|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
13-332 |
3.14e-24 |
|
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: 104.34 E-value: 3.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 13 AWSPAQNhpiYLATGtsaqqldatfSTNASLEIFELD-------LSDPSLDMKSCATFSSSHRyhkliwgpykmdskgdv 85
Cdd:cd00200 16 AFSPDGK---LLATG----------SGDGTIKVWDLEtgellrtLKGHTGPVRDVAASADGTY----------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 86 sgvLIAGGENGNIILYDPSKiiaGDKEVVIAQndkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200 66 ---LASGSSDKTIRLWDLET---GECVRTLTG---HTSYVSSVA---FSPDgrILSSSSRDKTIKVWDVETGKCLTTLRG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 164 KTQPpedISCIAWNrQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDrlpVIQM 243
Cdd:cd00200 134 HTDW---VNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:cd00200 204 WDLS-TGKCLGTLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GS 280
|
....*....
gi 41349441 324 FDGRISVYS 332
Cdd:cd00200 281 ADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
89-333 |
4.73e-23 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 103.07 E-value: 4.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 89 LIAGGENGNIILYDpskiIAGDKEvvIAQNDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPp 168
Cdd:COG2319 177 LASGSDDGTVRLWD----LATGKL--LRTLTGHTGAVRSVAFS-PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGS- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 169 edISCIAWNRQVQHiLASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPDvATQMVLASEDDRlpvIQMWDLRf 248
Cdd:COG2319 249 --VRSVAFSPDGRL-LASGSADGTVRLWDLATGELLRTLTGHSGGVN--SVAFSPD-GKLLASGSDDGT---VRLWDLA- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 249 ASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRI 328
Cdd:COG2319 319 TGKLLRTLTGHTGAVRSVAFS-PDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTV 396
|
....*
gi 41349441 329 SVYSI 333
Cdd:COG2319 397 RLWDL 401
|
|
| ACE1-Sec16-like |
cd09233 |
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ... |
534-657 |
4.57e-09 |
|
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: 59.19 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 534 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKyFAKSQSKIT---RLITAVVMKNWKEIVESC---- 605
Cdd:cd09233 69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41349441 606 -----DLKNWREALAAVLTYAKPD-EFSALCDLlgtrleneGDSLLQTQ----ACLCYICAG 657
Cdd:cd09233 147 aeaewALGNWREHLAIILSNRTSNlDLEALVEL--------GDLLAQRGlveaAHICYLLAG 200
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
761-1059 |
5.49e-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: 57.47 E-value: 5.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 761 PKIPYEKQQLPKGRPGPVAgHHQMPRV--QTQQYYPHGENP-PPPGFimhGNVNPNAAGQLPTSPghmHTQVPPYPQPQP 837
Cdd:pfam03154 253 TQPPPPSQVSPQPLPQPSL-HGQMPPMphSLQTGPSHMQHPvPPQPF---PLTPQSSQSQVPPGP---SPAAPGQSQQRI 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 838 YQPAQPypfgtggSAMYRPQQPVAPPTSNAYPNTPYISSASSyTGQSQLYAAQ------HQASSPTSSPATSFPPPPS-- 909
Cdd:pfam03154 326 HTPPSQ-------SQLQSQQPPREQPLPPAPLSMPHIKPPPT-TPIPQLPNPQshkhppHLSGPSPFQMNSNLPPPPAlk 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 910 --SGASFQHGGPGAPP------SSSAYALPPGTTGTLPAASELPASQRTGPqngwnDPPALNRVPKKKKMPEN-FMP--P 978
Cdd:pfam03154 398 plSSLSTHHPPSAHPPplqlmpQSQQLPPPPAQPPVLTQSQSLPPPAASHP-----PTSGLHQVPSQSPFPQHpFVPggP 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 979 VPITSPIMNPLGDPQSQMLQQQPSAPvplSSQSSFPQPHLPGGQ--PFHGVQQPLGQTGMPPSFSKPNIEGAPGAPIGNT 1056
Cdd:pfam03154 473 PPITPPSGPPTSTSSAMPGIQPPSSA---SVSSSGPVPAAVSCPlpPVQIKEEALDEAEEPESPPPPPRSPSPEPTVVNT 549
|
...
gi 41349441 1057 FQH 1059
Cdd:pfam03154 550 PSH 552
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
712-1077 |
3.44e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 54.94 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 712 SQYANLLAAQGSIAAALAFLPDNTNQPNIMQLRDRlCRAQGEPVAGHESPKIPYekqqlPKGRPGPVAGHHQMPRVQTQQ 791
Cdd:PHA03247 2632 SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRR-ARRLGRAAQASSPPQRPR-----RRAARPTVGSLTSLADPPPPP 2705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 792 YYPHgenPPPPGFIMHGNVNPNAAGQLPTSPGHMHTQVPPYPQPQPYQPAQPYPFGT-----GGSAMYRPQQPVAPPTSN 866
Cdd:PHA03247 2706 PTPE---PAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARppttaGPPAPAPPAAPAAGPPRR 2782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 867 AYPntPYISSASSYTgqsqlyAAQHQASSPTSSPATSFPPPPSSGASFQHGGPGAPPSSSAYALPPGTTGTLPAASELPA 946
Cdd:PHA03247 2783 LTR--PAVASLSESR------ESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGG 2854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 947 S-------QRTGPQNGWNDPPALNRVPKKKKMPENFMP------PVPITSPIMNPLGDPQSQMlQQQPSAPVPLSSQSSF 1013
Cdd:PHA03247 2855 SvapggdvRRRPPSRSPAAKPAAPARPPVRRLARPAVSrstesfALPPDQPERPPQPQAPPPP-QPQPQPPPPPQPQPPP 2933
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41349441 1014 PQPHLPGGqPFHGVQQPLGQTGMPPSFSKPNIEG-APGAPIGNTFQHVQSLPTKKITKKPIPDEH 1077
Cdd:PHA03247 2934 PPPPRPQP-PLAPTTDPAGAGEPSGAVPQPWLGAlVPGRVAVPRFRVPQPAPSREAPASSTPPLT 2997
|
|
| Sec16_C |
pfam12931 |
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal ... |
534-728 |
5.66e-07 |
|
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal region is the part that binds to Sec23, a COPII vesicle coat protein. This association is part of the transport vesicle coat structure.
Pssm-ID: 432884 Cd Length: 279 Bit Score: 52.56 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 534 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKY----FAKSQSKITRLItAVVMK----NWKEIVE- 603
Cdd:pfam12931 1 IRALLLTGDREKALWLAL-DKKLwAHALLIASTLGKEKWKEVVQEFvrseFKGSNNKSGESL-AALYQvfagNSEEAVDe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 604 --------SCDLKNWREALAAVLTYAKPDEFSALCDlLGTRLENEGdslLQTQACLCYICAG---NVEKLVACWTKAQDG 672
Cdd:pfam12931 79 lvppsknaLWALDNWRETLALVLSNRSPGDVEALLA-LGDLLAQYG---RTEAAHICFLLAGlplSQTVLLGADHVRFPS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 673 SHPLSLQDLI--EkvvILRKAVQLTqAMDTSTVGV--LLAAKMsQYANLLAAQGSIAAAL 728
Cdd:pfam12931 155 TFGNDLESILltE---IYEYALSLS-PPQPPFVGLphLLPYKL-QHAAVLAEYGLVSEAQ 209
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
203-333 |
7.31e-04 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 43.92 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 203 PIIKVSdhsNRMHCSGLAWHPDVATQMVLASEDDrlpVIQMWDLrfASSPLRV-LENHARGILAIAWSMADPELLLSCGK 281
Cdd:PLN00181 525 PVVELA---SRSKLSGICWNSYIKSQVASSNFEG---VVQVWDV--ARSQLVTeMKEHEKRVWSIDYSSADPTLLASGSD 596
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 41349441 282 DAKILCSNPNTGEVLYELPTNTQWCFdIQWCPRNPAVLSAASFDGRISVYSI 333
Cdd:PLN00181 597 DGSVKLWSINQGVSIGTIKTKANICC-VQFPSESGRSLAFGSADHKVYYYDL 647
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
13-332 |
3.14e-24 |
|
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: 104.34 E-value: 3.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 13 AWSPAQNhpiYLATGtsaqqldatfSTNASLEIFELD-------LSDPSLDMKSCATFSSSHRyhkliwgpykmdskgdv 85
Cdd:cd00200 16 AFSPDGK---LLATG----------SGDGTIKVWDLEtgellrtLKGHTGPVRDVAASADGTY----------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 86 sgvLIAGGENGNIILYDPSKiiaGDKEVVIAQndkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200 66 ---LASGSSDKTIRLWDLET---GECVRTLTG---HTSYVSSVA---FSPDgrILSSSSRDKTIKVWDVETGKCLTTLRG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 164 KTQPpedISCIAWNrQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDrlpVIQM 243
Cdd:cd00200 134 HTDW---VNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:cd00200 204 WDLS-TGKCLGTLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GS 280
|
....*....
gi 41349441 324 FDGRISVYS 332
Cdd:cd00200 281 ADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
121-340 |
1.84e-23 |
|
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: 102.03 E-value: 1.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 121 HTGPVRALDVNIfQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPPEDISCIAWNRQV-------------------- 180
Cdd:cd00200 8 HTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLasgssdktirlwdletgecv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 181 ------------------QHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvaTQMVLASEDDRLpvIQ 242
Cdd:cd00200 87 rtltghtsyvssvafspdGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNS--VAFSPD--GTFVASSSQDGT--IK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 243 MWDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPrNPAVLSAA 322
Cdd:cd00200 161 LWDLR-TGKCVATLTGHTGEVNSVAFS-PDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP-DGYLLASG 237
|
250
....*....|....*...
gi 41349441 323 SFDGRISVYSIMGGSTDG 340
Cdd:cd00200 238 SEDGTIRVWDLRTGECVQ 255
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
89-333 |
4.73e-23 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 103.07 E-value: 4.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 89 LIAGGENGNIILYDpskiIAGDKEvvIAQNDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPp 168
Cdd:COG2319 177 LASGSDDGTVRLWD----LATGKL--LRTLTGHTGAVRSVAFS-PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGS- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 169 edISCIAWNRQVQHiLASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPDvATQMVLASEDDRlpvIQMWDLRf 248
Cdd:COG2319 249 --VRSVAFSPDGRL-LASGSADGTVRLWDLATGELLRTLTGHSGGVN--SVAFSPD-GKLLASGSDDGT---VRLWDLA- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 249 ASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRI 328
Cdd:COG2319 319 TGKLLRTLTGHTGAVRSVAFS-PDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTV 396
|
....*
gi 41349441 329 SVYSI 333
Cdd:COG2319 397 RLWDL 401
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
89-333 |
1.54e-21 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 98.44 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 89 LIAGGENGNIILYDpskiIAGDKEVVIAQNdkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGAKTQ 166
Cdd:COG2319 135 LASGSADGTVRLWD----LATGKLLRTLTG--HSGAVTSVA---FSPDgkLLASGSDDGTVRLWDLATGKLLRTLTGHTG 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 167 PpedISCIAWNRQvQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDRlpvIQMWDL 246
Cdd:COG2319 206 A---VRSVAFSPD-GKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRS--VAFSPD-GRLLASGSADGT---VRLWDL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 247 RfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDG 326
Cdd:COG2319 276 A-TGELLRTLTGHSGGVNSVAFS-PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLAS-GSDDG 352
|
....*..
gi 41349441 327 RISVYSI 333
Cdd:COG2319 353 TVRLWDL 359
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
121-336 |
2.01e-19 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 92.28 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 121 HTGPVRALDVNiFQTNLVASGANESEIYIWDLnnfATPMTPGAKTQPPEDISCIAWNRQvQHILASASPSGRATVWDLRK 200
Cdd:COG2319 77 HTAAVLSVAFS-PDGRLLASASADGTVRLWDL---ATGLLLRTLTGHTGAVRSVAFSPD-GKTLASGSADGTVRLWDLAT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 201 NEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDRlpvIQMWDLRfASSPLRVLENHARGILAIAWSmADPELLLSCG 280
Cdd:COG2319 152 GKLLRTLTGHSGAVTS--VAFSPD-GKLLASGSDDGT---VRLWDLA-TGKLLRTLTGHTGAVRSVAFS-PDGKLLASGS 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 41349441 281 KDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPrNPAVLSAASFDGRISVYSIMGG 336
Cdd:COG2319 224 ADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVRLWDLATG 278
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
89-247 |
3.33e-09 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 60.31 E-value: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 89 LIAGGENGNIILYDpskiIAGDKEVVIAQNdkHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTqpp 168
Cdd:COG2319 261 LASGSADGTVRLWD----LATGELLRTLTG--HSGGVNSVAFS-PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHT--- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 169 EDISCIAWNRQVQhILASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPD---VATqmvlASEDDRlpvIQMWD 245
Cdd:COG2319 331 GAVRSVAFSPDGK-TLASGSDDGTVRLWDLATGELLRTLTGHTGAVT--SVAFSPDgrtLAS----GSADGT---VRLWD 400
|
..
gi 41349441 246 LR 247
Cdd:COG2319 401 LA 402
|
|
| ACE1-Sec16-like |
cd09233 |
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ... |
534-657 |
4.57e-09 |
|
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: 59.19 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 534 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKyFAKSQSKIT---RLITAVVMKNWKEIVESC---- 605
Cdd:cd09233 69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41349441 606 -----DLKNWREALAAVLTYAKPD-EFSALCDLlgtrleneGDSLLQTQ----ACLCYICAG 657
Cdd:cd09233 147 aeaewALGNWREHLAIILSNRTSNlDLEALVEL--------GDLLAQRGlveaAHICYLLAG 200
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
761-1059 |
5.49e-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: 57.47 E-value: 5.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 761 PKIPYEKQQLPKGRPGPVAgHHQMPRV--QTQQYYPHGENP-PPPGFimhGNVNPNAAGQLPTSPghmHTQVPPYPQPQP 837
Cdd:pfam03154 253 TQPPPPSQVSPQPLPQPSL-HGQMPPMphSLQTGPSHMQHPvPPQPF---PLTPQSSQSQVPPGP---SPAAPGQSQQRI 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 838 YQPAQPypfgtggSAMYRPQQPVAPPTSNAYPNTPYISSASSyTGQSQLYAAQ------HQASSPTSSPATSFPPPPS-- 909
Cdd:pfam03154 326 HTPPSQ-------SQLQSQQPPREQPLPPAPLSMPHIKPPPT-TPIPQLPNPQshkhppHLSGPSPFQMNSNLPPPPAlk 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 910 --SGASFQHGGPGAPP------SSSAYALPPGTTGTLPAASELPASQRTGPqngwnDPPALNRVPKKKKMPEN-FMP--P 978
Cdd:pfam03154 398 plSSLSTHHPPSAHPPplqlmpQSQQLPPPPAQPPVLTQSQSLPPPAASHP-----PTSGLHQVPSQSPFPQHpFVPggP 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 979 VPITSPIMNPLGDPQSQMLQQQPSAPvplSSQSSFPQPHLPGGQ--PFHGVQQPLGQTGMPPSFSKPNIEGAPGAPIGNT 1056
Cdd:pfam03154 473 PPITPPSGPPTSTSSAMPGIQPPSSA---SVSSSGPVPAAVSCPlpPVQIKEEALDEAEEPESPPPPPRSPSPEPTVVNT 549
|
...
gi 41349441 1057 FQH 1059
Cdd:pfam03154 550 PSH 552
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
864-1077 |
2.32e-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: 55.16 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 864 TSNAYPNTPYISSASSYTGQSQlyaaQHQASSPTSSPATSFPPPPSSGASFQHGGPGAPPSSSAYALPPGTTgtlPAASE 943
Cdd:pfam03154 144 TSPSIPSPQDNESDSDSSAQQQ----ILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGS---PATSQ 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 944 LPASQRT--GPQNGWNDPPALN--RVPK--------KKKMPENFMPPVPITSPIMNPLGDPQSQMLQQQPS--------A 1003
Cdd:pfam03154 217 PPNQTQStaAPHTLIQQTPTLHpqRLPSphpplqpmTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPShmqhpvppQ 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 1004 PVPLSSQSS------FPQPHLPgGQPFHGVQQPLGQTgMPPSFSKPNIEGAPGAPIgnTFQHVQSLPTKKITKKPIPDEH 1077
Cdd:pfam03154 297 PFPLTPQSSqsqvppGPSPAAP-GQSQQRIHTPPSQS-QLQSQQPPREQPLPPAPL--SMPHIKPPPTTPIPQLPNPQSH 372
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
712-1077 |
3.44e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 54.94 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 712 SQYANLLAAQGSIAAALAFLPDNTNQPNIMQLRDRlCRAQGEPVAGHESPKIPYekqqlPKGRPGPVAGHHQMPRVQTQQ 791
Cdd:PHA03247 2632 SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRR-ARRLGRAAQASSPPQRPR-----RRAARPTVGSLTSLADPPPPP 2705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 792 YYPHgenPPPPGFIMHGNVNPNAAGQLPTSPGHMHTQVPPYPQPQPYQPAQPYPFGT-----GGSAMYRPQQPVAPPTSN 866
Cdd:PHA03247 2706 PTPE---PAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARppttaGPPAPAPPAAPAAGPPRR 2782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 867 AYPntPYISSASSYTgqsqlyAAQHQASSPTSSPATSFPPPPSSGASFQHGGPGAPPSSSAYALPPGTTGTLPAASELPA 946
Cdd:PHA03247 2783 LTR--PAVASLSESR------ESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGG 2854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 947 S-------QRTGPQNGWNDPPALNRVPKKKKMPENFMP------PVPITSPIMNPLGDPQSQMlQQQPSAPVPLSSQSSF 1013
Cdd:PHA03247 2855 SvapggdvRRRPPSRSPAAKPAAPARPPVRRLARPAVSrstesfALPPDQPERPPQPQAPPPP-QPQPQPPPPPQPQPPP 2933
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41349441 1014 PQPHLPGGqPFHGVQQPLGQTGMPPSFSKPNIEG-APGAPIGNTFQHVQSLPTKKITKKPIPDEH 1077
Cdd:PHA03247 2934 PPPPRPQP-PLAPTTDPAGAGEPSGAVPQPWLGAlVPGRVAVPRFRVPQPAPSREAPASSTPPLT 2997
|
|
| Sec16_C |
pfam12931 |
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal ... |
534-728 |
5.66e-07 |
|
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal region is the part that binds to Sec23, a COPII vesicle coat protein. This association is part of the transport vesicle coat structure.
Pssm-ID: 432884 Cd Length: 279 Bit Score: 52.56 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 534 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKY----FAKSQSKITRLItAVVMK----NWKEIVE- 603
Cdd:pfam12931 1 IRALLLTGDREKALWLAL-DKKLwAHALLIASTLGKEKWKEVVQEFvrseFKGSNNKSGESL-AALYQvfagNSEEAVDe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 604 --------SCDLKNWREALAAVLTYAKPDEFSALCDlLGTRLENEGdslLQTQACLCYICAG---NVEKLVACWTKAQDG 672
Cdd:pfam12931 79 lvppsknaLWALDNWRETLALVLSNRSPGDVEALLA-LGDLLAQYG---RTEAAHICFLLAGlplSQTVLLGADHVRFPS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 673 SHPLSLQDLI--EkvvILRKAVQLTqAMDTSTVGV--LLAAKMsQYANLLAAQGSIAAAL 728
Cdd:pfam12931 155 TFGNDLESILltE---IYEYALSLS-PPQPPFVGLphLLPYKL-QHAAVLAEYGLVSEAQ 209
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
252-336 |
3.59e-06 |
|
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: 50.03 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 252 PLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRISVY 331
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFS-PDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLAS-GSSDKTIRLW 78
|
....*
gi 41349441 332 SIMGG 336
Cdd:cd00200 79 DLETG 83
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
754-1064 |
2.38e-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: 48.61 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 754 PVAGHESPKIPYEKQQLPKgRPGPVAGHHQMPRVQTQQYYPHGENPPPPGFIMHGNVNPNAAGQLPTSPGHMHTQVPpyp 833
Cdd:pfam03154 201 PSAPSVPPQGSPATSQPPN-QTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMP--- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 834 qpqpyqpAQPYPFGTGGSAMyrpQQPVAPptsNAYPNTPyissassYTGQSQLYAAQHQASSPTSSPATSFPPPPSSGAS 913
Cdd:pfam03154 277 -------PMPHSLQTGPSHM---QHPVPP---QPFPLTP-------QSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQS 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 914 FQ--HGGPGAP-PSSSAYALPPGTTgtlpaaselPASQRTGPQNgwNDPPALNRVPKKKKMPENFMPPvpitsPIMNPLG 990
Cdd:pfam03154 337 QQppREQPLPPaPLSMPHIKPPPTT---------PIPQLPNPQS--HKHPPHLSGPSPFQMNSNLPPP-----PALKPLS 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 991 D-----------------PQSQMLQQQPSAPVPLSSQSSFPQP---HLPGGQPFHGVQQPLGQT-----GMPPSFSKPNI 1045
Cdd:pfam03154 401 SlsthhppsahppplqlmPQSQQLPPPPAQPPVLTQSQSLPPPaasHPPTSGLHQVPSQSPFPQhpfvpGGPPPITPPSG 480
|
330
....*....|....*....
gi 41349441 1046 EGAPGAPIGNTFQHVQSLP 1064
Cdd:pfam03154 481 PPTSTSSAMPGIQPPSSAS 499
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
776-1101 |
3.55e-05 |
|
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: 48.03 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 776 GPVAGHHQMPRVqTQQYYPHGENPPPPGfiMHGNVNPNAAGQLPTSPGHMHTQVPPYPQPQPYQPAQPYPFGTGgsamyR 855
Cdd:pfam17823 75 GTSAAHLNSTEV-TAEHTPHGTDLSEPA--TREGAADGAASRALAAAASSSPSSAAQSLPAAIAALPSEAFSAP-----R 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 856 PQQPVAPPTsnAYPNTPYISSASSYTGQSQLYAAQHQASSPTSSPATSFPPPPSSGASFQHGGPGAPPSSSAYAL--PPG 933
Cdd:pfam17823 147 AAACRANAS--AAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPARGISTAATATghPAA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 934 TTGTLPAASELPASQRTGPQNGWNDPPALNRVPKKKKMpenfmppVPITSPIMNpLGDPQSQMLQQQPSAPVPLSSQSSF 1013
Cdd:pfam17823 225 GTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGT-------VASAAGTIN-MGDPHARRLSPAKHMPSDTMARNPA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 1014 P--QPHLPGGQPFHGVQQPLGQTGMPPSFSKPNIEGAPGAPIGNTFQHVQSLPTKKI-TKKPIPDEHLILKTTFEDLIQr 1090
Cdd:pfam17823 297 ApmGAQAQGPIIQVSTDQPVHNTAGEPTPSPSNTTLEPNTPKSVASTNLAVVTTTKAqAKEPSASPVPVLHTSMIPEVE- 375
|
330
....*....|.
gi 41349441 1091 clssATDPQTK 1101
Cdd:pfam17823 376 ----ATSPTTQ 382
|
|
| Med15 |
pfam09606 |
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
711-1116 |
4.52e-05 |
|
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.
Pssm-ID: 312941 [Multi-domain] Cd Length: 732 Bit Score: 47.70 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 711 MSQYANLLAAQGSIAAALAflpdNTNQPNIMQLRDRLcrAQGEPVAGHESPKIPYEKQQLPKgRPGPVAGHHQMPRVQTQ 790
Cdd:pfam09606 117 PGTASNLLASLGRPQMPMG----GAGFPSQMSRVGRM--QPGGQAGGMMQPSSGQPGSGTPN-QMGPNGGPGQGQAGGMN 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 791 QyyphGENPPPpgfimhGNVNPNAAGQlPTSPGHMHTQVPPYPQPQPYQPAQPYPFGTGGSAMYRPQQPVAPptsnaypn 870
Cdd:pfam09606 190 G----GQQGPM------GGQMPPQMGV-PGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQ-------- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 871 TPYISSASSYTGQSQLYAAQHQASSPTSSPATSFPPPPSS-GASFQHGGPGAPPSSSAYALPP---GTTGTLPAASELPA 946
Cdd:pfam09606 251 QGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQpGAMPNVMSIGDQNNYQQQQTRQqqqQQGGNHPAAHQQQM 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 947 SQ------RTGPQNGWNDPPALNRV--------PKKKKMPENFMPPVPITSPIMNPLGDPQSQMLQQQPSAPVPLSSQSS 1012
Cdd:pfam09606 331 NQsvgqggQVVALGGLNHLETWNPGnfgglganPMQRGQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGPGSQ 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 1013 FPQPHLPGGQPF-HGVQQPLGQTGMPPSFSKPNIEGAPGAPIGNTFQHVQSLPTKKITKKPIPDEHLILKTTFEDLIQRC 1091
Cdd:pfam09606 411 PPQSHPGGMIPSpALIPSPSPQMSQQPAQQRTIGQDSPGGSLNTPGQSAVNSPLNPQEEQLYREKYRQLTKYIEPLKRMI 490
|
410 420
....*....|....*....|....*
gi 41349441 1092 LSSATDPQTKRKLDDASKRLEFLYD 1116
Cdd:pfam09606 491 AKMENDPGDIDKMNKMKRLLEILSN 515
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
855-1052 |
9.41e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.86 E-value: 9.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 855 RPQQPVAPPTSNAyPNTPYISSASSytgqsqlyAAQHQASSPTSSPATSFPPPPS-SGASFQHGGPGAPPsssayALPPG 933
Cdd:PHA03247 2585 RARRPDAPPQSAR-PRAPVDDRGDP--------RGPAPPSPLPPDTHAPDPPPPSpSPAANEPDPHPPPT-----VPPPE 2650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 934 TTGTLPAASELPASQRTGPQNGWNDPPALNRVPKKKKMPenfmPPV-PITSpimnpLGDPQSqmlQQQPSAPVPLSSQSS 1012
Cdd:PHA03247 2651 RPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAAR----PTVgSLTS-----LADPPP---PPPTPEPAPHALVSA 2718
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 41349441 1013 FPQPhlPGGQPFHGVQQPLGQTGMPPsfSKPNIEGAPGAP 1052
Cdd:PHA03247 2719 TPLP--PGPAAARQASPALPAAPAPP--AVPAGPATPGGP 2754
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
783-1077 |
2.01e-04 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 45.91 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 783 QMPRVQTQQYYPHGENPPPPGFIMHGNVNPNAAGQLPTSPGHMHTQVPPYPQPQPYQPAQPYPFGTG--GSAMYRPQQPV 860
Cdd:pfam03154 170 QPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTlhPQRLPSPHPPL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 861 APPTSNAYPNTPYISSASSYTGQSQLYAAQHQASSPTSSPATSFPPPPSSGASFQHGGPGAPPSSSAYALPPGTTGTLPA 940
Cdd:pfam03154 250 QPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPP 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 941 ASELPASQRtgPQNGWNDPPALNRVPKKKKMPENFMPPVPitspimnplgDPQSQMLQQQPSAPVPLSSQSSFPQPhlPG 1020
Cdd:pfam03154 330 SQSQLQSQQ--PPREQPLPPAPLSMPHIKPPPTTPIPQLP----------NPQSHKHPPHLSGPSPFQMNSNLPPP--PA 395
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41349441 1021 GQPFHGVqqplgQTGMPPSFSKP---------NIEGAPGAPIGNTfqHVQSLPTKKITKKPIPDEH 1077
Cdd:pfam03154 396 LKPLSSL-----STHHPPSAHPPplqlmpqsqQLPPPPAQPPVLT--QSQSLPPPAASHPPTSGLH 454
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
911-1146 |
2.32e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 45.46 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 911 GASFQHGGPGAPPSSSAYAlppgttgTLPAASELPASQR---TGPQNGWNDPPALNRV---PKKKKMPENFMPPV--PIT 982
Cdd:PRK10263 677 GEQYQHDVPVNAEDADAAA-------EAELARQFAQTQQqrySGEQPAGANPFSLDDFefsPMKALLDDGPHEPLftPIV 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 983 SPIMNPLGDPQSQMLQQQPSAPVPLSSQSSFPQPHLPGGQPFHGVQQPLGQtgmPPSFSKPNIEGAPGAPIGNTFQHVQS 1062
Cdd:PRK10263 750 EPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAP---QPQYQQPQQPVAPQPQYQQPQQPVAP 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 1063 LPTKKITKKPI---PDEHLILKTTFEDLIQRCLSSATDPQTKrklddaskrLEFLYDKLREqtLSPTITSGLHNIARSIE 1139
Cdd:PRK10263 827 QPQYQQPQQPVapqPQDTLLHPLLMRNGDSRPLHKPTTPLPS---------LDLLTPPPSE--VEPVDTFALEQMARLVE 895
|
250
....*....|....*...
gi 41349441 1140 TR-----------NYSEG 1146
Cdd:PRK10263 896 ARladfrikadvvNYSPG 913
|
|
| PRK14959 |
PRK14959 |
DNA polymerase III subunits gamma and tau; Provisional |
908-1021 |
4.42e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184923 [Multi-domain] Cd Length: 624 Bit Score: 44.29 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 908 PSSGASFQHGGPGAP-PSSSAYAL--PPGTTGTLPAAselPASQRTgPQNGWNDPPALNRVPkKKKMPENFMPPVPITSP 984
Cdd:PRK14959 373 PSGGGASAPSGSAAEgPASGGAATipTPGTQGPQGTA---PAAGMT-PSSAAPATPAPSAAP-SPRVPWDDAPPAPPRSG 447
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 41349441 985 IMnPLGDPQSQMLQQQPSAPVPLSSQS---------SFPQPHLPGG 1021
Cdd:PRK14959 448 IP-PRPAPRMPEASPVPGAPDSVASASdapptlgdpSDTAEHTPSG 492
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
203-333 |
7.31e-04 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 43.92 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 203 PIIKVSdhsNRMHCSGLAWHPDVATQMVLASEDDrlpVIQMWDLrfASSPLRV-LENHARGILAIAWSMADPELLLSCGK 281
Cdd:PLN00181 525 PVVELA---SRSKLSGICWNSYIKSQVASSNFEG---VVQVWDV--ARSQLVTeMKEHEKRVWSIDYSSADPTLLASGSD 596
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 41349441 282 DAKILCSNPNTGEVLYELPTNTQWCFdIQWCPRNPAVLSAASFDGRISVYSI 333
Cdd:PLN00181 597 DGSVKLWSINQGVSIGTIKTKANICC-VQFPSESGRSLAFGSADHKVYYYDL 647
|
|
| PHA02682 |
PHA02682 |
ORF080 virion core protein; Provisional |
856-1097 |
8.74e-04 |
|
ORF080 virion core protein; Provisional
Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 42.54 E-value: 8.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 856 PQQPvAPPTSNAYPNTPYISSASSYTGQSQLyAAQHQASSPTSSPATSFPPPPSSGASFQHGGPgAPPS--------SSA 927
Cdd:PHA02682 37 PAAP-CPPDADVDPLDKYSVKEAGRYYQSRL-KANSACMQRPSGQSPLAPSPACAAPAPACPAC-APAApapavtcpAPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 928 YALPPGTTGTLPAASELPASQRTGPQNgwndPPALNRVPKKkkmpenfmPPVPITSPImnplgdpqsqmlqqqPSAPvPL 1007
Cdd:PHA02682 114 PACPPATAPTCPPPAVCPAPARPAPAC----PPSTRQCPPA--------PPLPTPKPA---------------PAAK-PI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 1008 SSQSSFPQPHLPGGqpfhgvqqplgqtgmppsfSKPNIEGAPGApigntfqhvqslptKKITKKPIPDEHLILKTTFEDL 1087
Cdd:PHA02682 166 FLHNQLPPPDYPAA-------------------SCPTIETAPAA--------------SPVLEPRIPDKIIDADNDDKDL 212
|
250
....*....|
gi 41349441 1088 IQRCLSSATD 1097
Cdd:PHA02682 213 IKKELADIAD 222
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
749-966 |
1.59e-03 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 42.83 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 749 RAQGEPVAGHESPKIPYEKQQLPKG-------RPGPVAGHHQMPRVQTQQYYPHGENPPPpgFIMHGNVNPNAAGQlPTS 821
Cdd:pfam03154 324 RIHTPPSQSQLQSQQPPREQPLPPAplsmphiKPPPTTPIPQLPNPQSHKHPPHLSGPSP--FQMNSNLPPPPALK-PLS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 822 PGHMHTQVPPYPQPQPYQPAQPYPFGTGGSAMYRPQQPVAPPTSNAYPNTpyissASSYTGQSQLYAAQHQ--ASSPTSS 899
Cdd:pfam03154 401 SLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPT-----SGLHQVPSQSPFPQHPfvPGGPPPI 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41349441 900 PATSFPPPPSSGASFQHGGPGAPPSSSAYALPPGTTGTLPAA--SELPASQRTGPQNgwndPPALNRVP 966
Cdd:pfam03154 476 TPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVqiKEEALDEAEEPES----PPPPPRSP 540
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
855-1040 |
3.33e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.79 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 855 RPQQPVAPPTSNAYPNTPYISSASSYTGQSQLYAAQHQASSPTSSPATSFPPPPSSGASFQHGGPGAPPSSSAYALPPGT 934
Cdd:PRK12323 401 APPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAP 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 935 TGTLPAASELPASQRTGPqngWNDPPALNRVPKKKKMPENFMPPV--PITSPIMNPLGDPQSQMLQQQPSAPVPlsSQSS 1012
Cdd:PRK12323 481 ARAAPAAAPAPADDDPPP---WEELPPEFASPAPAQPDAAPAGWVaeSIPDPATADPDDAFETLAPAPAAAPAP--RAAA 555
|
170 180
....*....|....*....|....*...
gi 41349441 1013 FPQPHLPGGQPfhgvqqPLGQTGMPPSF 1040
Cdd:PRK12323 556 ATEPVVAPRPP------RASASGLPDMF 577
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
863-1074 |
8.58e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 40.45 E-value: 8.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 863 PTSNAYPNTPYISSASSYTGQSQLYAAQHQASSptsspatsfPPPPSSGASfqhggpgAPPSSSAYALPPGTTGTLPAAS 942
Cdd:PRK10263 309 PLLNGAPITEPVAVAAAATTATQSWAAPVEPVT---------QTPPVASVD-------VPPAQPTVAWQPVPGPQTGEPV 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 943 ELPASQRTGPQNGWNDPPALNRVPKKKkmpenfmpPVPITSPIMNPLGDPQSQMLQQQPSAPVPLSSQSSFPQPHLP-GG 1021
Cdd:PRK10263 373 IAPAPEGYPQQSQYAQPAVQYNEPLQQ--------PVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPvAG 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 41349441 1022 QPFHGVQQplGQTGMPPSFSKPniEGAPGAPIGNTFQHVQSLPTKK-ITKKPIP 1074
Cdd:PRK10263 445 NAWQAEEQ--QSTFAPQSTYQT--EQTYQQPAAQEPLYQQPQPVEQqPVVEPEP 494
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
775-1020 |
9.99e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 40.31 E-value: 9.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 775 PGPVAGHHQMPRVQTQQYYPhgenPPPPGFIMHGNVNPNAAGQLPTSPGH-MHTQVPPYPQPQPYQPAQPYPFGTGGSAM 853
Cdd:PHA03247 2723 PGPAAARQASPALPAAPAPP----AVPAGPATPGGPARPARPPTTAGPPApAPPAAPAAGPPRRLTRPAVASLSESRESL 2798
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 854 YRPQQPVAPPTSNAYPNTPYISSASSYTGQSQLYAAQhqaSSPTSSPATSFPPPPSSGASFQHGGPGA--PPSSSAYALP 931
Cdd:PHA03247 2799 PSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQ---PTAPPPPPGPPPPSLPLGGSVAPGGDVRrrPPSRSPAAKP 2875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349441 932 pgTTGTLPAASELPA---SQRTGPQNGWNDPPALNRVP----------------------KKKKMPENFMPPVPITSPIM 986
Cdd:PHA03247 2876 --AAPARPPVRRLARpavSRSTESFALPPDQPERPPQPqappppqpqpqpppppqpqpppPPPPRPQPPLAPTTDPAGAG 2953
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 41349441 987 NPLGD----------------PQSQMLQQQPSAPVPLSSQSSFPQPHLPG 1020
Cdd:PHA03247 2954 EPSGAvpqpwlgalvpgrvavPRFRVPQPAPSREAPASSTPPLTGHSLSR 3003
|
|
|