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Conserved domains on  [gi|755512847|ref|XP_011247863|]
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protein transport protein Sec31A isoform X11 [Mus musculus]

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 7.88e-25

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: 105.88  E-value: 7.88e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   13 AWSPAQNhpiYLATGtsaqqldatfSTNASLEIFELD-------LSDPSLDMKSCATFSSSHRyhkliwgphkmdskgdv 85
Cdd:cd00200    16 AFSPDGK---LLATG----------SGDGTIKVWDLEtgellrtLKGHTGPVRDVAASADGTY----------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   86 sgvLIAGGENGNIILYDPSKiiagdKEVVIAQKDkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200    66 ---LASGSSDKTIRLWDLET-----GECVRTLTG-HTSYVSSVA---FSPDgrILSSSSRDKTIKVWDVETGKCLTTLRG 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  164 KTQPpedISCIAWNrQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDrlpVIQM 243
Cdd:cd00200   134 HTDW---VNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKL 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  244 WDLRfASSPLRVLENHARGILAVAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:cd00200   204 WDLS-TGKCLGTLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GS 280


                  ....*....
gi 755512847  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 ...
 769-1014 2.14e-11

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: 68.26  E-value: 2.14e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   769 LPDNTNQPNIVQLRDRLCKAQGKPVSGQESSQSPYERQPLSKG--RPGPVAGHSQMPRVQTQQYYPHVRIAPTVTTWSNK 846
Cdd:pfam03154  311 PGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPhiKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNL 390

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   847 TP-------TALPSH-PPAAspsdtqgeNPPPPGFIMQGNVIPNPAAPLPTapghmpsqlpPYPQPQRPQNGWNDPP--A 916
Cdd:pfam03154  391 PPppalkplSSLSTHhPPSA--------HPPPLQLMPQSQQLPPPPAQPPV----------LTQSQSLPPPAASHPPtsG 452

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   917 LNRVPKKKKMPEN-FMP--PVPITSPIMNPSGDPQSQGLQQQPSTPgPLSSHASFPQQHLAGGQPFHGVQQPLAQTGMPP 993
Cdd:pfam03154  453 LHQVPSQSPFPQHpFVPggPPPITPPSGPPTSTSSAMPGIQPPSSA-SVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPE 531

                          250       260
                   ....*....|....*....|.
gi 755512847   994 SFSKPNTEGAPGAPIGNTIQH 1014
Cdd:pfam03154  532 SPPPPPRSPSPEPTVVNTPSH 552
ACE1-Sec16-like super family cl14807
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ...
 572-766 1.62e-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: 60.73  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  572 ITRALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLAQTQKKyFAKSQSKIT---RLITAVVMKNWREIVESC---- 643
Cdd:cd09233    69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  644 -----DLKNWREALAAVLTYAKPD-EFSALCdLLGTRLEREGDSLlrtQACLCYICAGnverlvacwtkAQDGSSPLS-- 715
Cdd:cd09233   147 aeaewALGNWREHLAIILSNRTSNlDLEALV-ELGDLLAQRGLVE---AAHICYLLAG-----------VPLGPYPSSps 211

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755512847  716 -----LQDLIEKVVILR--KAVQLT------QALDTNTVG--ALLAEKMsQYASLLAAQGSIAAAL 766
Cdd:cd09233   212 scllgGAVHNKSPRTFAtpEAIQLTeiyeyaLSLGNPQFGlpHLQPYKL-IHAARLAELGLVSEAL 276
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
 935-1101 2.03e-03

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.38  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  935 PITSPIMNPSGDPQSQGLQQQPSTPGPLSSHASFPQQHLAGGQPFHGVQQPLAQtgmPPSFSKPNTEGAPGAPIGNTIQH 1014
Cdd:PRK10263  747 PIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAP---QPQYQQPQQPVAPQPQYQQPQQP 823

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847 1015 VQALPTEKITKKPI---PEEHLILKTTFEDLIQRCLSSATDPQTKrklddaskrLEFLYDKLREqtLSPTIINGLHSIAR 1091
Cdd:PRK10263  824 VAPQPQYQQPQQPVapqPQDTLLHPLLMRNGDSRPLHKPTTPLPS---------LDLLTPPPSE--VEPVDTFALEQMAR 892

                         170       180
                  ....*....|....*....|.
gi 755512847 1092 SIETR-----------NYSEG 1101
Cdd:PRK10263  893 LVEARladfrikadvvNYSPG 913
 
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 7.88e-25

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: 105.88  E-value: 7.88e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   13 AWSPAQNhpiYLATGtsaqqldatfSTNASLEIFELD-------LSDPSLDMKSCATFSSSHRyhkliwgphkmdskgdv 85
Cdd:cd00200    16 AFSPDGK---LLATG----------SGDGTIKVWDLEtgellrtLKGHTGPVRDVAASADGTY----------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   86 sgvLIAGGENGNIILYDPSKiiagdKEVVIAQKDkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200    66 ---LASGSSDKTIRLWDLET-----GECVRTLTG-HTSYVSSVA---FSPDgrILSSSSRDKTIKVWDVETGKCLTTLRG 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  164 KTQPpedISCIAWNrQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDrlpVIQM 243
Cdd:cd00200   134 HTDW---VNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKL 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  244 WDLRfASSPLRVLENHARGILAVAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:cd00200   204 WDLS-TGKCLGTLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GS 280


                  ....*....
gi 755512847  324 FDGRISVYS 332
Cdd:cd00200   281 ADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
89-333 1.29e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 104.61  E-value: 1.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   89 LIAGGENGNIILYDpskiIAGDKEvvIAQKDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPp 168
Cdd:COG2319   177 LASGSDDGTVRLWD----LATGKL--LRTLTGHTGAVRSVAFS-PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGS- 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  169 edISCIAWNRQVQHiLASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPDvATQMVLASEDDRlpvIQMWDLRf 248
Cdd:COG2319   249 --VRSVAFSPDGRL-LASGSADGTVRLWDLATGELLRTLTGHSGGVN--SVAFSPD-GKLLASGSDDGT---VRLWDLA- 318

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  249 ASSPLRVLENHARGILAVAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRI 328
Cdd:COG2319   319 TGKLLRTLTGHTGAVRSVAFS-PDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTV 396


                  ....*
gi 755512847  329 SVYSI 333
Cdd:COG2319   397 RLWDL 401
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 769-1014 2.14e-11

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: 68.26  E-value: 2.14e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   769 LPDNTNQPNIVQLRDRLCKAQGKPVSGQESSQSPYERQPLSKG--RPGPVAGHSQMPRVQTQQYYPHVRIAPTVTTWSNK 846
Cdd:pfam03154  311 PGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPhiKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNL 390

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   847 TP-------TALPSH-PPAAspsdtqgeNPPPPGFIMQGNVIPNPAAPLPTapghmpsqlpPYPQPQRPQNGWNDPP--A 916
Cdd:pfam03154  391 PPppalkplSSLSTHhPPSA--------HPPPLQLMPQSQQLPPPPAQPPV----------LTQSQSLPPPAASHPPtsG 452

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   917 LNRVPKKKKMPEN-FMP--PVPITSPIMNPSGDPQSQGLQQQPSTPgPLSSHASFPQQHLAGGQPFHGVQQPLAQTGMPP 993
Cdd:pfam03154  453 LHQVPSQSPFPQHpFVPggPPPITPPSGPPTSTSSAMPGIQPPSSA-SVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPE 531

                          250       260
                   ....*....|....*....|.
gi 755512847   994 SFSKPNTEGAPGAPIGNTIQH 1014
Cdd:pfam03154  532 SPPPPPRSPSPEPTVVNTPSH 552
ACE1-Sec16-like cd09233
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ...
 572-766 1.62e-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: 60.73  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  572 ITRALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLAQTQKKyFAKSQSKIT---RLITAVVMKNWREIVESC---- 643
Cdd:cd09233    69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  644 -----DLKNWREALAAVLTYAKPD-EFSALCdLLGTRLEREGDSLlrtQACLCYICAGnverlvacwtkAQDGSSPLS-- 715
Cdd:cd09233   147 aeaewALGNWREHLAIILSNRTSNlDLEALV-ELGDLLAQRGLVE---AAHICYLLAG-----------VPLGPYPSSps 211

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755512847  716 -----LQDLIEKVVILR--KAVQLT------QALDTNTVG--ALLAEKMsQYASLLAAQGSIAAAL 766
Cdd:cd09233   212 scllgGAVHNKSPRTFAtpEAIQLTeiyeyaLSLGNPQFGlpHLQPYKL-IHAARLAELGLVSEAL 276
Sec16_C pfam12931
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal ...
 572-766 3.84e-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: 52.95  E-value: 3.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   572 ITRALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLAQTQKKY----FAKSQSKITRLItAVVMK----NWREIVE- 641
Cdd:pfam12931    1 IRALLLTGDREKALWLAL-DKKLwAHALLIASTLGKEKWKEVVQEFvrseFKGSNNKSGESL-AALYQvfagNSEEAVDe 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   642 --------SCDLKNWREALAAVLTYAKPDEFSALCDlLGTRLEREGdslLRTQACLCYICAgNVERLVACWTKAQDGSSP 713
Cdd:pfam12931   79 lvppsknaLWALDNWRETLALVLSNRSPGDVEALLA-LGDLLAQYG---RTEAAHICFLLA-GLPLSQTVLLGADHVRFP 153

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755512847   714 LSLQDLIEkvvilrkAVQLTQ----ALDTNTVGA-------LLAEKMsQYASLLAAQGSIAAAL 766
Cdd:pfam12931  154 STFGNDLE-------SILLTEiyeyALSLSPPQPpfvglphLLPYKL-QHAAVLAEYGLVSEAQ 209
PHA03247 PHA03247
large tegument protein UL36; Provisional
 792-1007 3.22e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.86  E-value: 3.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  792 PVSGQESSQSPYERQPLSKGRPG-PVAGHSQMPRVQTQQYYPHVRIAPTVTTWSNKTPTALPSHPPAASPsdtqgenPPP 870
Cdd:PHA03247 2775 PAAGPPRRLTRPAVASLSESRESlPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPG-------PPP 2847

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  871 PGFIMQGNVIP----------NPAAPLPTAPGHMPSQLPPYPQPQRPQNGWNDPPalnrvPKKKKMPENFMPPVPITSPI 940
Cdd:PHA03247 2848 PSLPLGGSVAPggdvrrrppsRSPAAKPAAPARPPVRRLARPAVSRSTESFALPP-----DQPERPPQPQAPPPPQPQPQ 2922

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755512847  941 MNPSGDPQSQgLQQQPSTPGPLSshasfPQQHLAG-GQPFHGVQQPLAQTGMPPSFSKPNTEGAPGAP 1007
Cdd:PHA03247 2923 PPPPPQPQPP-PPPPPRPQPPLA-----PTTDPAGaGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 935-1101 2.03e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.38  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  935 PITSPIMNPSGDPQSQGLQQQPSTPGPLSSHASFPQQHLAGGQPFHGVQQPLAQtgmPPSFSKPNTEGAPGAPIGNTIQH 1014
Cdd:PRK10263  747 PIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAP---QPQYQQPQQPVAPQPQYQQPQQP 823

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847 1015 VQALPTEKITKKPI---PEEHLILKTTFEDLIQRCLSSATDPQTKrklddaskrLEFLYDKLREqtLSPTIINGLHSIAR 1091
Cdd:PRK10263  824 VAPQPQYQQPQQPVapqPQDTLLHPLLMRNGDSRPLHKPTTPLPS---------LDLLTPPPSE--VEPVDTFALEQMAR 892

                         170       180
                  ....*....|....*....|.
gi 755512847 1092 SIETR-----------NYSEG 1101
Cdd:PRK10263  893 LVEARladfrikadvvNYSPG 913
 
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 7.88e-25

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: 105.88  E-value: 7.88e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   13 AWSPAQNhpiYLATGtsaqqldatfSTNASLEIFELD-------LSDPSLDMKSCATFSSSHRyhkliwgphkmdskgdv 85
Cdd:cd00200    16 AFSPDGK---LLATG----------SGDGTIKVWDLEtgellrtLKGHTGPVRDVAASADGTY----------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   86 sgvLIAGGENGNIILYDPSKiiagdKEVVIAQKDkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200    66 ---LASGSSDKTIRLWDLET-----GECVRTLTG-HTSYVSSVA---FSPDgrILSSSSRDKTIKVWDVETGKCLTTLRG 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  164 KTQPpedISCIAWNrQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDrlpVIQM 243
Cdd:cd00200   134 HTDW---VNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKL 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  244 WDLRfASSPLRVLENHARGILAVAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:cd00200   204 WDLS-TGKCLGTLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GS 280


                  ....*....
gi 755512847  324 FDGRISVYS 332
Cdd:cd00200   281 ADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 121-337 9.85e-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: 102.80  E-value: 9.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  121 HTGPVRALDVNIfQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPPEDISCIAWNRQvqhiLASASPSGRATVWDLRK 200
Cdd:cd00200     8 HTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTY----LASGSSDKTIRLWDLET 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  201 NEPIIKVSDHSNRMHCsgLAWHPDvaTQMVLASEDDRlpVIQMWDLRfASSPLRVLENHARGILAVAWSmADPELLLSCG 280
Cdd:cd00200    83 GECVRTLTGHTSYVSS--VAFSPD--GRILSSSSRDK--TIKVWDVE-TGKCLTTLRGHTDWVNSVAFS-PDGTFVASSS 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755512847  281 KDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSAASfDGRISVYSIMGGS 337
Cdd:cd00200   155 QDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSS-DGTIKLWDLSTGK 210
WD40 COG2319
WD40 repeat [General function prediction only];
89-333 1.29e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 104.61  E-value: 1.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   89 LIAGGENGNIILYDpskiIAGDKEvvIAQKDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPp 168
Cdd:COG2319   177 LASGSDDGTVRLWD----LATGKL--LRTLTGHTGAVRSVAFS-PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGS- 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  169 edISCIAWNRQVQHiLASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPDvATQMVLASEDDRlpvIQMWDLRf 248
Cdd:COG2319   249 --VRSVAFSPDGRL-LASGSADGTVRLWDLATGELLRTLTGHSGGVN--SVAFSPD-GKLLASGSDDGT---VRLWDLA- 318

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  249 ASSPLRVLENHARGILAVAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRI 328
Cdd:COG2319   319 TGKLLRTLTGHTGAVRSVAFS-PDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTV 396


                  ....*
gi 755512847  329 SVYSI 333
Cdd:COG2319   397 RLWDL 401
WD40 COG2319
WD40 repeat [General function prediction only];
89-333 4.41e-22

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 99.99  E-value: 4.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   89 LIAGGENGNIILYDpskiIAGDKEvvIAQKDKHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGAKTQ 166
Cdd:COG2319   135 LASGSADGTVRLWD----LATGKL--LRTLTGHSGAVTSVA---FSPDgkLLASGSDDGTVRLWDLATGKLLRTLTGHTG 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  167 PpedISCIAWNRQvQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDRlpvIQMWDL 246
Cdd:COG2319   206 A---VRSVAFSPD-GKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRS--VAFSPD-GRLLASGSADGT---VRLWDL 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  247 RfASSPLRVLENHARGILAVAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDG 326
Cdd:COG2319   276 A-TGELLRTLTGHSGGVNSVAFS-PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLAS-GSDDG 352


                  ....*..
gi 755512847  327 RISVYSI 333
Cdd:COG2319   353 TVRLWDL 359
WD40 COG2319
WD40 repeat [General function prediction only];
121-338 6.23e-20

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 93.82  E-value: 6.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  121 HTGPVRALDVNiFQTNLVASGANESEIYIWDLnnfATPMTPGAKTQPPEDISCIAWNRQvQHILASASPSGRATVWDLRK 200
Cdd:COG2319    77 HTAAVLSVAFS-PDGRLLASASADGTVRLWDL---ATGLLLRTLTGHTGAVRSVAFSPD-GKTLASGSADGTVRLWDLAT 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  201 NEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDRlpvIQMWDLRfASSPLRVLENHARGILAVAWSmADPELLLSCG 280
Cdd:COG2319   152 GKLLRTLTGHSGAVTS--VAFSPD-GKLLASGSDDGT---VRLWDLA-TGKLLRTLTGHTGAVRSVAFS-PDGKLLASGS 223

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 755512847  281 KDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPrNPAVLSAASFDGRISVYSIMGGSI 338
Cdd:COG2319   224 ADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVRLWDLATGEL 280
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 769-1014 2.14e-11

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: 68.26  E-value: 2.14e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   769 LPDNTNQPNIVQLRDRLCKAQGKPVSGQESSQSPYERQPLSKG--RPGPVAGHSQMPRVQTQQYYPHVRIAPTVTTWSNK 846
Cdd:pfam03154  311 PGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPhiKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNL 390

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   847 TP-------TALPSH-PPAAspsdtqgeNPPPPGFIMQGNVIPNPAAPLPTapghmpsqlpPYPQPQRPQNGWNDPP--A 916
Cdd:pfam03154  391 PPppalkplSSLSTHhPPSA--------HPPPLQLMPQSQQLPPPPAQPPV----------LTQSQSLPPPAASHPPtsG 452

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   917 LNRVPKKKKMPEN-FMP--PVPITSPIMNPSGDPQSQGLQQQPSTPgPLSSHASFPQQHLAGGQPFHGVQQPLAQTGMPP 993
Cdd:pfam03154  453 LHQVPSQSPFPQHpFVPggPPPITPPSGPPTSTSSAMPGIQPPSSA-SVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPE 531

                          250       260
                   ....*....|....*....|.
gi 755512847   994 SFSKPNTEGAPGAPIGNTIQH 1014
Cdd:pfam03154  532 SPPPPPRSPSPEPTVVNTPSH 552
ACE1-Sec16-like cd09233
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ...
 572-766 1.62e-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: 60.73  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  572 ITRALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLAQTQKKyFAKSQSKIT---RLITAVVMKNWREIVESC---- 643
Cdd:cd09233    69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  644 -----DLKNWREALAAVLTYAKPD-EFSALCdLLGTRLEREGDSLlrtQACLCYICAGnverlvacwtkAQDGSSPLS-- 715
Cdd:cd09233   147 aeaewALGNWREHLAIILSNRTSNlDLEALV-ELGDLLAQRGLVE---AAHICYLLAG-----------VPLGPYPSSps 211

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755512847  716 -----LQDLIEKVVILR--KAVQLT------QALDTNTVG--ALLAEKMsQYASLLAAQGSIAAAL 766
Cdd:cd09233   212 scllgGAVHNKSPRTFAtpEAIQLTeiyeyaLSLGNPQFGlpHLQPYKL-IHAARLAELGLVSEAL 276
WD40 COG2319
WD40 repeat [General function prediction only];
89-247 3.21e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 60.31  E-value: 3.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   89 LIAGGENGNIILYDpskiIAGDKEVVIaqKDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTqpp 168
Cdd:COG2319   261 LASGSADGTVRLWD----LATGELLRT--LTGHSGGVNSVAFS-PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHT--- 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  169 EDISCIAWNRQVQhILASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPD---VATqmvlASEDDRlpvIQMWD 245
Cdd:COG2319   331 GAVRSVAFSPDGK-TLASGSDDGTVRLWDLATGELLRTLTGHTGAVT--SVAFSPDgrtLAS----GSADGT---VRLWD 400


                  ..
gi 755512847  246 LR 247
Cdd:COG2319   401 LA 402
Sec16_C pfam12931
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal ...
 572-766 3.84e-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: 52.95  E-value: 3.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   572 ITRALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLAQTQKKY----FAKSQSKITRLItAVVMK----NWREIVE- 641
Cdd:pfam12931    1 IRALLLTGDREKALWLAL-DKKLwAHALLIASTLGKEKWKEVVQEFvrseFKGSNNKSGESL-AALYQvfagNSEEAVDe 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   642 --------SCDLKNWREALAAVLTYAKPDEFSALCDlLGTRLEREGdslLRTQACLCYICAgNVERLVACWTKAQDGSSP 713
Cdd:pfam12931   79 lvppsknaLWALDNWRETLALVLSNRSPGDVEALLA-LGDLLAQYG---RTEAAHICFLLA-GLPLSQTVLLGADHVRFP 153

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755512847   714 LSLQDLIEkvvilrkAVQLTQ----ALDTNTVGA-------LLAEKMsQYASLLAAQGSIAAAL 766
Cdd:pfam12931  154 STFGNDLE-------SILLTEiyeyALSLSPPQPpfvglphLLPYKL-QHAAVLAEYGLVSEAQ 209
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 789-1013 9.52e-07

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 53.23  E-value: 9.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   789 QGKPVSGQESSQSPYERQPLSKGRPGPVAGH------SQMPRVQTQQYYPHVRIA----------PTVTTWSNKTPTALP 852
Cdd:pfam03154  250 QPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHslqtgpSHMQHPVPPQPFPLTPQSsqsqvppgpsPAAPGQSQQRIHTPP 329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   853 SHPPAASPSDTQgENPPPPGFIMQGNVIPNPAAPLPTAPghmpsqlppypqpqrPQNGWNDPPALNrVPKKKKMPENfMP 932
Cdd:pfam03154  330 SQSQLQSQQPPR-EQPLPPAPLSMPHIKPPPTTPIPQLP---------------NPQSHKHPPHLS-GPSPFQMNSN-LP 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   933 PVPITSPIMN------PSGDP-------QSQGLQ----------QQPSTPGPLSSHASFPQQHLAGGQPfhgvqqPLAQ- 988
Cdd:pfam03154  392 PPPALKPLSSlsthhpPSAHPpplqlmpQSQQLPpppaqppvltQSQSLPPPAASHPPTSGLHQVPSQS------PFPQh 465

                          250       260
                   ....*....|....*....|....*...
gi 755512847   989 ---TGMPPSFSKPNTEGAPGAPIGNTIQ 1013
Cdd:pfam03154  466 pfvPGGPPPITPPSGPPTSTSSAMPGIQ 493
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 794-1032 1.49e-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: 52.46  E-value: 1.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   794 SGQESSQSPYERQPLSKGRPGPVAGHSQMPRVQTQQyyphvriAPTVTTWSNKTPTALPSHPPAASPSDTQGENPPPPGF 873
Cdd:pfam03154  158 SDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQ-------AATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTL 230

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   874 IMQGNV-----IPNPAAPLPTAPGHMPSQLPPYPQPQRPQNGWNDPPalnrVPKKKKMPENFMP-PVPiTSPIMNPSGDP 947
Cdd:pfam03154  231 IQQTPTlhpqrLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPP----MPHSLQTGPSHMQhPVP-PQPFPLTPQSS 305

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   948 QSQGlqqqPSTPGPLSSHASFPQQHLAGGQPFHGVQQPLAQTGMPPsfskpntegapgAPIgnTIQHVQALPTEKITKKP 1027
Cdd:pfam03154  306 QSQV----PPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPP------------APL--SMPHIKPPPTTPIPQLP 367


                   ....*
gi 755512847  1028 IPEEH 1032
Cdd:pfam03154  368 NPQSH 372
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 252-336 2.34e-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: 50.80  E-value: 2.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  252 PLRVLENHARGILAVAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRISVY 331
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFS-PDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLAS-GSSDKTIRLW 78


                  ....*
gi 755512847  332 SIMGG 336
Cdd:cd00200    79 DLETG 83
PHA03247 PHA03247
large tegument protein UL36; Provisional
 792-1007 3.22e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.86  E-value: 3.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  792 PVSGQESSQSPYERQPLSKGRPG-PVAGHSQMPRVQTQQYYPHVRIAPTVTTWSNKTPTALPSHPPAASPsdtqgenPPP 870
Cdd:PHA03247 2775 PAAGPPRRLTRPAVASLSESRESlPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPG-------PPP 2847

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  871 PGFIMQGNVIP----------NPAAPLPTAPGHMPSQLPPYPQPQRPQNGWNDPPalnrvPKKKKMPENFMPPVPITSPI 940
Cdd:PHA03247 2848 PSLPLGGSVAPggdvrrrppsRSPAAKPAAPARPPVRRLARPAVSRSTESFALPP-----DQPERPPQPQAPPPPQPQPQ 2922

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755512847  941 MNPSGDPQSQgLQQQPSTPGPLSshasfPQQHLAG-GQPFHGVQQPLAQTGMPPSFSKPNTEGAPGAP 1007
Cdd:PHA03247 2923 PPPPPQPQPP-PPPPPRPQPPLA-----PTTDPAGaGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
PHA03379 PHA03379
EBNA-3A; Provisional
 791-1029 8.52e-05

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 46.98  E-value: 8.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  791 KPVSGQESSQSPYERQ------PLSKGRPGPVAGHS---QMPRV-QTQQYYPHVRIAPT---VTTWSnKTPTALPSHPPA 857
Cdd:PHA03379  444 EPPPVHDLEPGPLHDQhsmapcPVAQLPPGPLQDLEpgdQLPGVvQDGRPACAPVPAPAgpiVRPWE-ASLSQVPGVAFA 522

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  858 A-SPSDTQGENPPPPGFIMQGNVIPNPAAPLPTAPGHMPSQLPPYPQpqrpqngWNDPPALNRVPKkkkmpenfmPPVPI 936
Cdd:PHA03379  523 PvMPQPMPVEPVPVPTVALERPVCPAPPLIAMQGPGETSGIVRVRER-------WRPAPWTPNPPR---------SPSQM 586

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  937 TSPIMNPSGDPQSQGLQQ----QP------STPGPLsSHASFPQQHLAGGQPFHGVQQPLAQTGM----PPSFS----KP 998
Cdd:PHA03379  587 SVRDRLARLRAEAQPYQAsvevQPpqltqvSPQQPM-EYPLEPEQQMFPGSPFSQVADVMRAGGVpamqPQYFDlplqQP 665

                         250       260       270
                  ....*....|....*....|....*....|.
gi 755512847  999 NTEGAPGAPIGNTIQHVQALPTEKITKKPIP 1029
Cdd:PHA03379  666 ISQGAPLAPLRASMGPVPPVPATQPQYFDIP 696
PHA03247 PHA03247
large tegument protein UL36; Provisional
 792-1033 1.81e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  792 PVSGQESSQSPYERQPLSKGRPGPVAGHSQMPRVQTQQYYPHVRIAPTV-----TTWSNKTPTALPSHPPAASPSDT-QG 865
Cdd:PHA03247 2702 PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATpggpaRPARPPTTAGPPAPAPPAAPAAGpPR 2781

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  866 ENPPPPGFIMQGNVIPNPAAPLPTAPGHMPSQLPPYPQPQRPQNGwNDPPALNRVPKKKKMPENFMPPVPITSPIMNPSG 945
Cdd:PHA03247 2782 RLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAG-PLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGG 2860

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  946 DPQSQGLQQQPSTPGPLSSHAsfPQQHLAGGQPfhgVQQPLAQTGMPPSFSKPNTEGAPGAPIGNTIQHVQALPTEKITK 1025
Cdd:PHA03247 2861 DVRRRPPSRSPAAKPAAPARP--PVRRLARPAV---SRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP 2935


                  ....*...
gi 755512847 1026 KPIPEEHL 1033
Cdd:PHA03247 2936 PPRPQPPL 2943
PHA03378 PHA03378
EBNA-3B; Provisional
 800-1017 3.57e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 44.67  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  800 QSPYERQPLSKGRPGPvAGHSQMPRVQTqqyyphvriAPTVTTWSNKTPTalPSHPPAASPSDTQ------GENPPP--- 870
Cdd:PHA03378  663 KPTWTQIGHIPYQPSP-TGANTMLPIQW---------APGTMQPPPRAPT--PMRPPAAPPGRAQrpaaatGRARPPaaa 730

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  871 PGFIMQGNVIPNPAAPLPTAPGHMPSQLPPYPQPqrpqngwndPPALNRVPKKKKMPENFMPPVPITSPIMNPSGDPQSQ 950
Cdd:PHA03378  731 PGRARPPAAAPGRARPPAAAPGRARPPAAAPGRA---------RPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQPPPQ 801

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755512847  951 GLQQQPSTPGPLSSHASFPQQHLAGGQPFHGVQQPLAQTGMPPSFSKPNTEGAPGAPIGNTIQH-VQA 1017
Cdd:PHA03378  802 AGPTSMQLMPRAAPGQQGPTKQILRQLLTGGVKRGRPSLKKPAALERQAAAGPTPSPGSGTSDKiVQA 869
PHA03247 PHA03247
large tegument protein UL36; Provisional
 813-1009 6.62e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 6.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  813 PGP-VAGHSQMPRVQTQQYYPHVRIAPtvttwsnKTPTALPShPPAASPSDTQGENPPPPGFIMQGNVIPNP---AAPLP 888
Cdd:PHA03247 2578 SEPaVTSRARRPDAPPQSARPRAPVDD-------RGDPRGPA-PPSPLPPDTHAPDPPPPSPSPAANEPDPHpppTVPPP 2649

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  889 TAPGHMPSQLPPYPQPQRPQNGwndPPALNRVPKKKKMPENFMPPV-PITS----PIMNPSGDPQSQGLQQQ-PSTPGPL 962
Cdd:PHA03247 2650 ERPRDDPAPGRVSRPRRARRLG---RAAQASSPPQRPRRRAARPTVgSLTSladpPPPPPTPEPAPHALVSAtPLPPGPA 2726

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755512847  963 SSHASFPQQHLAGGQPF--HGVQQPLAQT--GMPPSFSKPNTEGAPGAPIG 1009
Cdd:PHA03247 2727 AARQASPALPAAPAPPAvpAGPATPGGPArpARPPTTAGPPAPAPPAAPAA 2777
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 788-1071 1.22e-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: 43.07  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   788 AQGKPVSGQESSQSPYERQPlsKGRPGPVAGHSQMPRVQTQQYYPHVRIAPTVTTWSNKTPTALPSHPPAASPSDTQGEN 867
Cdd:pfam09606  206 VPGMPGPADAGAQMGQQAQA--NGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQP 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   868 PPPPGfIMQGNVIPNPAAPLPTAP------------GHMPSQLPPYPQPQRPQNGWNDPPALNRVPKKKKMPENF----M 931
Cdd:pfam09606  284 MGPPG-QQPGAMPNVMSIGDQNNYqqqqtrqqqqqqGGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFgglgA 362

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   932 PPVPITSPIMNPSGDP----------QSQGLQQ--QPSTPGPLSSHASFPQQHLAGGQPF-HGVQQPLAQTG-MPPSFSK 997
Cdd:pfam09606  363 NPMQRGQPGMMSSPSPvpgqqvrqvtPNQFMRQspQPSVPSPQGPGSQPPQSHPGGMIPSpALIPSPSPQMSqQPAQQRT 442

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847   998 PNTEGaPGAPIGNTIQ---------HVQALPTEK---ITKKPIPEEHLILKttfedlIQRclssatDPQTKRKLDDASKR 1065
Cdd:pfam09606  443 IGQDS-PGGSLNTPGQsavnsplnpQEEQLYREKyrqLTKYIEPLKRMIAK------MEN------DPGDIDKMNKMKRL 509


                   ....*.
gi 755512847  1066 LEFLYD 1071
Cdd:pfam09606  510 LEILSN 515
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 935-1101 2.03e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.38  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847  935 PITSPIMNPSGDPQSQGLQQQPSTPGPLSSHASFPQQHLAGGQPFHGVQQPLAQtgmPPSFSKPNTEGAPGAPIGNTIQH 1014
Cdd:PRK10263  747 PIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAP---QPQYQQPQQPVAPQPQYQQPQQP 823

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512847 1015 VQALPTEKITKKPI---PEEHLILKTTFEDLIQRCLSSATDPQTKrklddaskrLEFLYDKLREqtLSPTIINGLHSIAR 1091
Cdd:PRK10263  824 VAPQPQYQQPQQPVapqPQDTLLHPLLMRNGDSRPLHKPTTPLPS---------LDLLTPPPSE--VEPVDTFALEQMAR 892

                         170       180
                  ....*....|....*....|.
gi 755512847 1092 SIETR-----------NYSEG 1101
Cdd:PRK10263  893 LVEARladfrikadvvNYSPG 913
 
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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