|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
226-434 |
1.05e-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: 351.93 E-value: 1.05e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 226 KWVETLVVADSKMVEYHGQPQVESYVLTIMNMVAGLFHDPSIGNPIHISIVRLIILEDEEKDLKITHHAEETLKNFCRWQ 305
Cdd:cd04273 1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 306 KNINIKGDDHPQHHDTAILLTRKDLCaSMNQPCETLGLSHVSGLCHPQLSCSVSEDTGMPLAFTVAHELGHSFGIQHDGT 385
Cdd:cd04273 81 KKLNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 133778949 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 |
4.63e-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: 4.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 34 DIVHPVRVDAGgsflsyelwpRVLRKRDVSTTQASSAFYQLQYQGRELLFNLTTNPYLMAPGFVSEIRRHSTLGHAHIQT 113
Cdd:pfam01562 1 EVVIPVRLDPS----------RRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPV 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 133778949 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 |
3.64e-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: 3.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 684 TVSRTFKETEGQGYVDIGLIPAGAREILIEEVAEAANFLALRSeDPDKYFLNGGWTIQ-WNGDYRVAGTTFTYARKGN-W 761
Cdd:pfam05986 1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPaL 79
|
90 100 110
....*....|....*....|....*....|....*
gi 133778949 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 |
9.66e-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: 98.96 E-value: 9.66e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 133778949 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 |
2.93e-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: 68.38 E-value: 2.93e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 133778949 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 ... |
1502-1557 |
4.08e-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: 4.08e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 133778949 1502 WVVGPWGQCSAPCGGGVQRRLVRCVNTqTGLAEEDSDLCSHEAWPESSRPCATEDC 1557
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 |
1.27e-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: 64.01 E-value: 1.27e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 133778949 808 WHYGPWSKCTVTCGTGVQRQSLYCM-ERQAGVVAEEYCNTLNRPDERQRkCSEEPC 862
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVqKGGGSIVPDSECSAQKKPPETQS-CNLKPC 55
|
|
| PHA03247 super family |
cl33720 |
large tegument protein UL36; Provisional |
1023-1361 |
2.86e-11 |
|
large tegument protein UL36; Provisional
The actual alignment was detected with superfamily member PHA03247:
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 69.20 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1023 PHPDLVDNGGWTAPPHIRPTESPSDTPVPTAGALGAEAEDIQGSWSPSPLLSEASYSPPGLE------------------ 1084
Cdd:PHA03247 2601 PVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSrprrarrlgraaqasspp 2680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1085 --------QTSINPLANFL---TEEDTPMGAPELGFPSLPWPPA-SVDDMMTPVGPGNPdellvkedeqSPPSTPwsdrN 1152
Cdd:PHA03247 2681 qrprrraaRPTVGSLTSLAdppPPPPTPEPAPHALVSATPLPPGpAAARQASPALPAAP----------APPAVP----A 2746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1153 KLSTDGNPLGHTSPALPQSPI-PTQPSPPSISPTQASPSPDVVEVSTGWNAA---WDP------------VLEADLKPGH 1216
Cdd:PHA03247 2747 GPATPGGPARPARPPTTAGPPaPAPPAAPAAGPPRRLTRPAVASLSESRESLpspWDPadppaavlapaaALPPAASPAG 2826
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1217 GELPSTVEVASPPLLPMATVPGIWGRDSPLEPGTPTFSSPELSSQHLK--TLTMPGTLLLTVPTDLRSPGPSGQPQTPnl 1294
Cdd:PHA03247 2827 PLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKpaAPARPPVRRLARPAVSRSTESFALPPDQ-- 2904
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 133778949 1295 egtqsPGLLPTPARETQTNSSKDPEVQPL-QPSLEEDGDPADPLPARNASWQVGNWSQCSTTCGLGAI 1361
Cdd:PHA03247 2905 -----PERPPQPQAPPPPQPQPQPPPPPQpQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGAL 2967
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1395-1450 |
3.25e-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: 59.77 E-value: 3.25e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 133778949 1395 WRTGNWSKCSRNCGGGSSTRDVQCVDTRDLRPLRPFHCqPGPTKPPNRQLCGTQPC 1450
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSEC-SAQKKPPETQSCNLKPC 55
|
|
| ADAMTS_CR_3 super family |
cl41950 |
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ... |
584-682 |
6.23e-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: 58.18 E-value: 6.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 584 FRHTQCSQFDGMLYK-----GKLHKW---VPVPNDDNPCELHCRPSNSSNTEKLRDAVVDGTPCYQSRISRD----ICLN 651
Cdd:pfam19236 5 FMSQQCARTDGQPLRsspggASFYHWgaaVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDgtlsLCVL 84
|
90 100 110
....*....|....*....|....*....|.
gi 133778949 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 ... |
1344-1392 |
8.27e-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: 55.92 E-value: 8.27e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 133778949 1344 WQVGNWSQCSTTCGLGAIWRLVSCSSG------NDEDCTLASRPQPARHCHLRPC 1392
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 |
4.82e-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: 53.61 E-value: 4.82e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 133778949 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 ... |
1453-1499 |
8.83e-08 |
|
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.
The actual alignment was detected with superfamily member pfam19030:
Pssm-ID: 465950 [Multi-domain] Cd Length: 55 Bit Score: 50.14 E-value: 8.83e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 133778949 1453 WYTSSWRECSEACGGGEQQRLVTCPEPG--------LCEESLRPNNSRPCNTHPC 1499
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 |
1.05e-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: 351.93 E-value: 1.05e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 226 KWVETLVVADSKMVEYHGQPQVESYVLTIMNMVAGLFHDPSIGNPIHISIVRLIILEDEEKDLKITHHAEETLKNFCRWQ 305
Cdd:cd04273 1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 306 KNINIKGDDHPQHHDTAILLTRKDLCaSMNQPCETLGLSHVSGLCHPQLSCSVSEDTGMPLAFTVAHELGHSFGIQHDGT 385
Cdd:cd04273 81 KKLNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 133778949 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 |
4.63e-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: 4.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 34 DIVHPVRVDAGgsflsyelwpRVLRKRDVSTTQASSAFYQLQYQGRELLFNLTTNPYLMAPGFVSEIRRHSTLGHAHIQT 113
Cdd:pfam01562 1 EVVIPVRLDPS----------RRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPV 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 133778949 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 |
3.64e-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: 3.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 684 TVSRTFKETEGQGYVDIGLIPAGAREILIEEVAEAANFLALRSeDPDKYFLNGGWTIQ-WNGDYRVAGTTFTYARKGN-W 761
Cdd:pfam05986 1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPaL 79
|
90 100 110
....*....|....*....|....*....|....*
gi 133778949 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 |
4.16e-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: 4.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 226 KWVETLVVADSKMVEYHGQPQ--VESYVLTIMNMVAglfhdpSIGNPIHISIVrLIILE---DEEKdLKITHHAEETLKN 300
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTtvVRQRVFQVVNLVN------SIYKELNIRVV-LVGLEiwtDEDK-IDVSGDANDTLRN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 301 FCRWQKNiNIKgddHPQHHDTAILLTRKDLCASmnqpceTLGLSHVSGLCHPQLSCSVSED---TGMPLAFTVAHELGHS 377
Cdd:pfam01421 73 FLKWRQE-YLK---KRKPHDVAQLLSGVEFGGT------TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHN 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 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 |
9.66e-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: 98.96 E-value: 9.66e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 133778949 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 |
2.93e-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: 68.38 E-value: 2.93e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 133778949 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 ... |
1502-1557 |
4.08e-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: 4.08e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 133778949 1502 WVVGPWGQCSAPCGGGVQRRLVRCVNTqTGLAEEDSDLCSHEAWPESSRPCATEDC 1557
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 |
1.27e-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: 64.01 E-value: 1.27e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 133778949 808 WHYGPWSKCTVTCGTGVQRQSLYCM-ERQAGVVAEEYCNTLNRPDERQRkCSEEPC 862
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVqKGGGSIVPDSECSAQKKPPETQS-CNLKPC 55
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1023-1361 |
2.86e-11 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 69.20 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1023 PHPDLVDNGGWTAPPHIRPTESPSDTPVPTAGALGAEAEDIQGSWSPSPLLSEASYSPPGLE------------------ 1084
Cdd:PHA03247 2601 PVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSrprrarrlgraaqasspp 2680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1085 --------QTSINPLANFL---TEEDTPMGAPELGFPSLPWPPA-SVDDMMTPVGPGNPdellvkedeqSPPSTPwsdrN 1152
Cdd:PHA03247 2681 qrprrraaRPTVGSLTSLAdppPPPPTPEPAPHALVSATPLPPGpAAARQASPALPAAP----------APPAVP----A 2746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1153 KLSTDGNPLGHTSPALPQSPI-PTQPSPPSISPTQASPSPDVVEVSTGWNAA---WDP------------VLEADLKPGH 1216
Cdd:PHA03247 2747 GPATPGGPARPARPPTTAGPPaPAPPAAPAAGPPRRLTRPAVASLSESRESLpspWDPadppaavlapaaALPPAASPAG 2826
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1217 GELPSTVEVASPPLLPMATVPGIWGRDSPLEPGTPTFSSPELSSQHLK--TLTMPGTLLLTVPTDLRSPGPSGQPQTPnl 1294
Cdd:PHA03247 2827 PLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKpaAPARPPVRRLARPAVSRSTESFALPPDQ-- 2904
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 133778949 1295 egtqsPGLLPTPARETQTNSSKDPEVQPL-QPSLEEDGDPADPLPARNASWQVGNWSQCSTTCGLGAI 1361
Cdd:PHA03247 2905 -----PERPPQPQAPPPPQPQPQPPPPPQpQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGAL 2967
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1395-1450 |
3.25e-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: 59.77 E-value: 3.25e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 133778949 1395 WRTGNWSKCSRNCGGGSSTRDVQCVDTRDLRPLRPFHCqPGPTKPPNRQLCGTQPC 1450
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSEC-SAQKKPPETQSCNLKPC 55
|
|
| ADAMTS_CR_3 |
pfam19236 |
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ... |
584-682 |
6.23e-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: 58.18 E-value: 6.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 584 FRHTQCSQFDGMLYK-----GKLHKW---VPVPNDDNPCELHCRPSNSSNTEKLRDAVVDGTPCYQSRISRD----ICLN 651
Cdd:pfam19236 5 FMSQQCARTDGQPLRsspggASFYHWgaaVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDgtlsLCVL 84
|
90 100 110
....*....|....*....|....*....|.
gi 133778949 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 ... |
1344-1392 |
8.27e-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: 55.92 E-value: 8.27e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 133778949 1344 WQVGNWSQCSTTCGLGAIWRLVSCSSG------NDEDCTLASRPQPARHCHLRPC 1392
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKgggsivPDSECSAQKKPPETQSCNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
866-922 |
4.82e-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: 53.61 E-value: 4.82e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 133778949 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 ... |
1453-1499 |
8.83e-08 |
|
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.
Pssm-ID: 465950 [Multi-domain] Cd Length: 55 Bit Score: 50.14 E-value: 8.83e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 133778949 1453 WYTSSWRECSEACGGGEQQRLVTCPEPG--------LCEESLRPNNSRPCNTHPC 1499
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKGggsivpdsECSAQKKPPETQSCNLKPC 55
|
|
| TSP_1 |
pfam00090 |
Thrombospondin type 1 domain; |
527-577 |
2.09e-07 |
|
Thrombospondin type 1 domain;
Pssm-ID: 459668 [Multi-domain] Cd Length: 49 Bit Score: 48.95 E-value: 2.09e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 133778949 527 SGWSAWSDCSRSCGVGVRSSERQCTQPVPKnrGKYCVGERKRSQLCNLPAC 577
Cdd:pfam00090 1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPG--GEPCTGDDIETQACKMDKC 49
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
808-863 |
1.27e-05 |
|
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
Pssm-ID: 214559 [Multi-domain] Cd Length: 53 Bit Score: 44.11 E-value: 1.27e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 133778949 808 WHYGPWSKCTVTCGTGVQRQSLYCmERQAGVVAEEYCNTlnrPDERQRKCSEEPCP 863
Cdd:smart00209 2 SEWSEWSPCSVTCGGGVQTRTRSC-CSPPPQNGGGPCTG---EDVETRACNEQPCP 53
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
1026-1317 |
2.32e-05 |
|
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: 49.14 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1026 DLVDNGGWTAPPHIRPTESPSDTPVPTAGALGAEAEDiqgSWSPSPLLSEASYSPPgleqtsiNPLANFLTEEDTPMgap 1105
Cdd:pfam05109 390 DITVSGLGTAPKTLIITRTATNATTTTHKVIFSKAPE---STTTSPTLNTTGFAAP-------NTTTGLPSSTHVPT--- 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1106 ELGFPSLPWPPASVDDMMTPVGPGNpdellvkeDEQSPPSTPWSDRNKLSTDGNPLGHTSP-ALPQSPIP--TQPSPPSI 1182
Cdd:pfam05109 457 NLTAPASTGPTVSTADVTSPTPAGT--------TSGASPVTPSPSPRDNGTESKAPDMTSPtSAVTTPTPnaTSPTPAVT 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1183 SPTQASPSPDVVEVSTgwnaawdpvLEADLKPGHGELPSTVEVASPPllPMATVPGIwGRDSP---LEPGTPTFSSP--- 1256
Cdd:pfam05109 529 TPTPNATSPTLGKTSP---------TSAVTTPTPNATSPTPAVTTPT--PNATIPTL-GKTSPtsaVTTPTPNATSPtvg 596
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 133778949 1257 ELSSQHLKT-LTMPGT----LLLTVPTDLRSPGPSGQPQTPNlEGTQSPGLLPTPARETQTNSSKD 1317
Cdd:pfam05109 597 ETSPQANTTnHTLGGTsstpVVTSPPKNATSAVTTGQHNITS-SSTSSMSLRPSSISETLSPSTSD 661
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
1005-1338 |
4.05e-05 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 48.23 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1005 DYNFINFHEDLS----YGSFEEPHPDLVDNggwtaPPHIRP-TESPSDTPVPTAGALGAEAEDI-QGSWSPSPLLSEASY 1078
Cdd:NF033839 137 DEAVSKFEKDSSssssSGSSTKPETPQPEN-----PEHQKPtTPAPDTKPSPQPEGKKPSVPDInQEKEKAKLAVATYMS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1079 SPPGLEQTSINPLANFLTEEDTPMGAPELGFPSLPwppaSVDDMMTPVGPGNP--------DELLVKEDEQSPPSTPWSD 1150
Cdd:NF033839 212 KILDDIQKHHLQKEKHRQIVALIKELDELKKQALS----EIDNVNTKVEIENTvhkifadmDAVVTKFKKGLTQDTPKEP 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1151 RNKLSTDGNPLGHTSPALPQSPIPTQPSP--PSISPTQASPSPDVVEVSTGWNAAWDPVLEADlKPGHGELPST--VEVA 1226
Cdd:NF033839 288 GNKKPSAPKPGMQPSPQPEKKEVKPEPETpkPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETP-KPEVKPQPEKpkPEVK 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1227 SPPLLPMATVPGiwgrdsplEPGTPTFS-SPELSSQHLKTLTMPGTLLLTVPTDLRSPGPS--GQPQTPNLEGTQSPgll 1303
Cdd:NF033839 367 PQPEKPKPEVKP--------QPETPKPEvKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEvkPQPEKPKPEVKPQP--- 435
|
330 340 350
....*....|....*....|....*....|....*...
gi 133778949 1304 PTPARETQTNSSK-DPEV--QPLQPSLEEDGDPADPLP 1338
Cdd:NF033839 436 EKPKPEVKPQPEKpKPEVkpQPETPKPEVKPQPEKPKP 473
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
1499-1558 |
4.97e-05 |
|
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
Pssm-ID: 214559 [Multi-domain] Cd Length: 53 Bit Score: 42.19 E-value: 4.97e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1499 CTQWvvGPWGQCSAPCGGGVQRRLVRCVNtqtGLAEEDSDLCSHEAwpESSRPCATEDCE 1558
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. |
1395-1450 |
3.45e-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: 3.45e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 133778949 1395 WRTGNWSKCSRNCGGGSSTRDVQCVDtrdlrPLRPFHCQPGPTKPPNRQLCGTQPC 1450
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 |
1.05e-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: 351.93 E-value: 1.05e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 226 KWVETLVVADSKMVEYHGQPQVESYVLTIMNMVAGLFHDPSIGNPIHISIVRLIILEDEEKDLKITHHAEETLKNFCRWQ 305
Cdd:cd04273 1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 306 KNINIKGDDHPQHHDTAILLTRKDLCaSMNQPCETLGLSHVSGLCHPQLSCSVSEDTGMPLAFTVAHELGHSFGIQHDGT 385
Cdd:cd04273 81 KKLNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 133778949 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 |
4.63e-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: 4.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 34 DIVHPVRVDAGgsflsyelwpRVLRKRDVSTTQASSAFYQLQYQGRELLFNLTTNPYLMAPGFVSEIRRHSTLGHAHIQT 113
Cdd:pfam01562 1 EVVIPVRLDPS----------RRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPV 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 133778949 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 |
1.65e-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: 1.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 228 VETLVVADSKMVEYHgQPQVES---YVLTIMNMVAGLFHDPSIGNPIHISIVRLIILEDEEKDLKITHHAEETLKNFCRW 304
Cdd:cd04267 3 IELVVVADHRMVSYF-NSDENIlqaYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSFW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 305 QKninikgdDHPQHHDTAILLTRKDLCAsmnqpCETLGLSHVSGLCHPQLSCSVSEDTGMPL--AFTVAHELGHSFGIQH 382
Cdd:cd04267 82 RA-------EGPIRHDNAVLLTAQDFIE-----GDILGLAYVGSMCNPYSSVGVVEDTGFTLltALTMAHELGHNLGAEH 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 133778949 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 |
1.47e-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: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 226 KWVETLVVADSKMVEYHGQ--PQVESYVLTIMNMVAGLFHdpSIGnpIHISIVRLIILEDEEKdLKITHHAEETLKNFCR 303
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSnlSKVRQRVIEIVNIVDSIYR--PLN--IRVVLVGLEIWTDKDK-ISVSGDAGETLNRFLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 304 W-QKNINikgddHPQHHDTAILLTRKDLCAsmnqpcETLGLSHVSGLCHPQLSCSVSEDTGMPL---AFTVAHELGHSFG 379
Cdd:cd04269 76 WkRSNLL-----PRKPHDNAQLLTGRDFDG------NTVGLAYVGGMCSPKYSGGVVQDHSRNLllfAVTMAHELGHNLG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 133778949 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 |
3.64e-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: 3.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 684 TVSRTFKETEGQGYVDIGLIPAGAREILIEEVAEAANFLALRSeDPDKYFLNGGWTIQ-WNGDYRVAGTTFTYARKGN-W 761
Cdd:pfam05986 1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPaL 79
|
90 100 110
....*....|....*....|....*....|....*
gi 133778949 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 |
4.16e-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: 4.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 226 KWVETLVVADSKMVEYHGQPQ--VESYVLTIMNMVAglfhdpSIGNPIHISIVrLIILE---DEEKdLKITHHAEETLKN 300
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTtvVRQRVFQVVNLVN------SIYKELNIRVV-LVGLEiwtDEDK-IDVSGDANDTLRN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 301 FCRWQKNiNIKgddHPQHHDTAILLTRKDLCASmnqpceTLGLSHVSGLCHPQLSCSVSED---TGMPLAFTVAHELGHS 377
Cdd:pfam01421 73 FLKWRQE-YLK---KRKPHDVAQLLSGVEFGGT------TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHN 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 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 |
9.66e-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: 98.96 E-value: 9.66e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 133778949 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 |
2.13e-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: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 228 VETLVVADSKMVEYHGQ-PQVESYVLTIMNMVAGLFHDpsIGNP-IHISIVRLIILEDEEKDLKITHH------AEETLK 299
Cdd:cd04272 3 PELFVVVDYDHQSEFFSnEQLIRYLAVMVNAANLRYRD--LKSPrIRLLLVGITISKDPDFEPYIHPInygyidAAETLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 300 NFcrwqkNINIKGDDHPQHHDTAILLTRKDLCASMNQPCET--LGLSHVSGLCHpQLSCSVSEDTGMPL--AFTVAHELG 375
Cdd:cd04272 81 NF-----NEYVKKKRDYFNPDVVFLVTGLDMSTYSGGSLQTgtGGYAYVGGACT-ENRVAMGEDTPGSYygVYTMTHELA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 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 |
2.48e-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: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 316 PQHHDTAILLTRKDLcasmnqPCETLGLSHVSGLCHPQLSCSVSEDTGMP---LAFTVAHELGHSFGIQHDGTGNDCESI 392
Cdd:cd00203 49 IDKADIAILVTRQDF------DGGTGGWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAHELGHALGFYHDHDRKDRDDY 122
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 133778949 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 |
2.93e-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: 68.38 E-value: 2.93e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 133778949 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 ... |
1502-1557 |
4.08e-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: 4.08e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 133778949 1502 WVVGPWGQCSAPCGGGVQRRLVRCVNTqTGLAEEDSDLCSHEAWPESSRPCATEDC 1557
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQK-GGGSIVPDSECSAQKKPPETQSCNLKPC 55
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
224-402 |
5.17e-13 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 69.37 E-value: 5.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 224 KEKWVETLVVADSKMVEYHGQPQVESYVLTIMNMVAGLFHDPSignPIHISIVRLIILEDEEKDlkiTHHAEETLKNFCR 303
Cdd:pfam13688 1 STRTVALLVAADCSYVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCPY---TPPACSTGDSSDR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 304 WQKNINIKGDDHPQHHDTAILLTrkdlcasmNQPCETLGLSHVSGLCHPQLSCSVSEDTGMP--------LAFTVAHELG 375
Cdd:pfam13688 75 LSEFQDFSAWRGTQNDDLAYLFL--------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSGNnvvvstatEWQVFAHEIG 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 133778949 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 |
1.27e-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: 64.01 E-value: 1.27e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 133778949 808 WHYGPWSKCTVTCGTGVQRQSLYCM-ERQAGVVAEEYCNTLNRPDERQRkCSEEPC 862
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVqKGGGSIVPDSECSAQKKPPETQS-CNLKPC 55
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1023-1361 |
2.86e-11 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 69.20 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1023 PHPDLVDNGGWTAPPHIRPTESPSDTPVPTAGALGAEAEDIQGSWSPSPLLSEASYSPPGLE------------------ 1084
Cdd:PHA03247 2601 PVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSrprrarrlgraaqasspp 2680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1085 --------QTSINPLANFL---TEEDTPMGAPELGFPSLPWPPA-SVDDMMTPVGPGNPdellvkedeqSPPSTPwsdrN 1152
Cdd:PHA03247 2681 qrprrraaRPTVGSLTSLAdppPPPPTPEPAPHALVSATPLPPGpAAARQASPALPAAP----------APPAVP----A 2746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1153 KLSTDGNPLGHTSPALPQSPI-PTQPSPPSISPTQASPSPDVVEVSTGWNAA---WDP------------VLEADLKPGH 1216
Cdd:PHA03247 2747 GPATPGGPARPARPPTTAGPPaPAPPAAPAAGPPRRLTRPAVASLSESRESLpspWDPadppaavlapaaALPPAASPAG 2826
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1217 GELPSTVEVASPPLLPMATVPGIWGRDSPLEPGTPTFSSPELSSQHLK--TLTMPGTLLLTVPTDLRSPGPSGQPQTPnl 1294
Cdd:PHA03247 2827 PLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKpaAPARPPVRRLARPAVSRSTESFALPPDQ-- 2904
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 133778949 1295 egtqsPGLLPTPARETQTNSSKDPEVQPL-QPSLEEDGDPADPLPARNASWQVGNWSQCSTTCGLGAI 1361
Cdd:PHA03247 2905 -----PERPPQPQAPPPPQPQPQPPPPPQpQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGAL 2967
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1395-1450 |
3.25e-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: 59.77 E-value: 3.25e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 133778949 1395 WRTGNWSKCSRNCGGGSSTRDVQCVDTRDLRPLRPFHCqPGPTKPPNRQLCGTQPC 1450
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSEC-SAQKKPPETQSCNLKPC 55
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
969-1385 |
9.36e-11 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 67.27 E-value: 9.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 969 PRPSPASSPKPvsisnaiDEEELDPPGPVfvddfyydynfinfhedlsygsfEEPHPDLVDNGGWTAPPhirPTESPSDT 1048
Cdd:PHA03247 2609 RGPAPPSPLPP-------DTHAPDPPPPS-----------------------PSPAANEPDPHPPPTVP---PPERPRDD 2655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1049 PVPTAGALGAEAEdiQGSWSPSPLLSEASYSPPGLEQTsINPLANFL---TEEDTPMGAPELGFPSLPWPPA-SVDDMMT 1124
Cdd:PHA03247 2656 PAPGRVSRPRRAR--RLGRAAQASSPPQRPRRRAARPT-VGSLTSLAdppPPPPTPEPAPHALVSATPLPPGpAAARQAS 2732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1125 PVGPGNPdellvkedeqSPPSTPwsdrNKLSTDGNPLGHTSPALPQSPI-PTQPSPPSISPTQASPSPDVVEVSTGWNAA 1203
Cdd:PHA03247 2733 PALPAAP----------APPAVP----AGPATPGGPARPARPPTTAGPPaPAPPAAPAAGPPRRLTRPAVASLSESRESL 2798
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1204 ---WDP------------VLEADLKPGHGELPSTVEVASPPLLPMATVPGIWGRDSPLEPGTPTFSSPELSSQHLK--TL 1266
Cdd:PHA03247 2799 pspWDPadppaavlapaaALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKpaAP 2878
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1267 TMPGTLLLTVPTDLRSPGPSGQPQTPnlegtqsPGLLPTPARETQTNsskdPEVQPLQPSLEEDGDPADPLPARNASWQV 1346
Cdd:PHA03247 2879 ARPPVRRLARPAVSRSTESFALPPDQ-------PERPPQPQAPPPPQ----PQPQPPPPPQPQPPPPPPPRPQPPLAPTT 2947
|
410 420 430
....*....|....*....|....*....|....*....
gi 133778949 1347 GNWSQCSTTCGLGAIWRLVSCSSGNDEDCTLASRPQPAR 1385
Cdd:PHA03247 2948 DPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSR 2986
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1035-1336 |
5.85e-10 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 64.57 E-value: 5.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1035 APPHIRPTESPSDTPVPTAGALGAEAEDIQGSWSPSP-----------LLSEASYSPPGLEQTSINPLANFLT----EED 1099
Cdd:PHA03247 2770 APPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADppaavlapaaaLPPAASPAGPLPPPTSAQPTAPPPPpgppPPS 2849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1100 TPMG------------APELGFPSLPWPPA--SVDDMMTPVGPGNPDELLVKEDEQSPPSTPWSDRNKLSTDGNPlghtS 1165
Cdd:PHA03247 2850 LPLGgsvapggdvrrrPPSRSPAAKPAAPArpPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPP----P 2925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1166 PALPQSPIPTQPSPPSisptQASPSPDVVEVSTGWNAAWDPVLEAdLKPGHGELPSTVEVASPPLLPMATVPGIWGRDSP 1245
Cdd:PHA03247 2926 PPQPQPPPPPPPRPQP----PLAPTTDPAGAGEPSGAVPQPWLGA-LVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHS 3000
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1246 LEPGTPTFSSPELssqHLKTLTMPGTLLLT--VPTDLR-SPGPSGQPQTPNLEGTQSPGLLPTParetqtnsSKDPEVQP 1322
Cdd:PHA03247 3001 LSRVSSWASSLAL---HEETDPPPVSLKQTlwPPDDTEdSDADSLFDSDSERSDLEALDPLPPE--------PHDPFAHE 3069
|
330
....*....|....
gi 133778949 1323 LQPSLEEDGDPADP 1336
Cdd:PHA03247 3070 PDPATPEAGARESP 3083
|
|
| ADAMTS_CR_3 |
pfam19236 |
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ... |
584-682 |
6.23e-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: 58.18 E-value: 6.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 584 FRHTQCSQFDGMLYK-----GKLHKW---VPVPNDDNPCELHCRPSNSSNTEKLRDAVVDGTPCYQSRISRD----ICLN 651
Cdd:pfam19236 5 FMSQQCARTDGQPLRsspggASFYHWgaaVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDgtlsLCVL 84
|
90 100 110
....*....|....*....|....*....|.
gi 133778949 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 ... |
1344-1392 |
8.27e-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: 55.92 E-value: 8.27e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 133778949 1344 WQVGNWSQCSTTCGLGAIWRLVSCSSG------NDEDCTLASRPQPARHCHLRPC 1392
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKgggsivPDSECSAQKKPPETQSCNLKPC 55
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
866-922 |
4.82e-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: 53.61 E-value: 4.82e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 133778949 866 WWAGEWQPCSRSCGPeGLSRRAVFCIRSMGLDEQRAlelSACEHLPRPLAETPCNRH 922
Cdd:pfam19030 1 WVAGPWGECSVTCGG-GVQTRLVQCVQKGGGSIVPD---SECSAQKKPPETQSCNLK 53
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1035-1339 |
1.37e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 60.34 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1035 APPHIRPTE--SPS-DTPVPTAGALGAEAEDIQGSWS-PSP-LLSEASYSPP----------GLEQtsinplanfLTEED 1099
Cdd:PHA03247 2477 APVYRRPAEarFPFaAGAAPDPGGGGPPDPDAPPAPSrLAPaILPDEPVGEPvhprmltwirGLEE---------LASDD 2547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1100 TpmGAPELGFPSLPWPPASVDDMMTPVGPGNPDELLVKEDEQSPPSTPWSDRNKlsTDGNPLGhtSPALPQSPIPTQPSP 1179
Cdd:PHA03247 2548 A--GDPPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPR--APVDDRG--DPRGPAPPSPLPPDT 2621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1180 PSISPTQASPSPDVVEVSTGWNAAWDPVLEADLKPGHGEL---------------PSTVEVASPPLLPMATVPGIWGRDS 1244
Cdd:PHA03247 2622 HAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVsrprrarrlgraaqaSSPPQRPRRRAARPTVGSLTSLADP 2701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1245 PLEPGTPTfSSPELSSQHLKTLTMPGTLLLTVPTDLRSPGPSGQPQTPNLEGTQS-PGLLPTPARETQTNSSKDP----- 1318
Cdd:PHA03247 2702 PPPPPTPE-PAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPArPARPPTTAGPPAPAPPAAPaagpp 2780
|
330 340
....*....|....*....|....*..
gi 133778949 1319 ------EVQPLQPSLEEDGDPADPLPA 1339
Cdd:PHA03247 2781 rrltrpAVASLSESRESLPSPWDPADP 2807
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
1453-1499 |
8.83e-08 |
|
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.
Pssm-ID: 465950 [Multi-domain] Cd Length: 55 Bit Score: 50.14 E-value: 8.83e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 133778949 1453 WYTSSWRECSEACGGGEQQRLVTCPEPG--------LCEESLRPNNSRPCNTHPC 1499
Cdd:pfam19030 1 WVAGPWGECSVTCGGGVQTRLVQCVQKGggsivpdsECSAQKKPPETQSCNLKPC 55
|
|
| TSP_1 |
pfam00090 |
Thrombospondin type 1 domain; |
527-577 |
2.09e-07 |
|
Thrombospondin type 1 domain;
Pssm-ID: 459668 [Multi-domain] Cd Length: 49 Bit Score: 48.95 E-value: 2.09e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 133778949 527 SGWSAWSDCSRSCGVGVRSSERQCTQPVPKnrGKYCVGERKRSQLCNLPAC 577
Cdd:pfam00090 1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPG--GEPCTGDDIETQACKMDKC 49
|
|
| TSP1_spondin |
pfam19028 |
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ... |
527-577 |
8.62e-07 |
|
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: 47.27 E-value: 8.62e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 133778949 527 SGWSAWSDCSRSCGVGVRSSERQCTQPvPKNRGKYCvGERKRSQLCNLPAC 577
Cdd:pfam19028 4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPC-PELLERRPCNLPPC 52
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
1100-1339 |
5.56e-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: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1100 TPMGAPELGFPSLPWPPASvddmmtPVGPGNPDELLVKEDEQSPPSTPwSDR---NKLSTDGNPLghtSPAL-------P 1169
Cdd:PLN03209 314 TPMEELLAKIPSQRVPPKE------SDAADGPKPVPTKPVTPEAPSPP-IEEeppQPKAVVPRPL---SPYTayedlkpP 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1170 QSPIPTQPS--PPSISPTQASPSPDVVEVSTGWNAAWD-PVLEA------------------DLKPGHGELPSTVEVASP 1228
Cdd:PLN03209 384 TSPIPTPPSssPASSKSVDAVAKPAEPDVVPSPGSASNvPEVEPaqveakktrplspyaryeDLKPPTSPSPTAPTGVSP 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1229 PLLPMATVPGIWGRDSPLEPGTPTFSSPELSSQHLKTLTMPGTLLLTVPTDLrSPGPSGQPQTPNLEGTQSPGLLPTPAR 1308
Cdd:PLN03209 464 SVSSTSSVPAVPDTAPATAATDAAAPPPANMRPLSPYAVYDDLKPPTSPSPA-APVGKVAPSSTNEVVKVGNSAPPTALA 542
|
250 260 270
....*....|....*....|....*....|...
gi 133778949 1309 ETQTNssKDPEVQPLQP--SLEEDGDPADPLPA 1339
Cdd:PLN03209 543 DEQHH--AQPKPRPLSPytMYEDLKPPTSPTPS 573
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
808-863 |
1.27e-05 |
|
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
Pssm-ID: 214559 [Multi-domain] Cd Length: 53 Bit Score: 44.11 E-value: 1.27e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 133778949 808 WHYGPWSKCTVTCGTGVQRQSLYCmERQAGVVAEEYCNTlnrPDERQRKCSEEPCP 863
Cdd:smart00209 2 SEWSEWSPCSVTCGGGVQTRTRSC-CSPPPQNGGGPCTG---EDVETRACNEQPCP 53
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
1038-1335 |
1.66e-05 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 49.69 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1038 HIRPTESPSDTPVPTAG-----ALGAEAEDIQGSWSPSpllseaSYSPPGLEQTSINPLANFLTEEDTPMGAPELG-FPS 1111
Cdd:PTZ00449 507 HDEPPEGPEASGLPPKApgdkeGEEGEHEDSKESDEPK------EGGKPGETKEGEVGKKPGPAKEHKPSKIPTLSkKPE 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1112 LPWPPASVDDMMTPVGPGNPdelLVKEDEQSPPSTPWSDRNKL-STDGNPLGHTSPALPQSPI----PTQPSPPSISPTQ 1186
Cdd:PTZ00449 581 FPKDPKHPKDPEEPKKPKRP---RSAQRPTRPKSPKLPELLDIpKSPKRPESPKSPKRPPPPQrpssPERPEGPKIIKSP 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1187 ASP-SPDVvevstgwnaAWDPVLEADLKPGHGELPSTVEVASPPLLPMATVPGIWGRDSPLEPGTPTFSSPELSSQHLKT 1265
Cdd:PTZ00449 658 KPPkSPKP---------PFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTPRPLPPKLPRD 728
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1266 LTMPgtllLTVPTDLRSPGPS-GQPQTPNLE----------GTQSPGLLP----TPARETQTNSSKDPEVQPLQPSLEED 1330
Cdd:PTZ00449 729 EEFP----FEPIGDPDAEQPDdIEFFTPPEEertffhetpaDTPLPDILAeefkEEDIHAETGEPDEAMKRPDSPSEHED 804
|
....*
gi 133778949 1331 GDPAD 1335
Cdd:PTZ00449 805 KPPGD 809
|
|
| Reprolysin_2 |
pfam13574 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
340-422 |
1.78e-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: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 340 TLGLSHVSGLCHPQLSCsVSEDTGMPLAFT-------------VAHELGHSFGIQHDGTG--NDCESI----------GK 394
Cdd:pfam13574 86 ELGLAYVGQICQKGASS-PKTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDCDGsqYASSGCernaatsvcsAN 164
|
90 100
....*....|....*....|....*...
gi 133778949 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 |
2.31e-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: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 231 LVVADSKMVEYHGQPQVESYVLTIMNMVAGL--------FHDPSIGNpIHISIVRLIIL-EDEEKDLKITHHaeetlkNF 301
Cdd:cd04270 6 LLVADHRFYKYMGRGEEETTINYLISHIDRVddiyrntdWDGGGFKG-IGFQIKRIRIHtTPDEVDPGNKFY------NK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 302 C-------RWQKNINIKgddhpQHHD---TAILLTRKDLcaSMNqpceTLGLSHVS--------GLCHPQLSCSV----S 359
Cdd:cd04270 79 SfpnwgveKFLVKLLLE-----QFSDdvcLAHLFTYRDF--DMG----TLGLAYVGsprdnsagGICEKAYYYSNgkkkY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 360 EDTGMPLAF-------------TVAHELGHSFGIQHDGTGNDC---ESIGKRpFIMSPQLLY-DRGIPLTWSRCSREYIT 422
Cdd:cd04270 148 LNTGLTTTVnygkrvptkesdlVTAHELGHNFGSPHDPDIAECapgESQGGN-YIMYARATSgDKENNKKFSPCSKKSIS 226
|
250
....*....|....*..
gi 133778949 423 RFLDRGWGLCLDDRPSK 439
Cdd:cd04270 227 KVLEVKSNSCFVERSQS 243
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
1026-1317 |
2.32e-05 |
|
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: 49.14 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1026 DLVDNGGWTAPPHIRPTESPSDTPVPTAGALGAEAEDiqgSWSPSPLLSEASYSPPgleqtsiNPLANFLTEEDTPMgap 1105
Cdd:pfam05109 390 DITVSGLGTAPKTLIITRTATNATTTTHKVIFSKAPE---STTTSPTLNTTGFAAP-------NTTTGLPSSTHVPT--- 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1106 ELGFPSLPWPPASVDDMMTPVGPGNpdellvkeDEQSPPSTPWSDRNKLSTDGNPLGHTSP-ALPQSPIP--TQPSPPSI 1182
Cdd:pfam05109 457 NLTAPASTGPTVSTADVTSPTPAGT--------TSGASPVTPSPSPRDNGTESKAPDMTSPtSAVTTPTPnaTSPTPAVT 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1183 SPTQASPSPDVVEVSTgwnaawdpvLEADLKPGHGELPSTVEVASPPllPMATVPGIwGRDSP---LEPGTPTFSSP--- 1256
Cdd:pfam05109 529 TPTPNATSPTLGKTSP---------TSAVTTPTPNATSPTPAVTTPT--PNATIPTL-GKTSPtsaVTTPTPNATSPtvg 596
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 133778949 1257 ELSSQHLKT-LTMPGT----LLLTVPTDLRSPGPSGQPQTPNlEGTQSPGLLPTPARETQTNSSKD 1317
Cdd:pfam05109 597 ETSPQANTTnHTLGGTsstpVVTSPPKNATSAVTTGQHNITS-SSTSSMSLRPSSISETLSPSTSD 661
|
|
| Reprolysin_3 |
pfam13582 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
271-383 |
3.32e-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: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 271 IHISIVRLIILED-EEKDLKIThhAEETLKNFCRWQKNiNIKGDDHPQHHdtaiLLTRKDlcasmnqPCETLGLSHVSGL 349
Cdd:pfam13582 20 IRLQLAAIIITTSaDTPYTSSD--ALEILDELQEVNDT-RIGQYGYDLGH----LFTGRD-------GGGGGGIAYVGGV 85
|
90 100 110
....*....|....*....|....*....|....*..
gi 133778949 350 CHPQLSCSVSEDTGMP---LAFTVAHELGHSFGIQHD 383
Cdd:pfam13582 86 CNSGSKFGVNSGSGPVgdtGADTFAHEIGHNFGLNHT 122
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
1005-1338 |
4.05e-05 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 48.23 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1005 DYNFINFHEDLS----YGSFEEPHPDLVDNggwtaPPHIRP-TESPSDTPVPTAGALGAEAEDI-QGSWSPSPLLSEASY 1078
Cdd:NF033839 137 DEAVSKFEKDSSssssSGSSTKPETPQPEN-----PEHQKPtTPAPDTKPSPQPEGKKPSVPDInQEKEKAKLAVATYMS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1079 SPPGLEQTSINPLANFLTEEDTPMGAPELGFPSLPwppaSVDDMMTPVGPGNP--------DELLVKEDEQSPPSTPWSD 1150
Cdd:NF033839 212 KILDDIQKHHLQKEKHRQIVALIKELDELKKQALS----EIDNVNTKVEIENTvhkifadmDAVVTKFKKGLTQDTPKEP 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1151 RNKLSTDGNPLGHTSPALPQSPIPTQPSP--PSISPTQASPSPDVVEVSTGWNAAWDPVLEADlKPGHGELPST--VEVA 1226
Cdd:NF033839 288 GNKKPSAPKPGMQPSPQPEKKEVKPEPETpkPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETP-KPEVKPQPEKpkPEVK 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1227 SPPLLPMATVPGiwgrdsplEPGTPTFS-SPELSSQHLKTLTMPGTLLLTVPTDLRSPGPS--GQPQTPNLEGTQSPgll 1303
Cdd:NF033839 367 PQPEKPKPEVKP--------QPETPKPEvKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEvkPQPEKPKPEVKPQP--- 435
|
330 340 350
....*....|....*....|....*....|....*...
gi 133778949 1304 PTPARETQTNSSK-DPEV--QPLQPSLEEDGDPADPLP 1338
Cdd:NF033839 436 EKPKPEVKPQPEKpKPEVkpQPETPKPEVKPQPEKPKP 473
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
1499-1558 |
4.97e-05 |
|
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
Pssm-ID: 214559 [Multi-domain] Cd Length: 53 Bit Score: 42.19 E-value: 4.97e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1499 CTQWvvGPWGQCSAPCGGGVQRRLVRCVNtqtGLAEEDSDLCSHEAwpESSRPCATEDCE 1558
Cdd:smart00209 1 WSEW--SEWSPCSVTCGGGVQTRTRSCCS---PPPQNGGGPCTGED--VETRACNEQPCP 53
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1110-1326 |
9.42e-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: 47.45 E-value: 9.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1110 PSLPWPPASVDD----MMTPVGPGNPDELLVKEDEQSPPSTPWSDRNKLSTDGNPLGHTSpalpqspIPTQPSPPSISPT 1185
Cdd:pfam03154 146 PSIPSPQDNESDsdssAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPS-------VPPQGSPATSQPP 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1186 QASPSPdvvevstgwnaawdpvleadlKPGHGELPSTVEVaSPPLLPMAtvpgiwgrDSPLEPGTPTFSSPELSSQHLKT 1265
Cdd:pfam03154 219 NQTQST---------------------AAPHTLIQQTPTL-HPQRLPSP--------HPPLQPMTQPPPPSQVSPQPLPQ 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1266 LTMPGTL------LLTVPTDLRSPGP---------SGQPQTPNLEGTQSPG----LLPTPARETQTNSSKDPEVQPLQPS 1326
Cdd:pfam03154 269 PSLHGQMppmphsLQTGPSHMQHPVPpqpfpltpqSSQSQVPPGPSPAAPGqsqqRIHTPPSQSQLQSQQPPREQPLPPA 348
|
|
| TSP1_ADAMTS |
pfam19030 |
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ... |
529-577 |
1.25e-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: 41.28 E-value: 1.25e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 133778949 529 WSA--WSDCSRSCGVGVRSSERQCTQPVPK--NRGKYCVGERK--RSQLCNLPAC 577
Cdd:pfam19030 1 WVAgpWGECSVTCGGGVQTRLVQCVQKGGGsiVPDSECSAQKKppETQSCNLKPC 55
|
|
| DUF4045 |
pfam13254 |
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ... |
1079-1343 |
1.95e-04 |
|
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.
Pssm-ID: 433066 [Multi-domain] Cd Length: 415 Bit Score: 45.93 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1079 SPPGLEQT--------SINPLANFLTEEDTPMGAPELGFP-SLPWPPAS------VDDMMTPVGPGNPDELLVKedeqsp 1143
Cdd:pfam13254 32 LPPGLSRQnsfasnrgSVAGPSGSLSPGLSPTKLSREGSPeSTSRPSSShseatiVRHSKDDERPSTPDEGFVK------ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1144 PSTPWSDRNKLSTDGNPLGHTSPALPQSPiptqPSPPSI------SPTQASpspdvvevstgwnaaWdpvLEADL-KPgh 1216
Cdd:pfam13254 106 PALPRHSRSSSALSNTGSEEDSPSLPTSP----PSPSKTmdpkrwSPTKSS---------------W---LESALnRP-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1217 gELPSTVEVASPPLLP--MATVPGI--------WGRDSPLEPGTPT-FSSPELSSQHLKTLTMPGTLLLTVPTdlrSPGP 1285
Cdd:pfam13254 162 -ESPKPKAQPSQPAQPawMKELNKIrqsrasvdLGRPNSFKEVTPVgLMRSPAPGGHSKSPSVSGISADSSPT---KEEP 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 133778949 1286 SGQPQTPNLEGTQSPGLLPTPARETQTNSSKDPEVQPLQPSLEEDGDPADPLPARNAS 1343
Cdd:pfam13254 238 SEEADTLSTDKEQSPAPTSASEPPPKTKELPKDSEEPAAPSKSAEASTEKKEPDTESS 295
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
964-1308 |
3.74e-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: 45.53 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 964 PNQLAPRPSPASSPKPVSISNAIDEEELdPPGPvfvddfyydynfinfhEDLSYGSFEEPHPdlvdngGWTAPPHIRPTE 1043
Cdd:pfam03154 248 PLQPMTQPPPPSQVSPQPLPQPSLHGQM-PPMP----------------HSLQTGPSHMQHP------VPPQPFPLTPQS 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1044 SPSDTPVPTAGALGAEAEdiQGSWSPSPLLSEASYSPPgLEQtsinPLAnflteeDTPMGAPELGFPslpwPPASVDDMM 1123
Cdd:pfam03154 305 SQSQVPPGPSPAAPGQSQ--QRIHTPPSQSQLQSQQPP-REQ----PLP------PAPLSMPHIKPP----PTTPIPQLP 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1124 TPVGPGNPDELLVKEDEQS----PPSTPWSDRNKLSTDGNPLGHTSPA--LPQS-PIPTQPS-PPSISPTQASPSPDVVE 1195
Cdd:pfam03154 368 NPQSHKHPPHLSGPSPFQMnsnlPPPPALKPLSSLSTHHPPSAHPPPLqlMPQSqQLPPPPAqPPVLTQSQSLPPPAASH 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1196 VSTGwnaAWDPVLEADLKPGHGELPStvevASPPLLPmatvpgiwgrdsplePGTPTFSSPELSSQHLKTLTMPGTLLLT 1275
Cdd:pfam03154 448 PPTS---GLHQVPSQSPFPQHPFVPG----GPPPITP---------------PSGPPTSTSSAMPGIQPPSSASVSSSGP 505
|
330 340 350
....*....|....*....|....*....|...
gi 133778949 1276 VPTDLRSPGPSGQPQTPNLEGTQSPGLLPTPAR 1308
Cdd:pfam03154 506 VPAAVSCPLPPVQIKEEALDEAEEPESPPPPPR 538
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
963-1223 |
1.23e-03 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 43.38 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 963 IPNQLAPRPSP--ASSPKPVSISNAIDE-----EELDPPGPVFVDDfyydynfinfhEDLS-YGSFEEPHPDlvdnggwT 1034
Cdd:PLN03209 323 IPSQRVPPKESdaADGPKPVPTKPVTPEapsppIEEEPPQPKAVVP-----------RPLSpYTAYEDLKPP-------T 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1035 APPHIRPTESPSDTPVPTAGALGAEAEDIQgswSPSPLLSEASYSPPGLEQTSINPLANFLTEED-TPMGAPELGFPSLP 1113
Cdd:PLN03209 385 SPIPTPPSSSPASSKSVDAVAKPAEPDVVP---SPGSASNVPEVEPAQVEAKKTRPLSPYARYEDlKPPTSPSPTAPTGV 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1114 WPPASVDDMMTPVGPGNPDELLVKEDEQSPPSTPWSDRNKLSTDGNPLGHTSPALPQSPIPTQPSPPsiSPTQASPSPDV 1193
Cdd:PLN03209 462 SPSVSSTSSVPAVPDTAPATAATDAAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNE--VVKVGNSAPPT 539
|
250 260 270
....*....|....*....|....*....|....*.
gi 133778949 1194 VEVSTGWNAAWDP------VLEADLKPGHGELPSTV 1223
Cdd:PLN03209 540 ALADEQHHAQPKPrplspyTMYEDLKPPTSPTPSPV 575
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1023-1194 |
1.36e-03 |
|
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: 43.60 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1023 PHPDLVDNGGWTAPPHI---RPTESPSDTPVPTA-GALGAEAEDIQGSWSPSPL--------LSEASYSPPGLEQTSINP 1090
Cdd:pfam03154 362 PIPQLPNPQSHKHPPHLsgpSPFQMNSNLPPPPAlKPLSSLSTHHPPSAHPPPLqlmpqsqqLPPPPAQPPVLTQSQSLP 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1091 L--ANFLTEEDTPMGAPELGFPSLPWPPASVDDMMTPVGP---GNPDELLVKEDEQSPPSTPWSDRNKLSTDGNPLGHTS 1165
Cdd:pfam03154 442 PpaASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPptsTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKE 521
|
170 180
....*....|....*....|....*....
gi 133778949 1166 PALPQSPIPTQPSPPSISPtqaSPSPDVV 1194
Cdd:pfam03154 522 EALDEAEEPESPPPPPRSP---SPEPTVV 547
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1023-1217 |
2.76e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.62 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1023 PHPDLVDNGGWTAPPHIRP--TESPSDTPVPTAGALG----AEAEDIQGSWSPSPLLSE--ASYSPPGLEQTSINPLANF 1094
Cdd:PHA03247 2806 DPPAAVLAPAAALPPAASPagPLPPPTSAQPTAPPPPpgppPPSLPLGGSVAPGGDVRRrpPSRSPAAKPAAPARPPVRR 2885
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1095 L-----TEEDTPMGAPELGFPSLPWPPAsvddmmtPVGPGNPDELLVKEDEQSPPSTPWSDRNKLSTDGNP--------- 1160
Cdd:PHA03247 2886 LarpavSRSTESFALPPDQPERPPQPQA-------PPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPagagepsga 2958
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 133778949 1161 -----LGHTSPALPQSPIPTQPSPPSISPTQASPSPDVVEVSTGWNAAWDPVLEADLKPGHG 1217
Cdd:PHA03247 2959 vpqpwLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPP 3020
|
|
| PHA03377 |
PHA03377 |
EBNA-3C; Provisional |
973-1350 |
2.78e-03 |
|
EBNA-3C; Provisional
Pssm-ID: 177614 [Multi-domain] Cd Length: 1000 Bit Score: 42.35 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 973 PASSPKPVSISnaideeelDPPGP---------VFVDDFYYDYNFINFHEDLSYGSFEEPHPDLVDNG---GWTAPPHIR 1040
Cdd:PHA03377 481 PPQSPPTVAIK--------PAPPPsrrrrgacvVYDDDIIEVIDVETTEEEESVTQPAKPHRKVQDGFqrsGRRQKRATP 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1041 PTESPSDTPVPTAGalgaeaediqgswspSPLLSEASYSPPGLEQTSINPLAnflteEDTPMGAPELGFPSLPWPPASVD 1120
Cdd:PHA03377 553 PKVSPSDRGPPKAS---------------PPVMAPPSTGPRVMATPSTGPRD-----MAPPSTGPRQQAKCKDGPPASGP 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1121 DMMTPVGPGNPD-----------ELLVKEDEQSPPSTPW---SDRNKLSTDGNPLGHTSPAL-PQSPIPTQ-PSP---PS 1181
Cdd:PHA03377 613 HEKQPPSSAPRDmapsvvrmflrERLLEQSTGPKPKSFWemrAGRDGSGIQQEPSSRRQPATqSTPPRPSWlPSVfvlPS 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1182 ISPTQASPS------------PDVVEVSTGWNAAWDPvLEADLKPGHGELPSTVEVAS---PPLLPMATVPGIWgrdSPL 1246
Cdd:PHA03377 693 VDAGRAQPSeeshlssmsptqPISHEEQPRYEDPDDP-LDLSLHPDQAPPPSHQAPYSgheEPQAQQAPYPGYW---EPR 768
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1247 EPGTPTFSSPELSSQHLKTLTMPGTlllTVPTDLRSPGPS--------------GQPQTPnlEGTQSPGLLPT---PARE 1309
Cdd:PHA03377 769 PPQAPYLGYQEPQAQGVQVSSYPGY---AGPWGLRAQHPRyrhswaywsqypghGHPQGP--WAPRPPHLPPQwdgSAGH 843
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 133778949 1310 TQTNSSKDPEVQP--LQPSLEEDGDPADPLPARNASWQVGNWS 1350
Cdd:PHA03377 844 GQDQVSQFPHLQSetGPPRLQLSQVPQLPYSQTLVSSSAPSWS 886
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
1395-1450 |
3.45e-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: 3.45e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 133778949 1395 WRTGNWSKCSRNCGGGSSTRDVQCVDtrdlrPLRPFHCQPGPTKPPNRQLCGTQPC 1450
Cdd:smart00209 2 SEWSEWSPCSVTCGGGVQTRTRSCCS-----PPPQNGGGPCTGEDVETRACNEQPC 52
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1025-1192 |
3.96e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.23 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1025 PDLVDNGGWTAPPHIRPTESPSDTPVPTAGALGAEAEDiqGSWSPSplLSEASYSPPGLEQTSINPLANFLTEEDTPMGA 1104
Cdd:PHA03247 258 PPVVGEGADRAPETARGATGPPPPPEAAAPNGAAAPPD--GVWGAA--LAGAPLALPAPPDPPPPAPAGDAEEEDDEDGA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1105 PE-------------LGFPSL---PW-PPASVDDM-----------------------MTPVGPGNPDELLVKEDEQSPP 1144
Cdd:PHA03247 334 MEvvsplprprqhypLGFPKRrrpTWtPPSSLEDLsagrhhpkraslptrkrrsarhaATPFARGPGGDDQTRPAAPVPA 413
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 133778949 1145 STPWSDRNKLS-----TDGNPLGHTSPALPQSPIPT-QPSPPSISPTQASPSPD 1192
Cdd:PHA03247 414 SVPTPAPTPVPasappPPATPLPSAEPGSDDGPAPPpERQPPAPATEPAPDDPD 467
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
1033-1350 |
4.57e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 41.98 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1033 WTAPPHIRPTESPSDTPVPTAGALGAEAEDIQGSWSPSPLLSEASYSPPGLEQTSiNPLANFLTEEDTPMG---APELGF 1109
Cdd:PHA03378 542 YTEDLDIESDEPASTEPVHDQLLPAPGLGPLQIQPLTSPTTSQLASSAPSYAQTP-WPVPHPSQTPEPPTTqshIPETSA 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1110 PSlPWPPASVDDMMTPVG--------PGNPDELLVKEDEQSPPSTPWSDRNKLSTDGNPLGHtSPALPQSPIPTQPSPPS 1181
Cdd:PHA03378 621 PR-QWPMPLRPIPMRPLRmqpitfnvLVFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPTGA-NTMLPIQWAPGTMQPPP 698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1182 ISPTQASPSPDVVEVSTGWNAAWDPVLEADLKPGHGELPSTvevASPPLLPMATVPGIWGRDSplepGTPTFSSPELSSQ 1261
Cdd:PHA03378 699 RAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAA---APGRARPPAAAPGRARPPA----AAPGRARPPAAAP 771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778949 1262 HLKTLTMPGTlllTVPTDLRSP--GPSGQPQTpnlEGTQSPGLLPTPARETQTNSSKDPEVQPLQPSLEEdGDPADPLPA 1339
Cdd:PHA03378 772 GAPTPQPPPQ---APPAPQQRPrgAPTPQPPP---QAGPTSMQLMPRAAPGQQGPTKQILRQLLTGGVKR-GRPSLKKPA 844
|
330
....*....|.
gi 133778949 1340 RNASWQVGNWS 1350
Cdd:PHA03378 845 ALERQAAAGPT 855
|
|
| TSP1_spondin |
pfam19028 |
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ... |
1452-1499 |
5.38e-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: 36.49 E-value: 5.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 133778949 1452 PWytSSWRECSEACGGGEQQR---LVTCPEPG--LCEESLRpnnSRPCNTHPC 1499
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 ... |
1345-1392 |
9.45e-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: 9.45e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 133778949 1345 QVGNWSQCSTTCGLGAIWRLvscsSGNDEDCTLAsrpQPARHCHLRPC 1392
Cdd:pfam19035 4 QSTEWSPCSKTCGMGVSTRV----SNDNAECKLV---TETRLCQLRPC 44
|
|
| |
