NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|116256340|ref|NP_001070676|]
View 

protein transport protein Sec31A isoform 3 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 3.22e-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: 3.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   13 AWSPAQNhpiYLATGtsaqqldatfSTNASLEIFELD-------LSDPSLDMKSCATFSSSHRyhkliwgpykmdskgdv 85
Cdd:cd00200    16 AFSPDGK---LLATG----------SGDGTIKVWDLEtgellrtLKGHTGPVRDVAASADGTY----------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   86 sgvLIAGGENGNIILYDPSKiiaGDKEVVIAQndkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200    66 ---LASGSSDKTIRLWDLET---GECVRTLTG---HTSYVSSVA---FSPDgrILSSSSRDKTIKVWDVETGKCLTTLRG 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  164 KTQPpedISCIAWNrQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDrlpVIQM 243
Cdd:cd00200   134 HTDW---VNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKL 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:cd00200   204 WDLS-TGKCLGTLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GS 280


                  ....*....
gi 116256340  324 FDGRISVYS 332
Cdd:cd00200   281 ADGTIRIWD 289
ACE1-Sec16-like super family cl14807
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ...
 573-696 4.68e-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: 4.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  573 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKyFAKSQSKIT---RLITAVVMKNWKEIVESC---- 644
Cdd:cd09233    69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116256340  645 -----DLKNWREALAAVLTYAKPD-EFSALCDLlgtrleneGDSLLQTQ----ACLCYICAG 696
Cdd:cd09233   147 aeaewALGNWREHLAIILSNRTSNlDLEALVEL--------GDLLAQRGlveaAHICYLLAG 200
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 793-1088 2.06e-05

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


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 49.00  E-value: 2.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   793 PVAGHESPKIPYEKQQLPKgRPGPVAGHHQMPRVQTQQYYPHGENPPPPGFIMHGNVNPNAAGQLPTSPGHMHTQVPpyp 872
Cdd:pfam03154  201 PSAPSVPPQGSPATSQPPN-QTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMP--- 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   873 qpqpyqpAQPYPFGTGGSAMyrpQQPVAPptsNAYPNTPyissassYTGQSQLYAAQHQASSPTSSPATSFPPPPSSGAS 952
Cdd:pfam03154  277 -------PMPHSLQTGPSHM---QHPVPP---QPFPLTP-------QSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQS 336

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   953 FQ----HGGPGAPPSSSAYALPPGTTGPQ----NGWNDPPALNrVPKKKKMPENFMPPvpitsPIMNPLGD--------- 1015
Cdd:pfam03154  337 QQppreQPLPPAPLSMPHIKPPPTTPIPQlpnpQSHKHPPHLS-GPSPFQMNSNLPPP-----PALKPLSSlsthhppsa 410

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  1016 --------PQSQMLQQQPSAPVPLSSQSSFPQP---HLPGGQPFHGVQQPLGQT-----GMPPSFSKPNIEGAPGAPIGN 1079
Cdd:pfam03154  411 hppplqlmPQSQQLPPPPAQPPVLTQSQSLPPPaasHPPTSGLHQVPSQSPFPQhpfvpGGPPPITPPSGPPTSTSSAMP 490


                   ....*....
gi 116256340  1080 TFQHVQSLP 1088
Cdd:pfam03154  491 GIQPPSSAS 499
 
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 3.22e-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: 3.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   13 AWSPAQNhpiYLATGtsaqqldatfSTNASLEIFELD-------LSDPSLDMKSCATFSSSHRyhkliwgpykmdskgdv 85
Cdd:cd00200    16 AFSPDGK---LLATG----------SGDGTIKVWDLEtgellrtLKGHTGPVRDVAASADGTY----------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   86 sgvLIAGGENGNIILYDPSKiiaGDKEVVIAQndkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200    66 ---LASGSSDKTIRLWDLET---GECVRTLTG---HTSYVSSVA---FSPDgrILSSSSRDKTIKVWDVETGKCLTTLRG 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  164 KTQPpedISCIAWNrQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDrlpVIQM 243
Cdd:cd00200   134 HTDW---VNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKL 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:cd00200   204 WDLS-TGKCLGTLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GS 280


                  ....*....
gi 116256340  324 FDGRISVYS 332
Cdd:cd00200   281 ADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
89-333 4.86e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 103.07  E-value: 4.86e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   89 LIAGGENGNIILYDpskiIAGDKEvvIAQNDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPp 168
Cdd:COG2319   177 LASGSDDGTVRLWD----LATGKL--LRTLTGHTGAVRSVAFS-PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGS- 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  169 edISCIAWNRQVQHiLASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPDvATQMVLASEDDRlpvIQMWDLRf 248
Cdd:COG2319   249 --VRSVAFSPDGRL-LASGSADGTVRLWDLATGELLRTLTGHSGGVN--SVAFSPD-GKLLASGSDDGT---VRLWDLA- 318

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  249 ASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRI 328
Cdd:COG2319   319 TGKLLRTLTGHTGAVRSVAFS-PDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTV 396


                  ....*
gi 116256340  329 SVYSI 333
Cdd:COG2319   397 RLWDL 401
ACE1-Sec16-like cd09233
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ...
 573-696 4.68e-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: 4.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  573 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKyFAKSQSKIT---RLITAVVMKNWKEIVESC---- 644
Cdd:cd09233    69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116256340  645 -----DLKNWREALAAVLTYAKPD-EFSALCDLlgtrleneGDSLLQTQ----ACLCYICAG 696
Cdd:cd09233   147 aeaewALGNWREHLAIILSNRTSNlDLEALVEL--------GDLLAQRGlveaAHICYLLAG 200
Sec16_C pfam12931
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal ...
 573-767 6.34e-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: 6.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   573 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKY----FAKSQSKITRLItAVVMK----NWKEIVE- 642
Cdd:pfam12931    1 IRALLLTGDREKALWLAL-DKKLwAHALLIASTLGKEKWKEVVQEFvrseFKGSNNKSGESL-AALYQvfagNSEEAVDe 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   643 --------SCDLKNWREALAAVLTYAKPDEFSALCDlLGTRLENEGdslLQTQACLCYICAG---NVEKLVACWTKAQDG 711
Cdd:pfam12931   79 lvppsknaLWALDNWRETLALVLSNRSPGDVEALLA-LGDLLAQYG---RTEAAHICFLLAGlplSQTVLLGADHVRFPS 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   712 SHPLSLQDLI--EkvvILRKAVQLTqAMDTSTVGV--LLAAKMsQYANLLAAQGSIAAAL 767
Cdd:pfam12931  155 TFGNDLESILltE---IYEYALSLS-PPQPPFVGLphLLPYKL-QHAAVLAEYGLVSEAQ 209
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 793-1088 2.06e-05

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 49.00  E-value: 2.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   793 PVAGHESPKIPYEKQQLPKgRPGPVAGHHQMPRVQTQQYYPHGENPPPPGFIMHGNVNPNAAGQLPTSPGHMHTQVPpyp 872
Cdd:pfam03154  201 PSAPSVPPQGSPATSQPPN-QTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMP--- 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   873 qpqpyqpAQPYPFGTGGSAMyrpQQPVAPptsNAYPNTPyissassYTGQSQLYAAQHQASSPTSSPATSFPPPPSSGAS 952
Cdd:pfam03154  277 -------PMPHSLQTGPSHM---QHPVPP---QPFPLTP-------QSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQS 336

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   953 FQ----HGGPGAPPSSSAYALPPGTTGPQ----NGWNDPPALNrVPKKKKMPENFMPPvpitsPIMNPLGD--------- 1015
Cdd:pfam03154  337 QQppreQPLPPAPLSMPHIKPPPTTPIPQlpnpQSHKHPPHLS-GPSPFQMNSNLPPP-----PALKPLSSlsthhppsa 410

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  1016 --------PQSQMLQQQPSAPVPLSSQSSFPQP---HLPGGQPFHGVQQPLGQT-----GMPPSFSKPNIEGAPGAPIGN 1079
Cdd:pfam03154  411 hppplqlmPQSQQLPPPPAQPPVLTQSQSLPPPaasHPPTSGLHQVPSQSPFPQhpfvpGGPPPITPPSGPPTSTSSAMP 490


                   ....*....
gi 116256340  1080 TFQHVQSLP 1088
Cdd:pfam03154  491 GIQPPSSAS 499
PHA03247 PHA03247
large tegument protein UL36; Provisional
 814-1101 3.69e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 3.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  814 PGPVAGHHQMPRVQTQQYYPhgenPPPPGFIMHGNVNPNAAGQLPTSPGH-MHTQVPPYPQPQPYQPAQPYPFGTGGSAM 892
Cdd:PHA03247 2723 PGPAAARQASPALPAAPAPP----AVPAGPATPGGPARPARPPTTAGPPApAPPAAPAAGPPRRLTRPAVASLSESRESL 2798

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  893 YRPQQPVAPPTSNAYPNTPYISSASSYTGQSQLYAAQhqassptssPATSFPPPPSSGASFQHGG---PGA-----PPSS 964
Cdd:PHA03247 2799 PSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQ---------PTAPPPPPGPPPPSLPLGGsvaPGGdvrrrPPSR 2869

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  965 SAYALPPGTTGPQNGWNDPPALNRVPKKKKMPenfmPPVPITSPIMNPLGDPQSQMLQQQPSAPVPLSSQSSFPQPHLPG 1044
Cdd:PHA03247 2870 SPAAKPAAPARPPVRRLARPAVSRSTESFALP----PDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAP 2945

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 116256340 1045 GQPFHGVQQPLGQTGMPpsfskPNIEGAPGAPIGNTFQHVQSLPTKKITKKPIPDEH 1101
Cdd:PHA03247 2946 TTDPAGAGEPSGAVPQP-----WLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLT 2997
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 203-333 7.48e-04

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 43.92  E-value: 7.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  203 PIIKVSdhsNRMHCSGLAWHPDVATQMVLASEDDrlpVIQMWDLrfASSPLRV-LENHARGILAIAWSMADPELLLSCGK 281
Cdd:PLN00181  525 PVVELA---SRSKLSGICWNSYIKSQVASSNFEG---VVQVWDV--ARSQLVTeMKEHEKRVWSIDYSSADPTLLASGSD 596

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 116256340  282 DAKILCSNPNTGEVLYELPTNTQWCFdIQWCPRNPAVLSAASFDGRISVYSI 333
Cdd:PLN00181  597 DGSVKLWSINQGVSIGTIKTKANICC-VQFPSESGRSLAFGSADHKVYYYDL 647
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 13-332 3.22e-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: 3.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   13 AWSPAQNhpiYLATGtsaqqldatfSTNASLEIFELD-------LSDPSLDMKSCATFSSSHRyhkliwgpykmdskgdv 85
Cdd:cd00200    16 AFSPDGK---LLATG----------SGDGTIKVWDLEtgellrtLKGHTGPVRDVAASADGTY----------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   86 sgvLIAGGENGNIILYDPSKiiaGDKEVVIAQndkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200    66 ---LASGSSDKTIRLWDLET---GECVRTLTG---HTSYVSSVA---FSPDgrILSSSSRDKTIKVWDVETGKCLTTLRG 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  164 KTQPpedISCIAWNrQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDrlpVIQM 243
Cdd:cd00200   134 HTDW---VNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKL 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:cd00200   204 WDLS-TGKCLGTLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GS 280


                  ....*....
gi 116256340  324 FDGRISVYS 332
Cdd:cd00200   281 ADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
89-333 4.86e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 103.07  E-value: 4.86e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   89 LIAGGENGNIILYDpskiIAGDKEvvIAQNDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPp 168
Cdd:COG2319   177 LASGSDDGTVRLWD----LATGKL--LRTLTGHTGAVRSVAFS-PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGS- 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  169 edISCIAWNRQVQHiLASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPDvATQMVLASEDDRlpvIQMWDLRf 248
Cdd:COG2319   249 --VRSVAFSPDGRL-LASGSADGTVRLWDLATGELLRTLTGHSGGVN--SVAFSPD-GKLLASGSDDGT---VRLWDLA- 318

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  249 ASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRI 328
Cdd:COG2319   319 TGKLLRTLTGHTGAVRSVAFS-PDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTV 396


                  ....*
gi 116256340  329 SVYSI 333
Cdd:COG2319   397 RLWDL 401
WD40 COG2319
WD40 repeat [General function prediction only];
89-333 1.58e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 98.44  E-value: 1.58e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   89 LIAGGENGNIILYDpskiIAGDKEVVIAQNdkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGAKTQ 166
Cdd:COG2319   135 LASGSADGTVRLWD----LATGKLLRTLTG--HSGAVTSVA---FSPDgkLLASGSDDGTVRLWDLATGKLLRTLTGHTG 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  167 PpedISCIAWNRQvQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDRlpvIQMWDL 246
Cdd:COG2319   206 A---VRSVAFSPD-GKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRS--VAFSPD-GRLLASGSADGT---VRLWDL 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  247 RfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDG 326
Cdd:COG2319   276 A-TGELLRTLTGHSGGVNSVAFS-PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLAS-GSDDG 352


                  ....*..
gi 116256340  327 RISVYSI 333
Cdd:COG2319   353 TVRLWDL 359
WD40 COG2319
WD40 repeat [General function prediction only];
121-336 2.06e-19

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 92.28  E-value: 2.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  121 HTGPVRALDVNiFQTNLVASGANESEIYIWDLnnfATPMTPGAKTQPPEDISCIAWNRQvQHILASASPSGRATVWDLRK 200
Cdd:COG2319    77 HTAAVLSVAFS-PDGRLLASASADGTVRLWDL---ATGLLLRTLTGHTGAVRSVAFSPD-GKTLASGSADGTVRLWDLAT 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  201 NEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDRlpvIQMWDLRfASSPLRVLENHARGILAIAWSmADPELLLSCG 280
Cdd:COG2319   152 GKLLRTLTGHSGAVTS--VAFSPD-GKLLASGSDDGT---VRLWDLA-TGKLLRTLTGHTGAVRSVAFS-PDGKLLASGS 223

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 116256340  281 KDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPrNPAVLSAASFDGRISVYSIMGG 336
Cdd:COG2319   224 ADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVRLWDLATG 278
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 171-337 1.71e-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: 1.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  171 ISCIAWNRQvQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMhcSGLAWHPDvATQMVLASEDDrlpVIQMWDLRfAS 250
Cdd:cd00200    12 VTCVAFSPD-GKLLATGSGDGTIKVWDLETGELLRTLKGHTGPV--RDVAASAD-GTYLASGSSDK---TIRLWDLE-TG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  251 SPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPrNPAVLSAASFDGRISV 330
Cdd:cd00200    84 ECVRTLTGHTSYVSSVAFS-PDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSP-DGTFVASSSQDGTIKL 161


                  ....*..
gi 116256340  331 YSIMGGS 337
Cdd:cd00200   162 WDLRTGK 168
WD40 COG2319
WD40 repeat [General function prediction only];
89-247 3.42e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 60.31  E-value: 3.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   89 LIAGGENGNIILYDpskiIAGDKEVVIAQNdkHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTqpp 168
Cdd:COG2319   261 LASGSADGTVRLWD----LATGELLRTLTG--HSGGVNSVAFS-PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHT--- 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  169 EDISCIAWNRQVQhILASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPD---VATqmvlASEDDRlpvIQMWD 245
Cdd:COG2319   331 GAVRSVAFSPDGK-TLASGSDDGTVRLWDLATGELLRTLTGHTGAVT--SVAFSPDgrtLAS----GSADGT---VRLWD 400


                  ..
gi 116256340  246 LR 247
Cdd:COG2319   401 LA 402
ACE1-Sec16-like cd09233
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ...
 573-696 4.68e-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: 4.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  573 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKyFAKSQSKIT---RLITAVVMKNWKEIVESC---- 644
Cdd:cd09233    69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116256340  645 -----DLKNWREALAAVLTYAKPD-EFSALCDLlgtrleneGDSLLQTQ----ACLCYICAG 696
Cdd:cd09233   147 aeaewALGNWREHLAIILSNRTSNlDLEALVEL--------GDLLAQRGlveaAHICYLLAG 200
Sec16_C pfam12931
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal ...
 573-767 6.34e-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: 6.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   573 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKY----FAKSQSKITRLItAVVMK----NWKEIVE- 642
Cdd:pfam12931    1 IRALLLTGDREKALWLAL-DKKLwAHALLIASTLGKEKWKEVVQEFvrseFKGSNNKSGESL-AALYQvfagNSEEAVDe 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   643 --------SCDLKNWREALAAVLTYAKPDEFSALCDlLGTRLENEGdslLQTQACLCYICAG---NVEKLVACWTKAQDG 711
Cdd:pfam12931   79 lvppsknaLWALDNWRETLALVLSNRSPGDVEALLA-LGDLLAQYG---RTEAAHICFLLAGlplSQTVLLGADHVRFPS 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   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 3.68e-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: 3.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  252 PLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRISVY 331
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFS-PDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLAS-GSSDKTIRLW 78


                  ....*
gi 116256340  332 SIMGG 336
Cdd:cd00200    79 DLETG 83
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 793-1088 2.06e-05

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 49.00  E-value: 2.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   793 PVAGHESPKIPYEKQQLPKgRPGPVAGHHQMPRVQTQQYYPHGENPPPPGFIMHGNVNPNAAGQLPTSPGHMHTQVPpyp 872
Cdd:pfam03154  201 PSAPSVPPQGSPATSQPPN-QTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMP--- 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   873 qpqpyqpAQPYPFGTGGSAMyrpQQPVAPptsNAYPNTPyissassYTGQSQLYAAQHQASSPTSSPATSFPPPPSSGAS 952
Cdd:pfam03154  277 -------PMPHSLQTGPSHM---QHPVPP---QPFPLTP-------QSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQS 336

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   953 FQ----HGGPGAPPSSSAYALPPGTTGPQ----NGWNDPPALNrVPKKKKMPENFMPPvpitsPIMNPLGD--------- 1015
Cdd:pfam03154  337 QQppreQPLPPAPLSMPHIKPPPTTPIPQlpnpQSHKHPPHLS-GPSPFQMNSNLPPP-----PALKPLSSlsthhppsa 410

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  1016 --------PQSQMLQQQPSAPVPLSSQSSFPQP---HLPGGQPFHGVQQPLGQT-----GMPPSFSKPNIEGAPGAPIGN 1079
Cdd:pfam03154  411 hppplqlmPQSQQLPPPPAQPPVLTQSQSLPPPaasHPPTSGLHQVPSQSPFPQhpfvpGGPPPITPPSGPPTSTSSAMP 490


                   ....*....
gi 116256340  1080 TFQHVQSLP 1088
Cdd:pfam03154  491 GIQPPSSAS 499
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 914-1101 2.07e-05

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 49.00  E-value: 2.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   914 SSASSYTGQSQLYAAQHQASSptsspatsfPPPPSSGASFQHGGPGAPPSSSAYALP----PGTTGPQNGWNDP------ 983
Cdd:pfam03154  160 SSAQQQILQTQPPVLQAQSGA---------ASPPSPPPPGTTQAATAGPTPSAPSVPpqgsPATSQPPNQTQSTaaphtl 230

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   984 ----------------PALNRVPKKKKMPENfmPPVPITSPIMNPLGDPQSQMLQQQPS--------APVPLSSQSS--- 1036
Cdd:pfam03154  231 iqqtptlhpqrlpsphPPLQPMTQPPPPSQV--SPQPLPQPSLHGQMPPMPHSLQTGPShmqhpvppQPFPLTPQSSqsq 308

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116256340  1037 ---FPQPHLPgGQPFHGVQQPLGQTgMPPSFSKPNIEGAPGAPIgnTFQHVQSLPTKKITKKPIPDEH 1101
Cdd:pfam03154  309 vppGPSPAAP-GQSQQRIHTPPSQS-QLQSQQPPREQPLPPAPL--SMPHIKPPPTTPIPQLPNPQSH 372
PHA03247 PHA03247
large tegument protein UL36; Provisional
 814-1101 3.69e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 3.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  814 PGPVAGHHQMPRVQTQQYYPhgenPPPPGFIMHGNVNPNAAGQLPTSPGH-MHTQVPPYPQPQPYQPAQPYPFGTGGSAM 892
Cdd:PHA03247 2723 PGPAAARQASPALPAAPAPP----AVPAGPATPGGPARPARPPTTAGPPApAPPAAPAAGPPRRLTRPAVASLSESRESL 2798

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  893 YRPQQPVAPPTSNAYPNTPYISSASSYTGQSQLYAAQhqassptssPATSFPPPPSSGASFQHGG---PGA-----PPSS 964
Cdd:PHA03247 2799 PSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQ---------PTAPPPPPGPPPPSLPLGGsvaPGGdvrrrPPSR 2869

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  965 SAYALPPGTTGPQNGWNDPPALNRVPKKKKMPenfmPPVPITSPIMNPLGDPQSQMLQQQPSAPVPLSSQSSFPQPHLPG 1044
Cdd:PHA03247 2870 SPAAKPAAPARPPVRRLARPAVSRSTESFALP----PDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAP 2945

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 116256340 1045 GQPFHGVQQPLGQTGMPpsfskPNIEGAPGAPIGNTFQHVQSLPTKKITKKPIPDEH 1101
Cdd:PHA03247 2946 TTDPAGAGEPSGAVPQP-----WLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLT 2997
PHA03247 PHA03247
large tegument protein UL36; Provisional
 792-1078 3.24e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 3.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  792 EPVAGHESPKIPYEKQqlpkgRPGPVAGHHQMPRVQTQQYYPHGENPPPPGF---IMHGNVNPNAAGQLPTSPGHmhTQV 868
Cdd:PHA03247 2637 EPDPHPPPTVPPPERP-----RDDPAPGRVSRPRRARRLGRAAQASSPPQRPrrrAARPTVGSLTSLADPPPPPP--TPE 2709

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  869 PPYPQPQPYQPAQPYPFGTGGSAMYRPQQPVAPPTSNA-----YPNTPYISSASS-----------------------YT 920
Cdd:PHA03247 2710 PAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGpatpgGPARPARPPTTAgppapappaapaagpprrltrpaVA 2789

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  921 GQSQLYAAQHQASSPTSSPATSFPPPPSSGASFQHGGPGAPPSSSAYALPPGTTGP------QNGWNDP--PALNRVPKK 992
Cdd:PHA03247 2790 SLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPpppslpLGGSVAPggDVRRRPPSR 2869

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  993 KKMPENFMPPVPITSPIMNPLGDPQSQMLQQQPSAPVPLSSQSSFPQPHLPGGQPFHGVQQPLGQT-GMPPSFSKPNIEG 1071
Cdd:PHA03247 2870 SPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPpPRPQPPLAPTTDP 2949


                  ....*...
gi 116256340 1072 AP-GAPIG 1078
Cdd:PHA03247 2950 AGaGEPSG 2957
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 750-1140 4.52e-04

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: 44.61  E-value: 4.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   750 MSQYANLLAAQGSIAAALAflpdNTNQPNIMQLRDRLcrAQGEPVAGHESPKIPYEKQQLPKgRPGPVAGHHQMPRVQTQ 829
Cdd:pfam09606  117 PGTASNLLASLGRPQMPMG----GAGFPSQMSRVGRM--QPGGQAGGMMQPSSGQPGSGTPN-QMGPNGGPGQGQAGGMN 189

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   830 QyyphGENPPPpgfimhGNVNPNAAGQlPTSPGHMHTQVPPYPQPQPYQPAQPYPFGTGGSAMYRPQQPVAPptsnaypn 909
Cdd:pfam09606  190 G----GQQGPM------GGQMPPQMGV-PGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQ-------- 250

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   910 TPYISSASSYTGQSQLYAAQHQASSPTSSPATSFPPPPSS-GASFQHGGPGAPPSSSAYALPP-----GTTGPQNGWNDP 983
Cdd:pfam09606  251 QGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQpGAMPNVMSIGDQNNYQQQQTRQqqqqqGGNHPAAHQQQM 330

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   984 -----PALNRVPKKKKM------PENF----MPPVPITSPIMNPLGDP------------QSQMLQQQPSAPVPLSSQSS 1036
Cdd:pfam09606  331 nqsvgQGGQVVALGGLNhletwnPGNFgglgANPMQRGQPGMMSSPSPvpgqqvrqvtpnQFMRQSPQPSVPSPQGPGSQ 410

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  1037 FPQPHLPGGQPF-HGVQQPLGQTGMPPSFSKPNIEGAPGAPIGNTFQHVQSLPTKKITKKPIPDEHLILKTTFEDLIQRC 1115
Cdd:pfam09606  411 PPQSHPGGMIPSpALIPSPSPQMSQQPAQQRTIGQDSPGGSLNTPGQSAVNSPLNPQEEQLYREKYRQLTKYIEPLKRMI 490

                          410       420
                   ....*....|....*....|....*
gi 116256340  1116 LSSATDPQTKRKLDDASKRLEFLYD 1140
Cdd:pfam09606  491 AKMENDPGDIDKMNKMKRLLEILSN 515
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 895-1121 6.38e-04

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 43.31  E-value: 6.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  895 PQQPvAPPTSNAYPNTPYISSASSYTGQSQLyAAQHQASSPTSSPATSFPPPPSSGASFQHGGPgAPPsssayALPPGTT 974
Cdd:PHA02682   37 PAAP-CPPDADVDPLDKYSVKEAGRYYQSRL-KANSACMQRPSGQSPLAPSPACAAPAPACPAC-APA-----APAPAVT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  975 GPQNGWNDPPAlnrvpkkkkmpenfmppvpiTSPIMNPlgdPQSQMLQQQPSAPVPLSSQSSFPQPHLPGGQPFHGVQQP 1054
Cdd:PHA02682  109 CPAPAPACPPA--------------------TAPTCPP---PAVCPAPARPAPACPPSTRQCPPAPPLPTPKPAPAAKPI 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116256340 1055 LGQTGMP----PSFSKPNIEGAPGApigntfqhvqslptKKITKKPIPDEHLILKTTFEDLIQRCLSSATD 1121
Cdd:PHA02682  166 FLHNQLPppdyPAASCPTIETAPAA--------------SPVLEPRIPDKIIDADNDDKDLIKKELADIAD 222
PHA03378 PHA03378
EBNA-3B; Provisional
 888-1059 6.74e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.90  E-value: 6.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  888 GGSAMYRPQQPVAPPTSNAYPNTPYISSASSYTGQSQLYAAQHQASSPTSSPATSFPPPPSSGASfqhgGPGAPPSSSAY 967
Cdd:PHA03378  647 VFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPTGANTMLPIQWAPGTMQPPPRAPTPMRPPAAPP----GRAQRPAAATG 722

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  968 ALPPGTTGPQNGWNDPPALNRVPKKKKMPENFMPPVPITSPIMNPLGDPQSQMLQQQPSA-PVPLSSQSSFPQPHLPGGQ 1046
Cdd:PHA03378  723 RARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQApPAPQQRPRGAPTPQPPPQA 802

                         170
                  ....*....|....*..
gi 116256340 1047 PFHGVQ----QPLGQTG 1059
Cdd:PHA03378  803 GPTSMQlmprAAPGQQG 819
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 822-1101 7.34e-04

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.99  E-value: 7.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   822 QMPRVQTQQYYPHGENPPPPGFIMHGNVNPNAAGQLPTSPGHMHTQVPPYPQPQPYQPAQPYPFGTG--GSAMYRPQQPV 899
Cdd:pfam03154  170 QPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTlhPQRLPSPHPPL 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   900 APPTSNAYPNTPYISSASSYTGQSQLYAAQHQASSPTSSPATSFPPPPSSGASFQHGGPGAPPSSSAYALPPGTTGPQng 979
Cdd:pfam03154  250 QPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHT-- 327

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   980 wndPPALNRVPKKKKMPENFMPPVPITSPIMNP--------LGDPQSQMLQQQPSAPVPLSSQSSFPQPhlPGGQPFHGV 1051
Cdd:pfam03154  328 ---PPSQSQLQSQQPPREQPLPPAPLSMPHIKPppttpipqLPNPQSHKHPPHLSGPSPFQMNSNLPPP--PALKPLSSL 402

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 116256340  1052 qqplgQTGMPPSFSKP---------NIEGAPGAPIGNTfqHVQSLPTKKITKKPIPDEH 1101
Cdd:pfam03154  403 -----STHHPPSAHPPplqlmpqsqQLPPPPAQPPVLT--QSQSLPPPAASHPPTSGLH 454
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 203-333 7.48e-04

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 43.92  E-value: 7.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  203 PIIKVSdhsNRMHCSGLAWHPDVATQMVLASEDDrlpVIQMWDLrfASSPLRV-LENHARGILAIAWSMADPELLLSCGK 281
Cdd:PLN00181  525 PVVELA---SRSKLSGICWNSYIKSQVASSNFEG---VVQVWDV--ARSQLVTeMKEHEKRVWSIDYSSADPTLLASGSD 596

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 116256340  282 DAKILCSNPNTGEVLYELPTNTQWCFdIQWCPRNPAVLSAASFDGRISVYSI 333
Cdd:PLN00181  597 DGSVKLWSINQGVSIGTIKTKANICC-VQFPSESGRSLAFGSADHKVYYYDL 647
PHA03247 PHA03247
large tegument protein UL36; Provisional
 894-1078 1.04e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  894 RPQQPVAPPTSNAyPNTPYISSASSytgqsqlyAAQHQASSPTSSPATSFPPPPS-SGASFQHGGPGAPPS--------- 963
Cdd:PHA03247 2585 RARRPDAPPQSAR-PRAPVDDRGDP--------RGPAPPSPLPPDTHAPDPPPPSpSPAANEPDPHPPPTVppperprdd 2655

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  964 -----------SSAYALPPGTTGPQNGWNDPPA---------LNRVPKKKKMPENfmPPVPITSPIMNPLGdPQS--QML 1021
Cdd:PHA03247 2656 papgrvsrprrARRLGRAAQASSPPQRPRRRAArptvgsltsLADPPPPPPTPEP--APHALVSATPLPPG-PAAarQAS 2732

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 116256340 1022 QQQPSAPVPLSSQSSfpqPHLPGGQpfhgvqqplGQTGMPPSFSKPNIEGAPGAPIG 1078
Cdd:PHA03247 2733 PALPAAPAPPAVPAG---PATPGGP---------ARPARPPTTAGPPAPAPPAAPAA 2777
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 1004-1170 1.10e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.54  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340 1004 PITSPIMNPLGDPQSQMLQQQPSAPVPLSSQSSFPQPHLPGGQPFHGVQQPLGQtgmPPSFSKPNIEGAPGAPIGNTFQH 1083
Cdd:PRK10263  747 PIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAP---QPQYQQPQQPVAPQPQYQQPQQP 823

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340 1084 VQSLPTKKITKKPI---PDEHLILKTTFEDLIQRCLSSATDPQTKrklddaskrLEFLYDKLREqtLSPTITSGLHNIAR 1160
Cdd:PRK10263  824 VAPQPQYQQPQQPVapqPQDTLLHPLLMRNGDSRPLHKPTTPLPS---------LDLLTPPPSE--VEPVDTFALEQMAR 892

                         170       180
                  ....*....|....*....|.
gi 116256340 1161 SIETR-----------NYSEG 1170
Cdd:PRK10263  893 LVEARladfrikadvvNYSPG 913
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 788-1045 3.46e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 41.68  E-value: 3.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   788 RAQGEPVAGHESPKIPYEKQQLPKG-------RPGPVAGHHQMPRVQTQQYYPHGENPPPpgFIMHGNVNPNAAGQLPTS 860
Cdd:pfam03154  324 RIHTPPSQSQLQSQQPPREQPLPPAplsmphiKPPPTTPIPQLPNPQSHKHPPHLSGPSP--FQMNSNLPPPPALKPLSS 401

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   861 PGHMHTQVPPYPQPQPYQPAQPYpfgtggsamyrPQQPVAPPTSNAYPNTPyiSSASSYTGQSQLyaaqHQASSPTSSPA 940
Cdd:pfam03154  402 LSTHHPPSAHPPPLQLMPQSQQL-----------PPPPAQPPVLTQSQSLP--PPAASHPPTSGL----HQVPSQSPFPQ 464

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340   941 TSFPPPPSSGASFQHGGPGAPPSSSAYALPPGTTGPQNGWNDPPAlnrvpkkkkmPENFMPPVPITSPIMNPLGDPQSQM 1020
Cdd:pfam03154  465 HPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAA----------VSCPLPPVQIKEEALDEAEEPESPP 534

                          250       260       270
                   ....*....|....*....|....*....|..
gi 116256340  1021 LQQQPSAPVPL-------SSQSSFPQPHLPGG 1045
Cdd:pfam03154  535 PPPRSPSPEPTvvntpshASQSARFYKHLDRG 566
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 902-1073 9.88e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.45  E-value: 9.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  902 PTSNAYPNTPYISSASSYTGQSQLYAAQHQASSPTSSPATSFPPPPSSGASFQ------HGGPGAPPSSSAYALPPGTTG 975
Cdd:PRK10263  309 PLLNGAPITEPVAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPTVAWQpvpgpqTGEPVIAPAPEGYPQQSQYAQ 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116256340  976 PQNGWNDPPALNRVPKKKKMPENFMPPVPITSPIMNPLGDPQSQMLQQQPSAPVPLSSQSSFPQPHLPGGQPFHGVQQPL 1055
Cdd:PRK10263  389 PAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTY 468

                         170
                  ....*....|....*....
gi 116256340 1056 GQ-TGMPPSFSKPNIEGAP 1073
Cdd:PRK10263  469 QQpAAQEPLYQQPQPVEQQ 487
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH