|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
223-431 |
6.91e-114 |
|
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: 358.09 E-value: 6.91e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 223 KWVETLVVADSKMVEYHGQPQVESYVLTIMNMVAGLYHDPSIGNPIHITVVRLIILEDEEKDLKITHHADDTLKNFCRWQ 302
Cdd:cd04273 1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 303 KNVNMKGDDHPQHHDTAILLTRKDLCaTMNHPCETLGLSHVAGLCHPQLSCSVSEDTGLPLAFTVAHELGHSFGIQHDGT 382
Cdd:cd04273 81 KKLNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564364869 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 |
5.04e-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: 5.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 34 DIVHPVRVDAGgsflsyelwpRVLRKRDVSAAQASSAFYQLQYQGRELLFNLTTNPYLLAPGFVSEIRRRSNLSNVHIQT 113
Cdd:pfam01562 1 EVVIPVRLDPS----------RRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPV 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564364869 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 |
2.07e-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: 2.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 681 TVSRTFKEAEGMGYVDVGLIPAGAREILIEEVAEAANFLALRSeDPDKYFLNGGWTIQ-WNGDYQVAGTTFTYTRKGN-W 758
Cdd:pfam05986 1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPaL 79
|
90 100 110
....*....|....*....|....*....|....*
gi 564364869 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 |
5.07e-25 |
|
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: 99.73 E-value: 5.07e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564364869 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 |
2.36e-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: 68.77 E-value: 2.36e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 564364869 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 ... |
1499-1554 |
3.65e-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: 68.25 E-value: 3.65e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 564364869 1499 WVVGPWGQCSAPCGGGVQRRLVKCVNTqTGLAEEDSDLCSHEAWPESSRPCATEDC 1554
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 |
5.14e-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: 67.86 E-value: 5.14e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 564364869 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 ... |
1392-1447 |
4.42e-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: 62.47 E-value: 4.42e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 564364869 1392 WRAGNWSKCSRNCGGGSATRDVQCVDTRDLRPLRPFHCqPGPTKPPTRQLCGTQPC 1447
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSEC-SAQKKPPETQSCNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1341-1389 |
2.84e-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: 57.08 E-value: 2.84e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 564364869 1341 WQVGNWSQCSTTCGLGAIWRLVRCSSG------NDEDCTLSSRPQPARHCHLRPC 1389
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKgggsivPDSECSAQKKPPETQSCNLKPC 55
|
|
| PHA03247 super family |
cl33720 |
large tegument protein UL36; Provisional |
1035-1329 |
7.90e-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: 64.19 E-value: 7.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1035 PPHIRPTEPPSDSPVPTAGAPGAEEEGIQGSWSPSPllseasHSPPVLLENTPVNPLANFLTEEESPIGAPELGLPSVSW 1114
Cdd:PHA03247 2771 PPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPAD------PPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPG 2844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1115 PPASVDGMVTSVAPGNPdeLLVREDTQSQPSTPWSDRN----KLSKDGNPLGPTSPALPKSPF--PTQPSSPSNSTTQAS 1188
Cdd:PHA03247 2845 PPPPSLPLGGSVAPGGD--VRRRPPSRSPAAKPAAPARppvrRLARPAVSRSTESFALPPDQPerPPQPQAPPPPQPQPQ 2922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1189 LSPDAVEvstgwnvalDPVLEADLKPvHGELRPTVEMASPPLPSM--------ATVPG----VWGRESPLEPG--TSTSS 1254
Cdd:PHA03247 2923 PPPPPQP---------QPPPPPPPRP-QPPLAPTTDPAGAGEPSGavpqpwlgALVPGrvavPRFRVPQPAPSreAPASS 2992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1255 TPGLSSQNLKTLTVPGTFL-LTAPTDPGLLDQIQTPH----TEGTQS-------PGLLPRPAQETQTNSSKDPAVQPLQP 1322
Cdd:PHA03247 2993 TPPLTGHSLSRVSSWASSLaLHEETDPPPVSLKQTLWppddTEDSDAdslfdsdSERSDLEALDPLPPEPHDPFAHEPDP 3072
|
....*..
gi 564364869 1323 SLVEDGA 1329
Cdd:PHA03247 3073 ATPEAGA 3079
|
|
| ADAMTS_CR_3 super family |
cl41950 |
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ... |
581-679 |
2.66e-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: 53.56 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 581 FRHTQCSQFDSMLYK-----GKLHKW---VPVLNDENPCELHCRPFNYSNREKLRDAVMDGTPCYQGRISRD----ICID 648
Cdd:pfam19236 5 FMSQQCARTDGQPLRsspggASFYHWgaaVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDgtlsLCVL 84
|
90 100 110
....*....|....*....|....*....|.
gi 564364869 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 ... |
1450-1496 |
3.06e-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: 51.30 E-value: 3.06e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 564364869 1450 WYTSSWRECSEACGGGEQQRLVTCPEPG--------LCEESLRPNNTRPCNTHPC 1496
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 |
6.13e-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: 50.53 E-value: 6.13e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 564364869 863 WWVGDWQPCSRSCGpGGFFRRAVFCTRSVGLDEQRalePSACGHLPRPLAEIPC 916
Cdd:pfam19030 1 WVAGPWGECSVTCG-GGVQTRLVQCVQKGGGSIVP---DSECSAQKKPPETQSC 50
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
223-431 |
6.91e-114 |
|
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: 358.09 E-value: 6.91e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 223 KWVETLVVADSKMVEYHGQPQVESYVLTIMNMVAGLYHDPSIGNPIHITVVRLIILEDEEKDLKITHHADDTLKNFCRWQ 302
Cdd:cd04273 1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 303 KNVNMKGDDHPQHHDTAILLTRKDLCaTMNHPCETLGLSHVAGLCHPQLSCSVSEDTGLPLAFTVAHELGHSFGIQHDGT 382
Cdd:cd04273 81 KKLNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564364869 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 |
5.04e-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: 5.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 34 DIVHPVRVDAGgsflsyelwpRVLRKRDVSAAQASSAFYQLQYQGRELLFNLTTNPYLLAPGFVSEIRRRSNLSNVHIQT 113
Cdd:pfam01562 1 EVVIPVRLDPS----------RRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPV 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564364869 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 |
2.07e-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: 2.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 681 TVSRTFKEAEGMGYVDVGLIPAGAREILIEEVAEAANFLALRSeDPDKYFLNGGWTIQ-WNGDYQVAGTTFTYTRKGN-W 758
Cdd:pfam05986 1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPaL 79
|
90 100 110
....*....|....*....|....*....|....*
gi 564364869 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 |
3.02e-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: 3.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 223 KWVETLVVADSKMVEYHGQPQ--VESYVLTIMNMVAGLYhdpsigNPIHITVVrLIILE---DEEKdLKITHHADDTLKN 297
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTtvVRQRVFQVVNLVNSIY------KELNIRVV-LVGLEiwtDEDK-IDVSGDANDTLRN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 298 FCRWQKNVNMKgddhPQHHDTAILLTRKDLCATmnhpceTLGLSHVAGLCHPQLSCSVSED---TGLPLAFTVAHELGHS 374
Cdd:pfam01421 73 FLKWRQEYLKK----RKPHDVAQLLSGVEFGGT------TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHN 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 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 |
5.07e-25 |
|
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: 99.73 E-value: 5.07e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564364869 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 |
2.36e-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: 68.77 E-value: 2.36e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 564364869 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 ... |
1499-1554 |
3.65e-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: 68.25 E-value: 3.65e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 564364869 1499 WVVGPWGQCSAPCGGGVQRRLVKCVNTqTGLAEEDSDLCSHEAWPESSRPCATEDC 1554
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 |
5.14e-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: 67.86 E-value: 5.14e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 564364869 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 ... |
1392-1447 |
4.42e-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: 62.47 E-value: 4.42e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 564364869 1392 WRAGNWSKCSRNCGGGSATRDVQCVDTRDLRPLRPFHCqPGPTKPPTRQLCGTQPC 1447
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSEC-SAQKKPPETQSCNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1341-1389 |
2.84e-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: 57.08 E-value: 2.84e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 564364869 1341 WQVGNWSQCSTTCGLGAIWRLVRCSSG------NDEDCTLSSRPQPARHCHLRPC 1389
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKgggsivPDSECSAQKKPPETQSCNLKPC 55
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1035-1329 |
7.90e-10 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 64.19 E-value: 7.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1035 PPHIRPTEPPSDSPVPTAGAPGAEEEGIQGSWSPSPllseasHSPPVLLENTPVNPLANFLTEEESPIGAPELGLPSVSW 1114
Cdd:PHA03247 2771 PPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPAD------PPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPG 2844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1115 PPASVDGMVTSVAPGNPdeLLVREDTQSQPSTPWSDRN----KLSKDGNPLGPTSPALPKSPF--PTQPSSPSNSTTQAS 1188
Cdd:PHA03247 2845 PPPPSLPLGGSVAPGGD--VRRRPPSRSPAAKPAAPARppvrRLARPAVSRSTESFALPPDQPerPPQPQAPPPPQPQPQ 2922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1189 LSPDAVEvstgwnvalDPVLEADLKPvHGELRPTVEMASPPLPSM--------ATVPG----VWGRESPLEPG--TSTSS 1254
Cdd:PHA03247 2923 PPPPPQP---------QPPPPPPPRP-QPPLAPTTDPAGAGEPSGavpqpwlgALVPGrvavPRFRVPQPAPSreAPASS 2992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1255 TPGLSSQNLKTLTVPGTFL-LTAPTDPGLLDQIQTPH----TEGTQS-------PGLLPRPAQETQTNSSKDPAVQPLQP 1322
Cdd:PHA03247 2993 TPPLTGHSLSRVSSWASSLaLHEETDPPPVSLKQTLWppddTEDSDAdslfdsdSERSDLEALDPLPPEPHDPFAHEPDP 3072
|
....*..
gi 564364869 1323 SLVEDGA 1329
Cdd:PHA03247 3073 ATPEAGA 3079
|
|
| ADAMTS_CR_3 |
pfam19236 |
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ... |
581-679 |
2.66e-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: 53.56 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 581 FRHTQCSQFDSMLYK-----GKLHKW---VPVLNDENPCELHCRPFNYSNREKLRDAVMDGTPCYQGRISRD----ICID 648
Cdd:pfam19236 5 FMSQQCARTDGQPLRsspggASFYHWgaaVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDgtlsLCVL 84
|
90 100 110
....*....|....*....|....*....|.
gi 564364869 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 ... |
1450-1496 |
3.06e-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: 51.30 E-value: 3.06e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 564364869 1450 WYTSSWRECSEACGGGEQQRLVTCPEPG--------LCEESLRPNNTRPCNTHPC 1496
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKGggsivpdsECSAQKKPPETQSCNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
863-916 |
6.13e-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: 50.53 E-value: 6.13e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 564364869 863 WWVGDWQPCSRSCGpGGFFRRAVFCTRSVGLDEQRalePSACGHLPRPLAEIPC 916
Cdd:pfam19030 1 WVAGPWGECSVTCG-GGVQTRLVQCVQKGGGSIVP---DSECSAQKKPPETQSC 50
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
805-860 |
4.05e-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: 45.27 E-value: 4.05e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 564364869 805 WHYGPWSKCPVTCGTGVQRQSLYCmEKQAGIVDEGHCDHlsrPRDRKRKCNEEPCP 860
Cdd:smart00209 2 SEWSEWSPCSVTCGGGVQTRTRSC-CSPPPQNGGGPCTG---EDVETRACNEQPCP 53
|
|
| TSP1_spondin |
pfam19028 |
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ... |
524-574 |
4.65e-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: 45.35 E-value: 4.65e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 564364869 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. |
1496-1555 |
3.45e-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: 42.96 E-value: 3.45e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1496 CTQWvvGPWGQCSAPCGGGVQRRLVKCVNtqtGLAEEDSDLCSHEAwpESSRPCATEDCE 1555
Cdd:smart00209 1 WSEW--SEWSPCSVTCGGGVQTRTRSCCS---PPPQNGGGPCTGED--VETRACNEQPCP 53
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
1030-1313 |
1.19e-04 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 46.83 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1030 GGQTVPPHIRPTEPPSDSPVPTAGAP-GAEEEGIQGSWSPSPLLSEAS--HSPPVLLENTPVNPLANFLTEEESPIGAPE 1106
Cdd:pfam05109 484 GASPVTPSPSPRDNGTESKAPDMTSPtSAVTTPTPNATSPTPAVTTPTpnATSPTLGKTSPTSAVTTPTPNATSPTPAVT 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1107 LGLPSVSWPPASVDGMVTSVAPGNPDEllvrEDTQSQPSTPWSDRNKLSKDGNPLGPTSPALPKSPFPT----QPSSPSN 1182
Cdd:pfam05109 564 TPTPNATIPTLGKTSPTSAVTTPTPNA----TSPTVGETSPQANTTNHTLGGTSSTPVVTSPPKNATSAvttgQHNITSS 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1183 STTQASLSPDAVE----VSTGWNVALDPVLEADLKPVHGELRPTVEMASPPLPSMATvpgvwGRESPLEPGTSTSSTPGL 1258
Cdd:pfam05109 640 STSSMSLRPSSISetlsPSTSDNSTSHMPLLTSAHPTGGENITQVTPASTSTHHVST-----SSPAPRPGTTSQASGPGN 714
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 564364869 1259 SSqnlkTLTVPGTFLLTAPTDPGLLDQIQTPHTEGTQSPGLLPRPAQETQTNSSK 1313
Cdd:pfam05109 715 SS----TSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTSTGGKANSTTGGK 765
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
1452-1496 |
3.38e-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: 37.18 E-value: 3.38e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 564364869 1452 TSSWRECSEACGGGEQQRLVTC--PEPGLCEESLRPNN--TRPCNTHPC 1496
Cdd:smart00209 4 WSEWSPCSVTCGGGVQTRTRSCcsPPPQNGGGPCTGEDveTRACNEQPC 52
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
1395-1447 |
3.80e-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: 37.18 E-value: 3.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 564364869 1395 GNWSKCSRNCGGGSATRDVQCVDtrdlrPLRPFHCQPGPTKPPTRQLCGTQPC 1447
Cdd:smart00209 5 SEWSPCSVTCGGGVQTRTRSCCS-----PPPQNGGGPCTGEDVETRACNEQPC 52
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
477-511 |
7.34e-03 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 38.50 E-value: 7.34e-03
10 20 30
....*....|....*....|....*....|....*....
gi 564364869 477 LWCsVGTTCHSKMDAAV----DGTSCGKNKWCLNGECVP 511
Cdd:smart00608 99 LVC-WSLDYHLGTDPDIgmvkDGTKCGPGKVCINGQCVD 136
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
223-431 |
6.91e-114 |
|
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: 358.09 E-value: 6.91e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 223 KWVETLVVADSKMVEYHGQPQVESYVLTIMNMVAGLYHDPSIGNPIHITVVRLIILEDEEKDLKITHHADDTLKNFCRWQ 302
Cdd:cd04273 1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 303 KNVNMKGDDHPQHHDTAILLTRKDLCaTMNHPCETLGLSHVAGLCHPQLSCSVSEDTGLPLAFTVAHELGHSFGIQHDGT 382
Cdd:cd04273 81 KKLNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564364869 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 |
5.04e-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: 5.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 34 DIVHPVRVDAGgsflsyelwpRVLRKRDVSAAQASSAFYQLQYQGRELLFNLTTNPYLLAPGFVSEIRRRSNLSNVHIQT 113
Cdd:pfam01562 1 EVVIPVRLDPS----------RRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPV 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564364869 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 |
4.73e-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: 4.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 225 VETLVVADSKMVEYHgQPQVES---YVLTIMNMVAGLYHDPSIGNPIHITVVRLIILEDEEKDLKITHHADDTLKNFCRW 301
Cdd:cd04267 3 IELVVVADHRMVSYF-NSDENIlqaYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSFW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 302 QKNVnmkgddhPQHHDTAILLTRKDLCAtmnhpCETLGLSHVAGLCHPQLSCSVSEDTGLPL--AFTVAHELGHSFGIQH 379
Cdd:cd04267 82 RAEG-------PIRHDNAVLLTAQDFIE-----GDILGLAYVGSMCNPYSSVGVVEDTGFTLltALTMAHELGHNLGAEH 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 564364869 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 |
6.55e-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: 6.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 223 KWVETLVVADSKMVEYHGQ--PQVESYVLTIMNMVAGLYHdpsignPIHITVVrLIILE---DEEKdLKITHHADDTLKN 297
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSnlSKVRQRVIEIVNIVDSIYR------PLNIRVV-LVGLEiwtDKDK-ISVSGDAGETLNR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 298 FCRWQKNVNmkgdDHPQHHDTAILLTRKDLCATmnhpceTLGLSHVAGLCHPQLSCSVSEDTG---LPLAFTVAHELGHS 374
Cdd:cd04269 73 FLDWKRSNL----LPRKPHDNAQLLTGRDFDGN------TVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHN 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 564364869 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 |
2.07e-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: 2.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 681 TVSRTFKEAEGMGYVDVGLIPAGAREILIEEVAEAANFLALRSeDPDKYFLNGGWTIQ-WNGDYQVAGTTFTYTRKGN-W 758
Cdd:pfam05986 1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPaL 79
|
90 100 110
....*....|....*....|....*....|....*
gi 564364869 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 |
3.02e-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: 3.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 223 KWVETLVVADSKMVEYHGQPQ--VESYVLTIMNMVAGLYhdpsigNPIHITVVrLIILE---DEEKdLKITHHADDTLKN 297
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTtvVRQRVFQVVNLVNSIY------KELNIRVV-LVGLEiwtDEDK-IDVSGDANDTLRN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 298 FCRWQKNVNMKgddhPQHHDTAILLTRKDLCATmnhpceTLGLSHVAGLCHPQLSCSVSED---TGLPLAFTVAHELGHS 374
Cdd:pfam01421 73 FLKWRQEYLKK----RKPHDVAQLLSGVEFGGT------TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHN 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 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 |
5.07e-25 |
|
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: 99.73 E-value: 5.07e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564364869 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 |
6.70e-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: 6.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 225 VETLVVADSKMVEYHGQ-PQVESYVLTIMNMVAGLYHDpsIGNP-IHITVVRLIILEDEEKDLKITHHADD------TLK 296
Cdd:cd04272 3 PELFVVVDYDHQSEFFSnEQLIRYLAVMVNAANLRYRD--LKSPrIRLLLVGITISKDPDFEPYIHPINYGyidaaeTLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 297 NFcrwqkNVNMKGDDHPQHHDTAILLTRKDLCATMNHPCET--LGLSHVAGLCHpQLSCSVSEDTGLPL--AFTVAHELG 372
Cdd:cd04272 81 NF-----NEYVKKKRDYFNPDVVFLVTGLDMSTYSGGSLQTgtGGYAYVGGACT-ENRVAMGEDTPGSYygVYTMTHELA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 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 |
9.11e-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: 9.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 313 PQHHDTAILLTRKDlcatmnHPCETLGLSHVAGLCHPQLSCSVSEDTGLP---LAFTVAHELGHSFGIQHDGTGNDCESI 389
Cdd:cd00203 49 IDKADIAILVTRQD------FDGGTGGWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAHELGHALGFYHDHDRKDRDDY 122
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 564364869 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 |
2.36e-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: 68.77 E-value: 2.36e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 564364869 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 ... |
1499-1554 |
3.65e-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: 68.25 E-value: 3.65e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 564364869 1499 WVVGPWGQCSAPCGGGVQRRLVKCVNTqTGLAEEDSDLCSHEAWPESSRPCATEDC 1554
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 |
5.14e-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: 67.86 E-value: 5.14e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 564364869 805 WHYGPWSKCPVTCGTGVQRQSLYCMEKQAGIVDEGH-CDHLSRPRDRKRkCNEEPC 859
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSeCSAQKKPPETQS-CNLKPC 55
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
221-399 |
5.02e-13 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 69.37 E-value: 5.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 221 KEKWVETLVVADSKMVEYHGQPQVESYVLTIMNMVAGLYHDPSignPIHITVVRLIILEDEEKDLKI---THHADDTLKN 297
Cdd:pfam13688 1 STRTVALLVAADCSYVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCPYTPPacsTGDSSDRLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 298 FCRWQKNvnmkgdDHPQHHDTAILLTRKDlcatmnhpCETLGLSHVAGLCHPQLSCSVSEDTGLP--------LAFTVAH 369
Cdd:pfam13688 78 FQDFSAW------RGTQNDDLAYLFLMTN--------CSGGGLAWLGQLCNSGSAGSVSTRVSGNnvvvstatEWQVFAH 143
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 564364869 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 ... |
1392-1447 |
4.42e-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: 62.47 E-value: 4.42e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 564364869 1392 WRAGNWSKCSRNCGGGSATRDVQCVDTRDLRPLRPFHCqPGPTKPPTRQLCGTQPC 1447
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSEC-SAQKKPPETQSCNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1341-1389 |
2.84e-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: 57.08 E-value: 2.84e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 564364869 1341 WQVGNWSQCSTTCGLGAIWRLVRCSSG------NDEDCTLSSRPQPARHCHLRPC 1389
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKgggsivPDSECSAQKKPPETQSCNLKPC 55
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1035-1329 |
7.90e-10 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 64.19 E-value: 7.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1035 PPHIRPTEPPSDSPVPTAGAPGAEEEGIQGSWSPSPllseasHSPPVLLENTPVNPLANFLTEEESPIGAPELGLPSVSW 1114
Cdd:PHA03247 2771 PPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPAD------PPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPG 2844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1115 PPASVDGMVTSVAPGNPdeLLVREDTQSQPSTPWSDRN----KLSKDGNPLGPTSPALPKSPF--PTQPSSPSNSTTQAS 1188
Cdd:PHA03247 2845 PPPPSLPLGGSVAPGGD--VRRRPPSRSPAAKPAAPARppvrRLARPAVSRSTESFALPPDQPerPPQPQAPPPPQPQPQ 2922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1189 LSPDAVEvstgwnvalDPVLEADLKPvHGELRPTVEMASPPLPSM--------ATVPG----VWGRESPLEPG--TSTSS 1254
Cdd:PHA03247 2923 PPPPPQP---------QPPPPPPPRP-QPPLAPTTDPAGAGEPSGavpqpwlgALVPGrvavPRFRVPQPAPSreAPASS 2992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1255 TPGLSSQNLKTLTVPGTFL-LTAPTDPGLLDQIQTPH----TEGTQS-------PGLLPRPAQETQTNSSKDPAVQPLQP 1322
Cdd:PHA03247 2993 TPPLTGHSLSRVSSWASSLaLHEETDPPPVSLKQTLWppddTEDSDAdslfdsdSERSDLEALDPLPPEPHDPFAHEPDP 3072
|
....*..
gi 564364869 1323 SLVEDGA 1329
Cdd:PHA03247 3073 ATPEAGA 3079
|
|
| ADAMTS_CR_3 |
pfam19236 |
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ... |
581-679 |
2.66e-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: 53.56 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 581 FRHTQCSQFDSMLYK-----GKLHKW---VPVLNDENPCELHCRPFNYSNREKLRDAVMDGTPCYQGRISRD----ICID 648
Cdd:pfam19236 5 FMSQQCARTDGQPLRsspggASFYHWgaaVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDgtlsLCVL 84
|
90 100 110
....*....|....*....|....*....|.
gi 564364869 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 ... |
1450-1496 |
3.06e-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: 51.30 E-value: 3.06e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 564364869 1450 WYTSSWRECSEACGGGEQQRLVTCPEPG--------LCEESLRPNNTRPCNTHPC 1496
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKGggsivpdsECSAQKKPPETQSCNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
863-916 |
6.13e-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: 50.53 E-value: 6.13e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 564364869 863 WWVGDWQPCSRSCGpGGFFRRAVFCTRSVGLDEQRalePSACGHLPRPLAEIPC 916
Cdd:pfam19030 1 WVAGPWGECSVTCG-GGVQTRLVQCVQKGGGSIVP---DSECSAQKKPPETQSC 50
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1022-1336 |
2.70e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 52.63 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1022 SHSDLVDIGGQTVPPHIRPTEPPSDSPVPTAGAPGaeeegiqGSWSPSPLLSEASHSPPV-----LLENTPVNPLANFLT 1096
Cdd:PHA03247 2694 SLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAA-------RQASPALPAAPAPPAVPAgpatpGGPARPARPPTTAGP 2766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1097 EEESPIGAPELGLP-SVSWPPASVDGMVTSVAPGNPDEllvrEDTQSQPSTPWSDRNKLSKDGNPLGPTSPALPKSPFPT 1175
Cdd:PHA03247 2767 PAPAPPAAPAAGPPrRLTRPAVASLSESRESLPSPWDP----ADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPP 2842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1176 QPSSPSNSTTQASLSPdavevstGWNVALDPVLEADLKPVHGELRPTVEMASPPLPSMATVPGVWGRESPLEPGTSTSST 1255
Cdd:PHA03247 2843 PGPPPPSLPLGGSVAP-------GGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPP 2915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1256 PGLSSQNLKTLTVPGtfllTAPTDPGLLDQIQTPHTEGTQSPGllPRPAQETQTNSSKDPAVQPLQPSLVEDGAPTDLLP 1335
Cdd:PHA03247 2916 PPQPQPQPPPPPQPQ----PPPPPPPRPQPPLAPTTDPAGAGE--PSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAP 2989
|
.
gi 564364869 1336 A 1336
Cdd:PHA03247 2990 A 2990
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
805-860 |
4.05e-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: 45.27 E-value: 4.05e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 564364869 805 WHYGPWSKCPVTCGTGVQRQSLYCmEKQAGIVDEGHCDHlsrPRDRKRKCNEEPCP 860
Cdd:smart00209 2 SEWSEWSPCSVTCGGGVQTRTRSC-CSPPPQNGGGPCTG---EDVETRACNEQPCP 53
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
961-1336 |
4.59e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.86 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 961 PHQPVPRPS----------PASSPKPVSISNAIDEEDPELDPPGPvfvddfyydynfinfhedlsygsfeeshsdlvdig 1030
Cdd:PHA03247 2570 PPRPAPRPSepavtsrarrPDAPPQSARPRAPVDDRGDPRGPAPP----------------------------------- 2614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1031 gQTVPPHIRPTEPPSDSPVPTA-----GAPGAEEEGIQGSWSPSP----------LLSEASHS--------PPVLleNTP 1087
Cdd:PHA03247 2615 -SPLPPDTHAPDPPPPSPSPAAnepdpHPPPTVPPPERPRDDPAPgrvsrprrarRLGRAAQAssppqrprRRAA--RPT 2691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1088 VNPLANFL---TEEESPIGAPELGLPSVSWPPASVDGMVTSVA-PGNPdellVREDTQSQPSTPWSDrNKLSKDGNPLGP 1163
Cdd:PHA03247 2692 VGSLTSLAdppPPPPTPEPAPHALVSATPLPPGPAAARQASPAlPAAP----APPAVPAGPATPGGP-ARPARPPTTAGP 2766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1164 TSPALPKSPfPTQPSSPSNSTTQASLSPDAVEVSTGWnvalDPVLEADLKPVHGELRPTVEMASPPLPSMATVPGVwgrE 1243
Cdd:PHA03247 2767 PAPAPPAAP-AAGPPRRLTRPAVASLSESRESLPSPW----DPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPT---A 2838
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1244 SPLEPGTSTSSTPglssqnLKTLTVP-GTFLLTAPTDPglldQIQTPHTEGTQSPGLLPRPAQETQTNS---SKDPAVQP 1319
Cdd:PHA03247 2839 PPPPPGPPPPSLP------LGGSVAPgGDVRRRPPSRS----PAAKPAAPARPPVRRLARPAVSRSTESfalPPDQPERP 2908
|
410
....*....|....*..
gi 564364869 1320 LQPSLVEDGAPTDLLPA 1336
Cdd:PHA03247 2909 PQPQAPPPPQPQPQPPP 2925
|
|
| TSP1_spondin |
pfam19028 |
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ... |
524-574 |
4.65e-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: 45.35 E-value: 4.65e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 564364869 524 SGWSAWSVCSRSCGVGVRSSERQCTQPvPKNKGKYCVGERKRyRLCNLQAC 574
Cdd:pfam19028 4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELLER-RPCNLPPC 52
|
|
| TSP_1 |
pfam00090 |
Thrombospondin type 1 domain; |
524-574 |
4.72e-06 |
|
Thrombospondin type 1 domain;
Pssm-ID: 459668 [Multi-domain] Cd Length: 49 Bit Score: 45.10 E-value: 4.72e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 564364869 524 SGWSAWSVCSRSCGVGVRSSERQCTQPVPknKGKYCVGERKRYRLCNLQAC 574
Cdd:pfam00090 1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
|
|
| Reprolysin_2 |
pfam13574 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
337-419 |
1.33e-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: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 337 TLGLSHVAGLCHPQLSCsVSEDTGLPLAFT-------------VAHELGHSFGIQHDGTG--NDCESI----------GK 391
Cdd:pfam13574 86 ELGLAYVGQICQKGASS-PKTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDCDGsqYASSGCernaatsvcsAN 164
|
90 100
....*....|....*....|....*...
gi 564364869 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 |
2.58e-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: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 268 IHITVVRLIILED-EEKDLKIThhADDTLKNFCRWqknvNMKGDDHPQHhDTAILLTRKDlcatmnhPCETLGLSHVAGL 346
Cdd:pfam13582 20 IRLQLAAIIITTSaDTPYTSSD--ALEILDELQEV----NDTRIGQYGY-DLGHLFTGRD-------GGGGGGIAYVGGV 85
|
90 100 110
....*....|....*....|....*....|....*..
gi 564364869 347 CHPQLSCSVSED---TGLPLAFTVAHELGHSFGIQHD 380
Cdd:pfam13582 86 CNSGSKFGVNSGsgpVGDTGADTFAHEIGHNFGLNHT 122
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
1496-1555 |
3.45e-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: 42.96 E-value: 3.45e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1496 CTQWvvGPWGQCSAPCGGGVQRRLVKCVNtqtGLAEEDSDLCSHEAwpESSRPCATEDCE 1555
Cdd:smart00209 1 WSEW--SEWSPCSVTCGGGVQTRTRSCCS---PPPQNGGGPCTGED--VETRACNEQPCP 53
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
986-1339 |
3.51e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 48.78 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 986 EDPelDPPGPV---FV-DDFYYDYNFINFHEDLSYGSFEESHS-----------DLVDIGGQTVPPHIRPTEPPSD-SPV 1049
Cdd:PHA03247 2413 EQP--DPPGPPdvrFVgSEEIEELPFVSPGGDVLAGLAADGDPffartilgapfSLSLLLGELFPGAPVYRRPAEArFPF 2490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1050 PTAGAPGAEEEGIQGSWSPSPllseASHSPPVLLENTP----VNP--LANFLTEEE---SPIGAPELGLPSVSWPPASVD 1120
Cdd:PHA03247 2491 AAGAAPDPGGGGPPDPDAPPA----PSRLAPAILPDEPvgepVHPrmLTWIRGLEElasDDAGDPPPPLPPAAPPAAPDR 2566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1121 GMVTSVAPGNPDELLV--REDTQSQPSTPWSDRNKLSKDGNPLGPTSPA-LPKSPFPTQPSSPSNSttqaslsPDAVEVS 1197
Cdd:PHA03247 2567 SVPPPRPAPRPSEPAVtsRARRPDAPPQSARPRAPVDDRGDPRGPAPPSpLPPDTHAPDPPPPSPS-------PAANEPD 2639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1198 TGWNVALDPVLEADLKPVHGELRPTVEMASPPLPSMATVPGV-WGRES-------------PLEPGTSTSSTPGLSSQNL 1263
Cdd:PHA03247 2640 PHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQrPRRRAarptvgsltsladPPPPPPTPEPAPHALVSAT 2719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1264 KTLTVPGTFLLTAPTDPglLDQIQTPHTEGTQSPGLLPRPAQETQTNSSKDP-----------------AVQPLQPSLVE 1326
Cdd:PHA03247 2720 PLPPGPAAARQASPALP--AAPAPPAVPAGPATPGGPARPARPPTTAGPPAPappaapaagpprrltrpAVASLSESRES 2797
|
410
....*....|...
gi 564364869 1327 DGAPTDLLPAKNA 1339
Cdd:PHA03247 2798 LPSPWDPADPPAA 2810
|
|
| ZnMc_TACE_like |
cd04270 |
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ... |
228-436 |
4.17e-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: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 228 LVVADSKMVEYHGQPQVESYVLTIMNMVAG---LYHDPSIGNP----IHITVVRLIIL-EDEEKDLKITHHAddtlKNFC 299
Cdd:cd04270 6 LLVADHRFYKYMGRGEEETTINYLISHIDRvddIYRNTDWDGGgfkgIGFQIKRIRIHtTPDEVDPGNKFYN----KSFP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 300 RWQKNVNMKGDDHPQHHD---TAILLTRKDLcaTMNhpceTLGLSHVA--------GLCHPQLSCSV----SEDTGLPLA 364
Cdd:cd04270 82 NWGVEKFLVKLLLEQFSDdvcLAHLFTYRDF--DMG----TLGLAYVGsprdnsagGICEKAYYYSNgkkkYLNTGLTTT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 365 F-------------TVAHELGHSFGIQHDGTGNDC---ESIGKRpFIMSPQLLY-DRGIPLTWSRCSREYITRFLDRGWG 427
Cdd:cd04270 156 VnygkrvptkesdlVTAHELGHNFGSPHDPDIAECapgESQGGN-YIMYARATSgDKENNKKFSPCSKKSISKVLEVKSN 234
|
....*....
gi 564364869 428 LCLDDRPSK 436
Cdd:cd04270 235 SCFVERSQS 243
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
1030-1313 |
1.19e-04 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 46.83 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1030 GGQTVPPHIRPTEPPSDSPVPTAGAP-GAEEEGIQGSWSPSPLLSEAS--HSPPVLLENTPVNPLANFLTEEESPIGAPE 1106
Cdd:pfam05109 484 GASPVTPSPSPRDNGTESKAPDMTSPtSAVTTPTPNATSPTPAVTTPTpnATSPTLGKTSPTSAVTTPTPNATSPTPAVT 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1107 LGLPSVSWPPASVDGMVTSVAPGNPDEllvrEDTQSQPSTPWSDRNKLSKDGNPLGPTSPALPKSPFPT----QPSSPSN 1182
Cdd:pfam05109 564 TPTPNATIPTLGKTSPTSAVTTPTPNA----TSPTVGETSPQANTTNHTLGGTSSTPVVTSPPKNATSAvttgQHNITSS 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1183 STTQASLSPDAVE----VSTGWNVALDPVLEADLKPVHGELRPTVEMASPPLPSMATvpgvwGRESPLEPGTSTSSTPGL 1258
Cdd:pfam05109 640 STSSMSLRPSSISetlsPSTSDNSTSHMPLLTSAHPTGGENITQVTPASTSTHHVST-----SSPAPRPGTTSQASGPGN 714
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 564364869 1259 SSqnlkTLTVPGTFLLTAPTDPGLLDQIQTPHTEGTQSPGLLPRPAQETQTNSSK 1313
Cdd:pfam05109 715 SS----TSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTSTGGKANSTTGGK 765
|
|
| MISS |
pfam15822 |
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ... |
1040-1258 |
2.18e-04 |
|
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic MAPK-interacting and spindle-stabilising protein-like proteins. MISS is rich in prolines and has four potential MAPK-phosphorylation sites, a MAPK-docking site, a PEST sequence (PEST motif) and a bipartite nuclear localization signal. The endogenous protein accumulates during mouse meiotic maturation and is found as discrete dots on the MII spindle. MISS is the first example of a physiological MAPK-substrate that is stabilized in MII that specifically regulates MII spindle integrity during the CSF arrest.
Pssm-ID: 318115 [Multi-domain] Cd Length: 238 Bit Score: 44.59 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1040 PTEPPSDSPVPTAGAPGAEEEGIQGSwSPSPLLSeashSPPVLLENTPVNPLANFLteeesPIGAPELGL-PSVswPPas 1118
Cdd:pfam15822 8 PEQSPAKTSAVSNPKPGQPPQGWPGS-NPWNNPS----APPAVPSGLPPSTAPSTV-----PFGPAPTGMyPSI--PL-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364869 1119 vdgmvTSVAPGNPDELLVREDTQSQPSTPWSDrnKLSKDGNPLGPTSPalPKSPFP---------TQPSSPSNSTTQASL 1189
Cdd:pfam15822 74 -----TGPSPGPPAPFPPSGPSCPPPGGPYPA--PTVPGPGPIGPYPT--PNMPFPelprpygapTDPAAAAPSGPWGSM 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564364869 1190 SPDAVEVSTGWNVALDPVLEADLKPVHGELRPTVEMASPPLPSMATVPGVWGRESPLEPGTSTSSTPGL 1258
Cdd:pfam15822 145 SSGPWAPGMGGQYPAPNMPYPSPGPYPAVPPPQSPGAAPPVPWGTVPPGPWGPPAPYPDPTGSYPMPGL 213
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
526-574 |
1.04e-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: 38.59 E-value: 1.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 564364869 526 WSA--WSVCSRSCGVGVRSSERQCTQPVPK--NKGKYCVGERK--RYRLCNLQAC 574
Cdd:pfam19030 1 WVAgpWGECSVTCGGGVQTRLVQCVQKGGGsiVPDSECSAQKKppETQSCNLKPC 55
|
|
| TSP1_spondin |
pfam19028 |
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ... |
1449-1496 |
2.78e-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: 37.26 E-value: 2.78e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 564364869 1449 PWytSSWRECSEACGGGEQQR---LVTCPEPG--LCEESLRpnnTRPCNTHPC 1496
Cdd:pfam19028 5 EW--SEWSECSVTCGGGVQTRtrtVIVEPQNGgrPCPELLE---RRPCNLPPC 52
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
1452-1496 |
3.38e-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: 37.18 E-value: 3.38e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 564364869 1452 TSSWRECSEACGGGEQQRLVTC--PEPGLCEESLRPNN--TRPCNTHPC 1496
Cdd:smart00209 4 WSEWSPCSVTCGGGVQTRTRSCcsPPPQNGGGPCTGEDveTRACNEQPC 52
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
1395-1447 |
3.80e-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: 37.18 E-value: 3.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 564364869 1395 GNWSKCSRNCGGGSATRDVQCVDtrdlrPLRPFHCQPGPTKPPTRQLCGTQPC 1447
Cdd:smart00209 5 SEWSPCSVTCGGGVQTRTRSCCS-----PPPQNGGGPCTGEDVETRACNEQPC 52
|
|
| TSP1_CCN |
pfam19035 |
CCN3 Nov like TSP1 domain; This entry represents a sub-type of TSP1 domains found in ... |
1342-1389 |
4.33e-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: 36.54 E-value: 4.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 564364869 1342 QVGNWSQCSTTCGLGAIwrlVRCSSGNDEdCTLSsrpQPARHCHLRPC 1389
Cdd:pfam19035 4 QSTEWSPCSKTCGMGVS---TRVSNDNAE-CKLV---TETRLCQLRPC 44
|
|
| TSP_1 |
pfam00090 |
Thrombospondin type 1 domain; |
1449-1496 |
4.48e-03 |
|
Thrombospondin type 1 domain;
Pssm-ID: 459668 [Multi-domain] Cd Length: 49 Bit Score: 36.63 E-value: 4.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 564364869 1449 PWytSSWRECSEACGGGEQQRLVTC----PEPGLCEESLRPnnTRPCNTHPC 1496
Cdd:pfam00090 2 PW--SPWSPCSVTCGKGIQVRQRTCkspfPGGEPCTGDDIE--TQACKMDKC 49
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
477-511 |
7.34e-03 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 38.50 E-value: 7.34e-03
10 20 30
....*....|....*....|....*....|....*....
gi 564364869 477 LWCsVGTTCHSKMDAAV----DGTSCGKNKWCLNGECVP 511
Cdd:smart00608 99 LVC-WSLDYHLGTDPDIgmvkDGTKCGPGKVCINGQCVD 136
|
|
| |
