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Conserved domains on  [gi|152112289|sp|Q9Z2Q1|]
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RecName: Full=Protein transport protein Sec31A; AltName: Full=SEC31-like protein 1; AltName: Full=SEC31-related protein A; AltName: Full=Vesicle-associated protein 1

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 ...
 84-340 2.58e-29

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: 118.98  E-value: 2.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289   84 DVSGVLIAGGENGNIILYDPSkiiagDKEVVIAQKDkHTGPVRALDVnIFQTNLVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200    19 PDGKLLATGSGDGTIKVWDLE-----TGELLRTLKG-HTGPVRDVAA-SADGTYLASGSSDKTIRLWDLETGECVRTLTG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  164 KTQppeDISCIAWNRQvQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvaTQMVLASEDDRLpvVQM 243
Cdd:cd00200    92 HTS---YVSSVAFSPD-GRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNS--VAFSPD--GTFVASSSQDGT--IKL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPrNPAVLSAAS 323
Cdd:cd00200   162 WDLR-TGKCVATLTGHTGEVNSVAFS-PDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP-DGYLLASGS 238

                         250
                  ....*....|....*..
gi 152112289  324 FDGRIRVYSIMGGSIDG 340
Cdd:cd00200   239 EDGTIRVWDLRTGECVQ 255
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 807-1143 1.57e-09

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 62.65  E-value: 1.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  807 QPLPKGGPGPLAGHPQVsrvQSQQYYPQVRIAPTV--TTWSDRTPTALPShPPAACPSDTQGGNPPPPgfimhgnvvpnS 884
Cdd:PHA03247 2566 RSVPPPRPAPRPSEPAV---TSRARRPDAPPQSARprAPVDDRGDPRGPA-PPSPLPPDTHAPDPPPP-----------S 2630

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  885 PAPLPTSPGHMHSQPPPYPQPQPYQPAQQ-YSLGTGGSAVYRPQQPVAPPASKRYPNA-PYVSPVASYSGQP----HMYT 958
Cdd:PHA03247 2631 PSPAANEPDPHPPPTVPPPERPRDDPAPGrVSRPRRARRLGRAAQASSPPQRPRRRAArPTVGSLTSLADPPppppTPEP 2710

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  959 AQPASSPTSSSAPLPPPPSSGASFQHGGPGAPPSSSAYALP--------PGTTGTPPAASElPASQRTGPQNGWNDPPAL 1030
Cdd:PHA03247 2711 APHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPggparparPPTTAGPPAPAP-PAAPAAGPPRRLTRPAVA 2789

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289 1031 NRVPKKKKLPENFMP-----PVPITSPIMNPGGDPQPQGLQQQPSASGPRSSHASFPQPHL------AGGQPFHGIQQPL 1099
Cdd:PHA03247 2790 SLSESRESLPSPWDPadppaAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLplggsvAPGGDVRRRPPSR 2869

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 152112289 1100 AQTGMPPSFSKPNTEGAPGAPIGNTIQHvQALPTEKITKKPIPD 1143
Cdd:PHA03247 2870 SPAAKPAAPARPPVRRLARPAVSRSTES-FALPPDQPERPPQPQ 2912
ACE1-Sec16-like super family cl14807
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ...
 573-767 5.95e-09

Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat complex plays an important role in vesicular traffic of newly synthezised proteins from the endoplasmatic reticulum (ER) to the Golgi apparatus by mediating the formation of transport vesicles. COPII consists of an outer coat, made up of the scaffold proteins Sec31 and Sec13, and the cargo adaptor complex, Sec23 and Sec24, which are recruited by the small GTPase Sar1. Sec16 is involved in the early steps of the assembly process. Sec16 forms elongated heterotetramers with Sec13, Sec13-(Sec16)2-Sec13. It interacts with Sec13 by insertion of a single beta-blade to close the six-bladded beta propeller of Sec13. In the same way Sec13 interacts with Sec31 and Nup145C, a nuclear pore protein, all of these contain a structurally related ancestral coatomer element 1 (ACE1). Sec16 is believed to be a key component in maintaining the integrity of the ER exit site.


The actual alignment was detected with superfamily member cd09233:

Pssm-ID: 449359 [Multi-domain]  Cd Length: 314  Bit Score: 59.19  E-value: 5.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  573 ITRALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLAQTQKKyFAKSQSKIT---RLITAVVMKNWKEIVESC---- 644
Cdd:cd09233    69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  645 -----DLKNWREALAAVLTYAKPD-EFSALCDLlgarleseGDSLLRTQ----ACLCYICAGnverlvacwtkAQDGSNP 714
Cdd:cd09233   147 aeaewALGNWREHLAIILSNRTSNlDLEALVEL--------GDLLAQRGlveaAHICYLLAG-----------VPLGPYP 207

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  715 LS-------LQDLIEKVVILR--KAVQLT------QALDTNTVG--ALLAEKMsQYANLLAAQGSIAAAL 767
Cdd:cd09233   208 SSpsscllgGAVHNKSPRTFAtpEAIQLTeiyeyaLSLGNPQFGlpHLQPYKL-IHAARLAELGLVSEAL 276
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 84-340 2.58e-29

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: 118.98  E-value: 2.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289   84 DVSGVLIAGGENGNIILYDPSkiiagDKEVVIAQKDkHTGPVRALDVnIFQTNLVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200    19 PDGKLLATGSGDGTIKVWDLE-----TGELLRTLKG-HTGPVRDVAA-SADGTYLASGSSDKTIRLWDLETGECVRTLTG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  164 KTQppeDISCIAWNRQvQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvaTQMVLASEDDRLpvVQM 243
Cdd:cd00200    92 HTS---YVSSVAFSPD-GRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNS--VAFSPD--GTFVASSSQDGT--IKL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPrNPAVLSAAS 323
Cdd:cd00200   162 WDLR-TGKCVATLTGHTGEVNSVAFS-PDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP-DGYLLASGS 238

                         250
                  ....*....|....*..
gi 152112289  324 FDGRIRVYSIMGGSIDG 340
Cdd:cd00200   239 EDGTIRVWDLRTGECVQ 255
WD40 COG2319
WD40 repeat [General function prediction only];
89-333 7.12e-24

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 105.76  E-value: 7.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289   89 LIAGGENGNIILYDpskiIAGDKEvvIAQKDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPp 168
Cdd:COG2319   177 LASGSDDGTVRLWD----LATGKL--LRTLTGHTGAVRSVAFS-PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGS- 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  169 edISCIAWNRQVQHiLASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPDvATQMVLASEDDRlpvVQMWDLRf 248
Cdd:COG2319   249 --VRSVAFSPDGRL-LASGSADGTVRLWDLATGELLRTLTGHSGGVN--SVAFSPD-GKLLASGSDDGT---VRLWDLA- 318

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  249 ASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRI 328
Cdd:COG2319   319 TGKLLRTLTGHTGAVRSVAFS-PDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTV 396


                  ....*
gi 152112289  329 RVYSI 333
Cdd:COG2319   397 RLWDL 401
PHA03247 PHA03247
large tegument protein UL36; Provisional
 807-1143 1.57e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 62.65  E-value: 1.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  807 QPLPKGGPGPLAGHPQVsrvQSQQYYPQVRIAPTV--TTWSDRTPTALPShPPAACPSDTQGGNPPPPgfimhgnvvpnS 884
Cdd:PHA03247 2566 RSVPPPRPAPRPSEPAV---TSRARRPDAPPQSARprAPVDDRGDPRGPA-PPSPLPPDTHAPDPPPP-----------S 2630

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  885 PAPLPTSPGHMHSQPPPYPQPQPYQPAQQ-YSLGTGGSAVYRPQQPVAPPASKRYPNA-PYVSPVASYSGQP----HMYT 958
Cdd:PHA03247 2631 PSPAANEPDPHPPPTVPPPERPRDDPAPGrVSRPRRARRLGRAAQASSPPQRPRRRAArPTVGSLTSLADPPppppTPEP 2710

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  959 AQPASSPTSSSAPLPPPPSSGASFQHGGPGAPPSSSAYALP--------PGTTGTPPAASElPASQRTGPQNGWNDPPAL 1030
Cdd:PHA03247 2711 APHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPggparparPPTTAGPPAPAP-PAAPAAGPPRRLTRPAVA 2789

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289 1031 NRVPKKKKLPENFMP-----PVPITSPIMNPGGDPQPQGLQQQPSASGPRSSHASFPQPHL------AGGQPFHGIQQPL 1099
Cdd:PHA03247 2790 SLSESRESLPSPWDPadppaAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLplggsvAPGGDVRRRPPSR 2869

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 152112289 1100 AQTGMPPSFSKPNTEGAPGAPIGNTIQHvQALPTEKITKKPIPD 1143
Cdd:PHA03247 2870 SPAAKPAAPARPPVRRLARPAVSRSTES-FALPPDQPERPPQPQ 2912
ACE1-Sec16-like cd09233
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ...
 573-767 5.95e-09

Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat complex plays an important role in vesicular traffic of newly synthezised proteins from the endoplasmatic reticulum (ER) to the Golgi apparatus by mediating the formation of transport vesicles. COPII consists of an outer coat, made up of the scaffold proteins Sec31 and Sec13, and the cargo adaptor complex, Sec23 and Sec24, which are recruited by the small GTPase Sar1. Sec16 is involved in the early steps of the assembly process. Sec16 forms elongated heterotetramers with Sec13, Sec13-(Sec16)2-Sec13. It interacts with Sec13 by insertion of a single beta-blade to close the six-bladded beta propeller of Sec13. In the same way Sec13 interacts with Sec31 and Nup145C, a nuclear pore protein, all of these contain a structurally related ancestral coatomer element 1 (ACE1). Sec16 is believed to be a key component in maintaining the integrity of the ER exit site.


Pssm-ID: 187750 [Multi-domain]  Cd Length: 314  Bit Score: 59.19  E-value: 5.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  573 ITRALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLAQTQKKyFAKSQSKIT---RLITAVVMKNWKEIVESC---- 644
Cdd:cd09233    69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  645 -----DLKNWREALAAVLTYAKPD-EFSALCDLlgarleseGDSLLRTQ----ACLCYICAGnverlvacwtkAQDGSNP 714
Cdd:cd09233   147 aeaewALGNWREHLAIILSNRTSNlDLEALVEL--------GDLLAQRGlveaAHICYLLAG-----------VPLGPYP 207

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  715 LS-------LQDLIEKVVILR--KAVQLT------QALDTNTVG--ALLAEKMsQYANLLAAQGSIAAAL 767
Cdd:cd09233   208 SSpsscllgGAVHNKSPRTFAtpEAIQLTeiyeyaLSLGNPQFGlpHLQPYKL-IHAARLAELGLVSEAL 276
Sec16_C pfam12931
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal ...
 573-767 7.26e-08

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: 55.26  E-value: 7.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289   573 ITRALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLAQTQKKY----FAKSQSKITRLItAVVMK----NWKEIVE- 642
Cdd:pfam12931    1 IRALLLTGDREKALWLAL-DKKLwAHALLIASTLGKEKWKEVVQEFvrseFKGSNNKSGESL-AALYQvfagNSEEAVDe 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289   643 --------SCDLKNWREALAAVLTYAKPDEFSALCDlLGARLESEGdslLRTQACLCYICAgNVERLVACWTKAQDGSNP 714
Cdd:pfam12931   79 lvppsknaLWALDNWRETLALVLSNRSPGDVEALLA-LGDLLAQYG---RTEAAHICFLLA-GLPLSQTVLLGADHVRFP 153

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 152112289   715 LSLQDLIEkvvilrkAVQLTQ----ALDTNTVGA-------LLAEKMsQYANLLAAQGSIAAAL 767
Cdd:pfam12931  154 STFGNDLE-------SILLTEiyeyALSLSPPQPpfvglphLLPYKL-QHAAVLAEYGLVSEAQ 209
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 772-1127 3.38e-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: 51.69  E-value: 3.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289   772 DNTNQPDIVQLRDRLCRAQGRSVPGQESSRSSYEGQPLPKGGPGPLAGHPQVSRVQSQQYYPQVRIAPTVTTwSDRTPTA 851
Cdd:pfam03154  159 DSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTL-IQQTPTL 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289   852 LPSHPPAACPSDTQGGNPPPPGFI---------MHGNVVPnSPAPLPTSPGHMHSQP-----PPYPQPQPYQPAQQYSLG 917
Cdd:pfam03154  238 HPQRLPSPHPPLQPMTQPPPPSQVspqplpqpsLHGQMPP-MPHSLQTGPSHMQHPVppqpfPLTPQSSQSQVPPGPSPA 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289   918 TGGSAVYRPQQPVA--------PPASKRYPNAPYVSP---------------VASYSGQPHMYTAQPASSPTSSSAPLPP 974
Cdd:pfam03154  317 APGQSQQRIHTPPSqsqlqsqqPPREQPLPPAPLSMPhikpppttpipqlpnPQSHKHPPHLSGPSPFQMNSNLPPPPAL 396

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289   975 PPSSGASFQHGGPGAPPS----SSAYALPPgttgtPPAASELPASQRTGPQNGWNDPP--ALNRVPKKKKLPEN-FMP-- 1045
Cdd:pfam03154  397 KPLSSLSTHHPPSAHPPPlqlmPQSQQLPP-----PPAQPPVLTQSQSLPPPAASHPPtsGLHQVPSQSPFPQHpFVPgg 471

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  1046 PVPITSPiMNPGGDPQPQGLQQQPSASGPRSSHASFPQPHLAGGQPFHGIQQPLAQTGMPPSFSKPNTEGAPGAPIGNTI 1125
Cdd:pfam03154  472 PPPITPP-SGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPSPEPTVVNTP 550


                   ..
gi 152112289  1126 QH 1127
Cdd:pfam03154  551 SH 552
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 203-333 4.61e-04

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 44.69  E-value: 4.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  203 PIIKVSdhsNRMHCSGLAWHPDVATQMVLASEDDrlpVVQMWDLrfASSPLRV-LENHARGILAIAWSMADPELLLSCGK 281
Cdd:PLN00181  525 PVVELA---SRSKLSGICWNSYIKSQVASSNFEG---VVQVWDV--ARSQLVTeMKEHEKRVWSIDYSSADPTLLASGSD 596

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 152112289  282 DAKILCSNPNTGEVLYELPTNTQWCFdIQWCPRNPAVLSAASFDGRIRVYSI 333
Cdd:PLN00181  597 DGSVKLWSINQGVSIGTIKTKANICC-VQFPSESGRSLAFGSADHKVYYYDL 647
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 292-332 7.66e-03

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 35.37  E-value: 7.66e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 152112289    292 TGEVLYELPTNTQWCFDIQWCPRNPAVLSAaSFDGRIRVYS 332
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASG-SDDGTIKLWD 40
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 84-340 2.58e-29

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: 118.98  E-value: 2.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289   84 DVSGVLIAGGENGNIILYDPSkiiagDKEVVIAQKDkHTGPVRALDVnIFQTNLVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200    19 PDGKLLATGSGDGTIKVWDLE-----TGELLRTLKG-HTGPVRDVAA-SADGTYLASGSSDKTIRLWDLETGECVRTLTG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  164 KTQppeDISCIAWNRQvQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvaTQMVLASEDDRLpvVQM 243
Cdd:cd00200    92 HTS---YVSSVAFSPD-GRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNS--VAFSPD--GTFVASSSQDGT--IKL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPrNPAVLSAAS 323
Cdd:cd00200   162 WDLR-TGKCVATLTGHTGEVNSVAFS-PDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP-DGYLLASGS 238

                         250
                  ....*....|....*..
gi 152112289  324 FDGRIRVYSIMGGSIDG 340
Cdd:cd00200   239 EDGTIRVWDLRTGECVQ 255
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 13-332 2.13e-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: 107.81  E-value: 2.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289   13 AWSPAQNhpiYLATGtsaqqldatfSTNASLEIFELD-------LSDPSLDMKSCATFSSSHRyhkliwgphkmdskgdv 85
Cdd:cd00200    16 AFSPDGK---LLATG----------SGDGTIKVWDLEtgellrtLKGHTGPVRDVAASADGTY----------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289   86 sgvLIAGGENGNIILYDPSKiiagdKEVVIAQKDkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200    66 ---LASGSSDKTIRLWDLET-----GECVRTLTG-HTSYVSSVA---FSPDgrILSSSSRDKTIKVWDVETGKCLTTLRG 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  164 KTQPpedISCIAWNrQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDrlpVVQM 243
Cdd:cd00200   134 HTDW---VNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKL 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:cd00200   204 WDLS-TGKCLGTLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GS 280


                  ....*....
gi 152112289  324 FDGRIRVYS 332
Cdd:cd00200   281 ADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
89-333 7.12e-24

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 105.76  E-value: 7.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289   89 LIAGGENGNIILYDpskiIAGDKEvvIAQKDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPp 168
Cdd:COG2319   177 LASGSDDGTVRLWD----LATGKL--LRTLTGHTGAVRSVAFS-PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGS- 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  169 edISCIAWNRQVQHiLASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPDvATQMVLASEDDRlpvVQMWDLRf 248
Cdd:COG2319   249 --VRSVAFSPDGRL-LASGSADGTVRLWDLATGELLRTLTGHSGGVN--SVAFSPD-GKLLASGSDDGT---VRLWDLA- 318

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  249 ASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRI 328
Cdd:COG2319   319 TGKLLRTLTGHTGAVRSVAFS-PDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTV 396


                  ....*
gi 152112289  329 RVYSI 333
Cdd:COG2319   397 RLWDL 401
WD40 COG2319
WD40 repeat [General function prediction only];
89-333 2.63e-22

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 101.14  E-value: 2.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289   89 LIAGGENGNIILYDpskiIAGDKEvvIAQKDKHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGAKTQ 166
Cdd:COG2319   135 LASGSADGTVRLWD----LATGKL--LRTLTGHSGAVTSVA---FSPDgkLLASGSDDGTVRLWDLATGKLLRTLTGHTG 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  167 PpedISCIAWNRQvQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDRlpvVQMWDL 246
Cdd:COG2319   206 A---VRSVAFSPD-GKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRS--VAFSPD-GRLLASGSADGT---VRLWDL 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  247 RfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDG 326
Cdd:COG2319   276 A-TGELLRTLTGHSGGVNSVAFS-PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLAS-GSDDG 352


                  ....*..
gi 152112289  327 RIRVYSI 333
Cdd:COG2319   353 TVRLWDL 359
WD40 COG2319
WD40 repeat [General function prediction only];
121-338 4.60e-20

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 94.21  E-value: 4.60e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  121 HTGPVRALDVNiFQTNLVASGANESEIYIWDLnnfATPMTPGAKTQPPEDISCIAWNRQvQHILASASPSGRATVWDLRK 200
Cdd:COG2319    77 HTAAVLSVAFS-PDGRLLASASADGTVRLWDL---ATGLLLRTLTGHTGAVRSVAFSPD-GKTLASGSADGTVRLWDLAT 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  201 NEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDRlpvVQMWDLRfASSPLRVLENHARGILAIAWSmADPELLLSCG 280
Cdd:COG2319   152 GKLLRTLTGHSGAVTS--VAFSPD-GKLLASGSDDGT---VRLWDLA-TGKLLRTLTGHTGAVRSVAFS-PDGKLLASGS 223

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 152112289  281 KDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPrNPAVLSAASFDGRIRVYSIMGGSI 338
Cdd:COG2319   224 ADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVRLWDLATGEL 280
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 171-337 3.54e-17

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: 83.54  E-value: 3.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  171 ISCIAWNRQvQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMhcSGLAWHPDvATQMVLASEDDrlpVVQMWDLRfAS 250
Cdd:cd00200    12 VTCVAFSPD-GKLLATGSGDGTIKVWDLETGELLRTLKGHTGPV--RDVAASAD-GTYLASGSSDK---TIRLWDLE-TG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  251 SPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPrNPAVLSAASFDGRIRV 330
Cdd:cd00200    84 ECVRTLTGHTSYVSSVAFS-PDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSP-DGTFVASSSQDGTIKL 161


                  ....*..
gi 152112289  331 YSIMGGS 337
Cdd:cd00200   162 WDLRTGK 168
PHA03247 PHA03247
large tegument protein UL36; Provisional
 807-1143 1.57e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 62.65  E-value: 1.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  807 QPLPKGGPGPLAGHPQVsrvQSQQYYPQVRIAPTV--TTWSDRTPTALPShPPAACPSDTQGGNPPPPgfimhgnvvpnS 884
Cdd:PHA03247 2566 RSVPPPRPAPRPSEPAV---TSRARRPDAPPQSARprAPVDDRGDPRGPA-PPSPLPPDTHAPDPPPP-----------S 2630

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  885 PAPLPTSPGHMHSQPPPYPQPQPYQPAQQ-YSLGTGGSAVYRPQQPVAPPASKRYPNA-PYVSPVASYSGQP----HMYT 958
Cdd:PHA03247 2631 PSPAANEPDPHPPPTVPPPERPRDDPAPGrVSRPRRARRLGRAAQASSPPQRPRRRAArPTVGSLTSLADPPppppTPEP 2710

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  959 AQPASSPTSSSAPLPPPPSSGASFQHGGPGAPPSSSAYALP--------PGTTGTPPAASElPASQRTGPQNGWNDPPAL 1030
Cdd:PHA03247 2711 APHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPggparparPPTTAGPPAPAP-PAAPAAGPPRRLTRPAVA 2789

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289 1031 NRVPKKKKLPENFMP-----PVPITSPIMNPGGDPQPQGLQQQPSASGPRSSHASFPQPHL------AGGQPFHGIQQPL 1099
Cdd:PHA03247 2790 SLSESRESLPSPWDPadppaAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLplggsvAPGGDVRRRPPSR 2869

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 152112289 1100 AQTGMPPSFSKPNTEGAPGAPIGNTIQHvQALPTEKITKKPIPD 1143
Cdd:PHA03247 2870 SPAAKPAAPARPPVRRLARPAVSRSTES-FALPPDQPERPPQPQ 2912
ACE1-Sec16-like cd09233
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ...
 573-767 5.95e-09

Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat complex plays an important role in vesicular traffic of newly synthezised proteins from the endoplasmatic reticulum (ER) to the Golgi apparatus by mediating the formation of transport vesicles. COPII consists of an outer coat, made up of the scaffold proteins Sec31 and Sec13, and the cargo adaptor complex, Sec23 and Sec24, which are recruited by the small GTPase Sar1. Sec16 is involved in the early steps of the assembly process. Sec16 forms elongated heterotetramers with Sec13, Sec13-(Sec16)2-Sec13. It interacts with Sec13 by insertion of a single beta-blade to close the six-bladded beta propeller of Sec13. In the same way Sec13 interacts with Sec31 and Nup145C, a nuclear pore protein, all of these contain a structurally related ancestral coatomer element 1 (ACE1). Sec16 is believed to be a key component in maintaining the integrity of the ER exit site.


Pssm-ID: 187750 [Multi-domain]  Cd Length: 314  Bit Score: 59.19  E-value: 5.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  573 ITRALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLAQTQKKyFAKSQSKIT---RLITAVVMKNWKEIVESC---- 644
Cdd:cd09233    69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  645 -----DLKNWREALAAVLTYAKPD-EFSALCDLlgarleseGDSLLRTQ----ACLCYICAGnverlvacwtkAQDGSNP 714
Cdd:cd09233   147 aeaewALGNWREHLAIILSNRTSNlDLEALVEL--------GDLLAQRGlveaAHICYLLAG-----------VPLGPYP 207

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  715 LS-------LQDLIEKVVILR--KAVQLT------QALDTNTVG--ALLAEKMsQYANLLAAQGSIAAAL 767
Cdd:cd09233   208 SSpsscllgGAVHNKSPRTFAtpEAIQLTeiyeyaLSLGNPQFGlpHLQPYKL-IHAARLAELGLVSEAL 276
WD40 COG2319
WD40 repeat [General function prediction only];
89-247 1.07e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 58.77  E-value: 1.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289   89 LIAGGENGNIILYDpskiIAGDKEVVIaqKDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTqpp 168
Cdd:COG2319   261 LASGSADGTVRLWD----LATGELLRT--LTGHSGGVNSVAFS-PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHT--- 330

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 152112289  169 EDISCIAWNRQVQhILASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPDvATQMVLASEDDRlpvVQMWDLR 247
Cdd:COG2319   331 GAVRSVAFSPDGK-TLASGSDDGTVRLWDLATGELLRTLTGHTGAVT--SVAFSPD-GRTLASGSADGT---VRLWDLA 402
Sec16_C pfam12931
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal ...
 573-767 7.26e-08

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: 55.26  E-value: 7.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289   573 ITRALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLAQTQKKY----FAKSQSKITRLItAVVMK----NWKEIVE- 642
Cdd:pfam12931    1 IRALLLTGDREKALWLAL-DKKLwAHALLIASTLGKEKWKEVVQEFvrseFKGSNNKSGESL-AALYQvfagNSEEAVDe 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289   643 --------SCDLKNWREALAAVLTYAKPDEFSALCDlLGARLESEGdslLRTQACLCYICAgNVERLVACWTKAQDGSNP 714
Cdd:pfam12931   79 lvppsknaLWALDNWRETLALVLSNRSPGDVEALLA-LGDLLAQYG---RTEAAHICFLLA-GLPLSQTVLLGADHVRFP 153

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 152112289   715 LSLQDLIEkvvilrkAVQLTQ----ALDTNTVGA-------LLAEKMsQYANLLAAQGSIAAAL 767
Cdd:pfam12931  154 STFGNDLE-------SILLTEiyeyALSLSPPQPpfvglphLLPYKL-QHAAVLAEYGLVSEAQ 209
PHA03247 PHA03247
large tegument protein UL36; Provisional
 751-1120 3.42e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.94  E-value: 3.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  751 SQYANLLAAQGSIAAALAFLPDNTNQPDIVQLRDRlCRAQGRsvPGQESSrssyegqplPKGGPGPLAGHPQVSRVQS-- 828
Cdd:PHA03247 2632 SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRR-ARRLGR--AAQASS---------PPQRPRRRAARPTVGSLTSla 2699

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  829 QQYYPQVRIAPTVTTWSDRTPTAL-PSHPPAACPSDTQGGNPPPPGfimHGNVVPNSPAPLPT------SPGHMHSQPPP 901
Cdd:PHA03247 2700 DPPPPPPTPEPAPHALVSATPLPPgPAAARQASPALPAAPAPPAVP---AGPATPGGPARPARppttagPPAPAPPAAPA 2776

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  902 YPQPQPYQPAQQYSLGTGGSAVYRPQQPVAPPASKRYPNAPYVSPVASYSGQPHMYTAQPASSPTSSSAPLPPPPSsgas 981
Cdd:PHA03247 2777 AGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPL---- 2852

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  982 fqhGGPGAPPSSSAYALPPGTTGTPPAASELPASQRTGpqngwndPPALNRVPKKKKLPENFMPPVPITSPIMNPGGDPQ 1061
Cdd:PHA03247 2853 ---GGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLA-------RPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQ 2922

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 152112289 1062 PQGLQQQPSA--SGPRSSHASFPQPHLAG-GQPFHGIQQPLAQTGMPPSFSKPNTEGAPGAP 1120
Cdd:PHA03247 2923 PPPPPQPQPPppPPPRPQPPLAPTTDPAGaGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 252-336 8.19e-07

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: 52.34  E-value: 8.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  252 PLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRIRVY 331
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFS-PDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLAS-GSSDKTIRLW 78


                  ....*
gi 152112289  332 SIMGG 336
Cdd:cd00200    79 DLETG 83
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 772-1127 3.38e-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: 51.69  E-value: 3.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289   772 DNTNQPDIVQLRDRLCRAQGRSVPGQESSRSSYEGQPLPKGGPGPLAGHPQVSRVQSQQYYPQVRIAPTVTTwSDRTPTA 851
Cdd:pfam03154  159 DSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTL-IQQTPTL 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289   852 LPSHPPAACPSDTQGGNPPPPGFI---------MHGNVVPnSPAPLPTSPGHMHSQP-----PPYPQPQPYQPAQQYSLG 917
Cdd:pfam03154  238 HPQRLPSPHPPLQPMTQPPPPSQVspqplpqpsLHGQMPP-MPHSLQTGPSHMQHPVppqpfPLTPQSSQSQVPPGPSPA 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289   918 TGGSAVYRPQQPVA--------PPASKRYPNAPYVSP---------------VASYSGQPHMYTAQPASSPTSSSAPLPP 974
Cdd:pfam03154  317 APGQSQQRIHTPPSqsqlqsqqPPREQPLPPAPLSMPhikpppttpipqlpnPQSHKHPPHLSGPSPFQMNSNLPPPPAL 396

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289   975 PPSSGASFQHGGPGAPPS----SSAYALPPgttgtPPAASELPASQRTGPQNGWNDPP--ALNRVPKKKKLPEN-FMP-- 1045
Cdd:pfam03154  397 KPLSSLSTHHPPSAHPPPlqlmPQSQQLPP-----PPAQPPVLTQSQSLPPPAASHPPtsGLHQVPSQSPFPQHpFVPgg 471

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  1046 PVPITSPiMNPGGDPQPQGLQQQPSASGPRSSHASFPQPHLAGGQPFHGIQQPLAQTGMPPSFSKPNTEGAPGAPIGNTI 1125
Cdd:pfam03154  472 PPPITPP-SGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPSPEPTVVNTP 550


                   ..
gi 152112289  1126 QH 1127
Cdd:pfam03154  551 SH 552
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 203-333 4.61e-04

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 44.69  E-value: 4.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112289  203 PIIKVSdhsNRMHCSGLAWHPDVATQMVLASEDDrlpVVQMWDLrfASSPLRV-LENHARGILAIAWSMADPELLLSCGK 281
Cdd:PLN00181  525 PVVELA---SRSKLSGICWNSYIKSQVASSNFEG---VVQVWDV--ARSQLVTeMKEHEKRVWSIDYSSADPTLLASGSD 596

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 152112289  282 DAKILCSNPNTGEVLYELPTNTQWCFdIQWCPRNPAVLSAASFDGRIRVYSI 333
Cdd:PLN00181  597 DGSVKLWSINQGVSIGTIKTKANICC-VQFPSESGRSLAFGSADHKVYYYDL 647
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 292-332 7.66e-03

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 35.37  E-value: 7.66e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 152112289    292 TGEVLYELPTNTQWCFDIQWCPRNPAVLSAaSFDGRIRVYS 332
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASG-SDDGTIKLWD 40
 
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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