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Conserved domains on  [gi|1622939728|ref|XP_014993882|]
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protein transport protein Sec31A isoform X1 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

 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 3.40e-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: 3.40e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728   13 AWSPAQNhpiYLATGtsaqqldatfSTNASLEIFELD-------LSDPSLDMKSCATFSSSHRyhkliwgpykmdskgdv 85
Cdd:cd00200     16 AFSPDGK---LLATG----------SGDGTIKVWDLEtgellrtLKGHTGPVRDVAASADGTY----------------- 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728   86 sgvLIAGGENGNIILYDPSKiiaGDKEVVIAQndkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200     66 ---LASGSSDKTIRLWDLET---GECVRTLTG---HTSYVSSVA---FSPDgrILSSSSRDKTIKVWDVETGKCLTTLRG 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  164 KTQPpedISCIAWNrQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDiATQMVLASEDDrlpVIQM 243
Cdd:cd00200    134 HTDW---VNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKL 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:cd00200    204 WDLS-TGKCLGTLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GS 280


                   ....*....
gi 1622939728  324 FDGRISVYS 332
Cdd:cd00200    281 ADGTIRIWD 289
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 974-1159 4.45e-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: 60.94  E-value: 4.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  974 PPPPSSGASFQHGGPGAPPSSSAYALPPGTTgtlPAASELPASQRTET--HSVQDQAPMLEgPQNGWNDPPALNRVPKKK 1051
Cdd:pfam03154  181 ASPPSPPPPGTTQAATAGPTPSAPSVPPQGS---PATSQPPNQTQSTAapHTLIQQTPTLH-PQRLPSPHPPLQPMTQPP 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728 1052 KTPENfmPPVPITSPIMNPLGDPQSQMLQQQPS--------APIPLSSQSS------FPQPHLSgGQPFHGIQQPLGQTg 1117
Cdd:pfam03154  257 PPSQV--SPQPLPQPSLHGQMPPMPHSLQTGPShmqhpvppQPFPLTPQSSqsqvppGPSPAAP-GQSQQRIHTPPSQS- 332

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1622939728 1118 MPPSFSKPNIEGAPGAPIgnTFQHVQSLPTKKITKKPIPDEH 1159
Cdd:pfam03154  333 QLQSQQPPREQPLPPAPL--SMPHIKPPPTTPIPQLPNPQSH 372
ACE1-Sec16-like super family cl14807
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ...
 573-696 4.95e-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: 4.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  573 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKyFAKSQSKIT---RLITAVVMKNWKEIVESC---- 644
Cdd:cd09233     69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622939728  645 -----DLKNWREALAAVLTYAKPD-EFSALCDLlgtrleneGDSLLQTQ----ACLCYICAG 696
Cdd:cd09233    147 aeaewALGNWREHLAIILSNRTSNlDLEALVEL--------GDLLAQRGlveaAHICYLLAG 200
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 751-1134 1.79e-08

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 59.18  E-value: 1.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  751 SQYANLLAAQGSIAAALAFLPDNTNQPNIVQLRDRlCRAQGEPVAGHESPKIPyekqQLPKGRP--GPVGHHQMPRVQTQ 828
Cdd:PHA03247  2632 SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRR-ARRLGRAAQASSPPQRP----RRRAARPtvGSLTSLADPPPPPP 2706

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  829 QYYPhvriAPTVTTWSNKTPTAlPSHPPAASPSDTQGENPPPP--GFIMHGNVNPNAAGQLPTSPghmhtqvPPYPQPQP 906
Cdd:PHA03247  2707 TPEP----APHALVSATPLPPG-PAAARQASPALPAAPAPPAVpaGPATPGGPARPARPPTTAGP-------PAPAPPAA 2774

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  907 YQPAQPYPFGTGGSAMYRPQQPVAPPTSNAYPNTPYISSASSYSGQSQLYAAQHQASSPTSSPATSFPPPPSSgASFQHG 986
Cdd:PHA03247  2775 PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPP-PSLPLG 2853

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  987 GPGAPPSSSAYALPPGTTGTLPAASELPASQRTETHSVQDQAPMLEGPQNGwndppalnrvPKKKKTPENFMPPVPITSP 1066
Cdd:PHA03247  2854 GSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQ----------PERPPQPQAPPPPQPQPQP 2923

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622939728 1067 IMNPLGDPQSQMlQQQPSAPIPlssqssfPQPHLSG-GQPFHGIQQPLGQTGMPPSFSKPNIEGAPGAP 1134
Cdd:PHA03247  2924 PPPPQPQPPPPP-PPRPQPPLA-------PTTDPAGaGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
 
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 3.40e-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: 3.40e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728   13 AWSPAQNhpiYLATGtsaqqldatfSTNASLEIFELD-------LSDPSLDMKSCATFSSSHRyhkliwgpykmdskgdv 85
Cdd:cd00200     16 AFSPDGK---LLATG----------SGDGTIKVWDLEtgellrtLKGHTGPVRDVAASADGTY----------------- 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728   86 sgvLIAGGENGNIILYDPSKiiaGDKEVVIAQndkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200     66 ---LASGSSDKTIRLWDLET---GECVRTLTG---HTSYVSSVA---FSPDgrILSSSSRDKTIKVWDVETGKCLTTLRG 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  164 KTQPpedISCIAWNrQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDiATQMVLASEDDrlpVIQM 243
Cdd:cd00200    134 HTDW---VNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKL 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:cd00200    204 WDLS-TGKCLGTLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GS 280


                   ....*....
gi 1622939728  324 FDGRISVYS 332
Cdd:cd00200    281 ADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
89-333 5.17e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 103.07  E-value: 5.17e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728   89 LIAGGENGNIILYDpskiIAGDKEvvIAQNDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPp 168
Cdd:COG2319    177 LASGSDDGTVRLWD----LATGKL--LRTLTGHTGAVRSVAFS-PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGS- 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  169 edISCIAWNRQVQHiLASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPDiATQMVLASEDDRlpvIQMWDLRf 248
Cdd:COG2319    249 --VRSVAFSPDGRL-LASGSADGTVRLWDLATGELLRTLTGHSGGVN--SVAFSPD-GKLLASGSDDGT---VRLWDLA- 318

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  249 ASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRI 328
Cdd:COG2319    319 TGKLLRTLTGHTGAVRSVAFS-PDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTV 396


                   ....*
gi 1622939728  329 SVYSI 333
Cdd:COG2319    397 RLWDL 401
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 974-1159 4.45e-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: 60.94  E-value: 4.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  974 PPPPSSGASFQHGGPGAPPSSSAYALPPGTTgtlPAASELPASQRTET--HSVQDQAPMLEgPQNGWNDPPALNRVPKKK 1051
Cdd:pfam03154  181 ASPPSPPPPGTTQAATAGPTPSAPSVPPQGS---PATSQPPNQTQSTAapHTLIQQTPTLH-PQRLPSPHPPLQPMTQPP 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728 1052 KTPENfmPPVPITSPIMNPLGDPQSQMLQQQPS--------APIPLSSQSS------FPQPHLSgGQPFHGIQQPLGQTg 1117
Cdd:pfam03154  257 PPSQV--SPQPLPQPSLHGQMPPMPHSLQTGPShmqhpvppQPFPLTPQSSqsqvppGPSPAAP-GQSQQRIHTPPSQS- 332

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1622939728 1118 MPPSFSKPNIEGAPGAPIgnTFQHVQSLPTKKITKKPIPDEH 1159
Cdd:pfam03154  333 QLQSQQPPREQPLPPAPL--SMPHIKPPPTTPIPQLPNPQSH 372
ACE1-Sec16-like cd09233
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ...
 573-696 4.95e-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: 4.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  573 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKyFAKSQSKIT---RLITAVVMKNWKEIVESC---- 644
Cdd:cd09233     69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622939728  645 -----DLKNWREALAAVLTYAKPD-EFSALCDLlgtrleneGDSLLQTQ----ACLCYICAG 696
Cdd:cd09233    147 aeaewALGNWREHLAIILSNRTSNlDLEALVEL--------GDLLAQRGlveaAHICYLLAG 200
PHA03247 PHA03247
large tegument protein UL36; Provisional
 751-1134 1.79e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 59.18  E-value: 1.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  751 SQYANLLAAQGSIAAALAFLPDNTNQPNIVQLRDRlCRAQGEPVAGHESPKIPyekqQLPKGRP--GPVGHHQMPRVQTQ 828
Cdd:PHA03247  2632 SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRR-ARRLGRAAQASSPPQRP----RRRAARPtvGSLTSLADPPPPPP 2706

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  829 QYYPhvriAPTVTTWSNKTPTAlPSHPPAASPSDTQGENPPPP--GFIMHGNVNPNAAGQLPTSPghmhtqvPPYPQPQP 906
Cdd:PHA03247  2707 TPEP----APHALVSATPLPPG-PAAARQASPALPAAPAPPAVpaGPATPGGPARPARPPTTAGP-------PAPAPPAA 2774

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  907 YQPAQPYPFGTGGSAMYRPQQPVAPPTSNAYPNTPYISSASSYSGQSQLYAAQHQASSPTSSPATSFPPPPSSgASFQHG 986
Cdd:PHA03247  2775 PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPP-PSLPLG 2853

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  987 GPGAPPSSSAYALPPGTTGTLPAASELPASQRTETHSVQDQAPMLEGPQNGwndppalnrvPKKKKTPENFMPPVPITSP 1066
Cdd:PHA03247  2854 GSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQ----------PERPPQPQAPPPPQPQPQP 2923

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622939728 1067 IMNPLGDPQSQMlQQQPSAPIPlssqssfPQPHLSG-GQPFHGIQQPLGQTGMPPSFSKPNIEGAPGAP 1134
Cdd:PHA03247  2924 PPPPQPQPPPPP-PPRPQPPLA-------PTTDPAGaGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
Sec16_C pfam12931
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal ...
 573-767 6.51e-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: 6.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  573 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKY----FAKSQSKITRLItAVVMK----NWKEIVE- 642
Cdd:pfam12931    1 IRALLLTGDREKALWLAL-DKKLwAHALLIASTLGKEKWKEVVQEFvrseFKGSNNKSGESL-AALYQvfagNSEEAVDe 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  643 --------SCDLKNWREALAAVLTYAKPDEFSALCDlLGTRLENEGdslLQTQACLCYICAG---NVEKLVACWTKAQDG 711
Cdd:pfam12931   79 lvppsknaLWALDNWRETLALVLSNRSPGDVEALLA-LGDLLAQYG---RTEAAHICFLLAGlplSQTVLLGADHVRFPS 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  712 SHPLSLQDLI--EkvvILRKAVQLTqAMDTSTVGV--LLAAKMsQYANLLAAQGSIAAAL 767
Cdd:pfam12931  155 TFGNDLESILltE---IYEYALSLS-PPQPPFVGLphLLPYKL-QHAAVLAEYGLVSEAQ 209
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 203-333 4.25e-04

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 44.69  E-value: 4.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  203 PIIKVSdhsNRMHCSGLAWHPDIATQMVLASEDDrlpVIQMWDLrfASSPLRV-LENHARGILAIAWSMADPELLLSCGK 281
Cdd:PLN00181   525 PVVELA---SRSKLSGICWNSYIKSQVASSNFEG---VVQVWDV--ARSQLVTeMKEHEKRVWSIDYSSADPTLLASGSD 596

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622939728  282 DAKILCSNPNTGEVLYELPTNTQWCFdIQWCPRNPAVLSAASFDGRISVYSI 333
Cdd:PLN00181   597 DGSVKLWSINQGVSIGTIKTKANICC-VQFPSESGRSLAFGSADHKVYYYDL 647
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 774-1198 3.52e-03

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: 41.53  E-value: 3.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  774 TNQPNIVQLRDRLCRAQGEPVAGHESPKIPYEKQQLPKGRPG-PVGH----HQMPRVQTQQyyPHVRIAPTVTTWSNKTP 848
Cdd:pfam09606   90 AGQGTRPQMMGPMGPGPGGPMGQQMGGPGTASNLLASLGRPQmPMGGagfpSQMSRVGRMQ--PGGQAGGMMQPSSGQPG 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  849 TALPSHPPAASPSDTQGENPPPPGFIMH-GNVNPNAAGQlPTSPGHMHTQVPPYPQPQPYQPAQPYPfgTGGSAMYRPQQ 927
Cdd:pfam09606  168 SGTPNQMGPNGGPGQGQAGGMNGGQQGPmGGQMPPQMGV-PGMPGPADAGAQMGQQAQANGGMNPQQ--MGGAPNQVAMQ 244

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  928 PvAPPTSNAYPNtpyiSSASSYSGQSQLYAAQHQASSPTSSPATSFPPPPSSGASFQHGGPGAPPSSSAYALPP---GTT 1004
Cdd:pfam09606  245 Q-QQPQQQGQQS----QLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQqqqQQG 319

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728 1005 GTLPAA-------SELPASQRTETHSVQDQAPMLEGPQNGWNDPPAlnrvpkKKKTPENFMPPVPITSPIMNPLGDPQSQ 1077
Cdd:pfam09606  320 GNHPAAhqqqmnqSVGQGGQVVALGGLNHLETWNPGNFGGLGANPM------QRGQPGMMSSPSPVPGQQVRQVTPNQFM 393

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728 1078 MLQQQPSAPIPLSSQSSFPQPHLSGGQPF-HGIQQPLGQTGMPPSFSKPNIEGAPGAPIGNTFQHVQSLPTKKITKKPIP 1156
Cdd:pfam09606  394 RQSPQPSVPSPQGPGSQPPQSHPGGMIPSpALIPSPSPQMSQQPAQQRTIGQDSPGGSLNTPGQSAVNSPLNPQEEQLYR 473

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 1622939728 1157 DEHLILKTTFEDLIQRCLSSATDPQTKRKLDDASKRLEFLYD 1198
Cdd:pfam09606  474 EKYRQLTKYIEPLKRMIAKMENDPGDIDKMNKMKRLLEILSN 515
 
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 3.40e-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: 3.40e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728   13 AWSPAQNhpiYLATGtsaqqldatfSTNASLEIFELD-------LSDPSLDMKSCATFSSSHRyhkliwgpykmdskgdv 85
Cdd:cd00200     16 AFSPDGK---LLATG----------SGDGTIKVWDLEtgellrtLKGHTGPVRDVAASADGTY----------------- 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728   86 sgvLIAGGENGNIILYDPSKiiaGDKEVVIAQndkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200     66 ---LASGSSDKTIRLWDLET---GECVRTLTG---HTSYVSSVA---FSPDgrILSSSSRDKTIKVWDVETGKCLTTLRG 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  164 KTQPpedISCIAWNrQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDiATQMVLASEDDrlpVIQM 243
Cdd:cd00200    134 HTDW---VNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKL 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:cd00200    204 WDLS-TGKCLGTLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GS 280


                   ....*....
gi 1622939728  324 FDGRISVYS 332
Cdd:cd00200    281 ADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
89-333 5.17e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 103.07  E-value: 5.17e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728   89 LIAGGENGNIILYDpskiIAGDKEvvIAQNDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPp 168
Cdd:COG2319    177 LASGSDDGTVRLWD----LATGKL--LRTLTGHTGAVRSVAFS-PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGS- 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  169 edISCIAWNRQVQHiLASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPDiATQMVLASEDDRlpvIQMWDLRf 248
Cdd:COG2319    249 --VRSVAFSPDGRL-LASGSADGTVRLWDLATGELLRTLTGHSGGVN--SVAFSPD-GKLLASGSDDGT---VRLWDLA- 318

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  249 ASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRI 328
Cdd:COG2319    319 TGKLLRTLTGHTGAVRSVAFS-PDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTV 396


                   ....*
gi 1622939728  329 SVYSI 333
Cdd:COG2319    397 RLWDL 401
WD40 COG2319
WD40 repeat [General function prediction only];
89-333 1.41e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 98.83  E-value: 1.41e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728   89 LIAGGENGNIILYDpskiIAGDKEVVIAQNdkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGAKTQ 166
Cdd:COG2319    135 LASGSADGTVRLWD----LATGKLLRTLTG--HSGAVTSVA---FSPDgkLLASGSDDGTVRLWDLATGKLLRTLTGHTG 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  167 PpedISCIAWNRQvQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPD---IATqmvlASEDDRlpvIQM 243
Cdd:COG2319    206 A---VRSVAFSPD-GKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRS--VAFSPDgrlLAS----GSADGT---VRL 272

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:COG2319    273 WDLA-TGELLRTLTGHSGGVNSVAFS-PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLAS-GS 349

                          250
                   ....*....|
gi 1622939728  324 FDGRISVYSI 333
Cdd:COG2319    350 DDGTVRLWDL 359
WD40 COG2319
WD40 repeat [General function prediction only];
121-336 2.15e-19

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 92.28  E-value: 2.15e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  121 HTGPVRALDVNiFQTNLVASGANESEIYIWDLnnfATPMTPGAKTQPPEDISCIAWNRQvQHILASASPSGRATVWDLRK 200
Cdd:COG2319     77 HTAAVLSVAFS-PDGRLLASASADGTVRLWDL---ATGLLLRTLTGHTGAVRSVAFSPD-GKTLASGSADGTVRLWDLAT 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  201 NEPIIKVSDHSNRMHCsgLAWHPD---IATqmvlASEDDRlpvIQMWDLRfASSPLRVLENHARGILAIAWSmADPELLL 277
Cdd:COG2319    152 GKLLRTLTGHSGAVTS--VAFSPDgklLAS----GSDDGT---VRLWDLA-TGKLLRTLTGHTGAVRSVAFS-PDGKLLA 220

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622939728  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 1.81e-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: 1.81e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  171 ISCIAWNRQvQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMhcSGLAWHPDiATQMVLASEDDrlpVIQMWDLRfAS 250
Cdd:cd00200     12 VTCVAFSPD-GKLLATGSGDGTIKVWDLETGELLRTLKGHTGPV--RDVAASAD-GTYLASGSSDK---TIRLWDLE-TG 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  251 SPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPrNPAVLSAASFDGRISV 330
Cdd:cd00200     84 ECVRTLTGHTSYVSSVAFS-PDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSP-DGTFVASSSQDGTIKL 161


                   ....*..
gi 1622939728  331 YSIMGGS 337
Cdd:cd00200    162 WDLRTGK 168
WD40 COG2319
WD40 repeat [General function prediction only];
89-247 2.33e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 61.08  E-value: 2.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728   89 LIAGGENGNIILYDpskiIAGDKEVVIAQNdkHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTqpp 168
Cdd:COG2319    261 LASGSADGTVRLWD----LATGELLRTLTG--HSGGVNSVAFS-PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHT--- 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  169 EDISCIAWNRQVQhILASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPD---IATqmvlASEDDRlpvIQMWD 245
Cdd:COG2319    331 GAVRSVAFSPDGK-TLASGSDDGTVRLWDLATGELLRTLTGHTGAVT--SVAFSPDgrtLAS----GSADGT---VRLWD 400


                   ..
gi 1622939728  246 LR 247
Cdd:COG2319    401 LA 402
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 974-1159 4.45e-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: 60.94  E-value: 4.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  974 PPPPSSGASFQHGGPGAPPSSSAYALPPGTTgtlPAASELPASQRTET--HSVQDQAPMLEgPQNGWNDPPALNRVPKKK 1051
Cdd:pfam03154  181 ASPPSPPPPGTTQAATAGPTPSAPSVPPQGS---PATSQPPNQTQSTAapHTLIQQTPTLH-PQRLPSPHPPLQPMTQPP 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728 1052 KTPENfmPPVPITSPIMNPLGDPQSQMLQQQPS--------APIPLSSQSS------FPQPHLSgGQPFHGIQQPLGQTg 1117
Cdd:pfam03154  257 PPSQV--SPQPLPQPSLHGQMPPMPHSLQTGPShmqhpvppQPFPLTPQSSqsqvppGPSPAAP-GQSQQRIHTPPSQS- 332

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1622939728 1118 MPPSFSKPNIEGAPGAPIgnTFQHVQSLPTKKITKKPIPDEH 1159
Cdd:pfam03154  333 QLQSQQPPREQPLPPAPL--SMPHIKPPPTTPIPQLPNPQSH 372
ACE1-Sec16-like cd09233
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ...
 573-696 4.95e-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: 4.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  573 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKyFAKSQSKIT---RLITAVVMKNWKEIVESC---- 644
Cdd:cd09233     69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622939728  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 ...
 776-1141 1.15e-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: 59.78  E-value: 1.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  776 QPNIVQLRDRLCRAQGEPVAGHESPKIPYEKQQLPKGRPGPVGHHQMPRVQTQQYY-PHVRIAPTVTTWSNKTPT---AL 851
Cdd:pfam03154  170 QPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAaPHTLIQQTPTLHPQRLPSphpPL 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  852 PSHPPAASPSDTQGENPPPPgfIMHGNVNPnAAGQLPTSPGHMHTQV-----PPYPQPQPYQPAQPYPFGTGGSAMYRPQ 926
Cdd:pfam03154  250 QPMTQPPPPSQVSPQPLPQP--SLHGQMPP-MPHSLQTGPSHMQHPVppqpfPLTPQSSQSQVPPGPSPAAPGQSQQRIH 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  927 QPVA--------PPTSNAYPNTPYIS---SASSYSGQSQLYAAQ------HQASSPTSSPATSFPPPPS----SGASFQH 985
Cdd:pfam03154  327 TPPSqsqlqsqqPPREQPLPPAPLSMphiKPPPTTPIPQLPNPQshkhppHLSGPSPFQMNSNLPPPPAlkplSSLSTHH 406

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  986 ggpgaPPSssayALPPGTTgTLPAASELPASQRTEthSVQDQAPMLEGPQNGWNDPPALNRVPKKKKTPEN-FMP--PVP 1062
Cdd:pfam03154  407 -----PPS----AHPPPLQ-LMPQSQQLPPPPAQP--PVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHpFVPggPPP 474

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622939728 1063 ITSPIMNPLGDPQSQMLQQQPSApIPLSSQSSFPQPHLSGGQPFHGIQQPLGQTGMPPSFSKPNIEGAPGAPIGNTFQH 1141
Cdd:pfam03154  475 ITPPSGPPTSTSSAMPGIQPPSS-ASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPSPEPTVVNTPSH 552
PHA03247 PHA03247
large tegument protein UL36; Provisional
 751-1134 1.79e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 59.18  E-value: 1.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  751 SQYANLLAAQGSIAAALAFLPDNTNQPNIVQLRDRlCRAQGEPVAGHESPKIPyekqQLPKGRP--GPVGHHQMPRVQTQ 828
Cdd:PHA03247  2632 SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRR-ARRLGRAAQASSPPQRP----RRRAARPtvGSLTSLADPPPPPP 2706

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  829 QYYPhvriAPTVTTWSNKTPTAlPSHPPAASPSDTQGENPPPP--GFIMHGNVNPNAAGQLPTSPghmhtqvPPYPQPQP 906
Cdd:PHA03247  2707 TPEP----APHALVSATPLPPG-PAAARQASPALPAAPAPPAVpaGPATPGGPARPARPPTTAGP-------PAPAPPAA 2774

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  907 YQPAQPYPFGTGGSAMYRPQQPVAPPTSNAYPNTPYISSASSYSGQSQLYAAQHQASSPTSSPATSFPPPPSSgASFQHG 986
Cdd:PHA03247  2775 PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPP-PSLPLG 2853

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  987 GPGAPPSSSAYALPPGTTGTLPAASELPASQRTETHSVQDQAPMLEGPQNGwndppalnrvPKKKKTPENFMPPVPITSP 1066
Cdd:PHA03247  2854 GSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQ----------PERPPQPQAPPPPQPQPQP 2923

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622939728 1067 IMNPLGDPQSQMlQQQPSAPIPlssqssfPQPHLSG-GQPFHGIQQPLGQTGMPPSFSKPNIEGAPGAP 1134
Cdd:PHA03247  2924 PPPPQPQPPPPP-PPRPQPPLA-------PTTDPAGaGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
PHA03247 PHA03247
large tegument protein UL36; Provisional
 803-1136 2.06e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 55.71  E-value: 2.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  803 PYEKQQLPKGRPGPvgHHQMPRVQTQQYYPHVRIAPTvttwSNKTPTALP-----SHPPAASPSDTQGENPPPPGFIMHG 877
Cdd:PHA03247  2562 AAPDRSVPPPRPAP--RPSEPAVTSRARRPDAPPQSA----RPRAPVDDRgdprgPAPPSPLPPDTHAPDPPPPSPSPAA 2635

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  878 NvNPNAAGQLPTSPGHMHTQVPPYPQPQPYQPAQPYPFGTGGSA-MYRPQQPVAPPT---------SNAYPNTPYISSAS 947
Cdd:PHA03247  2636 N-EPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSpPQRPRRRAARPTvgsltsladPPPPPPTPEPAPHA 2714

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  948 SYSGQSQLYAAQHQASSPTSSPATSFPPPPSSGASFQHG--------GPGAPPSSSAYALPPG----------------- 1002
Cdd:PHA03247  2715 LVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGparparppTTAGPPAPAPPAAPAAgpprrltrpavaslses 2794

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728 1003 -------------TTGTLPAASELPASQR------TETHSVQDQAPMLEGP------QNGWNDP--PALNRVPKKKKTPE 1055
Cdd:PHA03247  2795 reslpspwdpadpPAAVLAPAAALPPAASpagplpPPTSAQPTAPPPPPGPpppslpLGGSVAPggDVRRRPPSRSPAAK 2874

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728 1056 NFMPPVPITSPIMNPLGDPQSQMLQQQPSAPIPLSSQSSFPQPHLSGGQPFHGIQQPLGQT-GMPPSFSKPNIEGAP-GA 1133
Cdd:PHA03247  2875 PAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPpPRPQPPLAPTTDPAGaGE 2954


                   ...
gi 1622939728 1134 PIG 1136
Cdd:PHA03247  2955 PSG 2957
Sec16_C pfam12931
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal ...
 573-767 6.51e-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: 6.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  573 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKY----FAKSQSKITRLItAVVMK----NWKEIVE- 642
Cdd:pfam12931    1 IRALLLTGDREKALWLAL-DKKLwAHALLIASTLGKEKWKEVVQEFvrseFKGSNNKSGESL-AALYQvfagNSEEAVDe 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  643 --------SCDLKNWREALAAVLTYAKPDEFSALCDlLGTRLENEGdslLQTQACLCYICAG---NVEKLVACWTKAQDG 711
Cdd:pfam12931   79 lvppsknaLWALDNWRETLALVLSNRSPGDVEALLA-LGDLLAQYG---RTEAAHICFLLAGlplSQTVLLGADHVRFPS 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  712 SHPLSLQDLI--EkvvILRKAVQLTqAMDTSTVGV--LLAAKMsQYANLLAAQGSIAAAL 767
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 3.88e-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: 3.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  252 PLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRISVY 331
Cdd:cd00200      1 LRRTLKGHTGGVTCVAFS-PDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLAS-GSSDKTIRLW 78


                   ....*
gi 1622939728  332 SIMGG 336
Cdd:cd00200     79 DLETG 83
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 203-333 4.25e-04

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 44.69  E-value: 4.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  203 PIIKVSdhsNRMHCSGLAWHPDIATQMVLASEDDrlpVIQMWDLrfASSPLRV-LENHARGILAIAWSMADPELLLSCGK 281
Cdd:PLN00181   525 PVVELA---SRSKLSGICWNSYIKSQVASSNFEG---VVQVWDV--ARSQLVTeMKEHEKRVWSIDYSSADPTLLASGSD 596

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622939728  282 DAKILCSNPNTGEVLYELPTNTQWCFdIQWCPRNPAVLSAASFDGRISVYSI 333
Cdd:PLN00181   597 DGSVKLWSINQGVSIGTIKTKANICC-VQFPSESGRSLAFGSADHKVYYYDL 647
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 774-1198 3.52e-03

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: 41.53  E-value: 3.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  774 TNQPNIVQLRDRLCRAQGEPVAGHESPKIPYEKQQLPKGRPG-PVGH----HQMPRVQTQQyyPHVRIAPTVTTWSNKTP 848
Cdd:pfam09606   90 AGQGTRPQMMGPMGPGPGGPMGQQMGGPGTASNLLASLGRPQmPMGGagfpSQMSRVGRMQ--PGGQAGGMMQPSSGQPG 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  849 TALPSHPPAASPSDTQGENPPPPGFIMH-GNVNPNAAGQlPTSPGHMHTQVPPYPQPQPYQPAQPYPfgTGGSAMYRPQQ 927
Cdd:pfam09606  168 SGTPNQMGPNGGPGQGQAGGMNGGQQGPmGGQMPPQMGV-PGMPGPADAGAQMGQQAQANGGMNPQQ--MGGAPNQVAMQ 244

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  928 PvAPPTSNAYPNtpyiSSASSYSGQSQLYAAQHQASSPTSSPATSFPPPPSSGASFQHGGPGAPPSSSAYALPP---GTT 1004
Cdd:pfam09606  245 Q-QQPQQQGQQS----QLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQqqqQQG 319

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728 1005 GTLPAA-------SELPASQRTETHSVQDQAPMLEGPQNGWNDPPAlnrvpkKKKTPENFMPPVPITSPIMNPLGDPQSQ 1077
Cdd:pfam09606  320 GNHPAAhqqqmnqSVGQGGQVVALGGLNHLETWNPGNFGGLGANPM------QRGQPGMMSSPSPVPGQQVRQVTPNQFM 393

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728 1078 MLQQQPSAPIPLSSQSSFPQPHLSGGQPF-HGIQQPLGQTGMPPSFSKPNIEGAPGAPIGNTFQHVQSLPTKKITKKPIP 1156
Cdd:pfam09606  394 RQSPQPSVPSPQGPGSQPPQSHPGGMIPSpALIPSPSPQMSQQPAQQRTIGQDSPGGSLNTPGQSAVNSPLNPQEEQLYR 473

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 1622939728 1157 DEHLILKTTFEDLIQRCLSSATDPQTKRKLDDASKRLEFLYD 1198
Cdd:pfam09606  474 EKYRQLTKYIEPLKRMIAKMENDPGDIDKMNKMKRLLEILSN 515
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 788-927 4.05e-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: 4.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939728  788 RAQGEPVAGHESP-KIPYEKQQLPKGRPGPVGHHQMPRVQTQQYYPHVRIAPTVTTWSNKTPTALPSHPPAASPS--DTQ 864
Cdd:pfam09770  210 PAQQPAPAPAQPPaAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILQRPQSPQPDPAQPSIQPQaqQFH 289

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622939728  865 GENPPPPGFIMHGNVNPNAAGQlPTSPGHMHTQVPPYPQPQPYQPAQPYPFGTGGSAMYRPQQ 927
Cdd:pfam09770  290 QQPPPVPVQPTQILQNPNRLSA-ARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPIITHPQQ 351
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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