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Conserved domains on  [gi|1622939758|ref|XP_014993894|]
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protein transport protein Sec31A isoform X9 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 13-332 3.26e-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: 3.26e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758   13 AWSPAQNhpiYLATGtsaqqldatfSTNASLEIFELD-------LSDPSLDMKSCATFSSSHRyhkliwgpykmdskgdv 85
Cdd:cd00200     16 AFSPDGK---LLATG----------SGDGTIKVWDLEtgellrtLKGHTGPVRDVAASADGTY----------------- 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758   86 sgvLIAGGENGNIILYDPSKiiaGDKEVVIAQndkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200     66 ---LASGSSDKTIRLWDLET---GECVRTLTG---HTSYVSSVA---FSPDgrILSSSSRDKTIKVWDVETGKCLTTLRG 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  164 KTQPpedISCIAWNrQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDiATQMVLASEDDrlpVIQM 243
Cdd:cd00200    134 HTDW---VNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKL 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:cd00200    204 WDLS-TGKCLGTLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GS 280


                   ....*....
gi 1622939758  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 4.75e-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: 4.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  573 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKyFAKSQSKIT---RLITAVVMKNWKEIVESC---- 644
Cdd:cd09233     69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622939758  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 ...
 943-1115 2.96e-07

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


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 55.16  E-value: 2.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  943 PPPPSSGASFQHGGPGAPPSSSAYALPPGTTgtlPAASELPASQRT--GPQNGWNDPPALN--RVPK--------KKKTP 1010
Cdd:pfam03154  181 ASPPSPPPPGTTQAATAGPTPSAPSVPPQGS---PATSQPPNQTQStaAPHTLIQQTPTLHpqRLPSphpplqpmTQPPP 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758 1011 ENFMPPVPITSPIMNPLGDPQSQMLQQQPS--------APIPLSSQSS------FPQPHLSgGQPFHGIQQPLGQTgMPP 1076
Cdd:pfam03154  258 PSQVSPQPLPQPSLHGQMPPMPHSLQTGPShmqhpvppQPFPLTPQSSqsqvppGPSPAAP-GQSQQRIHTPPSQS-QLQ 335

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1622939758 1077 SFSKPNIEGAPGAPIgnTFQHVQSLPTKKITKKPIPDEH 1115
Cdd:pfam03154  336 SQQPPREQPLPPAPL--SMPHIKPPPTTPIPQLPNPQSH 372
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 751-1092 5.01e-07

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.56  E-value: 5.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  751 SQYANLLAAQGSIAAALAFLPDNTNQPNIVQLRDRlCRAQGEPVAGHESPKIPYekqqlPKGRPGPVGhhqmPRVQTQQY 830
Cdd:PHA03247  2632 SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRR-ARRLGRAAQASSPPQRPR-----RRAARPTVG----SLTSLADP 2701

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  831 YPHGENPPPPgfimhgnvNPNAAGQLPTSPGhmhTQVPPYPQPQPYQPAQPYPFGTGGSAMYRPQQPVAPPTSnAYPNTP 910
Cdd:PHA03247  2702 PPPPPTPEPA--------PHALVSATPLPPG---PAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTT-AGPPAP 2769

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  911 YISSASSYSGQSQLYAAQHQASSPTSSPATSFPPPPSSGASFQHGGPGAPPSSSAYALPPGTTGTLPAASELPA--SQRT 988
Cdd:PHA03247  2770 APPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPgpPPPS 2849

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  989 GPQNGWNDP--PALNRVPKKKKTPENFMPPVPITSPIMNPLGDPQSQMLQQQPSAPIPLSSQSSFPQPHLSGGQPFHGIQ 1066
Cdd:PHA03247  2850 LPLGGSVAPggDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQP 2929

                          330       340
                   ....*....|....*....|....*...
gi 1622939758 1067 QPLGQT-GMPPSFSKPNIEGAP-GAPIG 1092
Cdd:PHA03247  2930 QPPPPPpPRPQPPLAPTTDPAGaGEPSG 2957
 
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 3.26e-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: 3.26e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758   13 AWSPAQNhpiYLATGtsaqqldatfSTNASLEIFELD-------LSDPSLDMKSCATFSSSHRyhkliwgpykmdskgdv 85
Cdd:cd00200     16 AFSPDGK---LLATG----------SGDGTIKVWDLEtgellrtLKGHTGPVRDVAASADGTY----------------- 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758   86 sgvLIAGGENGNIILYDPSKiiaGDKEVVIAQndkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200     66 ---LASGSSDKTIRLWDLET---GECVRTLTG---HTSYVSSVA---FSPDgrILSSSSRDKTIKVWDVETGKCLTTLRG 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  164 KTQPpedISCIAWNrQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDiATQMVLASEDDrlpVIQM 243
Cdd:cd00200    134 HTDW---VNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKL 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:cd00200    204 WDLS-TGKCLGTLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GS 280


                   ....*....
gi 1622939758  324 FDGRISVYS 332
Cdd:cd00200    281 ADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
89-333 4.93e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 103.07  E-value: 4.93e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758   89 LIAGGENGNIILYDpskiIAGDKEvvIAQNDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPp 168
Cdd:COG2319    177 LASGSDDGTVRLWD----LATGKL--LRTLTGHTGAVRSVAFS-PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGS- 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  169 edISCIAWNRQVQHiLASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPDiATQMVLASEDDRlpvIQMWDLRf 248
Cdd:COG2319    249 --VRSVAFSPDGRL-LASGSADGTVRLWDLATGELLRTLTGHSGGVN--SVAFSPD-GKLLASGSDDGT---VRLWDLA- 318

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  249 ASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRI 328
Cdd:COG2319    319 TGKLLRTLTGHTGAVRSVAFS-PDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTV 396


                   ....*
gi 1622939758  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 4.75e-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: 4.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  573 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKyFAKSQSKIT---RLITAVVMKNWKEIVESC---- 644
Cdd:cd09233     69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622939758  645 -----DLKNWREALAAVLTYAKPD-EFSALCDLlgtrleneGDSLLQTQ----ACLCYICAG 696
Cdd:cd09233    147 aeaewALGNWREHLAIILSNRTSNlDLEALVEL--------GDLLAQRGlveaAHICYLLAG 200
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 943-1115 2.96e-07

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 55.16  E-value: 2.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  943 PPPPSSGASFQHGGPGAPPSSSAYALPPGTTgtlPAASELPASQRT--GPQNGWNDPPALN--RVPK--------KKKTP 1010
Cdd:pfam03154  181 ASPPSPPPPGTTQAATAGPTPSAPSVPPQGS---PATSQPPNQTQStaAPHTLIQQTPTLHpqRLPSphpplqpmTQPPP 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758 1011 ENFMPPVPITSPIMNPLGDPQSQMLQQQPS--------APIPLSSQSS------FPQPHLSgGQPFHGIQQPLGQTgMPP 1076
Cdd:pfam03154  258 PSQVSPQPLPQPSLHGQMPPMPHSLQTGPShmqhpvppQPFPLTPQSSqsqvppGPSPAAP-GQSQQRIHTPPSQS-QLQ 335

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1622939758 1077 SFSKPNIEGAPGAPIgnTFQHVQSLPTKKITKKPIPDEH 1115
Cdd:pfam03154  336 SQQPPREQPLPPAPL--SMPHIKPPPTTPIPQLPNPQSH 372
PHA03247 PHA03247
large tegument protein UL36; Provisional
 751-1092 5.01e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.56  E-value: 5.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  751 SQYANLLAAQGSIAAALAFLPDNTNQPNIVQLRDRlCRAQGEPVAGHESPKIPYekqqlPKGRPGPVGhhqmPRVQTQQY 830
Cdd:PHA03247  2632 SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRR-ARRLGRAAQASSPPQRPR-----RRAARPTVG----SLTSLADP 2701

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  831 YPHGENPPPPgfimhgnvNPNAAGQLPTSPGhmhTQVPPYPQPQPYQPAQPYPFGTGGSAMYRPQQPVAPPTSnAYPNTP 910
Cdd:PHA03247  2702 PPPPPTPEPA--------PHALVSATPLPPG---PAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTT-AGPPAP 2769

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  911 YISSASSYSGQSQLYAAQHQASSPTSSPATSFPPPPSSGASFQHGGPGAPPSSSAYALPPGTTGTLPAASELPA--SQRT 988
Cdd:PHA03247  2770 APPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPgpPPPS 2849

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  989 GPQNGWNDP--PALNRVPKKKKTPENFMPPVPITSPIMNPLGDPQSQMLQQQPSAPIPLSSQSSFPQPHLSGGQPFHGIQ 1066
Cdd:PHA03247  2850 LPLGGSVAPggDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQP 2929

                          330       340
                   ....*....|....*....|....*...
gi 1622939758 1067 QPLGQT-GMPPSFSKPNIEGAP-GAPIG 1092
Cdd:PHA03247  2930 QPPPPPpPRPQPPLAPTTDPAGaGEPSG 2957
Sec16_C pfam12931
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal ...
 573-767 6.60e-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: 52.18  E-value: 6.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  573 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKY----FAKSQSKITRLItAVVMK----NWKEIVE- 642
Cdd:pfam12931    1 IRALLLTGDREKALWLAL-DKKLwAHALLIASTLGKEKWKEVVQEFvrseFKGSNNKSGESL-AALYQvfagNSEEAVDe 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  643 --------SCDLKNWREALAAVLTYAKPDEFSALCDlLGTRLENEGdslLQTQACLCYICAG---NVEKLVACWTKAQDG 711
Cdd:pfam12931   79 lvppsknaLWALDNWRETLALVLSNRSPGDVEALLA-LGDLLAQYG---RTEAAHICFLLAGlplSQTVLLGADHVRFPS 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  712 SHPLSLQDLI--EkvvILRKAVQLTqAMDTSTVGV--LLAAKMsQYANLLAAQGSIAAAL 767
Cdd:pfam12931  155 TFGNDLESILltE---IYEYALSLS-PPQPPFVGLphLLPYKL-QHAAVLAEYGLVSEAQ 209
PHA03247 PHA03247
large tegument protein UL36; Provisional
 893-1090 5.65e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 5.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  893 RPQQPVAPPTSnAYPNTPyissassysgqsqlyaaqhqassptSSPATSFPPPPSSGASFQHGGPGA--PPSSSAYALPp 970
Cdd:PHA03247  2823 SPAGPLPPPTS-AQPTAP-------------------------PPPPGPPPPSLPLGGSVAPGGDVRrrPPSRSPAAKP- 2875

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  971 gTTGTLPAASELPASQRTGPQNGWNDPPAlnrVPKKKKTPENFMPPVPITSPIMNPLGDPQSQMlQQQPSAPIPlssqss 1050
Cdd:PHA03247  2876 -AAPARPPVRRLARPAVSRSTESFALPPD---QPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP-PPRPQPPLA------ 2944

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1622939758 1051 fPQPHLSG-GQPFHGIQQPLGQTGMPPSFSKPNIEGAPGAP 1090
Cdd:PHA03247  2945 -PTTDPAGaGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 203-333 4.08e-04

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 44.69  E-value: 4.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  203 PIIKVSdhsNRMHCSGLAWHPDIATQMVLASEDDrlpVIQMWDLrfASSPLRV-LENHARGILAIAWSMADPELLLSCGK 281
Cdd:PLN00181   525 PVVELA---SRSKLSGICWNSYIKSQVASSNFEG---VVQVWDV--ARSQLVTeMKEHEKRVWSIDYSSADPTLLASGSD 596

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622939758  282 DAKILCSNPNTGEVLYELPTNTQWCFdIQWCPRNPAVLSAASFDGRISVYSI 333
Cdd:PLN00181   597 DGSVKLWSINQGVSIGTIKTKANICC-VQFPSESGRSLAFGSADHKVYYYDL 647
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 750-1154 1.60e-03

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 42.69  E-value: 1.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  750 MSQYANLLAAQGSIAAALAFLPDNTNQPNIVQLrdrlcrAQGEPVAGHESPKIPYEKQQLPKgRPGPVGHHQMPrvQTQQ 829
Cdd:pfam09606  117 PGTASNLLASLGRPQMPMGGAGFPSQMSRVGRM------QPGGQAGGMMQPSSGQPGSGTPN-QMGPNGGPGQG--QAGG 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  830 YYPHGENPPppgfimhGNVNPNAAGQlPTSPGHMHTQVPPYPQPQPYQPAQPYPfgTGGSAMYRPQQPvAPPTSNAYPNt 909
Cdd:pfam09606  188 MNGGQQGPM-------GGQMPPQMGV-PGMPGPADAGAQMGQQAQANGGMNPQQ--MGGAPNQVAMQQ-QQPQQQGQQS- 255

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  910 pyiSSASSYSGQSQLYAAQHQASSPTSSPATSFPPPPSSGASFQHGGPGAPPSSSAYALPP---GTTGTLPAASELPASQ 986
Cdd:pfam09606  256 ---QLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQqqqQQGGNHPAAHQQQMNQ 332

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  987 ------RTGPQNGWNDPPALNRV--------PKKKKTPENFMPPVPITSPIMNPLGDPQSQMLQQQPSAPIPLSSQSSFP 1052
Cdd:pfam09606  333 svgqggQVVALGGLNHLETWNPGnfgglganPMQRGQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGPGSQPP 412

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758 1053 QPHLSGGQPF-HGIQQPLGQTGMPPSFSKPNIEGAPGAPIGNTFQHVQSLPTKKITKKPIPDEHLILKTTFEDLIQRCLS 1131
Cdd:pfam09606  413 QSHPGGMIPSpALIPSPSPQMSQQPAQQRTIGQDSPGGSLNTPGQSAVNSPLNPQEEQLYREKYRQLTKYIEPLKRMIAK 492

                          410       420
                   ....*....|....*....|...
gi 1622939758 1132 SATDPQTKRKLDDASKRLEFLYD 1154
Cdd:pfam09606  493 MENDPGDIDKMNKMKRLLEILSN 515
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 13-332 3.26e-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: 3.26e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758   13 AWSPAQNhpiYLATGtsaqqldatfSTNASLEIFELD-------LSDPSLDMKSCATFSSSHRyhkliwgpykmdskgdv 85
Cdd:cd00200     16 AFSPDGK---LLATG----------SGDGTIKVWDLEtgellrtLKGHTGPVRDVAASADGTY----------------- 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758   86 sgvLIAGGENGNIILYDPSKiiaGDKEVVIAQndkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200     66 ---LASGSSDKTIRLWDLET---GECVRTLTG---HTSYVSSVA---FSPDgrILSSSSRDKTIKVWDVETGKCLTTLRG 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  164 KTQPpedISCIAWNrQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDiATQMVLASEDDrlpVIQM 243
Cdd:cd00200    134 HTDW---VNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKL 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:cd00200    204 WDLS-TGKCLGTLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GS 280


                   ....*....
gi 1622939758  324 FDGRISVYS 332
Cdd:cd00200    281 ADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
89-333 4.93e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 103.07  E-value: 4.93e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758   89 LIAGGENGNIILYDpskiIAGDKEvvIAQNDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPp 168
Cdd:COG2319    177 LASGSDDGTVRLWD----LATGKL--LRTLTGHTGAVRSVAFS-PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGS- 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  169 edISCIAWNRQVQHiLASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPDiATQMVLASEDDRlpvIQMWDLRf 248
Cdd:COG2319    249 --VRSVAFSPDGRL-LASGSADGTVRLWDLATGELLRTLTGHSGGVN--SVAFSPD-GKLLASGSDDGT---VRLWDLA- 318

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  249 ASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRI 328
Cdd:COG2319    319 TGKLLRTLTGHTGAVRSVAFS-PDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTV 396


                   ....*
gi 1622939758  329 SVYSI 333
Cdd:COG2319    397 RLWDL 401
WD40 COG2319
WD40 repeat [General function prediction only];
89-333 1.35e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 98.83  E-value: 1.35e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758   89 LIAGGENGNIILYDpskiIAGDKEVVIAQNdkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGAKTQ 166
Cdd:COG2319    135 LASGSADGTVRLWD----LATGKLLRTLTG--HSGAVTSVA---FSPDgkLLASGSDDGTVRLWDLATGKLLRTLTGHTG 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  167 PpedISCIAWNRQvQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPD---IATqmvlASEDDRlpvIQM 243
Cdd:COG2319    206 A---VRSVAFSPD-GKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRS--VAFSPDgrlLAS----GSADGT---VRL 272

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:COG2319    273 WDLA-TGELLRTLTGHSGGVNSVAFS-PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLAS-GS 349

                          250
                   ....*....|
gi 1622939758  324 FDGRISVYSI 333
Cdd:COG2319    350 DDGTVRLWDL 359
WD40 COG2319
WD40 repeat [General function prediction only];
121-336 2.05e-19

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 92.28  E-value: 2.05e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  121 HTGPVRALDVNiFQTNLVASGANESEIYIWDLnnfATPMTPGAKTQPPEDISCIAWNRQvQHILASASPSGRATVWDLRK 200
Cdd:COG2319     77 HTAAVLSVAFS-PDGRLLASASADGTVRLWDL---ATGLLLRTLTGHTGAVRSVAFSPD-GKTLASGSADGTVRLWDLAT 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  201 NEPIIKVSDHSNRMHCsgLAWHPD---IATqmvlASEDDRlpvIQMWDLRfASSPLRVLENHARGILAIAWSmADPELLL 277
Cdd:COG2319    152 GKLLRTLTGHSGAVTS--VAFSPDgklLAS----GSDDGT---VRLWDLA-TGKLLRTLTGHTGAVRSVAFS-PDGKLLA 220

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622939758  278 SCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPrNPAVLSAASFDGRISVYSIMGG 336
Cdd:COG2319    221 SGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVRLWDLATG 278
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 171-337 1.73e-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: 1.73e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  171 ISCIAWNRQvQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMhcSGLAWHPDiATQMVLASEDDrlpVIQMWDLRfAS 250
Cdd:cd00200     12 VTCVAFSPD-GKLLATGSGDGTIKVWDLETGELLRTLKGHTGPV--RDVAASAD-GTYLASGSSDK---TIRLWDLE-TG 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  251 SPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPrNPAVLSAASFDGRISV 330
Cdd:cd00200     84 ECVRTLTGHTSYVSSVAFS-PDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSP-DGTFVASSSQDGTIKL 161


                   ....*..
gi 1622939758  331 YSIMGGS 337
Cdd:cd00200    162 WDLRTGK 168
WD40 COG2319
WD40 repeat [General function prediction only];
89-247 2.24e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 61.08  E-value: 2.24e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758   89 LIAGGENGNIILYDpskiIAGDKEVVIAQNdkHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTqpp 168
Cdd:COG2319    261 LASGSADGTVRLWD----LATGELLRTLTG--HSGGVNSVAFS-PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHT--- 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  169 EDISCIAWNRQVQhILASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPD---IATqmvlASEDDRlpvIQMWD 245
Cdd:COG2319    331 GAVRSVAFSPDGK-TLASGSDDGTVRLWDLATGELLRTLTGHTGAVT--SVAFSPDgrtLAS----GSADGT---VRLWD 400


                   ..
gi 1622939758  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 4.75e-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: 4.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  573 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKyFAKSQSKIT---RLITAVVMKNWKEIVESC---- 644
Cdd:cd09233     69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622939758  645 -----DLKNWREALAAVLTYAKPD-EFSALCDLlgtrleneGDSLLQTQ----ACLCYICAG 696
Cdd:cd09233    147 aeaewALGNWREHLAIILSNRTSNlDLEALVEL--------GDLLAQRGlveaAHICYLLAG 200
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 943-1115 2.96e-07

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 55.16  E-value: 2.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  943 PPPPSSGASFQHGGPGAPPSSSAYALPPGTTgtlPAASELPASQRT--GPQNGWNDPPALN--RVPK--------KKKTP 1010
Cdd:pfam03154  181 ASPPSPPPPGTTQAATAGPTPSAPSVPPQGS---PATSQPPNQTQStaAPHTLIQQTPTLHpqRLPSphpplqpmTQPPP 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758 1011 ENFMPPVPITSPIMNPLGDPQSQMLQQQPS--------APIPLSSQSS------FPQPHLSgGQPFHGIQQPLGQTgMPP 1076
Cdd:pfam03154  258 PSQVSPQPLPQPSLHGQMPPMPHSLQTGPShmqhpvppQPFPLTPQSSqsqvppGPSPAAP-GQSQQRIHTPPSQS-QLQ 335

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1622939758 1077 SFSKPNIEGAPGAPIgnTFQHVQSLPTKKITKKPIPDEH 1115
Cdd:pfam03154  336 SQQPPREQPLPPAPL--SMPHIKPPPTTPIPQLPNPQSH 372
PHA03247 PHA03247
large tegument protein UL36; Provisional
 751-1092 5.01e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.56  E-value: 5.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  751 SQYANLLAAQGSIAAALAFLPDNTNQPNIVQLRDRlCRAQGEPVAGHESPKIPYekqqlPKGRPGPVGhhqmPRVQTQQY 830
Cdd:PHA03247  2632 SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRR-ARRLGRAAQASSPPQRPR-----RRAARPTVG----SLTSLADP 2701

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  831 YPHGENPPPPgfimhgnvNPNAAGQLPTSPGhmhTQVPPYPQPQPYQPAQPYPFGTGGSAMYRPQQPVAPPTSnAYPNTP 910
Cdd:PHA03247  2702 PPPPPTPEPA--------PHALVSATPLPPG---PAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTT-AGPPAP 2769

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  911 YISSASSYSGQSQLYAAQHQASSPTSSPATSFPPPPSSGASFQHGGPGAPPSSSAYALPPGTTGTLPAASELPA--SQRT 988
Cdd:PHA03247  2770 APPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPgpPPPS 2849

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  989 GPQNGWNDP--PALNRVPKKKKTPENFMPPVPITSPIMNPLGDPQSQMLQQQPSAPIPLSSQSSFPQPHLSGGQPFHGIQ 1066
Cdd:PHA03247  2850 LPLGGSVAPggDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQP 2929

                          330       340
                   ....*....|....*....|....*...
gi 1622939758 1067 QPLGQT-GMPPSFSKPNIEGAP-GAPIG 1092
Cdd:PHA03247  2930 QPPPPPpPRPQPPLAPTTDPAGaGEPSG 2957
Sec16_C pfam12931
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal ...
 573-767 6.60e-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: 52.18  E-value: 6.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  573 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKY----FAKSQSKITRLItAVVMK----NWKEIVE- 642
Cdd:pfam12931    1 IRALLLTGDREKALWLAL-DKKLwAHALLIASTLGKEKWKEVVQEFvrseFKGSNNKSGESL-AALYQvfagNSEEAVDe 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  643 --------SCDLKNWREALAAVLTYAKPDEFSALCDlLGTRLENEGdslLQTQACLCYICAG---NVEKLVACWTKAQDG 711
Cdd:pfam12931   79 lvppsknaLWALDNWRETLALVLSNRSPGDVEALLA-LGDLLAQYG---RTEAAHICFLLAGlplSQTVLLGADHVRFPS 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  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 3.73e-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: 3.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  252 PLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRISVY 331
Cdd:cd00200      1 LRRTLKGHTGGVTCVAFS-PDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLAS-GSSDKTIRLW 78


                   ....*
gi 1622939758  332 SIMGG 336
Cdd:cd00200     79 DLETG 83
PHA03247 PHA03247
large tegument protein UL36; Provisional
 893-1090 5.65e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 5.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  893 RPQQPVAPPTSnAYPNTPyissassysgqsqlyaaqhqassptSSPATSFPPPPSSGASFQHGGPGA--PPSSSAYALPp 970
Cdd:PHA03247  2823 SPAGPLPPPTS-AQPTAP-------------------------PPPPGPPPPSLPLGGSVAPGGDVRrrPPSRSPAAKP- 2875

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  971 gTTGTLPAASELPASQRTGPQNGWNDPPAlnrVPKKKKTPENFMPPVPITSPIMNPLGDPQSQMlQQQPSAPIPlssqss 1050
Cdd:PHA03247  2876 -AAPARPPVRRLARPAVSRSTESFALPPD---QPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP-PPRPQPPLA------ 2944

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1622939758 1051 fPQPHLSG-GQPFHGIQQPLGQTGMPPSFSKPNIEGAPGAP 1090
Cdd:PHA03247  2945 -PTTDPAGaGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 793-1114 1.62e-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: 45.91  E-value: 1.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  793 PVAGHESPKIPYEKQQLPKGRPGPVGHHQMPRVQTQQYYPHGENPPPPGFIMHGNVNPNAAGQLPTSPGHMHTQVPpypq 872
Cdd:pfam03154  201 PSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMP---- 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  873 pqpyqpAQPYPFGTGGSAMYRP--QQPVAPPTSNAY---PNTPYISSASSYSGQSQLYAAQHQASSPTSSPATSFPPPPs 947
Cdd:pfam03154  277 ------PMPHSLQTGPSHMQHPvpPQPFPLTPQSSQsqvPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAP- 349

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  948 sgASFQHGGPgaPPSSSAYALPPGTTGTLPAASELPASQRTgPQNgWNDPPALNRV--------PKKKKTPENFMPPV-P 1018
Cdd:pfam03154  350 --LSMPHIKP--PPTTPIPQLPNPQSHKHPPHLSGPSPFQM-NSN-LPPPPALKPLsslsthhpPSAHPPPLQLMPQSqQ 423

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758 1019 ITSPIMNPLGDPQSQML------QQQPSAPIPLSSQSSFPQ-PHLSGGQPfhGIQQPLG-QTGMPPSFSKPNIEGAPGAP 1090
Cdd:pfam03154  424 LPPPPAQPPVLTQSQSLpppaasHPPTSGLHQVPSQSPFPQhPFVPGGPP--PITPPSGpPTSTSSAMPGIQPPSSASVS 501

                          330       340
                   ....*....|....*....|....*.
gi 1622939758 1091 IGNTFQHVQS--LPTKKITKKPiPDE 1114
Cdd:pfam03154  502 SSGPVPAAVScpLPPVQIKEEA-LDE 526
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 203-333 4.08e-04

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 44.69  E-value: 4.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  203 PIIKVSdhsNRMHCSGLAWHPDIATQMVLASEDDrlpVIQMWDLrfASSPLRV-LENHARGILAIAWSMADPELLLSCGK 281
Cdd:PLN00181   525 PVVELA---SRSKLSGICWNSYIKSQVASSNFEG---VVQVWDV--ARSQLVTeMKEHEKRVWSIDYSSADPTLLASGSD 596

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622939758  282 DAKILCSNPNTGEVLYELPTNTQWCFdIQWCPRNPAVLSAASFDGRISVYSI 333
Cdd:PLN00181   597 DGSVKLWSINQGVSIGTIKTKANICC-VQFPSESGRSLAFGSADHKVYYYDL 647
PHA03247 PHA03247
large tegument protein UL36; Provisional
 792-1116 9.09e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 9.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  792 EPVAGHESPKIPYEKqqlPKGRPGPvGHHQMPRVQTQQYYPHGENPPPPGF---IMHGNVNPNAAGQLPTSPGHmhTQVP 868
Cdd:PHA03247  2637 EPDPHPPPTVPPPER---PRDDPAP-GRVSRPRRARRLGRAAQASSPPQRPrrrAARPTVGSLTSLADPPPPPP--TPEP 2710

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  869 PYPQPQPYQPAQPYPFGTGGSAMYRPQQPVAPPTsnayPNTPYISSASSYSGQSQLYAAqhqassPTSSPATSFP---PP 945
Cdd:PHA03247  2711 APHALVSATPLPPGPAAARQASPALPAAPAPPAV----PAGPATPGGPARPARPPTTAG------PPAPAPPAAPaagPP 2780

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  946 PSSGASfqhggPGAPPSSSAYALP------PGTTGTLPAASELPASQRTGPqngwNDPPALNRVPKKKKTPENFMPPVPI 1019
Cdd:PHA03247  2781 RRLTRP-----AVASLSESRESLPspwdpaDPPAAVLAPAAALPPAASPAG----PLPPPTSAQPTAPPPPPGPPPPSLP 2851

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758 1020 TSPIMNPLGD----PQSQMLQQQPSAPiPLSSQSSFPQPHLSggQPFHGIQQPlgqtgmPPSFSKPNIEGAPGAPIGNTF 1095
Cdd:PHA03247  2852 LGGSVAPGGDvrrrPPSRSPAAKPAAP-ARPPVRRLARPAVS--RSTESFALP------PDQPERPPQPQAPPPPQPQPQ 2922

                          330       340
                   ....*....|....*....|.
gi 1622939758 1096 QHVQSLPTKKITKKPIPDEHL 1116
Cdd:PHA03247  2923 PPPPPQPQPPPPPPPRPQPPL 2943
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 750-1154 1.60e-03

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 42.69  E-value: 1.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  750 MSQYANLLAAQGSIAAALAFLPDNTNQPNIVQLrdrlcrAQGEPVAGHESPKIPYEKQQLPKgRPGPVGHHQMPrvQTQQ 829
Cdd:pfam09606  117 PGTASNLLASLGRPQMPMGGAGFPSQMSRVGRM------QPGGQAGGMMQPSSGQPGSGTPN-QMGPNGGPGQG--QAGG 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  830 YYPHGENPPppgfimhGNVNPNAAGQlPTSPGHMHTQVPPYPQPQPYQPAQPYPfgTGGSAMYRPQQPvAPPTSNAYPNt 909
Cdd:pfam09606  188 MNGGQQGPM-------GGQMPPQMGV-PGMPGPADAGAQMGQQAQANGGMNPQQ--MGGAPNQVAMQQ-QQPQQQGQQS- 255

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  910 pyiSSASSYSGQSQLYAAQHQASSPTSSPATSFPPPPSSGASFQHGGPGAPPSSSAYALPP---GTTGTLPAASELPASQ 986
Cdd:pfam09606  256 ---QLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQqqqQQGGNHPAAHQQQMNQ 332

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  987 ------RTGPQNGWNDPPALNRV--------PKKKKTPENFMPPVPITSPIMNPLGDPQSQMLQQQPSAPIPLSSQSSFP 1052
Cdd:pfam09606  333 svgqggQVVALGGLNHLETWNPGnfgglganPMQRGQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGPGSQPP 412

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758 1053 QPHLSGGQPF-HGIQQPLGQTGMPPSFSKPNIEGAPGAPIGNTFQHVQSLPTKKITKKPIPDEHLILKTTFEDLIQRCLS 1131
Cdd:pfam09606  413 QSHPGGMIPSpALIPSPSPQMSQQPAQQRTIGQDSPGGSLNTPGQSAVNSPLNPQEEQLYREKYRQLTKYIEPLKRMIAK 492

                          410       420
                   ....*....|....*....|...
gi 1622939758 1132 SATDPQTKRKLDDASKRLEFLYD 1154
Cdd:pfam09606  493 MENDPGDIDKMNKMKRLLEILSN 515
PHA03247 PHA03247
large tegument protein UL36; Provisional
 893-1092 1.70e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  893 RPQQPVAPPTSNAyPNTPyissassySGQSQLYAAQHQASSPTSSPATSFPPPPS-SGASFQHGGPG---APPSSSAYAL 968
Cdd:PHA03247  2585 RARRPDAPPQSAR-PRAP--------VDDRGDPRGPAPPSPLPPDTHAPDPPPPSpSPAANEPDPHPpptVPPPERPRDD 2655

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  969 PPGTTGTLP--AASELPASQRTGPQNGWNDPPA---------LNRVPKKKKTPENfmPPVPITSPIMNPLGdPQSQMlQQ 1037
Cdd:PHA03247  2656 PAPGRVSRPrrARRLGRAAQASSPPQRPRRRAArptvgsltsLADPPPPPPTPEP--APHALVSATPLPPG-PAAAR-QA 2731

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622939758 1038 QPSAPIPLSSQSSFPQPHLSGGQpfhgiqqplGQTGMPPSFSKPNIEGAPGAPIG 1092
Cdd:PHA03247  2732 SPALPAAPAPPAVPAGPATPGGP---------ARPARPPTTAGPPAPAPPAAPAA 2777
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 821-1054 1.90e-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: 42.45  E-value: 1.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  821 QMPRVQTQQYYPHGENPPPPGFIMHGNVNPNAAGQLPTSPGHMHTQVPPYPQPQPYQPAQPYPFGTG--GSAMYRPQQPV 898
Cdd:pfam03154  170 QPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTlhPQRLPSPHPPL 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  899 APPTSNAYPNTPYISSASSYSGQSQLYAAQHQASSPTSSPATSFPPPPSSGASFQHGGPGAPPSSSAYALPPGTTGTLPA 978
Cdd:pfam03154  250 QPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPP 329

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622939758  979 ASELPASQRtgPQNGWNDPPALNRVPKKKKTPENFMPPVPitspimnplgDPQSQMLQQQPSAPIPLSSQSSFPQP 1054
Cdd:pfam03154  330 SQSQLQSQQ--PPREQPLPPAPLSMPHIKPPPTTPIPQLP----------NPQSHKHPPHLSGPSPFQMNSNLPPP 393
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 943-1135 8.33e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 39.84  E-value: 8.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758  943 PPPPSSGASFQHGGPgAPPS--------SSAYALPPGTTGTLPAASELPASQRTGPQNgwndPPALNRVPKKkktpenfm 1014
Cdd:PHA02682    84 PSPACAAPAPACPAC-APAApapavtcpAPAPACPPATAPTCPPPAVCPAPARPAPAC----PPSTRQCPPA-------- 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939758 1015 PPVPITSPImnplgdpqsqmlqqqPSAPiPLSSQSSFPQPHLsggqpfhgiqqplgqtgmpPSFSKPNIEGAPGApignt 1094
Cdd:PHA02682   151 PPLPTPKPA---------------PAAK-PIFLHNQLPPPDY-------------------PAASCPTIETAPAA----- 190

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1622939758 1095 fqhvqslptKKITKKPIPDEHLILKTTFEDLIQRCLSSATD 1135
Cdd:PHA02682   191 ---------SPVLEPRIPDKIIDADNDDKDLIKKELADIAD 222
 
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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