|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 super family |
cl29593 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
13-332 |
3.35e-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.
The actual alignment was detected with superfamily member cd00200:
Pssm-ID: 475233 [Multi-domain] Cd Length: 289 Bit Score: 104.34 E-value: 3.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 13 AWSPAQNhpiYLATGtsaqqldatfSTNASLEIFELD-------LSDPSLDMKSCATFSSSHRyhkliwgpykmdskgdv 85
Cdd:cd00200 16 AFSPDGK---LLATG----------SGDGTIKVWDLEtgellrtLKGHTGPVRDVAASADGTY----------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 86 sgvLIAGGENGNIILYDPSKiiaGDKEVVIAQndkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200 66 ---LASGSSDKTIRLWDLET---GECVRTLTG---HTSYVSSVA---FSPDgrILSSSSRDKTIKVWDVETGKCLTTLRG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 164 KTQPpedISCIAWNrQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDiATQMVLASEDDrlpVIQM 243
Cdd:cd00200 134 HTDW---VNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:cd00200 204 WDLS-TGKCLGTLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GS 280
|
....*....
gi 1622939744 324 FDGRISVYS 332
Cdd:cd00200 281 ADGTIRIWD 289
|
|
| ACE1-Sec16-like super family |
cl14807 |
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ... |
573-696 |
4.88e-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.
The actual alignment was detected with superfamily member cd09233:
Pssm-ID: 449359 [Multi-domain] Cd Length: 314 Bit Score: 59.19 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 573 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKyFAKSQSKIT---RLITAVVMKNWKEIVESC---- 644
Cdd:cd09233 69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622939744 645 -----DLKNWREALAAVLTYAKPD-EFSALCDLlgtrleneGDSLLQTQ----ACLCYICAG 696
Cdd:cd09233 147 aeaewALGNWREHLAIILSNRTSNlDLEALVEL--------GDLLAQRGlveaAHICYLLAG 200
|
|
| Atrophin-1 super family |
cl38111 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
776-1126 |
6.11e-09 |
|
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.
The actual alignment was detected with superfamily member pfam03154:
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 60.55 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 776 QPNIVQLRDRLCRAQGEPVAGHESPKIPYEKQQLPKGRPGPVGHHQMPRVQTQQYY-PHVRIAPTVTTWSNKTPT---AL 851
Cdd:pfam03154 170 QPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAaPHTLIQQTPTLHPQRLPSphpPL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 852 PSHPPAASPSDTQGENPPPPgfIMHGNVNPnAAGQLPTSPGHMHTQV-----PPYPQPQPYQPAQPYPFGTGGSAMYRPQ 926
Cdd:pfam03154 250 QPMTQPPPPSQVSPQPLPQP--SLHGQMPP-MPHSLQTGPSHMQHPVppqpfPLTPQSSQSQVPPGPSPAAPGQSQQRIH 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 927 QPVA--------PPTSNAYPNTPYIS---SASSYSGQSQLYAAQ------HQASSPTSSPATSFPPPPS----SGASFQH 985
Cdd:pfam03154 327 TPPSqsqlqsqqPPREQPLPPAPLSMphiKPPPTTPIPQLPNPQshkhppHLSGPSPFQMNSNLPPPPAlkplSSLSTHH 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 986 GGPGAPPS----------SSAYALPPGTTETHSVqdqapmlegPQNGWNDPP--ALNRVPKKKKTPEN-FMP--PVPITS 1050
Cdd:pfam03154 407 PPSAHPPPlqlmpqsqqlPPPPAQPPVLTQSQSL---------PPPAASHPPtsGLHQVPSQSPFPQHpFVPggPPPITP 477
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622939744 1051 PIMNPLGDPQSQMLQQQPSApIPLSSQSSFPQPHLSGGQPFHGIQQPLGQTGMPPSFSKPNIEGAPGAPIGNTFQH 1126
Cdd:pfam03154 478 PSGPPTSTSSAMPGIQPPSS-ASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPSPEPTVVNTPSH 552
|
|
| |
|
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 |
3.35e-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: 3.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 13 AWSPAQNhpiYLATGtsaqqldatfSTNASLEIFELD-------LSDPSLDMKSCATFSSSHRyhkliwgpykmdskgdv 85
Cdd:cd00200 16 AFSPDGK---LLATG----------SGDGTIKVWDLEtgellrtLKGHTGPVRDVAASADGTY----------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 86 sgvLIAGGENGNIILYDPSKiiaGDKEVVIAQndkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200 66 ---LASGSSDKTIRLWDLET---GECVRTLTG---HTSYVSSVA---FSPDgrILSSSSRDKTIKVWDVETGKCLTTLRG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 164 KTQPpedISCIAWNrQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDiATQMVLASEDDrlpVIQM 243
Cdd:cd00200 134 HTDW---VNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:cd00200 204 WDLS-TGKCLGTLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GS 280
|
....*....
gi 1622939744 324 FDGRISVYS 332
Cdd:cd00200 281 ADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
89-333 |
5.09e-23 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 103.07 E-value: 5.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 89 LIAGGENGNIILYDpskiIAGDKEvvIAQNDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPp 168
Cdd:COG2319 177 LASGSDDGTVRLWD----LATGKL--LRTLTGHTGAVRSVAFS-PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGS- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 169 edISCIAWNRQVQHiLASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPDiATQMVLASEDDRlpvIQMWDLRf 248
Cdd:COG2319 249 --VRSVAFSPDGRL-LASGSADGTVRLWDLATGELLRTLTGHSGGVN--SVAFSPD-GKLLASGSDDGT---VRLWDLA- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 249 ASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRI 328
Cdd:COG2319 319 TGKLLRTLTGHTGAVRSVAFS-PDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTV 396
|
....*
gi 1622939744 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 ... |
573-696 |
4.88e-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: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 573 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKyFAKSQSKIT---RLITAVVMKNWKEIVESC---- 644
Cdd:cd09233 69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622939744 645 -----DLKNWREALAAVLTYAKPD-EFSALCDLlgtrleneGDSLLQTQ----ACLCYICAG 696
Cdd:cd09233 147 aeaewALGNWREHLAIILSNRTSNlDLEALVEL--------GDLLAQRGlveaAHICYLLAG 200
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
776-1126 |
6.11e-09 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 60.55 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 776 QPNIVQLRDRLCRAQGEPVAGHESPKIPYEKQQLPKGRPGPVGHHQMPRVQTQQYY-PHVRIAPTVTTWSNKTPT---AL 851
Cdd:pfam03154 170 QPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAaPHTLIQQTPTLHPQRLPSphpPL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 852 PSHPPAASPSDTQGENPPPPgfIMHGNVNPnAAGQLPTSPGHMHTQV-----PPYPQPQPYQPAQPYPFGTGGSAMYRPQ 926
Cdd:pfam03154 250 QPMTQPPPPSQVSPQPLPQP--SLHGQMPP-MPHSLQTGPSHMQHPVppqpfPLTPQSSQSQVPPGPSPAAPGQSQQRIH 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 927 QPVA--------PPTSNAYPNTPYIS---SASSYSGQSQLYAAQ------HQASSPTSSPATSFPPPPS----SGASFQH 985
Cdd:pfam03154 327 TPPSqsqlqsqqPPREQPLPPAPLSMphiKPPPTTPIPQLPNPQshkhppHLSGPSPFQMNSNLPPPPAlkplSSLSTHH 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 986 GGPGAPPS----------SSAYALPPGTTETHSVqdqapmlegPQNGWNDPP--ALNRVPKKKKTPEN-FMP--PVPITS 1050
Cdd:pfam03154 407 PPSAHPPPlqlmpqsqqlPPPPAQPPVLTQSQSL---------PPPAASHPPtsGLHQVPSQSPFPQHpFVPggPPPITP 477
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622939744 1051 PIMNPLGDPQSQMLQQQPSApIPLSSQSSFPQPHLSGGQPFHGIQQPLGQTGMPPSFSKPNIEGAPGAPIGNTFQH 1126
Cdd:pfam03154 478 PSGPPTSTSSAMPGIQPPSS-ASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPSPEPTVVNTPSH 552
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
751-1119 |
8.80e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 57.26 E-value: 8.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 751 SQYANLLAAQGSIAAALAFLPDNTNQPNIVQLRDRlCRAQGEPVAGHESPKIPyekqQLPKGRP--GPVGHHQMPRVQTQ 828
Cdd:PHA03247 2632 SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRR-ARRLGRAAQASSPPQRP----RRRAARPtvGSLTSLADPPPPPP 2706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 829 QYYPhvriAPTVTTWSNKTPTAlPSHPPAASPSDTQGENPPPP--GFIMHGNVNPNAAGQLPTSPGH-MHTQVPPYPQPQ 905
Cdd:PHA03247 2707 TPEP----APHALVSATPLPPG-PAAARQASPALPAAPAPPAVpaGPATPGGPARPARPPTTAGPPApAPPAAPAAGPPR 2781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 906 PYQPAQPYPFGTGGSAMYRPQQPVAPPTSNAYPNTPYISSASSYSGQSQLYAAQhqaSSPTSSPATSFPPPPSSGASFQH 985
Cdd:PHA03247 2782 RLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQ---PTAPPPPPGPPPPSLPLGGSVAP 2858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 986 GGPGA--PPSSSAYALPPGTTETHSVQDQAPMLEGPQNGWNDPPAlnrVPKKKKTPENFMPPVPITSPIMNPLGDPQSQM 1063
Cdd:PHA03247 2859 GGDVRrrPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPD---QPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP 2935
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622939744 1064 lQQQPSAPIPlssqssfPQPHLSG-GQPFHGIQQPLGQTGMPPSFSKPNIEGAPGAP 1119
Cdd:PHA03247 2936 -PPRPQPPLA-------PTTDPAGaGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
|
|
| Sec16_C |
pfam12931 |
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal ... |
573-767 |
6.31e-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: 6.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 573 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKY----FAKSQSKITRLItAVVMK----NWKEIVE- 642
Cdd:pfam12931 1 IRALLLTGDREKALWLAL-DKKLwAHALLIASTLGKEKWKEVVQEFvrseFKGSNNKSGESL-AALYQvfagNSEEAVDe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 643 --------SCDLKNWREALAAVLTYAKPDEFSALCDlLGTRLENEGdslLQTQACLCYICAG---NVEKLVACWTKAQDG 711
Cdd:pfam12931 79 lvppsknaLWALDNWRETLALVLSNRSPGDVEALLA-LGDLLAQYG---RTEAAHICFLLAGlplSQTVLLGADHVRFPS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 712 SHPLSLQDLI--EkvvILRKAVQLTqAMDTSTVGV--LLAAKMsQYANLLAAQGSIAAAL 767
Cdd:pfam12931 155 TFGNDLESILltE---IYEYALSLS-PPQPPFVGLphLLPYKL-QHAAVLAEYGLVSEAQ 209
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
203-333 |
4.19e-04 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 44.69 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 203 PIIKVSdhsNRMHCSGLAWHPDIATQMVLASEDDrlpVIQMWDLrfASSPLRV-LENHARGILAIAWSMADPELLLSCGK 281
Cdd:PLN00181 525 PVVELA---SRSKLSGICWNSYIKSQVASSNFEG---VVQVWDV--ARSQLVTeMKEHEKRVWSIDYSSADPTLLASGSD 596
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1622939744 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 |
3.35e-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: 3.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 13 AWSPAQNhpiYLATGtsaqqldatfSTNASLEIFELD-------LSDPSLDMKSCATFSSSHRyhkliwgpykmdskgdv 85
Cdd:cd00200 16 AFSPDGK---LLATG----------SGDGTIKVWDLEtgellrtLKGHTGPVRDVAASADGTY----------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 86 sgvLIAGGENGNIILYDPSKiiaGDKEVVIAQndkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200 66 ---LASGSSDKTIRLWDLET---GECVRTLTG---HTSYVSSVA---FSPDgrILSSSSRDKTIKVWDVETGKCLTTLRG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 164 KTQPpedISCIAWNrQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDiATQMVLASEDDrlpVIQM 243
Cdd:cd00200 134 HTDW---VNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:cd00200 204 WDLS-TGKCLGTLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GS 280
|
....*....
gi 1622939744 324 FDGRISVYS 332
Cdd:cd00200 281 ADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
89-333 |
5.09e-23 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 103.07 E-value: 5.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 89 LIAGGENGNIILYDpskiIAGDKEvvIAQNDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPp 168
Cdd:COG2319 177 LASGSDDGTVRLWD----LATGKL--LRTLTGHTGAVRSVAFS-PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGS- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 169 edISCIAWNRQVQHiLASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPDiATQMVLASEDDRlpvIQMWDLRf 248
Cdd:COG2319 249 --VRSVAFSPDGRL-LASGSADGTVRLWDLATGELLRTLTGHSGGVN--SVAFSPD-GKLLASGSDDGT---VRLWDLA- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 249 ASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRI 328
Cdd:COG2319 319 TGKLLRTLTGHTGAVRSVAFS-PDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTV 396
|
....*
gi 1622939744 329 SVYSI 333
Cdd:COG2319 397 RLWDL 401
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
89-333 |
1.39e-21 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 98.83 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 89 LIAGGENGNIILYDpskiIAGDKEVVIAQNdkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGAKTQ 166
Cdd:COG2319 135 LASGSADGTVRLWD----LATGKLLRTLTG--HSGAVTSVA---FSPDgkLLASGSDDGTVRLWDLATGKLLRTLTGHTG 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 167 PpedISCIAWNRQvQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPD---IATqmvlASEDDRlpvIQM 243
Cdd:COG2319 206 A---VRSVAFSPD-GKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRS--VAFSPDgrlLAS----GSADGT---VRL 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:COG2319 273 WDLA-TGELLRTLTGHSGGVNSVAFS-PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLAS-GS 349
|
250
....*....|
gi 1622939744 324 FDGRISVYSI 333
Cdd:COG2319 350 DDGTVRLWDL 359
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
121-336 |
2.12e-19 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 92.28 E-value: 2.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 121 HTGPVRALDVNiFQTNLVASGANESEIYIWDLnnfATPMTPGAKTQPPEDISCIAWNRQvQHILASASPSGRATVWDLRK 200
Cdd:COG2319 77 HTAAVLSVAFS-PDGRLLASASADGTVRLWDL---ATGLLLRTLTGHTGAVRSVAFSPD-GKTLASGSADGTVRLWDLAT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 201 NEPIIKVSDHSNRMHCsgLAWHPD---IATqmvlASEDDRlpvIQMWDLRfASSPLRVLENHARGILAIAWSmADPELLL 277
Cdd:COG2319 152 GKLLRTLTGHSGAVTS--VAFSPDgklLAS----GSDDGT---VRLWDLA-TGKLLRTLTGHTGAVRSVAFS-PDGKLLA 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622939744 278 SCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPrNPAVLSAASFDGRISVYSIMGG 336
Cdd:COG2319 221 SGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVRLWDLATG 278
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
171-337 |
1.78e-16 |
|
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: 81.23 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 171 ISCIAWNRQvQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMhcSGLAWHPDiATQMVLASEDDrlpVIQMWDLRfAS 250
Cdd:cd00200 12 VTCVAFSPD-GKLLATGSGDGTIKVWDLETGELLRTLKGHTGPV--RDVAASAD-GTYLASGSSDK---TIRLWDLE-TG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 251 SPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPrNPAVLSAASFDGRISV 330
Cdd:cd00200 84 ECVRTLTGHTSYVSSVAFS-PDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSP-DGTFVASSSQDGTIKL 161
|
....*..
gi 1622939744 331 YSIMGGS 337
Cdd:cd00200 162 WDLRTGK 168
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
89-247 |
2.30e-09 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 61.08 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 89 LIAGGENGNIILYDpskiIAGDKEVVIAQNdkHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTqpp 168
Cdd:COG2319 261 LASGSADGTVRLWD----LATGELLRTLTG--HSGGVNSVAFS-PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHT--- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 169 EDISCIAWNRQVQhILASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPD---IATqmvlASEDDRlpvIQMWD 245
Cdd:COG2319 331 GAVRSVAFSPDGK-TLASGSDDGTVRLWDLATGELLRTLTGHTGAVT--SVAFSPDgrtLAS----GSADGT---VRLWD 400
|
..
gi 1622939744 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 ... |
573-696 |
4.88e-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: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 573 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKyFAKSQSKIT---RLITAVVMKNWKEIVESC---- 644
Cdd:cd09233 69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622939744 645 -----DLKNWREALAAVLTYAKPD-EFSALCDLlgtrleneGDSLLQTQ----ACLCYICAG 696
Cdd:cd09233 147 aeaewALGNWREHLAIILSNRTSNlDLEALVEL--------GDLLAQRGlveaAHICYLLAG 200
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
776-1126 |
6.11e-09 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 60.55 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 776 QPNIVQLRDRLCRAQGEPVAGHESPKIPYEKQQLPKGRPGPVGHHQMPRVQTQQYY-PHVRIAPTVTTWSNKTPT---AL 851
Cdd:pfam03154 170 QPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAaPHTLIQQTPTLHPQRLPSphpPL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 852 PSHPPAASPSDTQGENPPPPgfIMHGNVNPnAAGQLPTSPGHMHTQV-----PPYPQPQPYQPAQPYPFGTGGSAMYRPQ 926
Cdd:pfam03154 250 QPMTQPPPPSQVSPQPLPQP--SLHGQMPP-MPHSLQTGPSHMQHPVppqpfPLTPQSSQSQVPPGPSPAAPGQSQQRIH 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 927 QPVA--------PPTSNAYPNTPYIS---SASSYSGQSQLYAAQ------HQASSPTSSPATSFPPPPS----SGASFQH 985
Cdd:pfam03154 327 TPPSqsqlqsqqPPREQPLPPAPLSMphiKPPPTTPIPQLPNPQshkhppHLSGPSPFQMNSNLPPPPAlkplSSLSTHH 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 986 GGPGAPPS----------SSAYALPPGTTETHSVqdqapmlegPQNGWNDPP--ALNRVPKKKKTPEN-FMP--PVPITS 1050
Cdd:pfam03154 407 PPSAHPPPlqlmpqsqqlPPPPAQPPVLTQSQSL---------PPPAASHPPtsGLHQVPSQSPFPQHpFVPggPPPITP 477
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622939744 1051 PIMNPLGDPQSQMLQQQPSApIPLSSQSSFPQPHLSGGQPFHGIQQPLGQTGMPPSFSKPNIEGAPGAPIGNTFQH 1126
Cdd:pfam03154 478 PSGPPTSTSSAMPGIQPPSS-ASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPSPEPTVVNTPSH 552
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
751-1119 |
8.80e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 57.26 E-value: 8.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 751 SQYANLLAAQGSIAAALAFLPDNTNQPNIVQLRDRlCRAQGEPVAGHESPKIPyekqQLPKGRP--GPVGHHQMPRVQTQ 828
Cdd:PHA03247 2632 SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRR-ARRLGRAAQASSPPQRP----RRRAARPtvGSLTSLADPPPPPP 2706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 829 QYYPhvriAPTVTTWSNKTPTAlPSHPPAASPSDTQGENPPPP--GFIMHGNVNPNAAGQLPTSPGH-MHTQVPPYPQPQ 905
Cdd:PHA03247 2707 TPEP----APHALVSATPLPPG-PAAARQASPALPAAPAPPAVpaGPATPGGPARPARPPTTAGPPApAPPAAPAAGPPR 2781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 906 PYQPAQPYPFGTGGSAMYRPQQPVAPPTSNAYPNTPYISSASSYSGQSQLYAAQhqaSSPTSSPATSFPPPPSSGASFQH 985
Cdd:PHA03247 2782 RLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQ---PTAPPPPPGPPPPSLPLGGSVAP 2858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 986 GGPGA--PPSSSAYALPPGTTETHSVQDQAPMLEGPQNGWNDPPAlnrVPKKKKTPENFMPPVPITSPIMNPLGDPQSQM 1063
Cdd:PHA03247 2859 GGDVRrrPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPD---QPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP 2935
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622939744 1064 lQQQPSAPIPlssqssfPQPHLSG-GQPFHGIQQPLGQTGMPPSFSKPNIEGAPGAP 1119
Cdd:PHA03247 2936 -PPRPQPPLA-------PTTDPAGaGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
|
|
| Sec16_C |
pfam12931 |
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal ... |
573-767 |
6.31e-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: 6.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 573 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKY----FAKSQSKITRLItAVVMK----NWKEIVE- 642
Cdd:pfam12931 1 IRALLLTGDREKALWLAL-DKKLwAHALLIASTLGKEKWKEVVQEFvrseFKGSNNKSGESL-AALYQvfagNSEEAVDe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 643 --------SCDLKNWREALAAVLTYAKPDEFSALCDlLGTRLENEGdslLQTQACLCYICAG---NVEKLVACWTKAQDG 711
Cdd:pfam12931 79 lvppsknaLWALDNWRETLALVLSNRSPGDVEALLA-LGDLLAQYG---RTEAAHICFLLAGlplSQTVLLGADHVRFPS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 712 SHPLSLQDLI--EkvvILRKAVQLTqAMDTSTVGV--LLAAKMsQYANLLAAQGSIAAAL 767
Cdd:pfam12931 155 TFGNDLESILltE---IYEYALSLS-PPQPPFVGLphLLPYKL-QHAAVLAEYGLVSEAQ 209
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
974-1144 |
1.48e-06 |
|
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: 52.85 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 974 PPPPSSGASFQHGGPGAPPSSSAYALPP--------------GTTETHSVQDQAPMLEgPQNGWNDPPALNRVPKKKKTP 1039
Cdd:pfam03154 181 ASPPSPPPPGTTQAATAGPTPSAPSVPPqgspatsqppnqtqSTAAPHTLIQQTPTLH-PQRLPSPHPPLQPMTQPPPPS 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 1040 ENfmPPVPITSPIMNPLGDPQSQMLQQQPS--------APIPLSSQSS------FPQPHLSgGQPFHGIQQPLGQTgMPP 1105
Cdd:pfam03154 260 QV--SPQPLPQPSLHGQMPPMPHSLQTGPShmqhpvppQPFPLTPQSSqsqvppGPSPAAP-GQSQQRIHTPPSQS-QLQ 335
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622939744 1106 SFSKPNIEGAPGAPIgnTFQHVQSLPTKKITKKPIPDEH 1144
Cdd:pfam03154 336 SQQPPREQPLPPAPL--SMPHIKPPPTTPIPQLPNPQSH 372
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
252-336 |
3.83e-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: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 252 PLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRISVY 331
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFS-PDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLAS-GSSDKTIRLW 78
|
....*
gi 1622939744 332 SIMGG 336
Cdd:cd00200 79 DLETG 83
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
203-333 |
4.19e-04 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 44.69 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 203 PIIKVSdhsNRMHCSGLAWHPDIATQMVLASEDDrlpVIQMWDLrfASSPLRV-LENHARGILAIAWSMADPELLLSCGK 281
Cdd:PLN00181 525 PVVELA---SRSKLSGICWNSYIKSQVASSNFEG---VVQVWDV--ARSQLVTeMKEHEKRVWSIDYSSADPTLLASGSD 596
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1622939744 282 DAKILCSNPNTGEVLYELPTNTQWCFdIQWCPRNPAVLSAASFDGRISVYSI 333
Cdd:PLN00181 597 DGSVKLWSINQGVSIGTIKTKANICC-VQFPSESGRSLAFGSADHKVYYYDL 647
|
|
| PAT1 |
pfam09770 |
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
788-927 |
3.99e-03 |
|
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.
Pssm-ID: 401645 [Multi-domain] Cd Length: 846 Bit Score: 41.56 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 788 RAQGEPVAGHESP-KIPYEKQQLPKGRPGPVGHHQMPRVQTQQYYPHVRIAPTVTTWSNKTPTALPSHPPAASPS--DTQ 864
Cdd:pfam09770 210 PAQQPAPAPAQPPaAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILQRPQSPQPDPAQPSIQPQaqQFH 289
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622939744 865 GENPPPPGFIMHGNVNPNAAGQlPTSPGHMHTQVPPYPQPQPYQPAQPYPFGTGGSAMYRPQQ 927
Cdd:pfam09770 290 QQPPPVPVQPTQILQNPNRLSA-ARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPIITHPQQ 351
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
980-1213 |
4.34e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 41.61 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 980 GASFQHGGPGAPPSSSAYALPPGTTETHSVQDQapMLEGPQNGWNDPPALNRV---PKKKKTPENFMPPV--PITSPIMN 1054
Cdd:PRK10263 677 GEQYQHDVPVNAEDADAAAEAELARQFAQTQQQ--RYSGEQPAGANPFSLDDFefsPMKALLDDGPHEPLftPIVEPVQQ 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 1055 PLGDPQSQMLQQQPSAPIPLSSQSSFPQPHLSGGQPFHGIQQPLGQtgmPPSFSKPNIEGAPGAPIGNTFQHVQSLPTKK 1134
Cdd:PRK10263 755 PQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAP---QPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQ 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 1135 ITKKPI---PDEHLILKTTFEDLIQRCLSSATDPQTKrklddaskrLEFLYDKLREqtLSPTITSGLHSIARSIETR--- 1208
Cdd:PRK10263 832 QPQQPVapqPQDTLLHPLLMRNGDSRPLHKPTTPLPS---------LDLLTPPPSE--VEPVDTFALEQMARLVEARlad 900
|
250
....*....|...
gi 1622939744 1209 --------NYSEG 1213
Cdd:PRK10263 901 frikadvvNYSPG 913
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
812-1056 |
7.93e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 40.69 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 812 GRPGPVGHHQMPRVQTQQYYPHVRIA-PTVTTWSNKTPTALPSHPPAASPSDTQGENPPPPGFIMHGNVNPNAAGQLPTS 890
Cdd:PHA03247 2752 GGPARPARPPTTAGPPAPAPPAAPAAgPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPP 2831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 891 PGHMHTQVPPYPQPQPYQPAQPYPFGTGGSAMYRP--QQPVAPPTSNAYPNTPYISSASSYSGQSQLYAAQHQASSPTSS 968
Cdd:PHA03247 2832 TSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPpsRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQP 2911
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939744 969 PATSFPPPPSSGASFQHGGPGAPPSSSAYALPPGTTETHSVQDQAPMLEGPQNGWNDPpalNRVP-KKKKTPENfMPPVP 1047
Cdd:PHA03247 2912 QAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVP---GRVAvPRFRVPQP-APSRE 2987
|
....*....
gi 1622939744 1048 ITSPIMNPL 1056
Cdd:PHA03247 2988 APASSTPPL 2996
|
|
| |
