1 domain; |
934-952 |
7.06e-03 |
|
Thrombospondin type 1 domain;
Pssm-ID: 459668 [Multi-domain] Cd Length: 49 Bit Score: 36.24 E-value: 7.06e-03
|
| TSP1_spondin |
pfam19028 |
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ... |
1435-1482 |
7.60e-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: 36.10 E-value: 7.60e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 568960639 1435 PWytSSWRECSEACGGGEQQR---LVTCPEPG--LCEESLRpnnSRPCNTHPC 1482
Cdd:pfam19028 5 EW--SEWSECSVTCGGGVQTRtrtVIVEPQNGgrPCPELLE---RRPCNLPPC 52
|
|
| TSP1_CCN |
pfam19035 |
CCN3 Nov like TSP1 domain; This entry represents a sub-type of TSP1 domains found in ... |
932-977 |
7.68e-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: 35.77 E-value: 7.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 568960639 932 GNWSQCSVTCGAGIRQRsvlcINNTDVPCdeaeRPITET-FCFLQPC 977
Cdd:pfam19035 6 TEWSPCSKTCGMGVSTR----VSNDNAEC----KLVTETrLCQLRPC 44
|
|
| |
