|
Name |
Accession |
Description |
Interval |
E-value |
| VWD |
pfam00094 |
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
398-550 |
2.90e-29 |
|
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.
:
Pssm-ID: 459671 [Multi-domain] Cd Length: 154 Bit Score: 115.16 E-value: 2.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 398 CSLEGGSFVTTFDARPYRFHGTCTYTLLQSPQLPNEGTLMAVYDKSGYSHSETSLVAIMYLSKKDKIVISEDEVITNNGD 477
Cdd:pfam00094 1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907182200 478 TKLLPYKTHNITIFRQTSTHLQMATTFGLELVFQMQPVFQVYITVGPQFKGQTRGLCGNFNGDTTDDFTTSMG 550
Cdd:pfam00094 81 KVSLPYKSDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
|
|
| VWD |
smart00216 |
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ... |
857-1019 |
9.38e-28 |
|
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.
:
Pssm-ID: 214566 [Multi-domain] Cd Length: 163 Bit Score: 111.34 E-value: 9.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 857 WTCqLSTQCPSTCVLYGEGHIITFDGQRFVFDGDCEYMLATDdcgaNSSQPTFKVLTENVICGkSGVTCSRAIKISLGGL 936
Cdd:smart00216 1 WCC-TQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQD----CSSEPTFSVLLKNVPCG-GGATCLKSVKVELNGD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 937 FITMADSN--YTVSGE-------EPLVHLKVKPSPLNLVLdidIPGRLNLTLVWNKHMSVSIKIrRATQQDALCGLCGNA 1007
Cdd:smart00216 75 EIELKDDNgkVTVNGQqvslpykTSDGSIQIRSSGGYLVV---ITSLGLIQVTFDGLTLLSVQL-PSKYRGKTCGLCGNF 150
|
170
....*....|..
gi 1907182200 1008 NGNMKDDFETRS 1019
Cdd:smart00216 151 DGEPEDDFRTPD 162
|
|
| VWD |
pfam00094 |
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
45-194 |
1.38e-25 |
|
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.
:
Pssm-ID: 459671 [Multi-domain] Cd Length: 154 Bit Score: 104.76 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 45 CSTWGAGHFSTFDGHEYNFQGMCNYIFTATCGDDVPATFSIQLRRDMEGN----ISRIIMELGASVVTVNKETISVRDIG 120
Cdd:pfam00094 1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGAsgvcLKSVTVIVGDLEITLQKGGTVLVNGQ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907182200 121 VVSLPYTSNGLQITPYGQSVQLVAKQLELELVITWGPDAHLTVQVETKYMGKLCGLCGNFDGKIDNEFLSEDGK 194
Cdd:pfam00094 81 KVSLPYKSDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
|
|
| C8 |
smart00832 |
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
1058-1130 |
1.81e-25 |
|
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.
:
Pssm-ID: 214843 Cd Length: 76 Bit Score: 101.65 E-value: 1.81e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907182200 1058 WAERKCNIINSQ--TFAACHSKVYHLPYYEACVRDACGCdtGGDCECLCDAVAAYAKACLDKGVCV-DWRTPDFCP 1130
Cdd:smart00832 3 YACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCAC--GGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
|
|
| C8 |
smart00832 |
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
589-661 |
1.14e-19 |
|
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.
:
Pssm-ID: 214843 Cd Length: 76 Bit Score: 85.08 E-value: 1.14e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907182200 589 AETHCSMLLKKGSVFEKCHSVVNPQPFYKRCVYQACNYEETFPHICSALGAYAHACSARGILLWGWRNSvDNC 661
Cdd:smart00832 4 ACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTP-TFC 75
|
|
| TIL |
pfam01826 |
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
303-358 |
3.56e-14 |
|
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.
:
Pssm-ID: 460351 Cd Length: 55 Bit Score: 68.57 E-value: 3.56e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907182200 303 CPANQVYQECGEVCIKTCSNPQH--SCSSPCTFGCFCPHGTLLDDisgNQSCVPVNQC 358
Cdd:pfam01826 1 CPANEVYSECGSACPPTCANLSPpdVCPEPCVEGCVCPPGFVRNS---GGKCVPPSDC 55
|
|
| Herpes_BLLF1 super family |
cl37540 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
1464-1901 |
7.91e-12 |
|
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.
The actual alignment was detected with superfamily member pfam05109:
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 71.10 E-value: 7.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1464 SPQTIfssIHPKTTLEATTPQHT---APLITSITSSITQAQSSFSTDKTYTSQhsqPSTMTAHQSRSLPTVTTSTKSTMG 1540
Cdd:pfam05109 399 APKTL---IITRTATNATTTTHKvifSKAPESTTTSPTLNTTGFAAPNTTTGL---PSSTHVPTNLTAPASTGPTVSTAD 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1541 LTGTPPVHTTSGTTS-----SPQTPRTTHPFSTVAVSNTKHTTGVSLETSVQTTIASPTPSAPQTSLATHLPFSSTSS-- 1613
Cdd:pfam05109 473 VTSPTPAGTTSGASPvtpspSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTpt 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1614 --VTPTSEVIITPTPQhtlssaSTSTTTGNILPTTIGQTGSPHTSVPVIYTTSAITQTKTSFSTDRTSTPT-SAPHLSET 1690
Cdd:pfam05109 553 pnATSPTPAVTTPTPN------ATIPTLGKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTLGGTSSTPVvTSPPKNAT 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1691 SAVTA--HQSTPTAVSANSIKPT-MSSTGTPvvHTTSGTTSSPQTPRTTHPSttvavSGTVHTTGLPSGTSVHTTTNFPT 1767
Cdd:pfam05109 627 SAVTTgqHNITSSSTSSMSLRPSsISETLSP--STSDNSTSHMPLLTSAHPT-----GGENITQVTPASTSTHHVSTSSP 699
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1768 HSGPQSSLSTHLPLFSTLSVTPTTEGLNTPTSPHSLSVASTSMPLMTVLPTTLEGTRPPHTSVPVTYTTTAATQTKSSFS 1847
Cdd:pfam05109 700 APRPGTTSQASGPGNSSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTSTGGKANSTTGGKHTTGHGARTSTEPT 779
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907182200 1848 TD---RTSTPHLSQSSTvtptqsTPIPATTNSLMTTGGLTGTPPVHTTSGTTSSPQT 1901
Cdd:pfam05109 780 TDyggDSTTPRTRYNAT------TYLPPSTSSKLRPRWTFTSPPVTTAQATVPVPPT 830
|
|
| TIL |
cd19941 |
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
765-828 |
3.22e-11 |
|
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.
:
Pssm-ID: 410995 Cd Length: 55 Bit Score: 60.41 E-value: 3.22e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907182200 765 CPEPKTFQSCsqssedkfGAACAPTCQMLATGIDCvPTKCESGCVCPKGLYENSDGQCVPAEEC 828
Cdd:cd19941 1 CPPNEVYSEC--------GSACPPTCANPNAPPPC-TKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
|
|
| DUF5585 super family |
cl39316 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
1732-2111 |
3.56e-11 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
The actual alignment was detected with superfamily member pfam17823:
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 68.06 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1732 TPRTTHPSTTVAVSGTVHTTGLPSGT--SVHTTTNFPTHSGPQSSLSTHlplfSTLSVTPTTEGLNTPTSPHSLSVASTS 1809
Cdd:pfam17823 55 SEQ*NFCAATAAPAPVTLTKGTSAAHlnSTEVTAEHTPHGTDLSEPATR----EGAADGAASRALAAAASSSPSSAAQSL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1810 MPLMTVLPTtlEGTRPPHTSVPvtytttaatqtkssfSTDRTSTPHLSQSSTVTPTQSTPIPATTNSLMTTGGLTGTPPV 1889
Cdd:pfam17823 131 PAAIAALPS--EAFSAPRAAAC---------------RANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1890 HTTSGTTSSPQTPHSTHPISTAAISRTTGISGT-----PFRTPMKTTITFPTPSSLQTSMATLfppfstsvmssteifnt 1964
Cdd:pfam17823 194 APTTAASSAPATLTPARGISTAATATGHPAAGTalaavGNSSPAAGTVTAAVGTVTPAALATL----------------- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1965 ptNPHSVSSASTSRPLSTSLPTTIKGTGTPQTPvsdiNTTSATTQAHSSFPTTRTSTSHLSLPSSMTSTL---TPASRSA 2041
Cdd:pfam17823 257 --AAAAGTVASAAGTINMGDPHARRLSPAKHMP----SDTMARNPAAPMGAQAQGPIIQVSTDQPVHNTAgepTPSPSNT 330
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907182200 2042 STLQYTPTPSSVSHSPLLTTPTASP--PSSAPTFVSPTAASTVISSALPTIHMTPTPSSRPTSSTGLLSTSK 2111
Cdd:pfam17823 331 TLEPNTPKSVASTNLAVVTTTKAQAkePSASPVPVLHTSMIPEVEATSPTTQPSPLLPTQGAAGPGILLAPE 402
|
|
| CT |
smart00041 |
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ... |
2220-2299 |
1.18e-09 |
|
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta (TGFbeta), nerve growth factor (NGF), platelet-derived growth factor (PDGF) and gonadotropin all form 2 highly twisted antiparallel pairs of beta-strands and contain three disulphide bonds. The domain is non-globular and little is conserved among these presumed homologues except for their cysteine residues. CT domains are predicted to form homodimers.
:
Pssm-ID: 214482 Cd Length: 82 Bit Score: 56.64 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 2220 EHQITYQGCVAN-VTLTRCQGFCASSVSFNkdTLQLESSCGCCQPLSTYKKQLSLPCPDpdapGQQLTLTLQVFSSCVCS 2298
Cdd:smart00041 5 RQTITYNGCTSVtVKNAFCEGKCGSASSYS--IQDVQHSCSCCQPHKTKTRQVRLRCPD----GSTVKKTVMHIEECGCE 78
|
.
gi 1907182200 2299 P 2299
Cdd:smart00041 79 P 79
|
|
| C8 |
pfam08742 |
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ... |
246-298 |
5.32e-09 |
|
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.
:
Pssm-ID: 462584 Cd Length: 68 Bit Score: 54.31 E-value: 5.32e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1907182200 246 VPKETLMLSCQADMaaCARPGQPNCSCATLSEYSRRCSMTGQPVRNWRTPALC 298
Cdd:pfam08742 18 VDPEPYFEACVYDM--CSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
|
|
| TIL |
cd19941 |
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
665-722 |
5.17e-06 |
|
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.
:
Pssm-ID: 410995 Cd Length: 55 Bit Score: 45.77 E-value: 5.17e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907182200 665 CTGNRTFSYDSQACDRTCLSLsDRETEChvSPVPVDGCNCPEGTYLNHKAECVHKAQC 722
Cdd:cd19941 1 CPPNEVYSECGSACPPTCANP-NAPPPC--TKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
|
|
| VWC_out |
smart00215 |
von Willebrand factor (vWF) type C domain; |
360-404 |
5.03e-05 |
|
von Willebrand factor (vWF) type C domain;
:
Pssm-ID: 214565 Cd Length: 67 Bit Score: 43.32 E-value: 5.03e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1907182200 360 CMLNGMVYGPGEITKTACQTCQCTMGRWTCTKQPC-PGHCSLEGGS 404
Cdd:smart00215 1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCgPKPCLLHNLS 46
|
|
| Herpes_BLLF1 super family |
cl37540 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
1260-1607 |
3.83e-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.
The actual alignment was detected with superfamily member pfam05109:
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 45.68 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1260 TTPKESTVSSGEYPQTtmaatpptspwpPTSIPKSTPTELPVTQATSkPTASSLSSSTKTTAELTESTTVTLLTLMPGMs 1339
Cdd:pfam05109 474 TSPTPAGTTSGASPVT------------PSPSPRDNGTESKAPDMTS-PTSAVTTPTPNATSPTPAVTTPTPNATSPTL- 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1340 tsqGKTSASyttqhqstsfhlTTISKWPTNGVSDTPGVHTSsgTPSSSHATHITYTPPTQVVSSITHSTGPPLG-TSVQT 1418
Cdd:pfam05109 540 ---GKTSPT------------SAVTTPTPNATSPTPAVTTP--TPNATIPTLGKTSPTSAVTTPTPNATSPTVGeTSPQA 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1419 TINFPTLSA-PQTSLVTPHPGLSSSSTALTSEILKTPTSSQMvsSASPQTIFSSIHPKTTLEATTpqhTAPLITSI---- 1493
Cdd:pfam05109 603 NTTNHTLGGtSSTPVVTSPPKNATSAVTTGQHNITSSSTSSM--SLRPSSISETLSPSTSDNSTS---HMPLLTSAhptg 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1494 TSSITQAQSSFSTDKTYTSQHSQPSTMTAHQSRSLPTVTTSTK-STMGLT-GTPPVHTTSGTTSSPQTPRTTHPFSTVAV 1571
Cdd:pfam05109 678 GENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKpGEVNVTkGTPPKNATSPQAPSGQKTAVPTVTSTGGK 757
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1907182200 1572 SNT----KHTTGVSLETSVQ-TTIASPTPSAPQT--SLATHLP 1607
Cdd:pfam05109 758 ANSttggKHTTGHGARTSTEpTTDYGGDSTTPRTryNATTYLP 800
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| VWD |
pfam00094 |
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
398-550 |
2.90e-29 |
|
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.
Pssm-ID: 459671 [Multi-domain] Cd Length: 154 Bit Score: 115.16 E-value: 2.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 398 CSLEGGSFVTTFDARPYRFHGTCTYTLLQSPQLPNEGTLMAVYDKSGYSHSETSLVAIMYLSKKDKIVISEDEVITNNGD 477
Cdd:pfam00094 1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907182200 478 TKLLPYKTHNITIFRQTSTHLQMATTFGLELVFQMQPVFQVYITVGPQFKGQTRGLCGNFNGDTTDDFTTSMG 550
Cdd:pfam00094 81 KVSLPYKSDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
|
|
| VWD |
smart00216 |
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ... |
387-550 |
4.86e-29 |
|
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.
Pssm-ID: 214566 [Multi-domain] Cd Length: 163 Bit Score: 115.19 E-value: 4.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 387 WTCTKQPCPGHCSLEGGSFVTTFDARPYRFHGTCTYTLLQSpqLPNEGTLMAVYDKSGYSHSETSLVAIMYLSKKDKIVI 466
Cdd:smart00216 1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQD--CSSEPTFSVLLKNVPCGGGATCLKSVKVELNGDEIEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 467 SEDEV-ITNNGDTKLLPYKTHNITI-FRQTSTHLQMATTFGLELVfQMQPVFQVYITVGPQFKGQTRGLCGNFNGDTTDD 544
Cdd:smart00216 79 KDDNGkVTVNGQQVSLPYKTSDGSIqIRSSGGYLVVITSLGLIQV-TFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157
|
....*.
gi 1907182200 545 FTTSMG 550
Cdd:smart00216 158 FRTPDG 163
|
|
| VWD |
smart00216 |
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ... |
857-1019 |
9.38e-28 |
|
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.
Pssm-ID: 214566 [Multi-domain] Cd Length: 163 Bit Score: 111.34 E-value: 9.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 857 WTCqLSTQCPSTCVLYGEGHIITFDGQRFVFDGDCEYMLATDdcgaNSSQPTFKVLTENVICGkSGVTCSRAIKISLGGL 936
Cdd:smart00216 1 WCC-TQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQD----CSSEPTFSVLLKNVPCG-GGATCLKSVKVELNGD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 937 FITMADSN--YTVSGE-------EPLVHLKVKPSPLNLVLdidIPGRLNLTLVWNKHMSVSIKIrRATQQDALCGLCGNA 1007
Cdd:smart00216 75 EIELKDDNgkVTVNGQqvslpykTSDGSIQIRSSGGYLVV---ITSLGLIQVTFDGLTLLSVQL-PSKYRGKTCGLCGNF 150
|
170
....*....|..
gi 1907182200 1008 NGNMKDDFETRS 1019
Cdd:smart00216 151 DGEPEDDFRTPD 162
|
|
| VWD |
pfam00094 |
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
45-194 |
1.38e-25 |
|
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.
Pssm-ID: 459671 [Multi-domain] Cd Length: 154 Bit Score: 104.76 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 45 CSTWGAGHFSTFDGHEYNFQGMCNYIFTATCGDDVPATFSIQLRRDMEGN----ISRIIMELGASVVTVNKETISVRDIG 120
Cdd:pfam00094 1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGAsgvcLKSVTVIVGDLEITLQKGGTVLVNGQ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907182200 121 VVSLPYTSNGLQITPYGQSVQLVAKQLELELVITWGPDAHLTVQVETKYMGKLCGLCGNFDGKIDNEFLSEDGK 194
Cdd:pfam00094 81 KVSLPYKSDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
|
|
| C8 |
smart00832 |
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
1058-1130 |
1.81e-25 |
|
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.
Pssm-ID: 214843 Cd Length: 76 Bit Score: 101.65 E-value: 1.81e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907182200 1058 WAERKCNIINSQ--TFAACHSKVYHLPYYEACVRDACGCdtGGDCECLCDAVAAYAKACLDKGVCV-DWRTPDFCP 1130
Cdd:smart00832 3 YACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCAC--GGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
|
|
| VWD |
smart00216 |
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ... |
45-193 |
2.27e-24 |
|
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.
Pssm-ID: 214566 [Multi-domain] Cd Length: 163 Bit Score: 101.71 E-value: 2.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 45 CSTWGAGHFSTFDGHEYNFQGMCNYIFTATCGDDvpATFSIQLRRDMEG----NISRIIMELGASVVTVNKETISVR-DI 119
Cdd:smart00216 12 CSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSE--PTFSVLLKNVPCGggatCLKSVKVELNGDEIELKDDNGKVTvNG 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907182200 120 GVVSLPYTSNGLQITPYgQSVQLVAKQLELELV-ITWGPDAHLTVQVETKYMGKLCGLCGNFDGKIDNEFLSEDG 193
Cdd:smart00216 90 QQVSLPYKTSDGSIQIR-SSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
|
|
| C8 |
pfam08742 |
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ... |
1062-1129 |
3.70e-22 |
|
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.
Pssm-ID: 462584 Cd Length: 68 Bit Score: 91.67 E-value: 3.70e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1062 KCNIINSQT-FAACHSKVYHLPYYEACVRDACGCdtGGDCECLCDAVAAYAKACLDKGVCV-DWRTPDFC 1129
Cdd:pfam08742 1 KCGLLSDSGpFAPCHSVVDPEPYFEACVYDMCSC--GGDDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
|
|
| VWD |
pfam00094 |
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
869-1019 |
1.23e-20 |
|
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.
Pssm-ID: 459671 [Multi-domain] Cd Length: 154 Bit Score: 90.51 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 869 CVLYGEGHIITFDGQRFVFDGDCEYMLAtDDCGANSSqPTFKVLTENVICGKSGVtCSRAIKISLGGLFITMADSNY-TV 947
Cdd:pfam00094 1 CSVSGDPHYVTFDGVKYTFPGTCTYVLA-KDCSEEPD-FSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGTvLV 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907182200 948 SGEEplVHLKVKPSPLNL------VLDIDIPGRLNLTLVWNKHMSVSIKIRRaTQQDALCGLCGNANGNMKDDFETRS 1019
Cdd:pfam00094 78 NGQK--VSLPYKSDGGEVeilgsgFVVVDLSPGVGLQVDGDGRGQLFVTLSP-SYQGKTCGLCGNYNGNQEDDFMTPD 152
|
|
| C8 |
smart00832 |
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
589-661 |
1.14e-19 |
|
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.
Pssm-ID: 214843 Cd Length: 76 Bit Score: 85.08 E-value: 1.14e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907182200 589 AETHCSMLLKKGSVFEKCHSVVNPQPFYKRCVYQACNYEETFPHICSALGAYAHACSARGILLWGWRNSvDNC 661
Cdd:smart00832 4 ACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTP-TFC 75
|
|
| C8 |
pfam08742 |
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ... |
592-661 |
2.09e-18 |
|
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.
Pssm-ID: 462584 Cd Length: 68 Bit Score: 81.27 E-value: 2.09e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 592 HCSMLLKKGsVFEKCHSVVNPQPFYKRCVYQACNYEETFPHICSALGAYAHACSARGILLWGWRNSvDNC 661
Cdd:pfam08742 1 KCGLLSDSG-PFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTP-TFC 68
|
|
| TIL |
pfam01826 |
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
303-358 |
3.56e-14 |
|
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.
Pssm-ID: 460351 Cd Length: 55 Bit Score: 68.57 E-value: 3.56e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907182200 303 CPANQVYQECGEVCIKTCSNPQH--SCSSPCTFGCFCPHGTLLDDisgNQSCVPVNQC 358
Cdd:pfam01826 1 CPANEVYSECGSACPPTCANLSPpdVCPEPCVEGCVCPPGFVRNS---GGKCVPPSDC 55
|
|
| TIL |
cd19941 |
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
303-358 |
2.21e-13 |
|
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.
Pssm-ID: 410995 Cd Length: 55 Bit Score: 66.57 E-value: 2.21e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907182200 303 CPANQVYQECGEVCIKTCSNPQH--SCSSPCTFGCFCPHGTLLDDisgNQSCVPVNQC 358
Cdd:cd19941 1 CPPNEVYSECGSACPPTCANPNAppPCTKQCVEGCFCPEGYVRNS---GGKCVPPSQC 55
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
1464-1901 |
7.91e-12 |
|
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: 71.10 E-value: 7.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1464 SPQTIfssIHPKTTLEATTPQHT---APLITSITSSITQAQSSFSTDKTYTSQhsqPSTMTAHQSRSLPTVTTSTKSTMG 1540
Cdd:pfam05109 399 APKTL---IITRTATNATTTTHKvifSKAPESTTTSPTLNTTGFAAPNTTTGL---PSSTHVPTNLTAPASTGPTVSTAD 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1541 LTGTPPVHTTSGTTS-----SPQTPRTTHPFSTVAVSNTKHTTGVSLETSVQTTIASPTPSAPQTSLATHLPFSSTSS-- 1613
Cdd:pfam05109 473 VTSPTPAGTTSGASPvtpspSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTpt 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1614 --VTPTSEVIITPTPQhtlssaSTSTTTGNILPTTIGQTGSPHTSVPVIYTTSAITQTKTSFSTDRTSTPT-SAPHLSET 1690
Cdd:pfam05109 553 pnATSPTPAVTTPTPN------ATIPTLGKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTLGGTSSTPVvTSPPKNAT 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1691 SAVTA--HQSTPTAVSANSIKPT-MSSTGTPvvHTTSGTTSSPQTPRTTHPSttvavSGTVHTTGLPSGTSVHTTTNFPT 1767
Cdd:pfam05109 627 SAVTTgqHNITSSSTSSMSLRPSsISETLSP--STSDNSTSHMPLLTSAHPT-----GGENITQVTPASTSTHHVSTSSP 699
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1768 HSGPQSSLSTHLPLFSTLSVTPTTEGLNTPTSPHSLSVASTSMPLMTVLPTTLEGTRPPHTSVPVTYTTTAATQTKSSFS 1847
Cdd:pfam05109 700 APRPGTTSQASGPGNSSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTSTGGKANSTTGGKHTTGHGARTSTEPT 779
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907182200 1848 TD---RTSTPHLSQSSTvtptqsTPIPATTNSLMTTGGLTGTPPVHTTSGTTSSPQT 1901
Cdd:pfam05109 780 TDyggDSTTPRTRYNAT------TYLPPSTSSKLRPRWTFTSPPVTTAQATVPVPPT 830
|
|
| TIL |
cd19941 |
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
765-828 |
3.22e-11 |
|
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.
Pssm-ID: 410995 Cd Length: 55 Bit Score: 60.41 E-value: 3.22e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907182200 765 CPEPKTFQSCsqssedkfGAACAPTCQMLATGIDCvPTKCESGCVCPKGLYENSDGQCVPAEEC 828
Cdd:cd19941 1 CPPNEVYSEC--------GSACPPTCANPNAPPPC-TKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
1732-2111 |
3.56e-11 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 68.06 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1732 TPRTTHPSTTVAVSGTVHTTGLPSGT--SVHTTTNFPTHSGPQSSLSTHlplfSTLSVTPTTEGLNTPTSPHSLSVASTS 1809
Cdd:pfam17823 55 SEQ*NFCAATAAPAPVTLTKGTSAAHlnSTEVTAEHTPHGTDLSEPATR----EGAADGAASRALAAAASSSPSSAAQSL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1810 MPLMTVLPTtlEGTRPPHTSVPvtytttaatqtkssfSTDRTSTPHLSQSSTVTPTQSTPIPATTNSLMTTGGLTGTPPV 1889
Cdd:pfam17823 131 PAAIAALPS--EAFSAPRAAAC---------------RANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1890 HTTSGTTSSPQTPHSTHPISTAAISRTTGISGT-----PFRTPMKTTITFPTPSSLQTSMATLfppfstsvmssteifnt 1964
Cdd:pfam17823 194 APTTAASSAPATLTPARGISTAATATGHPAAGTalaavGNSSPAAGTVTAAVGTVTPAALATL----------------- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1965 ptNPHSVSSASTSRPLSTSLPTTIKGTGTPQTPvsdiNTTSATTQAHSSFPTTRTSTSHLSLPSSMTSTL---TPASRSA 2041
Cdd:pfam17823 257 --AAAAGTVASAAGTINMGDPHARRLSPAKHMP----SDTMARNPAAPMGAQAQGPIIQVSTDQPVHNTAgepTPSPSNT 330
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907182200 2042 STLQYTPTPSSVSHSPLLTTPTASP--PSSAPTFVSPTAASTVISSALPTIHMTPTPSSRPTSSTGLLSTSK 2111
Cdd:pfam17823 331 TLEPNTPKSVASTNLAVVTTTKAQAkePSASPVPVLHTSMIPEVEATSPTTQPSPLLPTQGAAGPGILLAPE 402
|
|
| TIL |
pfam01826 |
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
765-828 |
4.63e-11 |
|
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.
Pssm-ID: 460351 Cd Length: 55 Bit Score: 59.71 E-value: 4.63e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907182200 765 CPEPKTFQSCsqssedkfGAACAPTCQMLATGIDCvPTKCESGCVCPKGLYENSDGQCVPAEEC 828
Cdd:pfam01826 1 CPANEVYSEC--------GSACPPTCANLSPPDVC-PEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1674-2115 |
1.36e-10 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 67.27 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1674 STDRTSTPTSAPHLSETSAvtAHQSTPTAVSAnsikPTMSStgtPVVHTTSGTTSSPqtPRTTHPSTTVAVSGTVHTTGL 1753
Cdd:PHA03247 2545 SDDAGDPPPPLPPAAPPAA--PDRSVPPPRPA----PRPSE---PAVTSRARRPDAP--PQSARPRAPVDDRGDPRGPAP 2613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1754 PSGTSVHTTTNFPTHSGPqSSLSTHLPLFSTLSVTPTTEGLNTPTSPH-SLSVASTSMPLMTVLPTTLEGTRPPHTSVPV 1832
Cdd:PHA03247 2614 PSPLPPDTHAPDPPPPSP-SPAANEPDPHPPPTVPPPERPRDDPAPGRvSRPRRARRLGRAAQASSPPQRPRRRAARPTV 2692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1833 TYTTTaatqtkSSFSTDRTSTPHLSQSSTVTPTQSTPIPATTNSLMTTGGLT-GTPPVHTTSGTTSSPQTPHSthPISTA 1911
Cdd:PHA03247 2693 GSLTS------LADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAApAPPAVPAGPATPGGPARPAR--PPTTA 2764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1912 AISRTTGISGTPfrTPMKTTITFPTPSSLQTSMATLFPPFSTSVMSSTEIFNTPTNPHSVSSASTSRPLSTSLPT----- 1986
Cdd:PHA03247 2765 GPPAPAPPAAPA--AGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTapppp 2842
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1987 --------TIKGTGTPQTPVSdintTSATTQAHSSFPTTRT--STSHLSLPSSMTST-------LTPASRSASTLQYTPT 2049
Cdd:PHA03247 2843 pgppppslPLGGSVAPGGDVR----RRPPSRSPAAKPAAPArpPVRRLARPAVSRSTesfalppDQPERPPQPQAPPPPQ 2918
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 2050 PSSVSHSPLLTTPTASPPSSAPTFVSPTAASTVISSALPTI------HMTP---------TPSSRPTSSTGLLSTSKTTS 2114
Cdd:PHA03247 2919 PQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVpqpwlgALVPgrvavprfrVPQPAPSREAPASSTPPLTG 2998
|
.
gi 1907182200 2115 H 2115
Cdd:PHA03247 2999 H 2999
|
|
| CT |
smart00041 |
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ... |
2220-2299 |
1.18e-09 |
|
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta (TGFbeta), nerve growth factor (NGF), platelet-derived growth factor (PDGF) and gonadotropin all form 2 highly twisted antiparallel pairs of beta-strands and contain three disulphide bonds. The domain is non-globular and little is conserved among these presumed homologues except for their cysteine residues. CT domains are predicted to form homodimers.
Pssm-ID: 214482 Cd Length: 82 Bit Score: 56.64 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 2220 EHQITYQGCVAN-VTLTRCQGFCASSVSFNkdTLQLESSCGCCQPLSTYKKQLSLPCPDpdapGQQLTLTLQVFSSCVCS 2298
Cdd:smart00041 5 RQTITYNGCTSVtVKNAFCEGKCGSASSYS--IQDVQHSCSCCQPHKTKTRQVRLRCPD----GSTVKKTVMHIEECGCE 78
|
.
gi 1907182200 2299 P 2299
Cdd:smart00041 79 P 79
|
|
| C8 |
pfam08742 |
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ... |
246-298 |
5.32e-09 |
|
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.
Pssm-ID: 462584 Cd Length: 68 Bit Score: 54.31 E-value: 5.32e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1907182200 246 VPKETLMLSCQADMaaCARPGQPNCSCATLSEYSRRCSMTGQPVRNWRTPALC 298
Cdd:pfam08742 18 VDPEPYFEACVYDM--CSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
|
|
| C8 |
smart00832 |
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
246-299 |
7.47e-08 |
|
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.
Pssm-ID: 214843 Cd Length: 76 Bit Score: 51.57 E-value: 7.47e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1907182200 246 VPKETLMLSCQADMaaCARPGQPNCSCATLSEYSRRCSMTGQPVRNWRTPALCP 299
Cdd:smart00832 25 VDPEPFFENCVYDT--CACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1773-2106 |
3.01e-07 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 56.16 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1773 SSLSTHLPLFSTLSVTPTTEGLNTPTSPhslSVASTSMPLMTVLP--------TTLEGTRPPHTSVPVTYTTTAATQTKS 1844
Cdd:TIGR00927 52 AAVSSQQPIKLASRDLSNDEMMMVSSDP---PKSSSEMEGEMLAPqatvgrdeATPSIAMENTPSPPRRTAKITPTTPKN 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1845 SFSTDRTSTPHLSQSSTVTP---------TQSTPIpATTNSLMTTGGLTGTPPVHTTSGT---TSSP------------- 1899
Cdd:TIGR00927 129 NYSPTAAGTERVKEDTPATPsralnhyisTSGRQR-VKSYTPKPRGEVKSSSPTQTREKVrkyTPSPlgrmvnsyapstf 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1900 ---QTPHSTHPISTAAISRTTGISGTPFRTPMKTTITFPTPSSLQtSMATLFPPFSTSVMSsTEIFNTPTN--------- 1967
Cdd:TIGR00927 208 mtmPRSHGITPRTTVKDSEITATYKMLETNPSKRTAGKTTPTPLK-GMTDNTPTFLTREVE-TDLLTSPRSvvekntltt 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1968 PHSVSSASTSRP---LSTSLPTTIKGTGTPQTPVSDINTTSATTQAHSSFPTTRTSTSHLSLPSSMTSTLTPASRSASTL 2044
Cdd:TIGR00927 286 PRRVESNSSTNHwglVGKNNLTTPQGTVLEHTPATSEGQVTISIMTGSSPAETKASTAAWKIRNPLSRTSAPAVRIASAT 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907182200 2045 --QYTPTPSSVSHSPLLTTPTASPPSSA-------PTFVSPTAASTVISSALPTIHMTPTPSSRPTSSTGL 2106
Cdd:TIGR00927 366 frGLEKNPSTAPSTPATPRVRAVLTTQVhhcvvvkPAPAVPTTPSPSLTTALFPEAPSPSPSALPPGQPDL 436
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
1879-2116 |
5.16e-07 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 54.76 E-value: 5.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1879 TTGGLTGTPPVHTTSGTTSSPQTPHSTHPISTAAISRTTGISGTPFRTPMKTTITFPTPSSLQTSMATLFPPFSTSVMSS 1958
Cdd:COG3469 2 SSVSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1959 TEIFNTPtnphsvsSASTSRPLSTSLPTTIKGTGTPQTPVSDINTTSATTQAHSSFPTTRTSTSHLSLPSSMTSTLTPAS 2038
Cdd:COG3469 82 ATAAAAA-------ATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907182200 2039 RSASTLQYTPTPSSVShspllTTPTASPPSSAPTFVSPTAASTvissalptihmTPTPSSRPTSSTGLLSTSKTTSHV 2116
Cdd:COG3469 155 GTETATGGTTTTSTTT-----TTTSASTTPSATTTATATTASG-----------ATTPSATTTATTTGPPTPGLPKHV 216
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1849-2177 |
6.54e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 55.33 E-value: 6.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1849 DRTSTPHLSQSSTVTP--TQSTPIPATTNSLMTTGGLTGTPPVHTTSGTTSSPQTPHSTHPISTAAISRTTGISGTPfRT 1926
Cdd:PHA03247 2604 DRGDPRGPAPPSPLPPdtHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPP-QR 2682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1927 PMKTTITfPTPSSLqTSMATLFPPFST---SVMSSTEIFNTPTNPHSVSSASTSRPLSTSLPTTIKGTGTPQTPVSDINT 2003
Cdd:PHA03247 2683 PRRRAAR-PTVGSL-TSLADPPPPPPTpepAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARP 2760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 2004 TSATTQAHSSFPTTRTSTSHLSLPSSMTSTLTPASRSASTLQYTPTPSSVSHSPLLTTPTASPPssAPTFVSPTAASTVI 2083
Cdd:PHA03247 2761 PTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP--AGPLPPPTSAQPTA 2838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 2084 SSALPTIHMTPTPSSRPTSSTGLLSTSKTTSHVPTFSSFSSKSTTAHLTSLTTQAATSGLLSSTMGMTNLPSSGSPDINH 2163
Cdd:PHA03247 2839 PPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQ 2918
|
330
....*....|....
gi 1907182200 2164 TTRPPGSSPLPTSA 2177
Cdd:PHA03247 2919 PQPQPPPPPQPQPP 2932
|
|
| TIL |
cd19941 |
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
665-722 |
5.17e-06 |
|
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.
Pssm-ID: 410995 Cd Length: 55 Bit Score: 45.77 E-value: 5.17e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907182200 665 CTGNRTFSYDSQACDRTCLSLsDRETEChvSPVPVDGCNCPEGTYLNHKAECVHKAQC 722
Cdd:cd19941 1 CPPNEVYSECGSACPPTCANP-NAPPPC--TKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
1640-1831 |
8.91e-06 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 50.91 E-value: 8.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1640 GNILPTTIGQTGSPHTSVPVIYTTSAITQTKTSFSTDRTSTPTSAPhlSETSAVTAHQSTPTAVSANSIKPTMSSTGTPV 1719
Cdd:COG3469 24 GAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASST--AATSSTTSTTATATAAAAAATSTSATLVATST 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1720 VHTTSGTTSSPQTPRTTHPSTTVAVSGTVHTTGLP--SGTSVHTTTNFPTHSGPQSSLSTHLPLFSTLSVTPTTEGLNTP 1797
Cdd:COG3469 102 ASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSgaSATSSAGSTTTTTTVSGTETATGGTTTTSTTTTTTSASTTPSA 181
|
170 180 190
....*....|....*....|....*....|....
gi 1907182200 1798 TSPHSLSVASTSMPLMTVLPTTleGTRPPHTSVP 1831
Cdd:COG3469 182 TTTATATTASGATTPSATTTAT--TTGPPTPGLP 213
|
|
| VWC_out |
smart00215 |
von Willebrand factor (vWF) type C domain; |
360-404 |
5.03e-05 |
|
von Willebrand factor (vWF) type C domain;
Pssm-ID: 214565 Cd Length: 67 Bit Score: 43.32 E-value: 5.03e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1907182200 360 CMLNGMVYGPGEITKTACQTCQCTMGRWTCTKQPC-PGHCSLEGGS 404
Cdd:smart00215 1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCgPKPCLLHNLS 46
|
|
| TIL |
pfam01826 |
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
665-722 |
2.88e-04 |
|
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.
Pssm-ID: 460351 Cd Length: 55 Bit Score: 40.83 E-value: 2.88e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907182200 665 CTGNRTFSYDSQACDRTCLSLSDR---ETEChvspvpVDGCNCPEGTYLNHKAECVHKAQC 722
Cdd:pfam01826 1 CPANEVYSECGSACPPTCANLSPPdvcPEPC------VEGCVCPPGFVRNSGGKCVPPSDC 55
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
1260-1607 |
3.83e-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: 45.68 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1260 TTPKESTVSSGEYPQTtmaatpptspwpPTSIPKSTPTELPVTQATSkPTASSLSSSTKTTAELTESTTVTLLTLMPGMs 1339
Cdd:pfam05109 474 TSPTPAGTTSGASPVT------------PSPSPRDNGTESKAPDMTS-PTSAVTTPTPNATSPTPAVTTPTPNATSPTL- 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1340 tsqGKTSASyttqhqstsfhlTTISKWPTNGVSDTPGVHTSsgTPSSSHATHITYTPPTQVVSSITHSTGPPLG-TSVQT 1418
Cdd:pfam05109 540 ---GKTSPT------------SAVTTPTPNATSPTPAVTTP--TPNATIPTLGKTSPTSAVTTPTPNATSPTVGeTSPQA 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1419 TINFPTLSA-PQTSLVTPHPGLSSSSTALTSEILKTPTSSQMvsSASPQTIFSSIHPKTTLEATTpqhTAPLITSI---- 1493
Cdd:pfam05109 603 NTTNHTLGGtSSTPVVTSPPKNATSAVTTGQHNITSSSTSSM--SLRPSSISETLSPSTSDNSTS---HMPLLTSAhptg 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1494 TSSITQAQSSFSTDKTYTSQHSQPSTMTAHQSRSLPTVTTSTK-STMGLT-GTPPVHTTSGTTSSPQTPRTTHPFSTVAV 1571
Cdd:pfam05109 678 GENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKpGEVNVTkGTPPKNATSPQAPSGQKTAVPTVTSTGGK 757
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1907182200 1572 SNT----KHTTGVSLETSVQ-TTIASPTPSAPQT--SLATHLP 1607
Cdd:pfam05109 758 ANSttggKHTTGHGARTSTEpTTDYGGDSTTPRTryNATTYLP 800
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
1361-1560 |
7.13e-04 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 44.74 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1361 TTISKWPTNGVSDTPGVHTSSGTPSSSHATHITYTPPTQVVSSITHSTGPPLGTSVQTTINFPTLSAPQTSLVTPHPGLS 1440
Cdd:COG3469 27 ATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATATAAAAAATSTSATLVATSTASGAN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1441 SSSTALTSeilkTPTSSQMVSSASPQTIFSSIHPKTTLEATTPQHTAPLITSITSSITQAQSSFSTDKTYTSQHSQPSTm 1520
Cdd:COG3469 107 TGTSTVTT----TSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATGGTTTTSTTTTTTSASTTPSA- 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907182200 1521 tahqsrslptvTTSTKSTMGLTGTPPVHTTSGTTSSPQTP 1560
Cdd:COG3469 182 -----------TTTATATTASGATTPSATTTATTTGPPTP 210
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1373-1626 |
1.69e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 43.83 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1373 DTPGvhTSSGTPS-----SSHATHITYTP----------PTQVVSSITHSTGPPLGTSVQTTINFPTLSAPQTSLVTPHP 1437
Cdd:TIGR00927 143 DTPA--TPSRALNhyistSGRQRVKSYTPkprgevksssPTQTREKVRKYTPSPLGRMVNSYAPSTFMTMPRSHGITPRT 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1438 GLSSSSTALTSEILKTPTSSQMVSSASPQT---IFSSIHPKTTLEATTPQHTAPLITSITSSITQAQSSFSTDKTYTSQH 1514
Cdd:TIGR00927 221 TVKDSEITATYKMLETNPSKRTAGKTTPTPlkgMTDNTPTFLTREVETDLLTSPRSVVEKNTLTTPRRVESNSSTNHWGL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1515 SQPSTMTAHQSRSL-PTVTTS----TKSTMglTGTPPVHTTSGTTS----SPqTPRTTHPfsTVAVSNTKHTTGVSLETS 1585
Cdd:TIGR00927 301 VGKNNLTTPQGTVLeHTPATSegqvTISIM--TGSSPAETKASTAAwkirNP-LSRTSAP--AVRIASATFRGLEKNPST 375
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1907182200 1586 VQTTIASPTPSAPQTSLATHLpfsstssvtptseVIITPTP 1626
Cdd:TIGR00927 376 APSTPATPRVRAVLTTQVHHC-------------VVVKPAP 403
|
|
| ser_rich_anae_1 |
NF033849 |
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ... |
1339-1591 |
7.65e-03 |
|
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 amino acids), which a highly serine-rich central region that averages over 300 aa in length. Species encoding members of this family of proteins tend to be anaerobic bacteria, including Gram-positive bacteria of the human gut microbiome and Chloroflexi from marine sediments.
Pssm-ID: 468206 [Multi-domain] Cd Length: 1122 Bit Score: 41.53 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1339 STSQGKTSASYTTQHQSTSfHLTTISKwpTNGVSDTPGVHTSSGT---PSSSHATHITYTPP--TQVVSSITHSTGPPLG 1413
Cdd:NF033849 276 TTGHGSTRGWSHTQSTSES-ESTGQSS--SVGTSESQSHGTTEGTsttDSSSHSQSSSYNVSsgTGVSSSHSDGTSQSTS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1414 TSVQTTINFPTLSAPQTSLVTPHPGLSSSSTaltseilktpTSSQMVSSASPQTIFSSIHPKTTLEATTPQHTAplITSI 1493
Cdd:NF033849 353 ISHSESSSESTGTSVGHSTSSSVSSSESSSR----------SSSSGVSGGFSGGIAGGGVTSEGLGASQGGSEG--WGSG 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1494 TSSITQAQSSFSTDKTYTSqHSQpSTMTAH-----QSRSLPTVTTSTKSTMGLTGTPPVHTTSGTTSSPQTPRTTHPFS- 1567
Cdd:NF033849 421 DSVQSVSQSYGSSSSTGTS-SGH-SDSSSHstssgQADSVSQGTSWSEGTGTSQGQSVGTSESWSTSQSETDSVGDSTGt 498
|
250 260
....*....|....*....|....*..
gi 1907182200 1568 --TVAVSNTK-HTTGVSLETSVQTTIA 1591
Cdd:NF033849 499 seSVSQGDGRsTGRSESQGTSLGTSGG 525
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| VWD |
pfam00094 |
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
398-550 |
2.90e-29 |
|
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.
Pssm-ID: 459671 [Multi-domain] Cd Length: 154 Bit Score: 115.16 E-value: 2.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 398 CSLEGGSFVTTFDARPYRFHGTCTYTLLQSPQLPNEGTLMAVYDKSGYSHSETSLVAIMYLSKKDKIVISEDEVITNNGD 477
Cdd:pfam00094 1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907182200 478 TKLLPYKTHNITIFRQTSTHLQMATTFGLELVFQMQPVFQVYITVGPQFKGQTRGLCGNFNGDTTDDFTTSMG 550
Cdd:pfam00094 81 KVSLPYKSDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
|
|
| VWD |
smart00216 |
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ... |
387-550 |
4.86e-29 |
|
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.
Pssm-ID: 214566 [Multi-domain] Cd Length: 163 Bit Score: 115.19 E-value: 4.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 387 WTCTKQPCPGHCSLEGGSFVTTFDARPYRFHGTCTYTLLQSpqLPNEGTLMAVYDKSGYSHSETSLVAIMYLSKKDKIVI 466
Cdd:smart00216 1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQD--CSSEPTFSVLLKNVPCGGGATCLKSVKVELNGDEIEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 467 SEDEV-ITNNGDTKLLPYKTHNITI-FRQTSTHLQMATTFGLELVfQMQPVFQVYITVGPQFKGQTRGLCGNFNGDTTDD 544
Cdd:smart00216 79 KDDNGkVTVNGQQVSLPYKTSDGSIqIRSSGGYLVVITSLGLIQV-TFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157
|
....*.
gi 1907182200 545 FTTSMG 550
Cdd:smart00216 158 FRTPDG 163
|
|
| VWD |
smart00216 |
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ... |
857-1019 |
9.38e-28 |
|
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.
Pssm-ID: 214566 [Multi-domain] Cd Length: 163 Bit Score: 111.34 E-value: 9.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 857 WTCqLSTQCPSTCVLYGEGHIITFDGQRFVFDGDCEYMLATDdcgaNSSQPTFKVLTENVICGkSGVTCSRAIKISLGGL 936
Cdd:smart00216 1 WCC-TQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQD----CSSEPTFSVLLKNVPCG-GGATCLKSVKVELNGD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 937 FITMADSN--YTVSGE-------EPLVHLKVKPSPLNLVLdidIPGRLNLTLVWNKHMSVSIKIrRATQQDALCGLCGNA 1007
Cdd:smart00216 75 EIELKDDNgkVTVNGQqvslpykTSDGSIQIRSSGGYLVV---ITSLGLIQVTFDGLTLLSVQL-PSKYRGKTCGLCGNF 150
|
170
....*....|..
gi 1907182200 1008 NGNMKDDFETRS 1019
Cdd:smart00216 151 DGEPEDDFRTPD 162
|
|
| VWD |
pfam00094 |
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
45-194 |
1.38e-25 |
|
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.
Pssm-ID: 459671 [Multi-domain] Cd Length: 154 Bit Score: 104.76 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 45 CSTWGAGHFSTFDGHEYNFQGMCNYIFTATCGDDVPATFSIQLRRDMEGN----ISRIIMELGASVVTVNKETISVRDIG 120
Cdd:pfam00094 1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGAsgvcLKSVTVIVGDLEITLQKGGTVLVNGQ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907182200 121 VVSLPYTSNGLQITPYGQSVQLVAKQLELELVITWGPDAHLTVQVETKYMGKLCGLCGNFDGKIDNEFLSEDGK 194
Cdd:pfam00094 81 KVSLPYKSDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
|
|
| C8 |
smart00832 |
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
1058-1130 |
1.81e-25 |
|
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.
Pssm-ID: 214843 Cd Length: 76 Bit Score: 101.65 E-value: 1.81e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907182200 1058 WAERKCNIINSQ--TFAACHSKVYHLPYYEACVRDACGCdtGGDCECLCDAVAAYAKACLDKGVCV-DWRTPDFCP 1130
Cdd:smart00832 3 YACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCAC--GGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
|
|
| VWD |
smart00216 |
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ... |
45-193 |
2.27e-24 |
|
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.
Pssm-ID: 214566 [Multi-domain] Cd Length: 163 Bit Score: 101.71 E-value: 2.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 45 CSTWGAGHFSTFDGHEYNFQGMCNYIFTATCGDDvpATFSIQLRRDMEG----NISRIIMELGASVVTVNKETISVR-DI 119
Cdd:smart00216 12 CSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSE--PTFSVLLKNVPCGggatCLKSVKVELNGDEIELKDDNGKVTvNG 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907182200 120 GVVSLPYTSNGLQITPYgQSVQLVAKQLELELV-ITWGPDAHLTVQVETKYMGKLCGLCGNFDGKIDNEFLSEDG 193
Cdd:smart00216 90 QQVSLPYKTSDGSIQIR-SSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
|
|
| C8 |
pfam08742 |
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ... |
1062-1129 |
3.70e-22 |
|
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.
Pssm-ID: 462584 Cd Length: 68 Bit Score: 91.67 E-value: 3.70e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1062 KCNIINSQT-FAACHSKVYHLPYYEACVRDACGCdtGGDCECLCDAVAAYAKACLDKGVCV-DWRTPDFC 1129
Cdd:pfam08742 1 KCGLLSDSGpFAPCHSVVDPEPYFEACVYDMCSC--GGDDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
|
|
| VWD |
pfam00094 |
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
869-1019 |
1.23e-20 |
|
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.
Pssm-ID: 459671 [Multi-domain] Cd Length: 154 Bit Score: 90.51 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 869 CVLYGEGHIITFDGQRFVFDGDCEYMLAtDDCGANSSqPTFKVLTENVICGKSGVtCSRAIKISLGGLFITMADSNY-TV 947
Cdd:pfam00094 1 CSVSGDPHYVTFDGVKYTFPGTCTYVLA-KDCSEEPD-FSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGTvLV 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907182200 948 SGEEplVHLKVKPSPLNL------VLDIDIPGRLNLTLVWNKHMSVSIKIRRaTQQDALCGLCGNANGNMKDDFETRS 1019
Cdd:pfam00094 78 NGQK--VSLPYKSDGGEVeilgsgFVVVDLSPGVGLQVDGDGRGQLFVTLSP-SYQGKTCGLCGNYNGNQEDDFMTPD 152
|
|
| C8 |
smart00832 |
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
589-661 |
1.14e-19 |
|
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.
Pssm-ID: 214843 Cd Length: 76 Bit Score: 85.08 E-value: 1.14e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907182200 589 AETHCSMLLKKGSVFEKCHSVVNPQPFYKRCVYQACNYEETFPHICSALGAYAHACSARGILLWGWRNSvDNC 661
Cdd:smart00832 4 ACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTP-TFC 75
|
|
| C8 |
pfam08742 |
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ... |
592-661 |
2.09e-18 |
|
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.
Pssm-ID: 462584 Cd Length: 68 Bit Score: 81.27 E-value: 2.09e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 592 HCSMLLKKGsVFEKCHSVVNPQPFYKRCVYQACNYEETFPHICSALGAYAHACSARGILLWGWRNSvDNC 661
Cdd:pfam08742 1 KCGLLSDSG-PFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTP-TFC 68
|
|
| TIL |
pfam01826 |
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
303-358 |
3.56e-14 |
|
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.
Pssm-ID: 460351 Cd Length: 55 Bit Score: 68.57 E-value: 3.56e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907182200 303 CPANQVYQECGEVCIKTCSNPQH--SCSSPCTFGCFCPHGTLLDDisgNQSCVPVNQC 358
Cdd:pfam01826 1 CPANEVYSECGSACPPTCANLSPpdVCPEPCVEGCVCPPGFVRNS---GGKCVPPSDC 55
|
|
| TIL |
cd19941 |
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
303-358 |
2.21e-13 |
|
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.
Pssm-ID: 410995 Cd Length: 55 Bit Score: 66.57 E-value: 2.21e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907182200 303 CPANQVYQECGEVCIKTCSNPQH--SCSSPCTFGCFCPHGTLLDDisgNQSCVPVNQC 358
Cdd:cd19941 1 CPPNEVYSECGSACPPTCANPNAppPCTKQCVEGCFCPEGYVRNS---GGKCVPPSQC 55
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
1464-1901 |
7.91e-12 |
|
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: 71.10 E-value: 7.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1464 SPQTIfssIHPKTTLEATTPQHT---APLITSITSSITQAQSSFSTDKTYTSQhsqPSTMTAHQSRSLPTVTTSTKSTMG 1540
Cdd:pfam05109 399 APKTL---IITRTATNATTTTHKvifSKAPESTTTSPTLNTTGFAAPNTTTGL---PSSTHVPTNLTAPASTGPTVSTAD 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1541 LTGTPPVHTTSGTTS-----SPQTPRTTHPFSTVAVSNTKHTTGVSLETSVQTTIASPTPSAPQTSLATHLPFSSTSS-- 1613
Cdd:pfam05109 473 VTSPTPAGTTSGASPvtpspSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTpt 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1614 --VTPTSEVIITPTPQhtlssaSTSTTTGNILPTTIGQTGSPHTSVPVIYTTSAITQTKTSFSTDRTSTPT-SAPHLSET 1690
Cdd:pfam05109 553 pnATSPTPAVTTPTPN------ATIPTLGKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTLGGTSSTPVvTSPPKNAT 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1691 SAVTA--HQSTPTAVSANSIKPT-MSSTGTPvvHTTSGTTSSPQTPRTTHPSttvavSGTVHTTGLPSGTSVHTTTNFPT 1767
Cdd:pfam05109 627 SAVTTgqHNITSSSTSSMSLRPSsISETLSP--STSDNSTSHMPLLTSAHPT-----GGENITQVTPASTSTHHVSTSSP 699
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1768 HSGPQSSLSTHLPLFSTLSVTPTTEGLNTPTSPHSLSVASTSMPLMTVLPTTLEGTRPPHTSVPVTYTTTAATQTKSSFS 1847
Cdd:pfam05109 700 APRPGTTSQASGPGNSSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTSTGGKANSTTGGKHTTGHGARTSTEPT 779
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907182200 1848 TD---RTSTPHLSQSSTvtptqsTPIPATTNSLMTTGGLTGTPPVHTTSGTTSSPQT 1901
Cdd:pfam05109 780 TDyggDSTTPRTRYNAT------TYLPPSTSSKLRPRWTFTSPPVTTAQATVPVPPT 830
|
|
| TIL |
cd19941 |
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
765-828 |
3.22e-11 |
|
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.
Pssm-ID: 410995 Cd Length: 55 Bit Score: 60.41 E-value: 3.22e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907182200 765 CPEPKTFQSCsqssedkfGAACAPTCQMLATGIDCvPTKCESGCVCPKGLYENSDGQCVPAEEC 828
Cdd:cd19941 1 CPPNEVYSEC--------GSACPPTCANPNAPPPC-TKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
1732-2111 |
3.56e-11 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 68.06 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1732 TPRTTHPSTTVAVSGTVHTTGLPSGT--SVHTTTNFPTHSGPQSSLSTHlplfSTLSVTPTTEGLNTPTSPHSLSVASTS 1809
Cdd:pfam17823 55 SEQ*NFCAATAAPAPVTLTKGTSAAHlnSTEVTAEHTPHGTDLSEPATR----EGAADGAASRALAAAASSSPSSAAQSL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1810 MPLMTVLPTtlEGTRPPHTSVPvtytttaatqtkssfSTDRTSTPHLSQSSTVTPTQSTPIPATTNSLMTTGGLTGTPPV 1889
Cdd:pfam17823 131 PAAIAALPS--EAFSAPRAAAC---------------RANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1890 HTTSGTTSSPQTPHSTHPISTAAISRTTGISGT-----PFRTPMKTTITFPTPSSLQTSMATLfppfstsvmssteifnt 1964
Cdd:pfam17823 194 APTTAASSAPATLTPARGISTAATATGHPAAGTalaavGNSSPAAGTVTAAVGTVTPAALATL----------------- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1965 ptNPHSVSSASTSRPLSTSLPTTIKGTGTPQTPvsdiNTTSATTQAHSSFPTTRTSTSHLSLPSSMTSTL---TPASRSA 2041
Cdd:pfam17823 257 --AAAAGTVASAAGTINMGDPHARRLSPAKHMP----SDTMARNPAAPMGAQAQGPIIQVSTDQPVHNTAgepTPSPSNT 330
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907182200 2042 STLQYTPTPSSVSHSPLLTTPTASP--PSSAPTFVSPTAASTVISSALPTIHMTPTPSSRPTSSTGLLSTSK 2111
Cdd:pfam17823 331 TLEPNTPKSVASTNLAVVTTTKAQAkePSASPVPVLHTSMIPEVEATSPTTQPSPLLPTQGAAGPGILLAPE 402
|
|
| TIL |
pfam01826 |
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
765-828 |
4.63e-11 |
|
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.
Pssm-ID: 460351 Cd Length: 55 Bit Score: 59.71 E-value: 4.63e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907182200 765 CPEPKTFQSCsqssedkfGAACAPTCQMLATGIDCvPTKCESGCVCPKGLYENSDGQCVPAEEC 828
Cdd:pfam01826 1 CPANEVYSEC--------GSACPPTCANLSPPDVC-PEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
1554-1954 |
9.87e-11 |
|
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: 67.25 E-value: 9.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1554 TSSPQTPRTTHPFSTVAVSNTKHTTGVSLETSVQTTIASPTPSAPQTSLATHLPFSSTSSVTPTSEVIITPTPQHTLSSA 1633
Cdd:pfam05109 422 SKAPESTTTSPTLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTES 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1634 STSTTTGnilPTTIGQTGSPHTSVPVIYTTSAiTQTKTSFSTDRTStPTSAPhLSETSAVTAHQSTPTAVSANSIKPTMS 1713
Cdd:pfam05109 502 KAPDMTS---PTSAVTTPTPNATSPTPAVTTP-TPNATSPTLGKTS-PTSAV-TTPTPNATSPTPAVTTPTPNATIPTLG 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1714 STGTpvvhTTSGTTSSPQTPRTTHPSTTVAVSGTVHTTGLPSGTSVHTTTnfPTHSGPQSSLSTH-LPLFSTLSVTPTTE 1792
Cdd:pfam05109 576 KTSP----TSAVTTPTPNATSPTVGETSPQANTTNHTLGGTSSTPVVTSP--PKNATSAVTTGQHnITSSSTSSMSLRPS 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1793 GLNTPTSPHSLSVASTSMPLMT-VLPTTLEGTRPPHTSVPVTYTTTAATQTKSSFSTDRTSTPHLSQSST----VTPTQS 1867
Cdd:pfam05109 650 SISETLSPSTSDNSTSHMPLLTsAHPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTkpgeVNVTKG 729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1868 TPIPATTNSLMTTGGLTGTPPVHTTSG----TTSSPQTPHSTHPISTAAISRTTGISGTPfRTPMKTTITFP--TPSSLQ 1941
Cdd:pfam05109 730 TPPKNATSPQAPSGQKTAVPTVTSTGGkansTTGGKHTTGHGARTSTEPTTDYGGDSTTP-RTRYNATTYLPpsTSSKLR 808
|
410
....*....|...
gi 1907182200 1942 TSMATLFPPFSTS 1954
Cdd:pfam05109 809 PRWTFTSPPVTTA 821
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
1667-2020 |
1.16e-10 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 66.52 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1667 TQTKTSFSTDRTSTPTSAPHLSetsavTAHQSTPTAVSANSikPTMSSTGTPVVHTTSGTTSSPqTPRTTHPSTTVAVSG 1746
Cdd:pfam17823 117 AAASSSPSSAAQSLPAAIAALP-----SEAFSAPRAAACRA--NASAAPRAAIAAASAPHAASP-APRTAASSTTAASST 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1747 TVHTTGLPSGTSVHTTTNFPTHSGPQSSLSTHLPlfstlsvtptteglntptsphSLSVASTSMPLMTVLPTTLEGTRPP 1826
Cdd:pfam17823 189 TAASSAPTTAASSAPATLTPARGISTAATATGHP---------------------AAGTALAAVGNSSPAAGTVTAAVGT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1827 HTSVPVTYTTTAATQTKSSFSTDRTSTPHlsqSSTVTPTQSTPipatTNSLMTTGGLTGTPPVHTTSGTTSSPQTPHSTH 1906
Cdd:pfam17823 248 VTPAALATLAAAAGTVASAAGTINMGDPH---ARRLSPAKHMP----SDTMARNPAAPMGAQAQGPIIQVSTDQPVHNTA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1907 PISTAAISRTTGISGTPfRTPMKTTITFPTPSSLQTSMATlfppfstsvMSSTEIFNTPTNPHSVSSASTSRPLSTSLPT 1986
Cdd:pfam17823 321 GEPTPSPSNTTLEPNTP-KSVASTNLAVVTTTKAQAKEPS---------ASPVPVLHTSMIPEVEATSPTTQPSPLLPTQ 390
|
330 340 350
....*....|....*....|....*....|....
gi 1907182200 1987 TIKGTGTPQTPvsDINTTSATTQAHSSFPTTRTS 2020
Cdd:pfam17823 391 GAAGPGILLAP--EQVATEATAGTASAGPTPRSS 422
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1674-2115 |
1.36e-10 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 67.27 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1674 STDRTSTPTSAPHLSETSAvtAHQSTPTAVSAnsikPTMSStgtPVVHTTSGTTSSPqtPRTTHPSTTVAVSGTVHTTGL 1753
Cdd:PHA03247 2545 SDDAGDPPPPLPPAAPPAA--PDRSVPPPRPA----PRPSE---PAVTSRARRPDAP--PQSARPRAPVDDRGDPRGPAP 2613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1754 PSGTSVHTTTNFPTHSGPqSSLSTHLPLFSTLSVTPTTEGLNTPTSPH-SLSVASTSMPLMTVLPTTLEGTRPPHTSVPV 1832
Cdd:PHA03247 2614 PSPLPPDTHAPDPPPPSP-SPAANEPDPHPPPTVPPPERPRDDPAPGRvSRPRRARRLGRAAQASSPPQRPRRRAARPTV 2692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1833 TYTTTaatqtkSSFSTDRTSTPHLSQSSTVTPTQSTPIPATTNSLMTTGGLT-GTPPVHTTSGTTSSPQTPHSthPISTA 1911
Cdd:PHA03247 2693 GSLTS------LADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAApAPPAVPAGPATPGGPARPAR--PPTTA 2764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1912 AISRTTGISGTPfrTPMKTTITFPTPSSLQTSMATLFPPFSTSVMSSTEIFNTPTNPHSVSSASTSRPLSTSLPT----- 1986
Cdd:PHA03247 2765 GPPAPAPPAAPA--AGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTapppp 2842
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1987 --------TIKGTGTPQTPVSdintTSATTQAHSSFPTTRT--STSHLSLPSSMTST-------LTPASRSASTLQYTPT 2049
Cdd:PHA03247 2843 pgppppslPLGGSVAPGGDVR----RRPPSRSPAAKPAAPArpPVRRLARPAVSRSTesfalppDQPERPPQPQAPPPPQ 2918
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 2050 PSSVSHSPLLTTPTASPPSSAPTFVSPTAASTVISSALPTI------HMTP---------TPSSRPTSSTGLLSTSKTTS 2114
Cdd:PHA03247 2919 PQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVpqpwlgALVPgrvavprfrVPQPAPSREAPASSTPPLTG 2998
|
.
gi 1907182200 2115 H 2115
Cdd:PHA03247 2999 H 2999
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
1730-2178 |
2.64e-10 |
|
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: 66.09 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1730 PQTPRTTHPSTTVAVSGTVHTTGLPSGTSVHTTTNFPTHSGPQSSLSTHLPLFSTLSVTPTTEGLNTPTSPHSLSVASTS 1809
Cdd:pfam05109 355 PNNTETDFKCKWTLTSGTPSGCENISGAFASNRTFDITVSGLGTAPKTLIITRTATNATTTTHKVIFSKAPESTTTSPTL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1810 MPLMTVLPTTLEGTrPPHTSVPvtytttaatqtkSSFSTDRTSTPHLSQSSTVTPTqstpiPATTNSLMT---------T 1880
Cdd:pfam05109 435 NTTGFAAPNTTTGL-PSSTHVP------------TNLTAPASTGPTVSTADVTSPT-----PAGTTSGASpvtpspsprD 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1881 GGLTGTPPVHTTSGTTSSPQTPHSTHPISTAAISRTTGISGTPFRTPMKTTITFPTPSSLQTSMATLFPPFSTSV----- 1955
Cdd:pfam05109 497 NGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIptlgk 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1956 MSSTEIFNTPTNPHSVSSASTSRPLSTSLPTTIKGT-GTPQTPVSDINTTSATTQAHSSFptTRTSTSHLSL-PSSMTST 2033
Cdd:pfam05109 577 TSPTSAVTTPTPNATSPTVGETSPQANTTNHTLGGTsSTPVVTSPPKNATSAVTTGQHNI--TSSSTSSMSLrPSSISET 654
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 2034 LTPASRSASTlqytptpssvSHSPLLTT--PTASPPSSAPTFVSPTAASTVISSALPTIHMTPTPSSRPTSSTGLLSTS- 2110
Cdd:pfam05109 655 LSPSTSDNST----------SHMPLLTSahPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEv 724
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907182200 2111 KTTSHVPTFSSFSSKSTTAHLTSLTTQAATSGLLSSTMGMTNLPSSGS-PDINHTTRPPGSSPLPTSAF 2178
Cdd:pfam05109 725 NVTKGTPPKNATSPQAPSGQKTAVPTVTSTGGKANSTTGGKHTTGHGArTSTEPTTDYGGDSTTPRTRY 793
|
|
| CT |
smart00041 |
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ... |
2220-2299 |
1.18e-09 |
|
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta (TGFbeta), nerve growth factor (NGF), platelet-derived growth factor (PDGF) and gonadotropin all form 2 highly twisted antiparallel pairs of beta-strands and contain three disulphide bonds. The domain is non-globular and little is conserved among these presumed homologues except for their cysteine residues. CT domains are predicted to form homodimers.
Pssm-ID: 214482 Cd Length: 82 Bit Score: 56.64 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 2220 EHQITYQGCVAN-VTLTRCQGFCASSVSFNkdTLQLESSCGCCQPLSTYKKQLSLPCPDpdapGQQLTLTLQVFSSCVCS 2298
Cdd:smart00041 5 RQTITYNGCTSVtVKNAFCEGKCGSASSYS--IQDVQHSCSCCQPHKTKTRQVRLRCPD----GSTVKKTVMHIEECGCE 78
|
.
gi 1907182200 2299 P 2299
Cdd:smart00041 79 P 79
|
|
| C8 |
pfam08742 |
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ... |
246-298 |
5.32e-09 |
|
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.
Pssm-ID: 462584 Cd Length: 68 Bit Score: 54.31 E-value: 5.32e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1907182200 246 VPKETLMLSCQADMaaCARPGQPNCSCATLSEYSRRCSMTGQPVRNWRTPALC 298
Cdd:pfam08742 18 VDPEPYFEACVYDM--CSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
1831-2174 |
7.19e-09 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 60.74 E-value: 7.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1831 PVTYTTTAATQTKSSFSTDRTSTPHLSQSSTVTPTQSTPIPATTNSLMTTGGLTGTPPVHTTSGTTSSPQTPHSTHPIST 1910
Cdd:pfam17823 69 PVTLTKGTSAAHLNSTEVTAEHTPHGTDLSEPATREGAADGAASRALAAAASSSPSSAAQSLPAAIAALPSEAFSAPRAA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1911 AAISRTTGISGTPFRTPMKTTITFPTPSSLQTsmatlfppfSTSVMSSTEIFNTPTNPHSVSSASTSRPLStSLPTTIKG 1990
Cdd:pfam17823 149 ACRANASAAPRAAIAAASAPHAASPAPRTAAS---------STTAASSTTAASSAPTTAASSAPATLTPAR-GISTAATA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1991 TGTPQtpvsdINTTSATTQAHSSFPTTRTSTSHLSLPSSMTSTLTPASRSASTLQY--TPTPSSVSHSPLLTTPT-ASPP 2067
Cdd:pfam17823 219 TGHPA-----AGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAAGTinMGDPHARRLSPAKHMPSdTMAR 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 2068 SSAPTFVSPTAASTV-ISSALPTIHMTPTPSSRPTSSTGLLSTSKTTSHVPTFSSFssksttahltslTTQAATSGLLSS 2146
Cdd:pfam17823 294 NPAAPMGAQAQGPIIqVSTDQPVHNTAGEPTPSPSNTTLEPNTPKSVASTNLAVVT------------TTKAQAKEPSAS 361
|
330 340
....*....|....*....|....*...
gi 1907182200 2147 TMGMtnLPSSGSPDINHTTRPPGSSPLP 2174
Cdd:pfam17823 362 PVPV--LHTSMIPEVEATSPTTQPSPLL 387
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1453-1968 |
1.12e-08 |
|
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: 60.94 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1453 TPTSSQMVSSASPQTIFSSIHPKTTLEATTPQHTAPLITSITSSITQAQSSFSTDKTYTSQHSQPSTMTAHQSRSlptvT 1532
Cdd:pfam03154 46 SPSAASTSSNDSKAESMKKSSKKIKEEAPSPLKSAKRQREKGASDTEEPERATAKKSKTQEISRPNSPSEGEGES----S 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1533 TSTKSTMGLTGTPPVHTTSGTTSSPQTPRTTHPFS---TVAVSNTKHTTGVSLETSVQTTIASPTPSAPQTSLATHLPFS 1609
Cdd:pfam03154 122 DGRSVNDEGSSDPKDIDQDNRSTSPSIPSPQDNESdsdSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1610 STSSVTPTSEVIITPTPQHTLSsaststttgnilpttigqTGSPHTsvpviyttsaITQTKTSFSTDRTSTP----TSAP 1685
Cdd:pfam03154 202 SAPSVPPQGSPATSQPPNQTQS------------------TAAPHT----------LIQQTPTLHPQRLPSPhpplQPMT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1686 HLSETSAVTAhQSTPtavsansiKPTMSSTGTPVVHTTSGTTSSPQTPRTTHPSTTVAVSGTVHTTGLPSGTSVHTTTNF 1765
Cdd:pfam03154 254 QPPPPSQVSP-QPLP--------QPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1766 PTHSGPQSSLSTHLPlfstlsvtPTTEGLN-TPTS-PHSLSVASTSMPLMtvlPTTLEGTRPPHTSVPVTYTTTAATQTK 1843
Cdd:pfam03154 325 IHTPPSQSQLQSQQP--------PREQPLPpAPLSmPHIKPPPTTPIPQL---PNPQSHKHPPHLSGPSPFQMNSNLPPP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1844 ------SSFSTDRTSTPH------LSQSSTVTP--------TQSTPIPATTNSLMTTGGLTGTPPvhttsgttsspQTPH 1903
Cdd:pfam03154 394 palkplSSLSTHHPPSAHppplqlMPQSQQLPPppaqppvlTQSQSLPPPAASHPPTSGLHQVPS-----------QSPF 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907182200 1904 STHPISTaaisrttgiSGTPFRTPMKTTitfptPSSLQTSMATLFPPFSTSVMSSTEIFNTPTNP 1968
Cdd:pfam03154 463 PQHPFVP---------GGPPPITPPSGP-----PTSTSSAMPGIQPPSSASVSSSGPVPAAVSCP 513
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1704-2099 |
1.23e-08 |
|
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: 60.55 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1704 SANSIKPTMSSTGTPVVHTTSGTTSSPQTPrtthPSTTVAVSGTVHTTGLPSGTSVHTTTNFPTHSGPQSSLSTHLPLFS 1783
Cdd:pfam03154 158 SDSSAQQQILQTQPPVLQAQSGAASPPSPP----PPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQ 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1784 TLSVTPT--------TEGLNTPTSPHSLSVASTSMPL----MTVLPTTLEgTRPPHTSVPVtytttaatqtkssfSTDRT 1851
Cdd:pfam03154 234 TPTLHPQrlpsphppLQPMTQPPPPSQVSPQPLPQPSlhgqMPPMPHSLQ-TGPSHMQHPV--------------PPQPF 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1852 STPHLSQSSTVTPTQSTPIPATTNSLMTTggltgtPPvhttSGTTSSPQTPHSTHPISTAAISR-------TTGISGTPF 1924
Cdd:pfam03154 299 PLTPQSSQSQVPPGPSPAAPGQSQQRIHT------PP----SQSQLQSQQPPREQPLPPAPLSMphikpppTTPIPQLPN 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1925 RTPMKTTITFPTPSSLQTSmATLFPPFSTSVMSSTEIFNTPTN---PHSVSSASTSRPLSTSLPTTIKGTGTPQTPVSDI 2001
Cdd:pfam03154 369 PQSHKHPPHLSGPSPFQMN-SNLPPPPALKPLSSLSTHHPPSAhppPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASH 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 2002 NTTSATTQA--HSSFPT-----------TRTSTSHLSLPSSMTSTLTPASRSASTLQYTPTPSSVSHSPLLTTPTASPPS 2068
Cdd:pfam03154 448 PPTSGLHQVpsQSPFPQhpfvpggpppiTPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALDEA 527
|
410 420 430
....*....|....*....|....*....|.
gi 1907182200 2069 SAPTFVSPTAAStviSSALPTIHMTPTPSSR 2099
Cdd:pfam03154 528 EEPESPPPPPRS---PSPEPTVVNTPSHASQ 555
|
|
| C8 |
smart00832 |
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
246-299 |
7.47e-08 |
|
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.
Pssm-ID: 214843 Cd Length: 76 Bit Score: 51.57 E-value: 7.47e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1907182200 246 VPKETLMLSCQADMaaCARPGQPNCSCATLSEYSRRCSMTGQPVRNWRTPALCP 299
Cdd:smart00832 25 VDPEPFFENCVYDT--CACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
1526-1902 |
9.81e-08 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 57.28 E-value: 9.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1526 RSLPTVTTSTKSTMGLT-GTPPVHTTSGTTSSPQTPRTTHpfstVAVSNTKHTTGVSLETSVQTTIASPTPSAPQTSLAT 1604
Cdd:pfam17823 57 Q*NFCAATAAPAPVTLTkGTSAAHLNSTEVTAEHTPHGTD----LSEPATREGAADGAASRALAAAASSSPSSAAQSLPA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1605 hlpfsstSSVTPTSEVIITPTPQhTLSSASTSTTTGNILPTTIGQTGSPHTSVPVIYTTSAITQTKTSF--STDRTSTPT 1682
Cdd:pfam17823 133 -------AIAALPSEAFSAPRAA-ACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSapTTAASSAPA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1683 SAPHLSETSAVTAHQSTPTAVSANSIKPTMSSTGTPVVHTTSGTTSSPQTPRTTHPSTTVAVSGTVHTTG---------- 1752
Cdd:pfam17823 205 TLTPARGISTAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAAGTINMGDpharrlspak 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1753 -LPSGTSVHT--TTNFPTHSGPQSSLSTHLPLFSTlSVTPTTEGLNTPTSPHS-LSVASTSMPLMTVlpTTLEGTRPPHT 1828
Cdd:pfam17823 285 hMPSDTMARNpaAPMGAQAQGPIIQVSTDQPVHNT-AGEPTPSPSNTTLEPNTpKSVASTNLAVVTT--TKAQAKEPSAS 361
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907182200 1829 SVPVTYtttaatqtkSSFSTDRTSTPHLSQSSTVTPTQSTPIPAT--TNSLMTTGGLTGTPPVHTTSGTTSSPQTP 1902
Cdd:pfam17823 362 PVPVLH---------TSMIPEVEATSPTTQPSPLLPTQGAAGPGIllAPEQVATEATAGTASAGPTPRSSGDPKTL 428
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1492-1907 |
2.76e-07 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 56.31 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1492 SITSSITQAQSSFSTDKTYTSQHSQPSTMTAHQSRSLPTVTTSTKSTMGLTGTPPVHTTSGTTSSPQ-TPRTTHPFSTVA 1570
Cdd:pfam03154 143 STSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQgSPATSQPPNQTQ 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1571 VSNTKHTTgvsletsVQTTIASPTPSAPqtslATHLPFSSTSSVTPTSEVIITPTPQhtlssaSTSTTTGNILPTTIgQT 1650
Cdd:pfam03154 223 STAAPHTL-------IQQTPTLHPQRLP----SPHPPLQPMTQPPPPSQVSPQPLPQ------PSLHGQMPPMPHSL-QT 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1651 GSPHTSVPVIYTTSAITQTKTSFSTDRTSTPTSAPHLSETSAVTAHQSTPTAVSANSIKPtMSSTGTPVVHTT-SGTTSS 1729
Cdd:pfam03154 285 GPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQP-LPPAPLSMPHIKpPPTTPI 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1730 PQTPRT---THPSTTVAVSGTVHTTGLPSGTSVHTTTNFPTHSGPqsslSTHLPlfsTLSVTPTTEGLNTP-------TS 1799
Cdd:pfam03154 364 PQLPNPqshKHPPHLSGPSPFQMNSNLPPPPALKPLSSLSTHHPP----SAHPP---PLQLMPQSQQLPPPpaqppvlTQ 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1800 PHSLSVASTSMPLMTVL-PTTLEGTRPPHTSVPVTYTTTAATQTKSSFSTdrTSTPHLSQSSTVTPTQSTPIPATTNSLM 1878
Cdd:pfam03154 437 SQSLPPPAASHPPTSGLhQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTS--SAMPGIQPPSSASVSSSGPVPAAVSCPL 514
|
410 420
....*....|....*....|....*....
gi 1907182200 1879 ttggltgtPPVHTTSGTTSSPQTPHSTHP 1907
Cdd:pfam03154 515 --------PPVQIKEEALDEAEEPESPPP 535
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1773-2106 |
3.01e-07 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 56.16 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1773 SSLSTHLPLFSTLSVTPTTEGLNTPTSPhslSVASTSMPLMTVLP--------TTLEGTRPPHTSVPVTYTTTAATQTKS 1844
Cdd:TIGR00927 52 AAVSSQQPIKLASRDLSNDEMMMVSSDP---PKSSSEMEGEMLAPqatvgrdeATPSIAMENTPSPPRRTAKITPTTPKN 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1845 SFSTDRTSTPHLSQSSTVTP---------TQSTPIpATTNSLMTTGGLTGTPPVHTTSGT---TSSP------------- 1899
Cdd:TIGR00927 129 NYSPTAAGTERVKEDTPATPsralnhyisTSGRQR-VKSYTPKPRGEVKSSSPTQTREKVrkyTPSPlgrmvnsyapstf 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1900 ---QTPHSTHPISTAAISRTTGISGTPFRTPMKTTITFPTPSSLQtSMATLFPPFSTSVMSsTEIFNTPTN--------- 1967
Cdd:TIGR00927 208 mtmPRSHGITPRTTVKDSEITATYKMLETNPSKRTAGKTTPTPLK-GMTDNTPTFLTREVE-TDLLTSPRSvvekntltt 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1968 PHSVSSASTSRP---LSTSLPTTIKGTGTPQTPVSDINTTSATTQAHSSFPTTRTSTSHLSLPSSMTSTLTPASRSASTL 2044
Cdd:TIGR00927 286 PRRVESNSSTNHwglVGKNNLTTPQGTVLEHTPATSEGQVTISIMTGSSPAETKASTAAWKIRNPLSRTSAPAVRIASAT 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907182200 2045 --QYTPTPSSVSHSPLLTTPTASPPSSA-------PTFVSPTAASTVISSALPTIHMTPTPSSRPTSSTGL 2106
Cdd:TIGR00927 366 frGLEKNPSTAPSTPATPRVRAVLTTQVhhcvvvkPAPAVPTTPSPSLTTALFPEAPSPSPSALPPGQPDL 436
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
1879-2116 |
5.16e-07 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 54.76 E-value: 5.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1879 TTGGLTGTPPVHTTSGTTSSPQTPHSTHPISTAAISRTTGISGTPFRTPMKTTITFPTPSSLQTSMATLFPPFSTSVMSS 1958
Cdd:COG3469 2 SSVSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1959 TEIFNTPtnphsvsSASTSRPLSTSLPTTIKGTGTPQTPVSDINTTSATTQAHSSFPTTRTSTSHLSLPSSMTSTLTPAS 2038
Cdd:COG3469 82 ATAAAAA-------ATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907182200 2039 RSASTLQYTPTPSSVShspllTTPTASPPSSAPTFVSPTAASTvissalptihmTPTPSSRPTSSTGLLSTSKTTSHV 2116
Cdd:COG3469 155 GTETATGGTTTTSTTT-----TTTSASTTPSATTTATATTASG-----------ATTPSATTTATTTGPPTPGLPKHV 216
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1849-2177 |
6.54e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 55.33 E-value: 6.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1849 DRTSTPHLSQSSTVTP--TQSTPIPATTNSLMTTGGLTGTPPVHTTSGTTSSPQTPHSTHPISTAAISRTTGISGTPfRT 1926
Cdd:PHA03247 2604 DRGDPRGPAPPSPLPPdtHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPP-QR 2682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1927 PMKTTITfPTPSSLqTSMATLFPPFST---SVMSSTEIFNTPTNPHSVSSASTSRPLSTSLPTTIKGTGTPQTPVSDINT 2003
Cdd:PHA03247 2683 PRRRAAR-PTVGSL-TSLADPPPPPPTpepAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARP 2760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 2004 TSATTQAHSSFPTTRTSTSHLSLPSSMTSTLTPASRSASTLQYTPTPSSVSHSPLLTTPTASPPssAPTFVSPTAASTVI 2083
Cdd:PHA03247 2761 PTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP--AGPLPPPTSAQPTA 2838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 2084 SSALPTIHMTPTPSSRPTSSTGLLSTSKTTSHVPTFSSFSSKSTTAHLTSLTTQAATSGLLSSTMGMTNLPSSGSPDINH 2163
Cdd:PHA03247 2839 PPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQ 2918
|
330
....*....|....
gi 1907182200 2164 TTRPPGSSPLPTSA 2177
Cdd:PHA03247 2919 PQPQPPPPPQPQPP 2932
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
1967-2175 |
1.65e-06 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 53.04 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1967 NPHSVSSASTSRPLSTSLPTTIKGTG------TPQTPVSDINTT--SATTQAHSSFPTTRTSTSHLSLPSSMTSTltpAS 2038
Cdd:pfam17823 82 NSTEVTAEHTPHGTDLSEPATREGAAdgaasrALAAAASSSPSSaaQSLPAAIAALPSEAFSAPRAAACRANASA---AP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 2039 RSASTLQYTPTPSSVSHSPLLTTPTASPPSSAPTFVSPTAASTVISSALPTihmtpTPSSRPTSSTGLLSTSKTTSHVPT 2118
Cdd:pfam17823 159 RAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPA-----RGISTAATATGHPAAGTALAAVGN 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907182200 2119 FSSFSSKSTTAHLT----SLTTQAATSGLLSSTMGMTNLpssGSPdinHTTRPPGSSPLPT 2175
Cdd:pfam17823 234 SSPAAGTVTAAVGTvtpaALATLAAAAGTVASAAGTINM---GDP---HARRLSPAKHMPS 288
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
1859-2072 |
4.13e-06 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 52.06 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1859 SSTVTPTQSTPIPATTNSlmTTGGLTGTPPVHTTSGTTSSPQTPHSTHPISTAAISRTTGISGTPFRTPMKTTITFPTPS 1938
Cdd:COG3469 5 STAASPTAGGASATAVTL--LGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1939 SLQTSMATLFPPFSTSVMSSTEiFNTPTNPHSVSSASTSRPLSTSLPTTikgtGTPQTPVSDINTTSATTQAHSSFPTTR 2018
Cdd:COG3469 83 TAAAAAATSTSATLVATSTASG-ANTGTSTVTTTSTGAGSVTSTTSSTA----GSTTTSGASATSSAGSTTTTTTVSGTE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907182200 2019 TSTSHLSLPSSMTSTLTPASRSASTLQYTPTPSSVSHSPLLTTPTASPPSSAPT 2072
Cdd:COG3469 158 TATGGTTTTSTTTTTTSASTTPSATTTATATTASGATTPSATTTATTTGPPTPG 211
|
|
| TIL |
cd19941 |
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
665-722 |
5.17e-06 |
|
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.
Pssm-ID: 410995 Cd Length: 55 Bit Score: 45.77 E-value: 5.17e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907182200 665 CTGNRTFSYDSQACDRTCLSLsDRETEChvSPVPVDGCNCPEGTYLNHKAECVHKAQC 722
Cdd:cd19941 1 CPPNEVYSECGSACPPTCANP-NAPPPC--TKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
1859-2088 |
7.45e-06 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 51.29 E-value: 7.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1859 SSTVTPTQSTPIPATTNSLMTTGGLTGTPPVHTTSGTTSSPQTPHSTHPISTAAISRTTGISGTpfrtpmkttiTFPTPS 1938
Cdd:COG3469 2 SSVSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTA----------ASSTAA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1939 SLQTSMATLFPPFSTSVMSSTEIFNTPTNPHSVSSASTSRPLSTSLPTTIKGTGTPQTPVSDINTTSATTQAHSSFPTTR 2018
Cdd:COG3469 72 TSSTTSTTATATAAAAAATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTT 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 2019 TSTSHLSLPSSMTSTLTPASRSASTLQYTPTPSsvshspllTTPTASPPSSAPTFVSPTAASTVISSALP 2088
Cdd:COG3469 152 TVSGTETATGGTTTTSTTTTTTSASTTPSATTT--------ATATTASGATTPSATTTATTTGPPTPGLP 213
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
1640-1831 |
8.91e-06 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 50.91 E-value: 8.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1640 GNILPTTIGQTGSPHTSVPVIYTTSAITQTKTSFSTDRTSTPTSAPhlSETSAVTAHQSTPTAVSANSIKPTMSSTGTPV 1719
Cdd:COG3469 24 GAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASST--AATSSTTSTTATATAAAAAATSTSATLVATST 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1720 VHTTSGTTSSPQTPRTTHPSTTVAVSGTVHTTGLP--SGTSVHTTTNFPTHSGPQSSLSTHLPLFSTLSVTPTTEGLNTP 1797
Cdd:COG3469 102 ASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSgaSATSSAGSTTTTTTVSGTETATGGTTTTSTTTTTTSASTTPSA 181
|
170 180 190
....*....|....*....|....*....|....
gi 1907182200 1798 TSPHSLSVASTSMPLMTVLPTTleGTRPPHTSVP 1831
Cdd:COG3469 182 TTTATATTASGATTPSATTTAT--TTGPPTPGLP 213
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
1688-1902 |
1.12e-05 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 50.52 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1688 SETSAVTAHQSTPTAVSANSIKPTMSSTGTPVVHTTSGTTSSPQTPRTTHPSTTVAVSGTVHTTGLPSGTSVHTTTNFPT 1767
Cdd:COG3469 1 SSSVSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1768 HSGPQSSLSTHLPLfsTLSVTPTTEGLNTPTSPHSLSVASTSMPLMTVLPTTLEGTRPPH-TSVPVTYTTTAATQTKSSF 1846
Cdd:COG3469 81 TATAAAAAATSTSA--TLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGAsATSSAGSTTTTTTVSGTET 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907182200 1847 STDRTSTPHLSQSSTVTPTQSTPIPATTnslmTTGGLTGTPPVHTTSGTTSSPQTP 1902
Cdd:COG3469 159 ATGGTTTTSTTTTTTSASTTPSATTTAT----ATTASGATTPSATTTATTTGPPTP 210
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1515-2105 |
2.54e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.94 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1515 SQPSTMTAHQSRSLPTVTTSTKSTMGLTGTPPVHTTSGTTSSPQTPRTTHPFSTVAVSntkHTTGVSLETSVQTTIASPT 1594
Cdd:PHA03247 2614 PSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLG---RAAQASSPPQRPRRRAARP 2690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1595 PSAPQTSLATHLPFSSTSSVTPTSEVIITPTPqhtlssASTSTTTGNILPTTIGQTGSPHTSVPVIYTTSAITQTKTSFS 1674
Cdd:PHA03247 2691 TVGSLTSLADPPPPPPTPEPAPHALVSATPLP------PGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTA 2764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1675 TDRTSTPTSAPHLSETSAVTAHQSTPTAVSANSIkptmsstgtpvvhttsgttSSPQTPrTTHPSTTVAVSGTVHTTGLP 1754
Cdd:PHA03247 2765 GPPAPAPPAAPAAGPPRRLTRPAVASLSESRESL-------------------PSPWDP-ADPPAAVLAPAAALPPAASP 2824
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1755 SGTSVHTTTNFPTHSGPQSSlsthlPLFSTLsvtpTTEGLNTPTSPHSLSVASTSMPLMTVLPttlegTRPPhtsvpvty 1834
Cdd:PHA03247 2825 AGPLPPPTSAQPTAPPPPPG-----PPPPSL----PLGGSVAPGGDVRRRPPSRSPAAKPAAP-----ARPP-------- 2882
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1835 tttaatqtkssfsTDRTSTPHLSQsstvtPTQSTPIPATTNSLMTTGGLTGTPPVHTTSGTTSSPQTPHSTHPISTAAIS 1914
Cdd:PHA03247 2883 -------------VRRLARPAVSR-----STESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLA 2944
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1915 RTTGISGTPfrtpmkttitFPTPSSLQTSMATLFPPfstsvmssteifNTPTNPHSVSSASTSRPLSTSLPTTIKGTGTP 1994
Cdd:PHA03247 2945 PTTDPAGAG----------EPSGAVPQPWLGALVPG------------RVAVPRFRVPQPAPSREAPASSTPPLTGHSLS 3002
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1995 QTpvsdinTTSATTQAHSSFPTTRtstshlslPSSMTSTLTPAS----RSASTLQYTPTPSSVSHSPLLTTPTASPPSSA 2070
Cdd:PHA03247 3003 RV------SSWASSLALHEETDPP--------PVSLKQTLWPPDdtedSDADSLFDSDSERSDLEALDPLPPEPHDPFAH 3068
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1907182200 2071 PTFVSPTAAStviSSALPTIHMTPTP-------SSRPTSSTG 2105
Cdd:PHA03247 3069 EPDPATPEAG---ARESPSSQFGPPPlsanaalSRRYVRSTG 3107
|
|
| PHA03255 |
PHA03255 |
BDLF3; Provisional |
1865-2060 |
3.14e-05 |
|
BDLF3; Provisional
Pssm-ID: 165513 [Multi-domain] Cd Length: 234 Bit Score: 47.59 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1865 TQSTPIPATTnslmttGGLTGTPPVHTTSGTTSSPQTPHSTHPISTAAisrttgisgtpfrtPMKTTITFPTPSSLQTSM 1944
Cdd:PHA03255 25 TSSGSSTASA------GNVTGTTAVTTPSPSASGPSTNQSTTLTTTSA--------------PITTTAILSTNTTTVTST 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1945 ATLFPPFSTSVMSSTeiFNTPTNPHSVSSASTSrplstslpttiKGTGTpQTPVSDINTTSATTQAHSSFPTTRTSTSHL 2024
Cdd:PHA03255 85 GTTVTPVPTTSNAST--INVTTKVTAQNITATE-----------AGTGT-STGVTSNVTTRSSSTTSATTRITNATTLAP 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907182200 2025 SLPSSMTSTLTPASRSASTLQYTPTPSSVSHSPLLT 2060
Cdd:PHA03255 151 TLSSKGTSNATKTTAELPTVPDERQPSLSYGLPLWT 186
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1870-2174 |
4.97e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.17 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1870 IPATTNSLMTTGGLTGTPPvhTTSGTTSSPQTPHSTHPISTAAISRTT--GISGTPFRTPMKTTITFPTPSSLQTSMATL 1947
Cdd:PHA03247 2591 APPQSARPRAPVDDRGDPR--GPAPPSPLPPDTHAPDPPPPSPSPAANepDPHPPPTVPPPERPRDDPAPGRVSRPRRAR 2668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1948 FPPFSTSVMSSTEIFNTPTNPHSVSS-ASTSRPLstslPTTIKGTGTPQTPVSDINTTSATTQAHSSFPTTrtsTSHLSL 2026
Cdd:PHA03247 2669 RLGRAAQASSPPQRPRRRAARPTVGSlTSLADPP----PPPPTPEPAPHALVSATPLPPGPAAARQASPAL---PAAPAP 2741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 2027 PSSMTSTLTPASRSAstlqyTPTPSSVShSPLLTTPTASPPSSAPTFVSPTAASTvISSALPTIHMTPTPSSRPTSSTGL 2106
Cdd:PHA03247 2742 PAVPAGPATPGGPAR-----PARPPTTA-GPPAPAPPAAPAAGPPRRLTRPAVAS-LSESRESLPSPWDPADPPAAVLAP 2814
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907182200 2107 LSTskttshvptfssfssksttahltsLTTQAATSGLLSSTMGMTNLPSSGSPDINHTTRPPGSSPLP 2174
Cdd:PHA03247 2815 AAA------------------------LPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAP 2858
|
|
| VWC_out |
smart00215 |
von Willebrand factor (vWF) type C domain; |
360-404 |
5.03e-05 |
|
von Willebrand factor (vWF) type C domain;
Pssm-ID: 214565 Cd Length: 67 Bit Score: 43.32 E-value: 5.03e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1907182200 360 CMLNGMVYGPGEITKTACQTCQCTMGRWTCTKQPC-PGHCSLEGGS 404
Cdd:smart00215 1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCgPKPCLLHNLS 46
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
1671-1890 |
1.27e-04 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 47.05 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1671 TSFSTDRTSTPTSAPHLSETSAVTAHQSTPTAVSANSIKPTMSSTGTPVVHTTSGTTSSPQTPRTTHPSTTVAVSGTVHT 1750
Cdd:COG3469 2 SSVSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1751 TGLPSGTSVHTTTNFPTHSGPQSSLSTHLPLFSTLSVTPTTEGLNTPTSPHSLSVASTSMPLMTVLPTTLEGTRPPHTSV 1830
Cdd:COG3469 82 ATAAAAAATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1831 PVTYTTTaatqtkSSFSTDRTSTPHLSQSSTVTPTQSTPIPATTNSLMTTGGLTGTPPVH 1890
Cdd:COG3469 162 GTTTTST------TTTTTSASTTPSATTTATATTASGATTPSATTTATTTGPPTPGLPKH 215
|
|
| ROM1 |
COG5422 |
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ... |
1852-2092 |
1.31e-04 |
|
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];
Pssm-ID: 227709 [Multi-domain] Cd Length: 1175 Bit Score: 47.58 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1852 STPHLSQSSTVTPtqstpipattnslmttggltgtPPVHTTSGT--TSSPQTPHSTHpISTAAISrttgISGTPFRTPMK 1929
Cdd:COG5422 78 SSPKLFQRRNSAG----------------------PITHSPSATssTSSLNSNDGDQ-FSPASDS----LSFNPSSTQSR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1930 TTITFPTPSSLQTSMATLFPPFSTSVMSSTEIFNTPTNPHSVSSASTSRPLStslPTTIKGTGTPQTPVSDINTTSATTQ 2009
Cdd:COG5422 131 KDSGPGDGSPVQKRKNPLLPSSSTHGTHPPIVFTDNNGSHAGAPNARSRKEI---PSLGSQSMQLPSPHFRQKFSSSDTS 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 2010 AHSSFPTTRTSTSHlslpSSMTSTLTPASRSASTLQYTPTPSSVSHSPLLTTPT-----ASPPSSAPTFVSPTAASTVIS 2084
Cdd:COG5422 208 NGFSYPSIRKNSRH----SSNSMPSFPHSSTAVLLKRHSGSSGASLISSNITPSssnseAMSTSSKRPYIYPALLSRVAV 283
|
....*...
gi 1907182200 2085 SALPTIHM 2092
Cdd:COG5422 284 EFKMRLQL 291
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1870-2111 |
1.36e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 47.63 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1870 IPATTnslMTTGGLTGTPPvHTTSGTTSSPQTPHSTHPISTAAISR---TTGISGTPfrtpmkttITFPTPSSlqtsmat 1946
Cdd:PHA03247 254 APAPP---PVVGEGADRAP-ETARGATGPPPPPEAAAPNGAAAPPDgvwGAALAGAP--------LALPAPPD------- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1947 lfPPFSTSVMSSTEIFNTPTNPHSVSSASTSRP-LSTSLPTTIKGTGTPQTPVSDINTTSATTQAHSSFPTTRTSTSHLS 2025
Cdd:PHA03247 315 --PPPPAPAGDAEEEDDEDGAMEVVSPLPRPRQhYPLGFPKRRRPTWTPPSSLEDLSAGRHHPKRASLPTRKRRSARHAA 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 2026 LPSSMTSTLTPASRSAstlqyTPTPSSVSHSPLLTTPTASPPSSAPTFVSPTAASTViSSALPTIHMTPTPSSRPTSSTG 2105
Cdd:PHA03247 393 TPFARGPGGDDQTRPA-----APVPASVPTPAPTPVPASAPPPPATPLPSAEPGSDD-GPAPPPERQPPAPATEPAPDDP 466
|
....*.
gi 1907182200 2106 LLSTSK 2111
Cdd:PHA03247 467 DDATRK 472
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
1864-2100 |
1.49e-04 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 47.37 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1864 PTQSTPIPATTNSLMTTG--GLTGTPPVHTTSGTTSSPQTPHSTHPISTAAISRTTGISGTPFRTPMKTTITF-----PT 1936
Cdd:PHA03378 571 PLQIQPLTSPTTSQLASSapSYAQTPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMRPLRMQPITFnvlvfPT 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1937 PSSLQTSMATLFPPfstsvmSSTEIFNTPTNPhSVSSASTSRPLSTSlpttikgTGTPQTPvsdinttsatTQAHSSFPT 2016
Cdd:PHA03378 651 PHQPPQVEITPYKP------TWTQIGHIPYQP-SPTGANTMLPIQWA-------PGTMQPP----------PRAPTPMRP 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 2017 TRTSTSHLSLPSSMTSTLTPASRSASTLQYTPTPSSVSHSPLLTTPTASPPSSAPTFVSPTAASTVISSALPTIHMTPTP 2096
Cdd:PHA03378 707 PAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAP 786
|
....
gi 1907182200 2097 SSRP 2100
Cdd:PHA03378 787 QQRP 790
|
|
| PHA03255 |
PHA03255 |
BDLF3; Provisional |
1642-1798 |
1.56e-04 |
|
BDLF3; Provisional
Pssm-ID: 165513 [Multi-domain] Cd Length: 234 Bit Score: 45.67 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1642 ILPTTIGQTGSPHTSVPVIYTTSAITQTKTSFSTDRTSTPTSAPHLSETSAVTahqsTPTAVSANSIKPTMSSTGTPVVH 1721
Cdd:PHA03255 17 ICETSLIWTSSGSSTASAGNVTGTTAVTTPSPSASGPSTNQSTTLTTTSAPIT----TTAILSTNTTTVTSTGTTVTPVP 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907182200 1722 TTSGTTSSPQTPRTTHPSTTVAVSGTvhttglpsGTSVHTTTNFPTHSGPQSSLSTHLPLFSTLSVTPTTEGLNTPT 1798
Cdd:PHA03255 93 TTSNASTINVTTKVTAQNITATEAGT--------GTSTGVTSNVTTRSSSTTSATTRITNATTLAPTLSSKGTSNAT 161
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1854-2193 |
2.50e-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: 46.30 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1854 PHLSQSSTVTPTQSTPIPATTNSLMTTGGLTGTPPVhttSGTTSSPQTPHSTHPISTAAisRTTGISGTPFRTPMKttit 1933
Cdd:pfam03154 171 PPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSV---PPQGSPATSQPPNQTQSTAA--PHTLIQQTPTLHPQR---- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1934 FPTPSSLQTSMATLFPPFSTSVMSsteifnTPTNPHSVSSASTSRPLSTSlPTTIKGTGTPQTpvsdINTTSATTQAHSS 2013
Cdd:pfam03154 242 LPSPHPPLQPMTQPPPPSQVSPQP------LPQPSLHGQMPPMPHSLQTG-PSHMQHPVPPQP----FPLTPQSSQSQVP 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 2014 fPTTRTSTSHlslPSSMTSTlTPASRSASTLQYTPTPSSVSHSPLlTTPTASPPSSAPTFVSPTAAS----TVISSALP- 2088
Cdd:pfam03154 311 -PGPSPAAPG---QSQQRIH-TPPSQSQLQSQQPPREQPLPPAPL-SMPHIKPPPTTPIPQLPNPQShkhpPHLSGPSPf 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 2089 --TIHMTPTPSSRPTSStglLSTskttsHVPTFSSFSSKSTTAHLTSLTTQAATSGLLSSTmgmTNLPSSGS--PDINHT 2164
Cdd:pfam03154 385 qmNSNLPPPPALKPLSS---LST-----HHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQS---QSLPPPAAshPPTSGL 453
|
330 340
....*....|....*....|....*....
gi 1907182200 2165 TRPPGSSPLPTSAFLSRSTSPTGSSSPST 2193
Cdd:pfam03154 454 HQVPSQSPFPQHPFVPGGPPPITPPSGPP 482
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
1518-1733 |
2.56e-04 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 46.28 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1518 STMTAHQSRSLPTVTTSTKSTMGLTGTPPVHTTSGTTSSPQTPRTTHPFSTVAVSNTKHTTGV-------SLETSVQTTI 1590
Cdd:COG3469 3 SVSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAasstaatSSTTSTTATA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1591 ASPTPSAPQTSLATHLPFSSTSSVTPTSEVIITPTPQHTLSSASTSTTTGNILPTTIGQTGSPHTSVPVIYTTSAITQTK 1670
Cdd:COG3469 83 TAAAAAATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATGG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907182200 1671 TSFSTDrTSTPTSAPhlsetsavtahqSTPTAVSANSikPTMSSTGTPVVHTTSGTTSSPQTP 1733
Cdd:COG3469 163 TTTTST-TTTTTSAS------------TTPSATTTAT--ATTASGATTPSATTTATTTGPPTP 210
|
|
| TIL |
pfam01826 |
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
665-722 |
2.88e-04 |
|
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.
Pssm-ID: 460351 Cd Length: 55 Bit Score: 40.83 E-value: 2.88e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907182200 665 CTGNRTFSYDSQACDRTCLSLSDR---ETEChvspvpVDGCNCPEGTYLNHKAECVHKAQC 722
Cdd:pfam01826 1 CPANEVYSECGSACPPTCANLSPPdvcPEPC------VEGCVCPPGFVRNSGGKCVPPSDC 55
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
1380-1605 |
3.60e-04 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 45.51 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1380 SSGTPSSSHATHITYTPPTQVVSSITHSTGPPLGTSVQTTinfptlSAPQTSLVTPHPGLSSSSTALTSEILKTPTSSQM 1459
Cdd:COG3469 8 ASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTG------SVVVAASGSAGSGTGTTAASSTAATSSTTSTTAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1460 VSSASPQTIFSSIHPKTTLEATTPQHTAPLITSITSSITQAQSSFSTDKTYTSQHSQPSTMTAHQSRSLPTVTTSTKSTm 1539
Cdd:COG3469 82 ATAAAAAATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETAT- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907182200 1540 glTGTPPVHTTSGTTSSPQTPRTTHPFSTVAVSNTKHTTgvsletsvqTTIASPTPSAPQTSLATH 1605
Cdd:COG3469 161 --GGTTTTSTTTTTTSASTTPSATTTATATTASGATTPS---------ATTTATTTGPPTPGLPKH 215
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
1530-1778 |
3.76e-04 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 45.51 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1530 TVTTSTKSTMGLTGTPPVHTTSGTTSSPQTPRTTHPFSTVAVSNTKHTTGV-SLETSVQTTIASPTPSAPQTSLATHLPf 1608
Cdd:COG3469 1 SSSVSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVaASGSAGSGTGTTAASSTAATSSTTSTT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1609 sstssvtptseviitptpqhtlssaststttgniLPTTIGQTGSPHTSVPVIYTTSAITQTKTSFSTDRTSTPTSAPhls 1688
Cdd:COG3469 80 ----------------------------------ATATAAAAAATSTSATLVATSTASGANTGTSTVTTTSTGAGSV--- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1689 eTSAVTAHQSTPTAVSANSIKPTMSSTGTP----VVHTTSGTTSSPQTPRTTHPSTTVAVSGTVHTTGLPSGTSVHTTTN 1764
Cdd:COG3469 123 -TSTTSSTAGSTTTSGASATSSAGSTTTTTtvsgTETATGGTTTTSTTTTTTSASTTPSATTTATATTASGATTPSATTT 201
|
250
....*....|....
gi 1907182200 1765 FPTHSGPQSSLSTH 1778
Cdd:COG3469 202 ATTTGPPTPGLPKH 215
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
1260-1607 |
3.83e-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: 45.68 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1260 TTPKESTVSSGEYPQTtmaatpptspwpPTSIPKSTPTELPVTQATSkPTASSLSSSTKTTAELTESTTVTLLTLMPGMs 1339
Cdd:pfam05109 474 TSPTPAGTTSGASPVT------------PSPSPRDNGTESKAPDMTS-PTSAVTTPTPNATSPTPAVTTPTPNATSPTL- 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1340 tsqGKTSASyttqhqstsfhlTTISKWPTNGVSDTPGVHTSsgTPSSSHATHITYTPPTQVVSSITHSTGPPLG-TSVQT 1418
Cdd:pfam05109 540 ---GKTSPT------------SAVTTPTPNATSPTPAVTTP--TPNATIPTLGKTSPTSAVTTPTPNATSPTVGeTSPQA 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1419 TINFPTLSA-PQTSLVTPHPGLSSSSTALTSEILKTPTSSQMvsSASPQTIFSSIHPKTTLEATTpqhTAPLITSI---- 1493
Cdd:pfam05109 603 NTTNHTLGGtSSTPVVTSPPKNATSAVTTGQHNITSSSTSSM--SLRPSSISETLSPSTSDNSTS---HMPLLTSAhptg 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1494 TSSITQAQSSFSTDKTYTSQHSQPSTMTAHQSRSLPTVTTSTK-STMGLT-GTPPVHTTSGTTSSPQTPRTTHPFSTVAV 1571
Cdd:pfam05109 678 GENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKpGEVNVTkGTPPKNATSPQAPSGQKTAVPTVTSTGGK 757
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1907182200 1572 SNT----KHTTGVSLETSVQ-TTIASPTPSAPQT--SLATHLP 1607
Cdd:pfam05109 758 ANSttggKHTTGHGARTSTEpTTDYGGDSTTPRTryNATTYLP 800
|
|
| PLN02217 |
PLN02217 |
probable pectinesterase/pectinesterase inhibitor |
1986-2116 |
3.85e-04 |
|
probable pectinesterase/pectinesterase inhibitor
Pssm-ID: 215130 [Multi-domain] Cd Length: 670 Bit Score: 45.85 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1986 TTIKGTGTPQTP--VSDINTTSATTQAHSSFPTTRTSTShlslpSSMTSTLTPAsrsastlqyTPTPSSVSHSPLLTTPT 2063
Cdd:PLN02217 548 AWIPGKGVPYIPglFAGNPGSTNSTPTGSAASSNTTFSS-----DSPSTVVAPS---------TSPPAGHLGSPPATPSK 613
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1907182200 2064 ASPPSSAPTFVSPTAASTVISSALPTIHMTPTPSSRPTSSTGLLSTSKTTSHV 2116
Cdd:PLN02217 614 IVSPSTSPPASHLGSPSTTPSSPESSIKVASTETASPESSIKVASTESSVSMV 666
|
|
| Nucleoporin_FG2 |
pfam15967 |
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of ... |
1910-2106 |
5.79e-04 |
|
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of chordate nucleoporins. The proteins carry many repeats of the FG sequence motif.
Pssm-ID: 435043 [Multi-domain] Cd Length: 586 Bit Score: 45.04 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1910 TAAISRTTGISGTPFRTPMKTTITFPTPSSLQTSM-ATLFPPFSTSVMSsteiFNTPTnphsvSSASTSRPLSTSLPTTi 1988
Cdd:pfam15967 24 AAAASNPGSTGGFSFGTLGAAPAATATTTTATLGLgGGLFGQKPATGFT----FGTPA-----SSTAATGPTGLTLGTP- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1989 KGTGTPQTPVSDINTTSATTQAHSSFPTTRTSTSHLSLPSSMTSTLTPASRSASTLQYTPTP-SSVSHSPLLTTPTASPP 2067
Cdd:pfam15967 94 AATTAASTGFSLGFNKPAASATPFSLPASSTSGGGLSLGSVLTSTAAQQGATGFTLNLGGTPaTTTAVSTGLSLGSTLTS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907182200 2068 SSAPTFVSPTAASTVISSALPTIHMTPT-PSSRPTSSTGL 2106
Cdd:pfam15967 174 LGGSLFQNTNSTGLGQTTLGLTLLATSTaPVSAPAASEGL 213
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
1712-2082 |
6.71e-04 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 45.06 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1712 MSSTGTPVVHTTSGTTSS--PQTPRTTHPSTTVAVS-GTVHTTGLPSGTSVHTTTNFPTHSGpQSSLSTHLplfSTLSVT 1788
Cdd:PHA03378 533 RAGRRAPCVYTEDLDIESdePASTEPVHDQLLPAPGlGPLQIQPLTSPTTSQLASSAPSYAQ-TPWPVPHP---SQTPEP 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1789 PTTEGLNTPTS-PHSLSVASTSMPL----MTVLPTTLEGTRPPHTSVPVTYtttaatqtkSSFSTDRTSTPHLS-QSSTV 1862
Cdd:PHA03378 609 PTTQSHIPETSaPRQWPMPLRPIPMrplrMQPITFNVLVFPTPHQPPQVEI---------TPYKPTWTQIGHIPyQPSPT 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1863 TPTQSTPIPATTNSLMTTGGLTG-TPPVHTTSGTTSSPQTPHSTHPISTAAISRTTGISGTPfrTPMKTTITFPTPSSLQ 1941
Cdd:PHA03378 680 GANTMLPIQWAPGTMQPPPRAPTpMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAP--GRARPPAAAPGRARPP 757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1942 TSMATLFPPFSTSVMSSTeifntPTNPHSVSSASTSRPlstslpttiKGTGTPQTPVSDINTTSATTQAHSSFPTTRTST 2021
Cdd:PHA03378 758 AAAPGRARPPAAAPGAPT-----PQPPPQAPPAPQQRP---------RGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQ 823
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907182200 2022 SHLSLPSSMTSTLTPASRSASTLQ------YTPTPSSVSHSPLLTTPTASPPSSAPT-------FVSPTAASTV 2082
Cdd:PHA03378 824 ILRQLLTGGVKRGRPSLKKPAALErqaaagPTPSPGSGTSDKIVQAPVFYPPVLQPIqvmrqlgSVRAAAASTV 897
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
1648-1803 |
6.89e-04 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 44.74 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1648 GQTGSPHTSVPVIYTTSAITQTKTSFSTDRTSTPTSAPHLSETSAVTAhqSTPTAVSANSIKPTMSSTGTPVVHTTSGTT 1727
Cdd:COG3469 69 TAATSSTTSTTATATAAAAAATSTSATLVATSTASGANTGTSTVTTTS--TGAGSVTSTTSSTAGSTTTSGASATSSAGS 146
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907182200 1728 SSPQTPRTTHPSTTVAVSGTVHTTGLPSGTSVHTTTNFPTHSGPQSSLSThlplfSTLSVTPTTEGLNTPTSPHSL 1803
Cdd:COG3469 147 TTTTTTVSGTETATGGTTTTSTTTTTTSASTTPSATTTATATTASGATTP-----SATTTATTTGPPTPGLPKHVL 217
|
|
| Hamartin |
pfam04388 |
Hamartin protein; This family includes the hamartin protein which is thought to function as a ... |
1823-2106 |
7.06e-04 |
|
Hamartin protein; This family includes the hamartin protein which is thought to function as a tumour suppressor. The hamartin protein interacts with the tuberin protein pfam03542. Tuberous sclerosis complex (TSC) is an autosomal dominant disorder and is characterized by the presence of hamartomas in many organs, such as brain, skin, heart, lung, and kidney. It is caused by mutation either TSC1 or TSC2 tumour suppressor gene. TSC1 encodes a protein, hamartin, containing two coiled-coil regions, which have been shown to mediate binding to tuberin. The TSC2 gene codes for tuberin pfam03542. These two proteins function within the same pathway(s) regulating cell cycle, cell growth, adhesion, and vesicular trafficking.
Pssm-ID: 461287 [Multi-domain] Cd Length: 730 Bit Score: 45.05 E-value: 7.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1823 TRPPHTSvpvtYTTTAATQTKSSFSTDRTSTPHLSQSS----TVTPTQSTPIPATTNSLMTTGGLTGTPPVHTTSGTTSS 1898
Cdd:pfam04388 277 TASPYTD----QQSSYGSSTSTPSSTPRLQLSSSSGTSppylSPPSIRLKTDSFPLWSPSSVCGMTTPPTSPGMVPTTPS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1899 PQTPHSTHPISTaaISRTTG--ISGTPFRTPMKTTITFPTPSSLQTSMATLFPPFSTSVMSSTEIFNTPTNPHSVSSAST 1976
Cdd:pfam04388 353 ELSPSSSHLSSR--GSSPPEaaGEATPETTPAKDSPYLKQPPPLSDSHVHRALPASSQPSSPPRKDGRSQSSFPPLSKQA 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1977 SRPLSTSLPTTIKGTGTP--QTPVSDINTT----------------------SATTQAHSSFPTTR------TSTSHLSL 2026
Cdd:pfam04388 431 PTNPNSRGLLEPPGDKSSvtLSELPDFIKDlalssedsvegaeeeaaisqelSEITTEKNETDCSRggldmpFSRTMESL 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 2027 PSSMTSTLTPASRSASTLQYTPTPSSVSHSPLLTTPTASPPSSAPTFvSPTAASTVISSalPTIHMTPTPSSRPTSSTGL 2106
Cdd:pfam04388 511 AGSQRSRNRIASYCSSTSQSDSHGPATTPESKPSALAEDGLRRTKSC-SFKQSFTPIEQ--PIESSDDCPTDEQDGENGL 587
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
1361-1560 |
7.13e-04 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 44.74 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1361 TTISKWPTNGVSDTPGVHTSSGTPSSSHATHITYTPPTQVVSSITHSTGPPLGTSVQTTINFPTLSAPQTSLVTPHPGLS 1440
Cdd:COG3469 27 ATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATATAAAAAATSTSATLVATSTASGAN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1441 SSSTALTSeilkTPTSSQMVSSASPQTIFSSIHPKTTLEATTPQHTAPLITSITSSITQAQSSFSTDKTYTSQHSQPSTm 1520
Cdd:COG3469 107 TGTSTVTT----TSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATGGTTTTSTTTTTTSASTTPSA- 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907182200 1521 tahqsrslptvTTSTKSTMGLTGTPPVHTTSGTTSSPQTP 1560
Cdd:COG3469 182 -----------TTTATATTASGATTPSATTTATTTGPPTP 210
|
|
| motB |
PRK12799 |
flagellar motor protein MotB; Reviewed |
1964-2099 |
8.18e-04 |
|
flagellar motor protein MotB; Reviewed
Pssm-ID: 183756 [Multi-domain] Cd Length: 421 Bit Score: 44.32 E-value: 8.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1964 TPTNPHSVSSASTSRPLSTSLPTTIKGTGTPQTPVSDINTTSATTqahSSFPTTRTSTSHLSlPSSMTSTLTPASRSAST 2043
Cdd:PRK12799 296 HGTVPVAAVTPSSAVTQSSAITPSSAAIPSPAVIPSSVTTQSATT---TQASAVALSSAGVL-PSDVTLPGTVALPAAEP 371
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907182200 2044 LQYTPTPSSVSHSPLLTTPTASPPSSAPTFVSPTAastvissalPTIHMTPTPSSR 2099
Cdd:PRK12799 372 VNMQPQPMSTTETQQSSTGNITSTANGPTTSLPAA---------PASNIPVSPTSR 418
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
1296-1748 |
8.97e-04 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 44.18 E-value: 8.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1296 PTELPVTQATSKPTasslssstkttaelTESTTVTLLTLMPGMSTSQGKTSASYTTqhqstsfhlTTISKWPTNGVSDTP 1375
Cdd:pfam17823 67 PAPVTLTKGTSAAH--------------LNSTEVTAEHTPHGTDLSEPATREGAAD---------GAASRALAAAASSSP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1376 GVHTSSGTPSSSHATHITYTPPTQVVSSITHSTGPplgtsvqttinfptlSAPQTSLVTPHPGLSSSSTALTSEILKTPT 1455
Cdd:pfam17823 124 SSAAQSLPAAIAALPSEAFSAPRAAACRANASAAP---------------RAAIAAASAPHAASPAPRTAASSTTAASST 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1456 SSqmVSSASPQTIFSSIHPKTTLEATTPQHTAPLITSITSSITQAQSSFSTDKTYTSQHSQPSTMTAHQSRSLPTVTTST 1535
Cdd:pfam17823 189 TA--ASSAPTTAASSAPATLTPARGISTAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVASA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1536 KSTMGlTGTPPVHTTSGTTSSPQTPRTTHPFSTVAVSNTKHTTGVSLETSVQTTIASPTPSAPQTSLATHLPFSSTSSVT 1615
Cdd:pfam17823 267 AGTIN-MGDPHARRLSPAKHMPSDTMARNPAAPMGAQAQGPIIQVSTDQPVHNTAGEPTPSPSNTTLEPNTPKSVASTNL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1616 PtseviitptpqhtlssaststttgnILPTTIGQTGSPHTS-VPVIYTTSAITQTKTSFSTDRTSTP----TSAPHLSET 1690
Cdd:pfam17823 346 A-------------------------VVTTTKAQAKEPSASpVPVLHTSMIPEVEATSPTTQPSPLLptqgAAGPGILLA 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907182200 1691 SAVTAHQSTPTAVSANsikPTMSSTGTPVVHTTSGTTSSPQTPR---TTHPSTTVAVSGTV 1748
Cdd:pfam17823 401 PEQVATEATAGTASAG---PTPRSSGDPKTLAMASCQLSTQGQYlvvTTDPLTPALVDKMF 458
|
|
| SOG2 |
pfam10428 |
RAM signalling pathway protein; SOG2 proteins in Saccharomyces cerevisiae are involved in cell ... |
1886-2086 |
9.85e-04 |
|
RAM signalling pathway protein; SOG2 proteins in Saccharomyces cerevisiae are involved in cell separation and cytokinesis.
Pssm-ID: 431280 Cd Length: 476 Bit Score: 44.32 E-value: 9.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1886 TPPVHTTSGTTSSPQtPHSTHPISTAAISRTTGISGTPFRTPMKttitFPTPSSLQTSMATLFPPFSTSVMSSTeifnTP 1965
Cdd:pfam10428 161 PPSPKKRAGRTKQPS-PSITSGGSPSSPAESSTRPSSSSVTPTR----RRRHAGSFSSKLPPLRSDTTIPHPGG----NL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1966 TNPHSVSSASTSRPLSTSLPttikGTGTPQTPVSDINTTSATTQAHSsfpttrtstshlslPSSMTSTLTPASRSASTLQ 2045
Cdd:pfam10428 232 SSPAPNGAQTPTPPRSATSP----GVPSSAPTLGTGSTGAISRSNHS--------------TSGSQSSLTSSSRSRSSSR 293
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907182200 2046 YTPTPSSVSHSPLLTTPtasPPSSAPTFVSPTAASTVISSA 2086
Cdd:pfam10428 294 SNTLLSTSGPSSLATTP---RPSSGESFAPTSTGSRINPLT 331
|
|
| ROM1 |
COG5422 |
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ... |
1407-1625 |
1.26e-03 |
|
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];
Pssm-ID: 227709 [Multi-domain] Cd Length: 1175 Bit Score: 44.11 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1407 STGPPLGTSVQTTINFPTLSAPQTSLVT-----PHPGLSSSSTALTSEILKTPTSSQMVSSASPQT-IFSSIHPKTTLEA 1480
Cdd:COG5422 28 SKQLLPPRRLQRKLNPISIRNGADNDIInseskESFGKYALGHQIFSSFSSSPKLFQRRNSAGPIThSPSATSSTSSLNS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1481 TTPQHTAPLITSITSSITQAQSSFSTDKTYTSQHS------QPSTMTaHQSRSLPTVTTSTKSTMGLTG---TPPVHTTS 1551
Cdd:COG5422 108 NDGDQFSPASDSLSFNPSSTQSRKDSGPGDGSPVQkrknplLPSSST-HGTHPPIVFTDNNGSHAGAPNarsRKEIPSLG 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907182200 1552 GTTSSPQTPRTTHPFSTVAVSNT---KHTTGVSLETSvqttiaSPTPSAPQTSLATHLPFSSTSSVTPTSEVIITPT 1625
Cdd:COG5422 187 SQSMQLPSPHFRQKFSSSDTSNGfsyPSIRKNSRHSS------NSMPSFPHSSTAVLLKRHSGSSGASLISSNITPS 257
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
1741-1985 |
1.32e-03 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 43.97 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1741 TVAVSGTVHTTGlpSGTSVHTTTNFPTHSGPQSSlsthlplfSTLSVTPTTEGLNTPTSPHSLSVASTSMPLMTVLPTTL 1820
Cdd:COG3469 1 SSSVSTAASPTA--GGASATAVTLLGAAATAASV--------TLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1821 EGTRPPHTSVPVTYtttaatqtkssfstdrTSTPHLSQSSTVTPTQSTPIPATTNSLMTTGGLTGTPPVHTTSGTTSSPQ 1900
Cdd:COG3469 71 ATSSTTSTTATATA----------------AAAAATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1901 TPHSTHPISTAAISRTTGISGTPFrtpmkTTITFPTPSSLQTSMATLFPPFSTSVMSSTEIFNTPTNPHSvSSASTSRPL 1980
Cdd:COG3469 135 TSGASATSSAGSTTTTTTVSGTET-----ATGGTTTTSTTTTTTSASTTPSATTTATATTASGATTPSAT-TTATTTGPP 208
|
....*
gi 1907182200 1981 STSLP 1985
Cdd:COG3469 209 TPGLP 213
|
|
| PRK11901 |
PRK11901 |
hypothetical protein; Reviewed |
1972-2113 |
1.43e-03 |
|
hypothetical protein; Reviewed
Pssm-ID: 237015 [Multi-domain] Cd Length: 327 Bit Score: 43.13 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1972 SSASTSRPLSTSLPTTIKGTGTPQT----PVSdinttSATTQAHSsfPTTRTSTSHLSLPSSMTSTLT-----------P 2036
Cdd:PRK11901 94 SPSAANNTSDGHDASGVKNTAPPQDisapPIS-----PTPTQAAP--PQTPNGQQRIELPGNISDALSqqqgqvnaasqN 166
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907182200 2037 ASRSASTLqyTPTPSSVSHSPLLTTPTASPPSSAPTFVSPTAASTVISSALPTIHMTPTPSSRPTSSTGLLSTSKTT 2113
Cdd:PRK11901 167 AQGNTSTL--PTAPATVAPSKGAKVPATAETHPTPPQKPATKKPAVNHHKTATVAVPPATSGKPKSGAASARALSSA 241
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1373-1626 |
1.69e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 43.83 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1373 DTPGvhTSSGTPS-----SSHATHITYTP----------PTQVVSSITHSTGPPLGTSVQTTINFPTLSAPQTSLVTPHP 1437
Cdd:TIGR00927 143 DTPA--TPSRALNhyistSGRQRVKSYTPkprgevksssPTQTREKVRKYTPSPLGRMVNSYAPSTFMTMPRSHGITPRT 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1438 GLSSSSTALTSEILKTPTSSQMVSSASPQT---IFSSIHPKTTLEATTPQHTAPLITSITSSITQAQSSFSTDKTYTSQH 1514
Cdd:TIGR00927 221 TVKDSEITATYKMLETNPSKRTAGKTTPTPlkgMTDNTPTFLTREVETDLLTSPRSVVEKNTLTTPRRVESNSSTNHWGL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1515 SQPSTMTAHQSRSL-PTVTTS----TKSTMglTGTPPVHTTSGTTS----SPqTPRTTHPfsTVAVSNTKHTTGVSLETS 1585
Cdd:TIGR00927 301 VGKNNLTTPQGTVLeHTPATSegqvTISIM--TGSSPAETKASTAAwkirNP-LSRTSAP--AVRIASATFRGLEKNPST 375
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1907182200 1586 VQTTIASPTPSAPQTSLATHLpfsstssvtptseVIITPTP 1626
Cdd:TIGR00927 376 APSTPATPRVRAVLTTQVHHC-------------VVVKPAP 403
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1851-2177 |
1.75e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.62 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1851 TSTPHLSQSSTVTPTQSTPIPATTNSLMTTGGLTGTPPVHTTSGT--TSSPQTPHSTHPISTAAISRTTGISGTPFRTPM 1928
Cdd:PHA03307 73 PGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPppTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASP 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1929 KttitfPTPSSLQTSMATLFPPFSTSVMSSTeifnTPTNPHSVSSASTSRPLSTSLPttiKGTGTPQTPVSDINTTSATT 2008
Cdd:PHA03307 153 P-----AAGASPAAVASDAASSRQAALPLSS----PEETARAPSSPPAEPPPSTPPA---AASPRPPRRSSPISASASSP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 2009 QA----HSSFPTTRTSTSHLSLPSSMTS----TLTPASRSAstLQYTPTPSSVSHSPLLTTPTASPPSSAPTFVSPTAAS 2080
Cdd:PHA03307 221 APapgrSAADDAGASSSDSSSSESSGCGwgpeNECPLPRPA--PITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSP 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 2081 TVISSALPTiHMTPTPSSRPTSSTGLLSTSKTTSHVPTFSsfssksttahltsltTQAATSGLLSStmgmtNLPSSGSPD 2160
Cdd:PHA03307 299 SPSSPGSGP-APSSPRASSSSSSSRESSSSSTSSSSESSR---------------GAAVSPGPSPS-----RSPSPSRPP 357
|
330
....*....|....*..
gi 1907182200 2161 INHTTRPPGSSPLPTSA 2177
Cdd:PHA03307 358 PPADPSSPRKRPRPSRA 374
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1663-2103 |
2.19e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.62 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1663 TSAITQTKTSFSTDRTSTPTSAPHLSETSAVtahqSTPTAVSANSIKP-TMSSTGTPvvhTTSGTTSSPQTPRTTHPSTT 1741
Cdd:PHA03307 54 TVVAGAAACDRFEPPTGPPPGPGTEAPANES----RSTPTWSLSTLAPaSPAREGSP---TPPGPSSPDPPPPTPPPASP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1742 VAVSGTVHTTGLPSGTSvhtttnfPTHSGPQSSLSTHLPlfstlsvtPTTEGLNTPTSPHSLSVASTSMPLMTVLPTtle 1821
Cdd:PHA03307 127 PPSPAPDLSEMLRPVGS-------PGPPPAASPPAAGAS--------PAAVASDAASSRQAALPLSSPEETARAPSS--- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1822 gtrPPHTSVPvtytttaatqtkssfSTDRTSTPHLSQSSTVTPTQSTPIPATTNSLMTTGGLTGTPPVHTTSGTTSSPQT 1901
Cdd:PHA03307 189 ---PPAEPPP---------------STPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1902 PHSTHPISTAAISRTTGISGTPfrTPMKTTITFPTPSSLQTSMATLFPPFStsvmssteifntPTNPHSVSSASTSRPLS 1981
Cdd:PHA03307 251 PENECPLPRPAPITLPTRIWEA--SGWNGPSSRPGPASSSSSPRERSPSPS------------PSSPGSGPAPSSPRASS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1982 TSlpttikgtGTPQTPVSDINTTSATTQAHSSFPTTRTSTSHLSlPSSMTSTLTPASRSAStlqytPTPSSVShspllTT 2061
Cdd:PHA03307 317 SS--------SSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPS-PSRPPPPADPSSPRKR-----PRPSRAP-----SS 377
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1907182200 2062 PTASPPSSAPtfvsPTAASTVISSALPTIHMTPTPSSRPTSS 2103
Cdd:PHA03307 378 PAASAGRPTR----RRARAAVAGRARRRDATGRFPAGRPRPS 415
|
|
| COG5099 |
COG5099 |
RNA-binding protein of the Puf family, translational repressor [Translation, ribosomal ... |
1640-2056 |
2.39e-03 |
|
RNA-binding protein of the Puf family, translational repressor [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227430 [Multi-domain] Cd Length: 777 Bit Score: 43.20 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1640 GNILPTTIGQ-TGSPHTsvPVIYTTSAITQTKTSFSTDRTSTPTSAphlsETSAVTAHqsTPTAVSANSIKPTMSSTGTP 1718
Cdd:COG5099 7 NNLLPSIKSQlHHSKKS--PPSSTTSQELMNGNSTPNSFSPIPSKA----SSSATFTL--NLPINNSVNHKITSSSSSRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1719 VVHTTSGTTSSPQTPRTTHPSTTvavSGTVHTTGLPSGTSVHTTTNFPTHSGPQSSLSTHLPLFSTLSVTPTTEGLNTP- 1797
Cdd:COG5099 79 KPSGSWSVAISSSTSGSQSLLME---LPSSSFNPSTSSRNKSNSALSSTQQGNANSSVTLSSSTASSMFNSNKLPLPNPn 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1798 ------TSPHSLSVASTSMPLMTVLPTTL----------EGTRPPHTSVPVTYTTTAATQTKSSfSTDRTSTPHLSQSST 1861
Cdd:COG5099 156 hsnsatTNQSGSSFINTPASSSSQPLTNLvvssikrfpyLTSLSPFFNYLIDPSSDSATASADT-SPSFNPPPNLSPNNL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1862 VTPTQSTPIPATTNSLMTTGGLTGTP-----------PVHTTSGTTSSPQTPHSTHPISTAAISRTTGISGTPFRTPMKT 1930
Cdd:COG5099 235 FSTSDLSPLPDTQSVENNIILNSSSSineltsiygsvPSIRNLRGLNSALVSFLNVSSSSLAFSALNGKEVSPTGSPSTR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1931 TITFPTPSSlqtsmatlfppfsTSVMSSTEIFNTPTNPHSvssastsrplstslpttikgtgtPQTPVSDINTTSATTQA 2010
Cdd:COG5099 315 SFARVLPKS-------------SPNNLLTEILTTGVNPPQ-----------------------SLPSLLNPVFLSTSTGF 358
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1907182200 2011 HSsfpttrTSTSHLSLPSSMTSTLTPASRSASTLQYTPTPSSVSHS 2056
Cdd:COG5099 359 SL------TNLSGYLNPNKNLKKNTLSSLSNLGYSSNVPSPSSSES 398
|
|
| ROM1 |
COG5422 |
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ... |
1661-1876 |
2.40e-03 |
|
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];
Pssm-ID: 227709 [Multi-domain] Cd Length: 1175 Bit Score: 43.34 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1661 YTTSAITQTKTSFSTDRTSTPTSAPHLSETSAVTAHQSTPTAVSANSIKPTMSSTG----TPVVHTTSGTTSSPQTPRTT 1736
Cdd:COG5422 66 YALGHQIFSSFSSSPKLFQRRNSAGPITHSPSATSSTSSLNSNDGDQFSPASDSLSfnpsSTQSRKDSGPGDGSPVQKRK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1737 HPSTTvavSGTVHTTGLPsgtsVHTTTNFPTHSGPQSSLST-HLPlfstlSVTPTTEGLNTPTSPHSLSVASTSMPLMtv 1815
Cdd:COG5422 146 NPLLP---SSSTHGTHPP----IVFTDNNGSHAGAPNARSRkEIP-----SLGSQSMQLPSPHFRQKFSSSDTSNGFS-- 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907182200 1816 LPTTleGTRPPHTSVPVTYTTTAATQTKSSFSTDRTSTPHLsqSSTVTPTQSTPIPATTNS 1876
Cdd:COG5422 212 YPSI--RKNSRHSSNSMPSFPHSSTAVLLKRHSGSSGASLI--SSNITPSSSNSEAMSTSS 268
|
|
| PHA03273 |
PHA03273 |
envelope glycoprotein C; Provisional |
1951-2056 |
2.86e-03 |
|
envelope glycoprotein C; Provisional
Pssm-ID: 223031 Cd Length: 486 Bit Score: 42.68 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1951 FSTSVMSSTEIFNTPTNPHSVSSASTSRPLSTSLPTTIKGTGTPQTpvSDINTTSATTQAhssfpttrtstshlSLPSSM 2030
Cdd:PHA03273 24 YASGASTSSSIENSDNSTAEMQSTPATPTHTTSNLTSPFGTGTDNS--TNANGTESTTQA--------------SQPHSH 87
|
90 100 110
....*....|....*....|....*....|..
gi 1907182200 2031 TSTLTPASRSASTLQYTP------TPSSVSHS 2056
Cdd:PHA03273 88 ETTITCTKSLISVPYYKSvdmnctTSVGVNYS 119
|
|
| PHA03255 |
PHA03255 |
BDLF3; Provisional |
1938-2106 |
3.10e-03 |
|
BDLF3; Provisional
Pssm-ID: 165513 [Multi-domain] Cd Length: 234 Bit Score: 41.81 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1938 SSLQTSMATLFPPFSTSVMSSTEIFNTPTNPHSVSSASTSRPLSTSLP-TTIKGTGTPQTPVSDINTT--SATTQAHSSF 2014
Cdd:PHA03255 20 TSLIWTSSGSSTASAGNVTGTTAVTTPSPSASGPSTNQSTTLTTTSAPiTTTAILSTNTTTVTSTGTTvtPVPTTSNAST 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 2015 PTTRTS-TSHLSLPSSMTSTLTPASRSASTLQYTPTPSSVSHSPLLTTPTASPPSSAptfvspTAASTVISSALPtihmT 2093
Cdd:PHA03255 100 INVTTKvTAQNITATEAGTGTSTGVTSNVTTRSSSTTSATTRITNATTLAPTLSSKG------TSNATKTTAELP----T 169
|
170
....*....|...
gi 1907182200 2094 PTPSSRPTSSTGL 2106
Cdd:PHA03255 170 VPDERQPSLSYGL 182
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
1211-1601 |
3.66e-03 |
|
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: 42.60 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1211 GSQPTTETTISTEFHSSTSANTPVAPSYLPGLPTPPPSAPSSTEELTVWTTPKESTVSSgeypqtTMAATPPTSPWPPTS 1290
Cdd:pfam05109 465 GPTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSP------TPAVTTPTPNATSPT 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1291 IPKSTPTE---LPVTQATSKPTASSLSSSTKTTAELTESTTVTLLTLMPGMSTSqgKTSASYTTQHQSTSFHLTTISKWP 1367
Cdd:pfam05109 539 LGKTSPTSavtTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTPNATS--PTVGETSPQANTTNHTLGGTSSTP 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1368 TngVSDTPGVHTSSGTPSSSHATHITYTPPTQVVSSITHSTGPplGTSVQTTINFPTLSapqtslvTPHPglssSSTALT 1447
Cdd:pfam05109 617 V--VTSPPKNATSAVTTGQHNITSSSTSSMSLRPSSISETLSP--STSDNSTSHMPLLT-------SAHP----TGGENI 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1448 SEILKTPTSSQMVSSASPqtifsSIHPKTTLEATTPQHTAPLITSITSSITQAQSSFSTDKTYTSQHSQPSTMTAHQSRS 1527
Cdd:pfam05109 682 TQVTPASTSTHHVSTSSP-----APRPGTTSQASGPGNSSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTSTGG 756
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1528 LPTVTTSTKSTMG---LTGTPPVHTTSGTTSSPQT---PRTTHPFSTVAVSNTKHTTGVSLETSVQTTIASPTPSAPQTS 1601
Cdd:pfam05109 757 KANSTTGGKHTTGhgaRTSTEPTTDYGGDSTTPRTrynATTYLPPSTSSKLRPRWTFTSPPVTTAQATVPVPPTSQPRFS 836
|
|
| PHA03255 |
PHA03255 |
BDLF3; Provisional |
1973-2117 |
6.31e-03 |
|
BDLF3; Provisional
Pssm-ID: 165513 [Multi-domain] Cd Length: 234 Bit Score: 40.66 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1973 SASTSRPLSTSLPTTIKGTGTPQTPVSDINTTSATTQAHSSFPTTRTS--TSHLSLPSSMTSTLTPASRSASTlqYTPTP 2050
Cdd:PHA03255 25 TSSGSSTASAGNVTGTTAVTTPSPSASGPSTNQSTTLTTTSAPITTTAilSTNTTTVTSTGTTVTPVPTTSNA--STINV 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907182200 2051 SSVSHSPLLTTPTASPPSSAPTFVSPTAASTVISSAlpTIHMTPTPSSRPT-SSTGLLSTSKTTSHVP 2117
Cdd:PHA03255 103 TTKVTAQNITATEAGTGTSTGVTSNVTTRSSSTTSA--TTRITNATTLAPTlSSKGTSNATKTTAELP 168
|
|
| ser_rich_anae_1 |
NF033849 |
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ... |
1339-1591 |
7.65e-03 |
|
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 amino acids), which a highly serine-rich central region that averages over 300 aa in length. Species encoding members of this family of proteins tend to be anaerobic bacteria, including Gram-positive bacteria of the human gut microbiome and Chloroflexi from marine sediments.
Pssm-ID: 468206 [Multi-domain] Cd Length: 1122 Bit Score: 41.53 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1339 STSQGKTSASYTTQHQSTSfHLTTISKwpTNGVSDTPGVHTSSGT---PSSSHATHITYTPP--TQVVSSITHSTGPPLG 1413
Cdd:NF033849 276 TTGHGSTRGWSHTQSTSES-ESTGQSS--SVGTSESQSHGTTEGTsttDSSSHSQSSSYNVSsgTGVSSSHSDGTSQSTS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1414 TSVQTTINFPTLSAPQTSLVTPHPGLSSSSTaltseilktpTSSQMVSSASPQTIFSSIHPKTTLEATTPQHTAplITSI 1493
Cdd:NF033849 353 ISHSESSSESTGTSVGHSTSSSVSSSESSSR----------SSSSGVSGGFSGGIAGGGVTSEGLGASQGGSEG--WGSG 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1494 TSSITQAQSSFSTDKTYTSqHSQpSTMTAH-----QSRSLPTVTTSTKSTMGLTGTPPVHTTSGTTSSPQTPRTTHPFS- 1567
Cdd:NF033849 421 DSVQSVSQSYGSSSSTGTS-SGH-SDSSSHstssgQADSVSQGTSWSEGTGTSQGQSVGTSESWSTSQSETDSVGDSTGt 498
|
250 260
....*....|....*....|....*..
gi 1907182200 1568 --TVAVSNTK-HTTGVSLETSVQTTIA 1591
Cdd:NF033849 499 seSVSQGDGRsTGRSESQGTSLGTSGG 525
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
1997-2174 |
8.85e-03 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 41.10 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1997 PVSDINTTSATTQAH-SSFPTTRTSTSH---LSLPSSMTSTLTPASRSASTLQYTPTPSSVSHSplLTTPTASPPS---S 2069
Cdd:pfam17823 66 APAPVTLTKGTSAAHlNSTEVTAEHTPHgtdLSEPATREGAADGAASRALAAAASSSPSSAAQS--LPAAIAALPSeafS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 2070 APTFVSPTAASTVISSALPTIHMTPTPSSrPTSSTGLLSTSKTTShvptFSSFSSKSTTAHLTSLTTQAATSGLLSSTMG 2149
Cdd:pfam17823 144 APRAAACRANASAAPRAAIAAASAPHAAS-PAPRTAASSTTAASS----TTAASSAPTTAASSAPATLTPARGISTAATA 218
|
170 180
....*....|....*....|....*
gi 1907182200 2150 mTNLPSSGSPdinhTTRPPGSSPLP 2174
Cdd:pfam17823 219 -TGHPAAGTA----LAAVGNSSPAA 238
|
|
| PHA02732 |
PHA02732 |
hypothetical protein; Provisional |
1859-2081 |
9.51e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 165099 [Multi-domain] Cd Length: 1467 Bit Score: 41.28 E-value: 9.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1859 SSTVTPTQSTPIPATTNSLMTTGGLTGTPPVHTTSGTTSSPQTPHSTHPISTAAISRTTGISGTPFRTPMKTTITFPTPS 1938
Cdd:PHA02732 1068 SPFTFVSPSYIFLNSWASSYVAPGFLGSPYALPYFMNQTSALVGNTALPKGLNVFSGYMFGAGTVASAFLYMNSTPQSPV 1147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1939 SLQTSMATLFPPFST-----SVMSSTEIFNTPTNPhSVSSASTSRPLSTSLPTTIKGTGTPQTPVSDINTTSAT---TQA 2010
Cdd:PHA02732 1148 LALLLAPYISYKFNAlslgfSITADAAIFSLFGIP-APQLLSSYIPTGSVLYQDPIFTYIPPGIIGMSGTNTFTfkaAQL 1226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907182200 2011 HSSFPTTRTSTSHLSLPSSMTSTLTPASRSAS--TLQYTPTPSSVSHSPLLTTPTASPPSSAPTFVSPTAAST 2081
Cdd:PHA02732 1227 QLSAASSPPAATTPTPPPSSSSSSSAQSISTSpgQIQIVLNGSTTIHINFLFFPALSTPKIGQILAMPIVNSS 1299
|
|
| PRK10856 |
PRK10856 |
cytoskeleton protein RodZ; |
2011-2105 |
9.59e-03 |
|
cytoskeleton protein RodZ;
Pssm-ID: 236776 [Multi-domain] Cd Length: 331 Bit Score: 40.78 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 2011 HSSFPTTRTSTSHLSLPSSMTSTLTPASRSASTLQYTPTPSSVSHSPLLTTPTASPPSSAPTFVSPTAASTVISSALPTI 2090
Cdd:PRK10856 149 QSSAELSQNSGQSVPLDTSTTTDPATTPAPAAPVDTTPTNSQTPAVATAPAPAVDPQQNAVVAPSQANVDTAATPAPAAP 228
|
90
....*....|....*
gi 1907182200 2091 HMTPTPSSRPTSSTG 2105
Cdd:PRK10856 229 ATPDGAAPLPTDQAG 243
|
|
| Metaviral_G |
pfam09595 |
Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. ... |
1971-2113 |
9.65e-03 |
|
Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. It is high in serine and threonine suggesting it is highly glycosylated.
Pssm-ID: 462833 [Multi-domain] Cd Length: 183 Bit Score: 39.55 E-value: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182200 1971 VSSASTSRPLSTSLPT-TIKGTGTPQTPVSDINTTS-ATTQAHSSFPTTRTSTSHLSLPSSMTSTLTPASRSASTLQYT- 2047
Cdd:pfam09595 22 QARSKCFEHASLILIGeSNKEAALIITDIIDININKqHPEQEHHENPPLNEAAKEAPSESEDAPDIDPNNQHPSQDRSEa 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907182200 2048 -PTPSSVSHSPLLTTPtASPPSSAPTFVSPTAASTVISSA----LPTIHMTPTPSSRPTSSTGLLSTSKTT 2113
Cdd:pfam09595 102 pPLEPAAKTKPSEHEP-ANPPDASNRLSPPDASTAAIREArtfrKPSTGKRNNPSSAQSDQSPPRANHEAI 171
|
|
| |
