|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
84-340 |
4.90e-30 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 121.29 E-value: 4.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 84 SSGVIAGGGDNGMLILYNVThilssGKEPVIAQKQkHTGAVRALDFNPFqvlqGNLLASGASDSEVFIWDLNNLNVPMTL 163
Cdd:cd00200 20 DGKLLATGSGDGTIKVWDLE-----TGELLRTLKG-HTGPVRDVAASAD----GTYLASGSSDKTIRLWDLETGECVRTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 164 GSKSQYseqppedVKALSWNrQAQHILSSAHPSGKAVVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDiaTQLVLCSEDDR 243
Cdd:cd00200 90 TGHTSY-------VSSVAFS-PDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNS--VAFSPD--GTFVASSSQDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 244 LpvIQLWDLRfASSPLKVLESHSRGILSVSWSqADAELLLTSAKDSQILCLNLESSEVVYKLPTQSSWCFEVQWCPrDPS 323
Cdd:cd00200 158 T--IKLWDLR-TGKCVATLTGHTGEVNSVAFS-PDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP-DGY 232
|
250
....*....|....*..
gi 1622966959 324 VFSAASFDGWISLYSVM 340
Cdd:cd00200 233 LLASGSEDGTIRVWDLR 249
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
6-339 |
1.54e-26 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 113.47 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 6 LERPAVQAWSPASQYPLYLATGTSAQQLDSSFSTNGTLEIFEVDFRDPSLDLKHKGVLSASSRFHklIWGSFGSGLLESS 85
Cdd:COG2319 13 SADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGH--TAAVLSVAFSPDG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 86 GVIAGGGDNGMLILYNVthilSSGKEPviAQKQKHTGAVRALDFNPfqvlQGNLLASGASDSEVFIWDLNNLNVPMTLgs 165
Cdd:COG2319 91 RLLASASADGTVRLWDL----ATGLLL--RTLTGHTGAVRSVAFSP----DGKTLASGSADGTVRLWDLATGKLLRTL-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 166 ksqysEQPPEDVKALSWNRQAQhILSSAHPSGKAVVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDiATQLVLCSEDDRlp 245
Cdd:COG2319 159 -----TGHSGAVTSVAFSPDGK-LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRS--VAFSPD-GKLLASGSADGT-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 246 vIQLWDLRfASSPLKVLESHSRGILSVSWSqADAELLLTSAKDSQILCLNLESSEVVYKLPTQSSWCFEVQWCPrDPSVF 325
Cdd:COG2319 228 -VRLWDLA-TGKLLRTLTGHSGSVRSVAFS-PDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSP-DGKLL 303
|
330
....*....|....
gi 1622966959 326 SAASFDGWISLYSV 339
Cdd:COG2319 304 ASGSDDGTVRLWDL 317
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
775-1082 |
1.51e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 59.57 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 775 PPVQQLRDRLFHAQGSAVLGQQSPPFPYPRIVVGAIPHSKETSyRLGSQPSHQVPTPSPRPRVFTPQSSPAMPLAPSHPS 854
Cdd:PHA03247 2626 PPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRAR-RLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPP 2704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 855 PYQgprmqnisdyrasgsqaiqPLPLGPGVRPASSQPQLLGGQRVQAPNPVGFPGTWPLPGSLLLMACPdiTQPGSTSLS 934
Cdd:PHA03247 2705 PPT-------------------PEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGP--ARPARPPTT 2763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 935 ETPRlfpllplrppgpshmvshAPAPPVSFLVPYPPGGPVAPCSSVLPTTGILTPHPGPQDSWKEAPAPGGNLQRNKLPE 1014
Cdd:PHA03247 2764 AGPP------------------APAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPA 2825
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622966959 1015 TFMAPAPITAPVMSLTPE--LQGILPLQ---PPVSGVSHAPPGAPGELSLQQLQHLPPEKMERKELPPEHQSL 1082
Cdd:PHA03247 2826 GPLPPPTSAQPTAPPPPPgpPPPSLPLGgsvAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESF 2898
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
829-1067 |
8.87e-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: 56.70 E-value: 8.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 829 PTPSPRPRVFTPQSSPAMPLAPSHPSPYQGPR--MQNISDYRA----SGSQAIQPLPLGPgvRPASSQPQLLGGQRVQAP 902
Cdd:pfam03154 197 AGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHtlIQQTPTLHPqrlpSPHPPLQPMTQPP--PPSQVSPQPLPQPSLHGQ 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 903 NPvgfPGTWPLPGSLLLMACPDITQP-GSTSLSETPRLFPLLPLRPPGPSHMVSHAPAPPVSFLVPYPPGgpvapcSSVL 981
Cdd:pfam03154 275 MP---PMPHSLQTGPSHMQHPVPPQPfPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPR------EQPL 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 982 PTTGILTPH--PGPQDSWKEAPAPggnlQRNKLPETFMAPAPITAPVmSLTPElqgilPLQPPVSGVS-HAPPGA-PGEL 1057
Cdd:pfam03154 346 PPAPLSMPHikPPPTTPIPQLPNP----QSHKHPPHLSGPSPFQMNS-NLPPP-----PALKPLSSLStHHPPSAhPPPL 415
|
250
....*....|.
gi 1622966959 1058 SLQ-QLQHLPP 1067
Cdd:pfam03154 416 QLMpQSQQLPP 426
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
120-153 |
7.71e-05 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 41.14 E-value: 7.71e-05
10 20 30
....*....|....*....|....*....|....
gi 1622966959 120 HTGAVRALDFNPfqvlQGNLLASGASDSEVFIWD 153
Cdd:smart00320 11 HTGPVTSVAFSP----DGKYLASGSDDGTIKLWD 40
|
|
| ACE1-Sec16-like |
cd09233 |
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ... |
575-695 |
1.43e-04 |
|
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat complex plays an important role in vesicular traffic of newly synthezised proteins from the endoplasmatic reticulum (ER) to the Golgi apparatus by mediating the formation of transport vesicles. COPII consists of an outer coat, made up of the scaffold proteins Sec31 and Sec13, and the cargo adaptor complex, Sec23 and Sec24, which are recruited by the small GTPase Sar1. Sec16 is involved in the early steps of the assembly process. Sec16 forms elongated heterotetramers with Sec13, Sec13-(Sec16)2-Sec13. It interacts with Sec13 by insertion of a single beta-blade to close the six-bladded beta propeller of Sec13. In the same way Sec13 interacts with Sec31 and Nup145C, a nuclear pore protein, all of these contain a structurally related ancestral coatomer element 1 (ACE1). Sec16 is believed to be a key component in maintaining the integrity of the ER exit site.
Pssm-ID: 187750 [Multi-domain] Cd Length: 314 Bit Score: 45.33 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 575 LLLGELGPAVELYLKEERFADAIILAQAGGADLLKQTQERYlAKKKTKISSLLACVVQ---KNWKDVVCTCS-------- 643
Cdd:cd09233 73 LLTGNRKEALELALDNGLWAHALLLASSLGKETWAEVVSRF-ARSESKLNDPLQTLYQlfsGNSPEAITELAdnpaeaew 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622966959 644 -LKNWREALALLLTYSSTEKfpelcDM-----LGTRMEQEGgraLTSEARLCYVCSGS 695
Cdd:cd09233 152 aLGNWREHLAIILSNRTSNL-----DLealveLGDLLAQRG---LVEAAHICYLLAGV 201
|
|
| PTZ00420 |
PTZ00420 |
coronin; Provisional |
80-208 |
4.56e-04 |
|
coronin; Provisional
Pssm-ID: 240412 [Multi-domain] Cd Length: 568 Bit Score: 44.17 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 80 GLLESSGVIA------GGGDNGMLILYNVTHilssgKEPVIAQKqKHTGAVRALDFNPfqvLQGNLLASGASDSEVFIWD 153
Cdd:PTZ00420 33 GIACSSGFVAvpweveGGGLIGAIRLENQMR-----KPPVIKLK-GHTSSILDLQFNP---CFSEILASGSEDLTIRVWE 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622966959 154 L--NNLNV-----PMTL--GSKSQyseqppedVKALSWNRQAQHILSSAHPSGKAVVWDLrKNE 208
Cdd:PTZ00420 104 IphNDESVkeikdPQCIlkGHKKK--------ISIIDWNPMNYYIMCSSGFDSFVNIWDI-ENE 158
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
120-153 |
5.53e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.48 E-value: 5.53e-04
10 20 30
....*....|....*....|....*....|....
gi 1622966959 120 HTGAVRALDFNPfqvlQGNLLASGASDSEVFIWD 153
Cdd:pfam00400 10 HTGSVTSLAFSP----DGKLLASGSDDGTVKVWD 39
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
84-340 |
4.90e-30 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 121.29 E-value: 4.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 84 SSGVIAGGGDNGMLILYNVThilssGKEPVIAQKQkHTGAVRALDFNPFqvlqGNLLASGASDSEVFIWDLNNLNVPMTL 163
Cdd:cd00200 20 DGKLLATGSGDGTIKVWDLE-----TGELLRTLKG-HTGPVRDVAASAD----GTYLASGSSDKTIRLWDLETGECVRTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 164 GSKSQYseqppedVKALSWNrQAQHILSSAHPSGKAVVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDiaTQLVLCSEDDR 243
Cdd:cd00200 90 TGHTSY-------VSSVAFS-PDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNS--VAFSPD--GTFVASSSQDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 244 LpvIQLWDLRfASSPLKVLESHSRGILSVSWSqADAELLLTSAKDSQILCLNLESSEVVYKLPTQSSWCFEVQWCPrDPS 323
Cdd:cd00200 158 T--IKLWDLR-TGKCVATLTGHTGEVNSVAFS-PDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP-DGY 232
|
250
....*....|....*..
gi 1622966959 324 VFSAASFDGWISLYSVM 340
Cdd:cd00200 233 LLASGSEDGTIRVWDLR 249
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
13-338 |
6.58e-30 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 120.90 E-value: 6.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 13 AWSPASQYplyLATGtsaqqldssfSTNGTLEIFEVDFRDPSLDLK-HKGVLSassrfhKLIWGSFGSgllessgVIAGG 91
Cdd:cd00200 16 AFSPDGKL---LATG----------SGDGTIKVWDLETGELLRTLKgHTGPVR------DVAASADGT-------YLASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 92 GDNGMLILYNVthilsSGKEPVIAQKQkHTGAVRALDFNPfqvlQGNLLASGASDSEVFIWDLNNLNVPMTLGSKSQyse 171
Cdd:cd00200 70 SSDKTIRLWDL-----ETGECVRTLTG-HTSYVSSVAFSP----DGRILSSSSRDKTIKVWDVETGKCLTTLRGHTD--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 172 qppeDVKALSWNrQAQHILSSAHPSGKAVVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDiATQLVLCSEDDrlpVIQLWD 251
Cdd:cd00200 137 ----WVNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKLWD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 252 LRfASSPLKVLESHSRGILSVSWSQaDAELLLTSAKDSQILCLNLESSEVVYKLPTQSSWCFEVQWCPRDPSVFSaASFD 331
Cdd:cd00200 206 LS-TGKCLGTLRGHENGVNSVAFSP-DGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GSAD 282
|
....*..
gi 1622966959 332 GWISLYS 338
Cdd:cd00200 283 GTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
6-339 |
1.54e-26 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 113.47 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 6 LERPAVQAWSPASQYPLYLATGTSAQQLDSSFSTNGTLEIFEVDFRDPSLDLKHKGVLSASSRFHklIWGSFGSGLLESS 85
Cdd:COG2319 13 SADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGH--TAAVLSVAFSPDG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 86 GVIAGGGDNGMLILYNVthilSSGKEPviAQKQKHTGAVRALDFNPfqvlQGNLLASGASDSEVFIWDLNNLNVPMTLgs 165
Cdd:COG2319 91 RLLASASADGTVRLWDL----ATGLLL--RTLTGHTGAVRSVAFSP----DGKTLASGSADGTVRLWDLATGKLLRTL-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 166 ksqysEQPPEDVKALSWNRQAQhILSSAHPSGKAVVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDiATQLVLCSEDDRlp 245
Cdd:COG2319 159 -----TGHSGAVTSVAFSPDGK-LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRS--VAFSPD-GKLLASGSADGT-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 246 vIQLWDLRfASSPLKVLESHSRGILSVSWSqADAELLLTSAKDSQILCLNLESSEVVYKLPTQSSWCFEVQWCPrDPSVF 325
Cdd:COG2319 228 -VRLWDLA-TGKLLRTLTGHSGSVRSVAFS-PDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSP-DGKLL 303
|
330
....*....|....
gi 1622966959 326 SAASFDGWISLYSV 339
Cdd:COG2319 304 ASGSDDGTVRLWDL 317
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
88-339 |
2.06e-26 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 113.08 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 88 IAGGGDNGMLILYNVThilsSGKEpvIAQKQKHTGAVRALDFNPfqvlQGNLLASGASDSEVFIWDLNNLNVPMTLGSKS 167
Cdd:COG2319 177 LASGSDDGTVRLWDLA----TGKL--LRTLTGHTGAVRSVAFSP----DGKLLASGSADGTVRLWDLATGKLLRTLTGHS 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 168 QYseqppedVKALSWNRQAQHILsSAHPSGKAVVWDLRKNEPIIKVSDHSNRMHcsGLAWHPDiATQLVLCSEDDRlpvI 247
Cdd:COG2319 247 GS-------VRSVAFSPDGRLLA-SGSADGTVRLWDLATGELLRTLTGHSGGVN--SVAFSPD-GKLLASGSDDGT---V 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 248 QLWDLRfASSPLKVLESHSRGILSVSWSqADAELLLTSAKDSQILCLNLESSEVVYKLPTQSSWCFEVQWCPrDPSVFSA 327
Cdd:COG2319 313 RLWDLA-TGKLLRTLTGHTGAVRSVAFS-PDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSP-DGRTLAS 389
|
250
....*....|..
gi 1622966959 328 ASFDGWISLYSV 339
Cdd:COG2319 390 GSADGTVRLWDL 401
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
88-339 |
6.58e-25 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 108.85 E-value: 6.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 88 IAGGGDNGMLILYNvthiLSSGKEpvIAQKQKHTGAVRALDFNPfqvlQGNLLASGASDSEVFIWDLNNLNVPMTLgsks 167
Cdd:COG2319 135 LASGSADGTVRLWD----LATGKL--LRTLTGHSGAVTSVAFSP----DGKLLASGSDDGTVRLWDLATGKLLRTL---- 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 168 qysEQPPEDVKALSWNRQAQhILSSAHPSGKAVVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDiATQLVLCSEDDRlpvI 247
Cdd:COG2319 201 ---TGHTGAVRSVAFSPDGK-LLASGSADGTVRLWDLATGKLLRTLTGHSGSVRS--VAFSPD-GRLLASGSADGT---V 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 248 QLWDLRfASSPLKVLESHSRGILSVSWSqADAELLLTSAKDSQILCLNLESSEVVYKLPTQSSWCFEVQWCPRDPSVFSa 327
Cdd:COG2319 271 RLWDLA-TGELLRTLTGHSGGVNSVAFS-PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLAS- 347
|
250
....*....|..
gi 1622966959 328 ASFDGWISLYSV 339
Cdd:COG2319 348 GSDDGTVRLWDL 359
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
775-1082 |
1.51e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 59.57 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 775 PPVQQLRDRLFHAQGSAVLGQQSPPFPYPRIVVGAIPHSKETSyRLGSQPSHQVPTPSPRPRVFTPQSSPAMPLAPSHPS 854
Cdd:PHA03247 2626 PPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRAR-RLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPP 2704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 855 PYQgprmqnisdyrasgsqaiqPLPLGPGVRPASSQPQLLGGQRVQAPNPVGFPGTWPLPGSLLLMACPdiTQPGSTSLS 934
Cdd:PHA03247 2705 PPT-------------------PEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGP--ARPARPPTT 2763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 935 ETPRlfpllplrppgpshmvshAPAPPVSFLVPYPPGGPVAPCSSVLPTTGILTPHPGPQDSWKEAPAPGGNLQRNKLPE 1014
Cdd:PHA03247 2764 AGPP------------------APAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPA 2825
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622966959 1015 TFMAPAPITAPVMSLTPE--LQGILPLQ---PPVSGVSHAPPGAPGELSLQQLQHLPPEKMERKELPPEHQSL 1082
Cdd:PHA03247 2826 GPLPPPTSAQPTAPPPPPgpPPPSLPLGgsvAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESF 2898
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
829-1067 |
8.87e-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: 56.70 E-value: 8.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 829 PTPSPRPRVFTPQSSPAMPLAPSHPSPYQGPR--MQNISDYRA----SGSQAIQPLPLGPgvRPASSQPQLLGGQRVQAP 902
Cdd:pfam03154 197 AGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHtlIQQTPTLHPqrlpSPHPPLQPMTQPP--PPSQVSPQPLPQPSLHGQ 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 903 NPvgfPGTWPLPGSLLLMACPDITQP-GSTSLSETPRLFPLLPLRPPGPSHMVSHAPAPPVSFLVPYPPGgpvapcSSVL 981
Cdd:pfam03154 275 MP---PMPHSLQTGPSHMQHPVPPQPfPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPR------EQPL 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 982 PTTGILTPH--PGPQDSWKEAPAPggnlQRNKLPETFMAPAPITAPVmSLTPElqgilPLQPPVSGVS-HAPPGA-PGEL 1057
Cdd:pfam03154 346 PPAPLSMPHikPPPTTPIPQLPNP----QSHKHPPHLSGPSPFQMNS-NLPPP-----PALKPLSSLStHHPPSAhPPPL 415
|
250
....*....|.
gi 1622966959 1058 SLQ-QLQHLPP 1067
Cdd:pfam03154 416 QLMpQSQQLPP 426
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
795-1077 |
9.14e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 56.87 E-value: 9.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 795 QQSPPFPYPRIVVGAiphsketsyrlgsqpshqvpTPSPRPRVFTPQSSPAMPLAPSHPSPYQGPrmqnisdyrasgsqA 874
Cdd:PHA03247 2704 PPPTPEPAPHALVSA--------------------TPLPPGPAAARQASPALPAAPAPPAVPAGP--------------A 2749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 875 IQPLPLGPGVRPASSQPqllggqrvQAPNPVGFPGTWPLPGslllmacpdITQPGSTSLSETPRLFPLLPLRPPGPSHMV 954
Cdd:PHA03247 2750 TPGGPARPARPPTTAGP--------PAPAPPAAPAAGPPRR---------LTRPAVASLSESRESLPSPWDPADPPAAVL 2812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 955 SHAPAPPVSflvpYPPGGPVAPCSSVLPTTGILTPHP-GPQDSWKEAPAPGGNLQRnKLPETFMAPAPIT---------- 1023
Cdd:PHA03247 2813 APAAALPPA----ASPAGPLPPPTSAQPTAPPPPPGPpPPSLPLGGSVAPGGDVRR-RPPSRSPAAKPAAparppvrrla 2887
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622966959 1024 APVMSLTPELQGILPLQP--PVSGVSHAPPGAPGELSLQQLQHLPPEKMERKELPP 1077
Cdd:PHA03247 2888 RPAVSRSTESFALPPDQPerPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPL 2943
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
824-1054 |
1.59e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 56.10 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 824 PSHQVPTPSPRPRVFTP--QSSPAMPLAPSHPSPYQGPRmqnisDYRASGSQAIQPLPLGPGVRPASSQPQllggQRVQA 901
Cdd:PHA03247 2564 PDRSVPPPRPAPRPSEPavTSRARRPDAPPQSARPRAPV-----DDRGDPRGPAPPSPLPPDTHAPDPPPP----SPSPA 2634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 902 PNPVGFPGTWPLPGSLLLMACPditQPGSTSLSETPRLFPLLPLRPPGPSHMVSHAPAPPVSFLVPY--PPGGPVAPCSS 979
Cdd:PHA03247 2635 ANEPDPHPPPTVPPPERPRDDP---APGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLadPPPPPPTPEPA 2711
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622966959 980 VLPTTGILTPHPGPQDSWKEAPAPggnlqrnklPETFMAPAPITAPVMSLTPELQGI--LPLQPPVSGVSHAPPGAP 1054
Cdd:PHA03247 2712 PHALVSATPLPPGPAAARQASPAL---------PAAPAPPAVPAGPATPGGPARPARppTTAGPPAPAPPAAPAAGP 2779
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
798-1055 |
3.29e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 54.94 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 798 PPFPYPRIVVGAIpHSKETSYRLGSQPSH-QVPT--PSPRPRVFTPQSSPAMPLAPSHPSPYQGPRmqniSDYRASGSQA 874
Cdd:PHA03247 2570 PPRPAPRPSEPAV-TSRARRPDAPPQSARpRAPVddRGDPRGPAPPSPLPPDTHAPDPPPPSPSPA----ANEPDPHPPP 2644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 875 IQPLPLGPGVRPASSQPQLLGGQRVQ--APNPVGFPGTW------PLPGSLLLMACPdiTQPGSTSLSETPRLFPLLPLR 946
Cdd:PHA03247 2645 TVPPPERPRDDPAPGRVSRPRRARRLgrAAQASSPPQRPrrraarPTVGSLTSLADP--PPPPPTPEPAPHALVSATPLP 2722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 947 PPGPSHMVShAPAPPVSFLVPYPPGGPVAPCSSVLP-----TTGILTPHP------GPQDSWKEAPAPGGNLQRNKLP-- 1013
Cdd:PHA03247 2723 PGPAAARQA-SPALPAAPAPPAVPAGPATPGGPARParpptTAGPPAPAPpaapaaGPPRRLTRPAVASLSESRESLPsp 2801
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1622966959 1014 -ETFMAPAPITAPVMSLTPELQGILPLQPPVSGVSHAPPGAPG 1055
Cdd:PHA03247 2802 wDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPG 2844
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
735-1099 |
4.41e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.48 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 735 PHGVSPGPATTYRVTQYANLLAAQGSLATAMSfLPHDCAQPPVqqlrdrlfhAQGSAVLGQQSPPfpyPRIVVGAIPHSK 814
Cdd:PHA03247 2703 PPPPTPEPAPHALVSATPLPPGPAAARQASPA-LPAAPAPPAV---------PAGPATPGGPARP---ARPPTTAGPPAP 2769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 815 ETSYRLGSQPSHQVPTPSPRPRVFTPQSSPAMPLAPSHPSPYQGPRMQNISDYRASGSQA--IQPLPLGPGVRPASSQPQ 892
Cdd:PHA03247 2770 APPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPppTSAQPTAPPPPPGPPPPS 2849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 893 L-LGG---------QRVQAPNPVGFPGTWPLPgSLLLMACPDITQPGSTSLSETPRLFPLLPLRPPGPSHMVSHAPAPPV 962
Cdd:PHA03247 2850 LpLGGsvapggdvrRRPPSRSPAAKPAAPARP-PVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ 2928
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 963 SFLVPYPPGGPVAPCSSVLPTTGILTPHPGPQDSWKEAPAPGG-NLQRNKLPEtfmaPAPITAPVMSLTPELQGIlplqp 1041
Cdd:PHA03247 2929 PQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRvAVPRFRVPQ----PAPSREAPASSTPPLTGH----- 2999
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622966959 1042 PVSGVS--------HAPPgAPGELSLQQLQHLPPEKmerkelppEHQSLKSSFEALLQRCSLSATD 1099
Cdd:PHA03247 3000 SLSRVSswasslalHEET-DPPPVSLKQTLWPPDDT--------EDSDADSLFDSDSERSDLEALD 3056
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
732-1080 |
1.95e-05 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 49.00 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 732 LRGPHGVSPGPATTYRVTQYANLLAAQGSLATAMSFLPHDCAQPPVQQLRDRLFHA--QGSAVLGQQSPPFPYPRIV-VG 808
Cdd:pfam03154 174 LQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTliQQTPTLHPQRLPSPHPPLQpMT 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 809 AIPHSKETSYRLGSQPSHQVPTP-----------------SPRPRVFTPQSSPA-MPLAPSHPSPYQGPRMQNISDYRAS 870
Cdd:pfam03154 254 QPPPPSQVSPQPLPQPSLHGQMPpmphslqtgpshmqhpvPPQPFPLTPQSSQSqVPPGPSPAAPGQSQQRIHTPPSQSQ 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 871 GSQAI----QPLPLGPGVRP------ASSQPQLLGGQ------RVQAPNPVGFPGTWPLPGSLLLMACPDITQPGST--- 931
Cdd:pfam03154 334 LQSQQppreQPLPPAPLSMPhikpppTTPIPQLPNPQshkhppHLSGPSPFQMNSNLPPPPALKPLSSLSTHHPPSAhpp 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 932 ------SLSETPRLFPLLPLRPPGPSHMVSHAPAPPVSFLVPYPPGGPVAPCSSVLPTTGILTPHPGPQDSwkeAPAPGG 1005
Cdd:pfam03154 414 plqlmpQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTS---TSSAMP 490
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622966959 1006 NLQrnklpetfmapapitaPVMSLTPELQGILPLQPPVSgvshAPPgapgelslQQLQHLPPEKMERKELPPEHQ 1080
Cdd:pfam03154 491 GIQ----------------PPSSASVSSSGPVPAAVSCP----LPP--------VQIKEEALDEAEEPESPPPPP 537
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
13-156 |
3.26e-05 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 47.60 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 13 AWSPASQYplyLATGtsaqqldssfSTNGTLEIFEVDFRDPSLDLKHKGVLSASSRFHkliwgsfgsgllESSGVIAGGG 92
Cdd:COG2319 295 AFSPDGKL---LASG----------SDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFS------------PDGKTLASGS 349
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622966959 93 DNGMLILYNvthiLSSGKEpvIAQKQKHTGAVRALDFNPfqvlQGNLLASGASDSEVFIWDLNN 156
Cdd:COG2319 350 DDGTVRLWD----LATGEL--LRTLTGHTGAVTSVAFSP----DGRTLASGSADGTVRLWDLAT 403
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
849-1082 |
3.97e-05 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 48.22 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 849 APSHPSPyqgprMQNISDYRASGSQAI---QPLPLgPGVRPASSQPQLLGGQRVQAPNPVGFPGTWPLPGSlllmACPDI 925
Cdd:pfam03154 145 SPSIPSP-----QDNESDSDSSAQQQIlqtQPPVL-QAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQ----GSPAT 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 926 TQPGSTSLSetprlfpllplrppgpshmvshaPAPPVSFLVPYPPGGPVAPCSSVLPTTGILTPHPGPQDSWKEAPAPGG 1005
Cdd:pfam03154 215 SQPPNQTQS-----------------------TAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSL 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 1006 NLQrnklpetfMAPAPitAPVMSLTPELQGILPLQP----PVSGVSHAPPGAPGELS--LQQLQHLPPEKME-RKELPPE 1078
Cdd:pfam03154 272 HGQ--------MPPMP--HSLQTGPSHMQHPVPPQPfpltPQSSQSQVPPGPSPAAPgqSQQRIHTPPSQSQlQSQQPPR 341
|
....
gi 1622966959 1079 HQSL 1082
Cdd:pfam03154 342 EQPL 345
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
258-341 |
4.21e-05 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 46.94 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 258 PLKVLESHSRGILSVSWSqADAELLLTSAKDSQILCLNLESSEVVYKLPTQSSWCFEVQWCPRDPSVFSaASFDGWISLY 337
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFS-PDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLAS-GSSDKTIRLW 78
|
....
gi 1622966959 338 SVMG 341
Cdd:cd00200 79 DLET 82
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
120-153 |
7.71e-05 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 41.14 E-value: 7.71e-05
10 20 30
....*....|....*....|....*....|....
gi 1622966959 120 HTGAVRALDFNPfqvlQGNLLASGASDSEVFIWD 153
Cdd:smart00320 11 HTGPVTSVAFSP----DGKYLASGSDDGTIKLWD 40
|
|
| ACE1-Sec16-like |
cd09233 |
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ... |
575-695 |
1.43e-04 |
|
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat complex plays an important role in vesicular traffic of newly synthezised proteins from the endoplasmatic reticulum (ER) to the Golgi apparatus by mediating the formation of transport vesicles. COPII consists of an outer coat, made up of the scaffold proteins Sec31 and Sec13, and the cargo adaptor complex, Sec23 and Sec24, which are recruited by the small GTPase Sar1. Sec16 is involved in the early steps of the assembly process. Sec16 forms elongated heterotetramers with Sec13, Sec13-(Sec16)2-Sec13. It interacts with Sec13 by insertion of a single beta-blade to close the six-bladded beta propeller of Sec13. In the same way Sec13 interacts with Sec31 and Nup145C, a nuclear pore protein, all of these contain a structurally related ancestral coatomer element 1 (ACE1). Sec16 is believed to be a key component in maintaining the integrity of the ER exit site.
Pssm-ID: 187750 [Multi-domain] Cd Length: 314 Bit Score: 45.33 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 575 LLLGELGPAVELYLKEERFADAIILAQAGGADLLKQTQERYlAKKKTKISSLLACVVQ---KNWKDVVCTCS-------- 643
Cdd:cd09233 73 LLTGNRKEALELALDNGLWAHALLLASSLGKETWAEVVSRF-ARSESKLNDPLQTLYQlfsGNSPEAITELAdnpaeaew 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622966959 644 -LKNWREALALLLTYSSTEKfpelcDM-----LGTRMEQEGgraLTSEARLCYVCSGS 695
Cdd:cd09233 152 aLGNWREHLAIILSNRTSNL-----DLealveLGDLLAQRG---LVEAAHICYLLAGV 201
|
|
| PTZ00420 |
PTZ00420 |
coronin; Provisional |
80-208 |
4.56e-04 |
|
coronin; Provisional
Pssm-ID: 240412 [Multi-domain] Cd Length: 568 Bit Score: 44.17 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 80 GLLESSGVIA------GGGDNGMLILYNVTHilssgKEPVIAQKqKHTGAVRALDFNPfqvLQGNLLASGASDSEVFIWD 153
Cdd:PTZ00420 33 GIACSSGFVAvpweveGGGLIGAIRLENQMR-----KPPVIKLK-GHTSSILDLQFNP---CFSEILASGSEDLTIRVWE 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622966959 154 L--NNLNV-----PMTL--GSKSQyseqppedVKALSWNRQAQHILSSAHPSGKAVVWDLrKNE 208
Cdd:PTZ00420 104 IphNDESVkeikdPQCIlkGHKKK--------ISIIDWNPMNYYIMCSSGFDSFVNIWDI-ENE 158
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
120-153 |
5.53e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.48 E-value: 5.53e-04
10 20 30
....*....|....*....|....*....|....
gi 1622966959 120 HTGAVRALDFNPfqvlQGNLLASGASDSEVFIWD 153
Cdd:pfam00400 10 HTGSVTSLAFSP----DGKLLASGSDDGTVKVWD 39
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
813-1114 |
3.76e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 41.59 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 813 SKETSYRLGSQPSH-QVPTPSPRPRVfTPQSSPAMPLAPSHPSPYQGPRMQNISDYRasgSQAIQPLPLGPGVRPASSQP 891
Cdd:PHA03378 579 SPTTSQLASSAPSYaQTPWPVPHPSQ-TPEPPTTQSHIPETSAPRQWPMPLRPIPMR---PLRMQPITFNVLVFPTPHQP 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 892 QllggqrvqAPNPVGFPGTWPLPGSLllMACPDITQPGSTSLSETPRLFPLLPLRPPGPSHMVSHAPA---PPVSFLVPY 968
Cdd:PHA03378 655 P--------QVEITPYKPTWTQIGHI--PYQPSPTGANTMLPIQWAPGTMQPPPRAPTPMRPPAAPPGraqRPAAATGRA 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 969 PPggPVAPCSSVLPTTGILTPHPGPQDSWKEAPAPGGNLQRNKLPE-TFMAPAPITAPVMsltpelqGILPLQPPVSGVS 1047
Cdd:PHA03378 725 RP--PAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAaAPGAPTPQPPPQA-------PPAPQQRPRGAPT 795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 1048 HAPP----GAPGELSLQQL--QHLPPEKMERKELPPEHQSLKSS--FEALLQRcsLSATDLVLALGAGVGIH------FF 1113
Cdd:PHA03378 796 PQPPpqagPTSMQLMPRAApgQQGPTKQILRQLLTGGVKRGRPSlkKPAALER--QAAAGPTPSPGSGTSDKivqapvFY 873
|
.
gi 1622966959 1114 P 1114
Cdd:PHA03378 874 P 874
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
796-1055 |
6.92e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 40.84 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 796 QSPPFPyprivvGAIPHSKETSYRLGSQPSHQVPTPS--PRPRVFTPQSSPAMPLAPsHPSPYQGPRMQNISDYRASGSQ 873
Cdd:PRK10263 342 QTPPVA------SVDVPPAQPTVAWQPVPGPQTGEPViaPAPEGYPQQSQYAQPAVQ-YNEPLQQPVQPQQPYYAPAAEQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 874 AIQPLPLGPGVRPASSQPQLlggqrVQAPNPVGFPGTWPLPGSLLLMACPDITQPGSTslsetprlfpllplrppgpshM 953
Cdd:PRK10263 415 PAQQPYYAPAPEQPAQQPYY-----APAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQT---------------------Y 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966959 954 VSHAPAPPvsflvPYPPGGPVAPCSSVLPTTGILTPHPG-PQDSWKEAPAPGGNLQRNKL-------PETFMAPAPITAP 1025
Cdd:PRK10263 469 QQPAAQEP-----LYQQPQPVEQQPVVEPEPVVEETKPArPPLYYFEEVEEKRAREREQLaawyqpiPEPVKEPEPIKSS 543
|
250 260 270
....*....|....*....|....*....|
gi 1622966959 1026 VMSLTPelqgilPLQPPVSGVSHAPPGAPG 1055
Cdd:PRK10263 544 LKAPSV------AAVPPVEAAAAVSPLASG 567
|
|
|