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Conserved domains on  [gi|119570208|gb|EAW49823|]
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SEC31-like 2 (S. cerevisiae), isoform CRA_c [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 265-495 1.05e-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.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 52.08  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  265 LRGPHGVSPGPATTYRVTQYANLLAAQGSLATAMSFLPRDCAQPPVQQlrdrlfhaqgsavlgqQSPPFPFPRIVVGATL 344
Cdd:pfam03154 174 LQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQT----------------QSTAAPHTLIQQTPTL 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  345 HSKETSSYRLGSQPSHQVPTPSPRPRVFTPQSSPAMPLAPSHPSPYQGPRtqnisdyRAPGPQAIQPLPLSPGVR----- 419
Cdd:pfam03154 238 HPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPS-------HMQHPVPPQPFPLTPQSSqsqvp 310

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  420 -------PGPQDSWKEAPAPRGNLQRNKLP-ETFMPPAPITAPvmSLTPELQGILPSQPPVSSVSHaPPGVPGELSLQL- 490
Cdd:pfam03154 311 pgpspaaPGQSQQRIHTPPSQSQLQSQQPPrEQPLPPAPLSMP--HIKPPPTTPIPQLPNPQSHKH-PPHLSGPSPFQMn 387


                  ....*
gi 119570208  491 QHLPP 495
Cdd:pfam03154 388 SNLPP 392
ACE1-Sec16-like super family cl14807
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ...
 98-228 2.37e-05

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: 46.48  E-value: 2.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  98 KDIDGLLSQA-------LLLGELGPAVELCLKEERFADAIILAQAGGTDLLKQTQERYlAKKKTKISSLLACVVQ---KN 167
Cdd:cd09233   56 VGTDIAEQKAlnrfrnlLLTGNRKEALELALDNGLWAHALLLASSLGKETWAEVVSRF-ARSESKLNDPLQTLYQlfsGN 134

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119570208 168 WKDVVCTCS---------LKNWREALALLLTySGTEKFPELCDM-LGTRMEQEGsraLTSEARLCYVCSGS 228
Cdd:cd09233  135 SPEAITELAdnpaeaewaLGNWREHLAIILS-NRTSNLDLEALVeLGDLLAQRG---LVEAAHICYLLAGV 201
 
Name Accession Description Interval E-value
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 265-495 1.05e-06

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 52.08  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  265 LRGPHGVSPGPATTYRVTQYANLLAAQGSLATAMSFLPRDCAQPPVQQlrdrlfhaqgsavlgqQSPPFPFPRIVVGATL 344
Cdd:pfam03154 174 LQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQT----------------QSTAAPHTLIQQTPTL 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  345 HSKETSSYRLGSQPSHQVPTPSPRPRVFTPQSSPAMPLAPSHPSPYQGPRtqnisdyRAPGPQAIQPLPLSPGVR----- 419
Cdd:pfam03154 238 HPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPS-------HMQHPVPPQPFPLTPQSSqsqvp 310

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  420 -------PGPQDSWKEAPAPRGNLQRNKLP-ETFMPPAPITAPvmSLTPELQGILPSQPPVSSVSHaPPGVPGELSLQL- 490
Cdd:pfam03154 311 pgpspaaPGQSQQRIHTPPSQSQLQSQQPPrEQPLPPAPLSMP--HIKPPPTTPIPQLPNPQSHKH-PPHLSGPSPFQMn 387


                  ....*
gi 119570208  491 QHLPP 495
Cdd:pfam03154 388 SNLPP 392
PHA03247 PHA03247
large tegument protein UL36; Provisional
 328-510 2.48e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 2.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  328 QQSPPFPFPRIVVGATLHSKETSSYRLGSQPSHQVPTPSPRPRV------FTPQSSPAMPLAPSHPSPYQGPRTQNISDY 401
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGpatpggPARPARPPTTAGPPAPAPPAAPAAGPPRRL 2783

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  402 RAPGPQAIQPLPLSPGVRPGPQDSWKEAPAPRGNLQRNKLPETFMPPAPITAPVMSLTPElQGILPSQPPVSSVS----- 476
Cdd:PHA03247 2784 TRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP-GPPPPSLPLGGSVApggdv 2862

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 119570208  477 --HAPPGVPGELSLQLQHLPPEKMERKELPPEHQSL 510
Cdd:PHA03247 2863 rrRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESF 2898
ACE1-Sec16-like cd09233
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ...
 98-228 2.37e-05

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: 46.48  E-value: 2.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  98 KDIDGLLSQA-------LLLGELGPAVELCLKEERFADAIILAQAGGTDLLKQTQERYlAKKKTKISSLLACVVQ---KN 167
Cdd:cd09233   56 VGTDIAEQKAlnrfrnlLLTGNRKEALELALDNGLWAHALLLASSLGKETWAEVVSRF-ARSESKLNDPLQTLYQlfsGN 134

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119570208 168 WKDVVCTCS---------LKNWREALALLLTySGTEKFPELCDM-LGTRMEQEGsraLTSEARLCYVCSGS 228
Cdd:cd09233  135 SPEAITELAdnpaeaewaLGNWREHLAIILS-NRTSNLDLEALVeLGDLLAQRG---LVEAAHICYLLAGV 201
 
Name Accession Description Interval E-value
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 265-495 1.05e-06

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 52.08  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  265 LRGPHGVSPGPATTYRVTQYANLLAAQGSLATAMSFLPRDCAQPPVQQlrdrlfhaqgsavlgqQSPPFPFPRIVVGATL 344
Cdd:pfam03154 174 LQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQT----------------QSTAAPHTLIQQTPTL 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  345 HSKETSSYRLGSQPSHQVPTPSPRPRVFTPQSSPAMPLAPSHPSPYQGPRtqnisdyRAPGPQAIQPLPLSPGVR----- 419
Cdd:pfam03154 238 HPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPS-------HMQHPVPPQPFPLTPQSSqsqvp 310

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  420 -------PGPQDSWKEAPAPRGNLQRNKLP-ETFMPPAPITAPvmSLTPELQGILPSQPPVSSVSHaPPGVPGELSLQL- 490
Cdd:pfam03154 311 pgpspaaPGQSQQRIHTPPSQSQLQSQQPPrEQPLPPAPLSMP--HIKPPPTTPIPQLPNPQSHKH-PPHLSGPSPFQMn 387


                  ....*
gi 119570208  491 QHLPP 495
Cdd:pfam03154 388 SNLPP 392
PHA03247 PHA03247
large tegument protein UL36; Provisional
 328-510 2.48e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 2.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  328 QQSPPFPFPRIVVGATLHSKETSSYRLGSQPSHQVPTPSPRPRV------FTPQSSPAMPLAPSHPSPYQGPRTQNISDY 401
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGpatpggPARPARPPTTAGPPAPAPPAAPAAGPPRRL 2783

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  402 RAPGPQAIQPLPLSPGVRPGPQDSWKEAPAPRGNLQRNKLPETFMPPAPITAPVMSLTPElQGILPSQPPVSSVS----- 476
Cdd:PHA03247 2784 TRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP-GPPPPSLPLGGSVApggdv 2862

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 119570208  477 --HAPPGVPGELSLQLQHLPPEKMERKELPPEHQSL 510
Cdd:PHA03247 2863 rrRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESF 2898
PHA03379 PHA03379
EBNA-3A; Provisional
 308-513 1.23e-05

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 48.52  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208 308 PPVQQLRDRLFHAQGSAVLG--QQSPPFPFPRIvvgatlhsketssyrlgsQPSHQVPTPSPRPRVF-TPQSSPAMPLA- 383
Cdd:PHA03379 446 PPVHDLEPGPLHDQHSMAPCpvAQLPPGPLQDL------------------EPGDQLPGVVQDGRPAcAPVPAPAGPIVr 507

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208 384 PSHPSPYQGPRtqnisdyRAPGPQAIQPLPLSP----------GVRPGPQDSWKEAPAPRGNLQRNKlpETFMP----PA 449
Cdd:PHA03379 508 PWEASLSQVPG-------VAFAPVMPQPMPVEPvpvptvalerPVCPAPPLIAMQGPGETSGIVRVR--ERWRPapwtPN 578

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119570208 450 PITAPV-MSLTPELQGILP-SQPPVSSVSHAPPgvpgelslQLQHLPPEKMERKELPPEHQSLKSS 513
Cdd:PHA03379 579 PPRSPSqMSVRDRLARLRAeAQPYQASVEVQPP--------QLTQVSPQQPMEYPLEPEQQMFPGS 636
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
255-485 1.37e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 48.33  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208 255 VMVLNRSLEQLRGPHG--VSPGPATTYRVTQYANLLAAQGSLATAMSFLPRDCAQPPVQQlrdrlfhAQGSAVLGQQSPP 332
Cdd:PRK12323 354 TMTLLRMLAFRPGQSGggAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAA-------AAARAVAAAPARR 426

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208 333 FPFPRIVVGATLHSKETSSYRLGSQPShQVPTPSPRPRVFTPQSSPAMPLAPSHPSPYQGPRTQNISDYRAPGPQAIQPL 412
Cdd:PRK12323 427 SPAPEALAAARQASARGPGGAPAPAPA-PAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPE 505

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119570208 413 PLSPGV---RPGPQDsWKEAPAPRGNLQRNKLPETFMPPAPITAPVMSLTPELQGILPSQPPVSSVSHAPPGVPGE 485
Cdd:PRK12323 506 FASPAPaqpDAAPAG-WVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDGD 580
PHA03247 PHA03247
large tegument protein UL36; Provisional
 268-513 2.19e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 2.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  268 PHGVSPGPATTYRVTQYANLLAAQGSLATAMsflPRDCAQPPVQQLRDRLFHAQGSAVLGQQSPPFPFPRIVVGATLHSK 347
Cdd:PHA03247 2741 PPAVPAGPATPGGPARPARPPTTAGPPAPAP---PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAA 2817

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  348 ETSSYRLGS---QPSHQVPTPSPRPRVFTPQS-SPAMPLAPSHP----SPYQGPRTQNISDYRAPGPQAIQPlPLSPGVR 419
Cdd:PHA03247 2818 LPPAASPAGplpPPTSAQPTAPPPPPGPPPPSlPLGGSVAPGGDvrrrPPSRSPAAKPAAPARPPVRRLARP-AVSRSTE 2896

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  420 PGPQDSWKEAPAPRGNLQRNKLPETFMPPAPITAPVMSLTPELQGILPSQPPVSSVSHAPPGVPGElslQLQHLPPEKME 499
Cdd:PHA03247 2897 SFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQP---WLGALVPGRVA 2973

                         250
                  ....*....|....*.
gi 119570208  500 --RKELPPEHQSLKSS 513
Cdd:PHA03247 2974 vpRFRVPQPAPSREAP 2989
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 329-472 2.21e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 47.77  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  329 QSPPFPFPRIVVgatlhSKETSSYRLGSQPSHQVPTPSPRPRVFTPQSSPAMPLAPSH---------------------- 386
Cdd:PRK10263  342 QTPPVASVDVPP-----AQPTVAWQPVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNeplqqpvqpqqpyyapaaeqpa 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  387 PSPYQGPRTQNISDYRAPGPQAIQPLPLSPGVRPGPQDSWKEAPA--PRGNLQRNKLPET-FMPPAPITAP-VMSLTPEL 462
Cdd:PRK10263  417 QQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTyqTEQTYQQPAAQEPlYQQPQPVEQQpVVEPEPVV 496

                         170
                  ....*....|
gi 119570208  463 QGILPSQPPV 472
Cdd:PRK10263  497 EETKPARPPL 506
ACE1-Sec16-like cd09233
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ...
 98-228 2.37e-05

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: 46.48  E-value: 2.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  98 KDIDGLLSQA-------LLLGELGPAVELCLKEERFADAIILAQAGGTDLLKQTQERYlAKKKTKISSLLACVVQ---KN 167
Cdd:cd09233   56 VGTDIAEQKAlnrfrnlLLTGNRKEALELALDNGLWAHALLLASSLGKETWAEVVSRF-ARSESKLNDPLQTLYQlfsGN 134

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119570208 168 WKDVVCTCS---------LKNWREALALLLTySGTEKFPELCDM-LGTRMEQEGsraLTSEARLCYVCSGS 228
Cdd:cd09233  135 SPEAITELAdnpaeaewaLGNWREHLAIILS-NRTSNLDLEALVeLGDLLAQRG---LVEAAHICYLLAGV 201
PHA03247 PHA03247
large tegument protein UL36; Provisional
 331-483 2.42e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  331 PPFPFPRIvvgatlHSKETSSYRLGSQPSHQVPTPSPRP-RVFTPQSSPAMPLAPSHPSPYQGPRTQNISDYRAPGPQAI 409
Cdd:PHA03247 2626 PPPPSPSP------AANEPDPHPPPTVPPPERPRDDPAPgRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLA 2699

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  410 QPLPLSPGVRPGPQDSWKEAPAPRGNLQRNK----LPETFMPPAPITAPVMSLTPELQGI--LPSQPPVSSVSHAPPGVP 483
Cdd:PHA03247 2700 DPPPPPPTPEPAPHALVSATPLPPGPAAARQaspaLPAAPAPPAVPAGPATPGGPARPARppTTAGPPAPAPPAAPAAGP 2779
PHA03247 PHA03247
large tegument protein UL36; Provisional
 308-505 3.52e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 3.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  308 PPVQQLRDRLFHAQGSAVLGQQSPPFPFPRIVVGATLHSKETSsyRLGSQPSHQVPTPSPRPRVFTPQSSPAMPLA---P 384
Cdd:PHA03247 2626 PPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRAR--RLGRAAQASSPPQRPRRRAARPTVGSLTSLAdppP 2703

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  385 SHPSPYQGPRTQNISDYRAPGPQAIQPLPLSPGVRPGPQDSWKEAPAPRGNLQRNKLPETFMPPA------PITAPVMSL 458
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPApappaaPAAGPPRRL 2783

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 119570208  459 TPELQGILPSQPPVSSVSHAPPGVPGELSLQLQHLPPEKMERKELPP 505
Cdd:PHA03247 2784 TRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP 2830
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 267-480 9.75e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.46  E-value: 9.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  267 GPHG----VSPGPATTYRVTQYANLLAAQGSLATAMSFLPRDCAQPPVQQLRDRLFHAQGSAVLGQQSPPFPFPRIVVGA 342
Cdd:PRK10263  365 GPQTgepvIAPAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAG 444

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  343 TLHSKETSSYRLGSQPSHQVPTPSPRPrvfTPQSSPAMPLAPSHPSPYQGPRtqnisdyraPGPQAIQPlplspgVRPgP 422
Cdd:PRK10263  445 NAWQAEEQQSTFAPQSTYQTEQTYQQP---AAQEPLYQQPQPVEQQPVVEPE---------PVVEETKP------ARP-P 505

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 119570208  423 QDSWKEAPAPRGNlQRNKLPETFMP-PAPITAPVMSLTPELQGILPSQPPVSSVSHAPP 480
Cdd:PRK10263  506 LYYFEEVEEKRAR-EREQLAAWYQPiPEPVKEPEPIKSSLKAPSVAAVPPVEAAAAVSP 563
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 354-508 1.21e-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: 45.14  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  354 LGSQPSHQVPTPSPRPRVFTPQSSPaMPLAPSHPSPYQGPRTQNISDYRAPGPQAIQPLPLSPgvrPGPQDSWKEAPAPr 433
Cdd:pfam03154 399 LSSLSTHHPPSAHPPPLQLMPQSQQ-LPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQS---PFPQHPFVPGGPP- 473

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  434 gnlqrnklpetfmPPAPITAPVMSLTPELQGIlpsQPPVSSVSHAPPGVPGELS-----LQLQHLPPEKMERKELPPEHQ 508
Cdd:pfam03154 474 -------------PITPPSGPPTSTSSAMPGI---QPPSSASVSSSGPVPAAVScplppVQIKEEALDEAEEPESPPPPP 537
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 329-483 1.69e-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: 44.76  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  329 QSPPFPFPRIVVGA--TLHSKETSSYRLGSQPSHQVP---TPSPRPRVFTPQSSPAMPLA-------PSH---PSPYQGP 393
Cdd:pfam03154 308 QVPPGPSPAAPGQSqqRIHTPPSQSQLQSQQPPREQPlppAPLSMPHIKPPPTTPIPQLPnpqshkhPPHlsgPSPFQMN 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  394 RTqnisdyrAPGPQAIQPLPLSPGVRPgpqdswKEAPAPRGNLQRNKLPetfMPPAPITAPVMSLTPELQGILPSQPPVS 473
Cdd:pfam03154 388 SN-------LPPPPALKPLSSLSTHHP------PSAHPPPLQLMPQSQQ---LPPPPAQPPVLTQSQSLPPPAASHPPTS 451

                         170
                  ....*....|
gi 119570208  474 SVSHAPPGVP 483
Cdd:pfam03154 452 GLHQVPSQSP 461
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 358-510 6.29e-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: 42.83  E-value: 6.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  358 PSHQVPTPSPRPRVFTPQSSPA-MPLAPSHPSPYQGPRTQnisdyraPGPQAIQPLPLSPGVRPGPQDSWKEAPAPRGNL 436
Cdd:pfam03154 177 QSGAASPPSPPPPGTTQAATAGpTPSAPSVPPQGSPATSQ-------PPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPL 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  437 QRNKLP----------------ETFMPPAPitAPVMSLTPELQGILPSQP----PVSSVSHAPPG----VPGElSLQLQH 492
Cdd:pfam03154 250 QPMTQPpppsqvspqplpqpslHGQMPPMP--HSLQTGPSHMQHPVPPQPfpltPQSSQSQVPPGpspaAPGQ-SQQRIH 326

                         170
                  ....*....|....*....
gi 119570208  493 LPPEKME-RKELPPEHQSL 510
Cdd:pfam03154 327 TPPSQSQlQSQQPPREQPL 345
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 359-483 1.14e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 41.98  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208 359 SHQVPTPSPRPRVFTPQSSPAMPLAPSHPSPYQGPRTQnisdyRAPGPQAIQPLPLSPGVRPGPQDSW-KEAPAPRGNLQ 437
Cdd:PTZ00449 617 LLDIPKSPKRPESPKSPKRPPPPQRPSSPERPEGPKII-----KSPKPPKSPKPPFDPKFKEKFYDDYlDAAAKSKETKT 691

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 119570208 438 RNKLPETFMPPAPITAPVMSLTP--ELQGILPSQPPVSSVSHAPPGVP 483
Cdd:PTZ00449 692 TVVLDESFESILKETLPETPGTPftTPRPLPPKLPRDEEFPFEPIGDP 739
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 358-471 1.92e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 40.61  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208 358 PSHQVPTPSPR---PRVFTPQSSPAMP--LAPSHPSPYQGPRTQNISDYRAPGPQAIQPLPLSPGVRPgpqdswkeAPAP 432
Cdd:PHA02682  91 PAPACPACAPAapaPAVTCPAPAPACPpaTAPTCPPPAVCPAPARPAPACPPSTRQCPPAPPLPTPKP--------APAA 162

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 119570208 433 RGNLQRNKLPETFMPPApiTAPVMSLTPELQGILPSQPP 471
Cdd:PHA02682 163 KPIFLHNQLPPPDYPAA--SCPTIETAPAASPVLEPRIP 199
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 355-484 2.10e-03

MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic MAPK-interacting and spindle-stabilising protein-like proteins. MISS is rich in prolines and has four potential MAPK-phosphorylation sites, a MAPK-docking site, a PEST sequence (PEST motif) and a bipartite nuclear localization signal. The endogenous protein accumulates during mouse meiotic maturation and is found as discrete dots on the MII spindle. MISS is the first example of a physiological MAPK-substrate that is stabilized in MII that specifically regulates MII spindle integrity during the CSF arrest.


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 40.35  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  355 GSQPSHQVPTPS-PRPRVFTPQSSPAMPLAPShPSpyqGPRTQNISDYRAPGPQAIQPLPLSPGVRPGP-------QDSW 426
Cdd:pfam15822 105 GPGPIGPYPTPNmPFPELPRPYGAPTDPAAAA-PS---GPWGSMSSGPWAPGMGGQYPAPNMPYPSPGPypavpppQSPG 180

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 119570208  427 KEAPAPRGNLQrnklPETFMPPAPITAPVMSL-TPELQGILPSQPPVSSVSHAPPGVPG 484
Cdd:pfam15822 181 AAPPVPWGTVP----PGPWGPPAPYPDPTGSYpMPGLYPTPNNPFQVPSGPSGAPPMPG 235
PHA03247 PHA03247
large tegument protein UL36; Provisional
 358-479 4.31e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 4.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  358 PSHQVPTPSPRPRVFTP--------------QSSPAMPLAPSHPSPYQGPRTQNISDYRAPGPQAIQPLP-------LSP 416
Cdd:PHA03247 2564 PDRSVPPPRPAPRPSEPavtsrarrpdappqSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPaanepdpHPP 2643

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119570208  417 GVRPGPQDSWKEAPAPRGNLQR-----------NKLPETFMPPA--PITAPVMSLT-PELQGILPSQPPVSSVSHAP 479
Cdd:PHA03247 2644 PTVPPPERPRDDPAPGRVSRPRrarrlgraaqaSSPPQRPRRRAarPTVGSLTSLAdPPPPPPTPEPAPHALVSATP 2720
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
348-506 5.05e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 39.86  E-value: 5.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208 348 ETSSYRLGSQPSHQVPTPSPRPRVFTPQSSPAMPLAPSHPSPYQGPRTQNISDYRA-PGPQAIQPLPLSPGVRPGPqdsw 426
Cdd:PRK12323 371 GAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRsPAPEALAAARQASARGPGG---- 446

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208 427 keAPAPrgnlqrnklpetfmPPAPITAPVMSLTPELQGILPSqPPVSSVSHAPPGVPGELSLQLQHLPPekmeRKELPPE 506
Cdd:PRK12323 447 --APAP--------------APAPAAAPAAAARPAAAGPRPV-AAAAAAAPARAAPAAAPAPADDDPPP----WEELPPE 505
PHA03247 PHA03247
large tegument protein UL36; Provisional
 267-527 5.57e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 5.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  267 GPHGVSPGPATTYRVTQYANLLAAQGSLATAMSFLPRDCAQPPVQQLRDRLFHAQGSAVLGQQSPPFPFPR-IVVGATLH 345
Cdd:PHA03247 2778 GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPsLPLGGSVA 2857

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  346 SKETSSYRLGSQPSHQVPTPSPRPRVFT---PQSSPAMPLAPSHPSPYQGPRTQNISDyrAPGPQAIQPLPLSPGVRPGP 422
Cdd:PHA03247 2858 PGGDVRRRPPSRSPAAKPAAPARPPVRRlarPAVSRSTESFALPPDQPERPPQPQAPP--PPQPQPQPPPPPQPQPPPPP 2935

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  423 QDSWKEAPAPRGNLQRNKLPETFMPPAPITAPVMSLTPELQGILPS---------QPPVSSVSHAPPGV---PGELSLQL 490
Cdd:PHA03247 2936 PPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQpapsreapaSSTPPLTGHSLSRVsswASSLALHE 3015

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 119570208  491 QHLPPEKMERKELPP----EHQSLKSSFEALLQRCSLSATD 527
Cdd:PHA03247 3016 ETDPPPVSLKQTLWPpddtEDSDADSLFDSDSERSDLEALD 3056
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 367-480 6.97e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 39.68  E-value: 6.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208  367 PRPRVFTPQSSPAMPLAPSHPSPyqGPRTQNISdyRAPGPQAIQPLPLSPGVRPGPQDSWKEAPAPRGNLQRNKLPETFM 446
Cdd:PRK10263  342 QTPPVASVDVPPAQPTVAWQPVP--GPQTGEPV--IAPAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQ 417

                          90       100       110
                  ....*....|....*....|....*....|....
gi 119570208  447 PPAPITAPVMSLTPELQGILPSQPPVSSVSHAPP 480
Cdd:PRK10263  418 QPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEE 451
PHA03247 PHA03247
large tegument protein UL36; Provisional
 355-429 7.82e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.54  E-value: 7.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119570208  355 GSQPSHQVPTPSPRPRVFTPQSSPAMPLAPSHPSPYQGPRTqniSDYRAPGPQAIQPLPLSPGVRPGPQDSWKEA 429
Cdd:PHA03247  402 DDQTRPAAPVPASVPTPAPTPVPASAPPPPATPLPSAEPGS---DDGPAPPPERQPPAPATEPAPDDPDDATRKA 473
PHA03378 PHA03378
EBNA-3B; Provisional
 357-485 8.01e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.28  E-value: 8.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208 357 QPSHQVPTPSPRPRVF-TPQSSPAMplAPSHPSPYQGPRTQNISDYRAPG--------PQAIQPLPLSPGVRPGPQDSwK 427
Cdd:PHA03378 695 QPPPRAPTPMRPPAAPpGRAQRPAA--ATGRARPPAAAPGRARPPAAAPGrarppaaaPGRARPPAAAPGRARPPAAA-P 771

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 119570208 428 EAPAPrgnlqrnkLPETFMPPAPITAPVMSLTPElqgiLPSQPPVSSVSHAPPGVPGE 485
Cdd:PHA03378 772 GAPTP--------QPPPQAPPAPQQRPRGAPTPQ----PPPQAGPTSMQLMPRAAPGQ 817
PHA03378 PHA03378
EBNA-3B; Provisional
 349-505 8.22e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.28  E-value: 8.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208 349 TSSYRLGSQPSHqVPTPSPRPRvftPQSSPAMPLAPSHPSPYQGPRTQNISDYRAP-GPQAIQPLPLSPGVRPGP----- 422
Cdd:PHA03378 581 TTSQLASSAPSY-AQTPWPVPH---PSQTPEPPTTQSHIPETSAPRQWPMPLRPIPmRPLRMQPITFNVLVFPTPhqppq 656

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208 423 ------QDSWKEAP---------APRGNLQRNKLPETFMPPAPITAPvmsLTPELQGILPSQPPVSSVSHAPPGVPGELS 487
Cdd:PHA03378 657 veitpyKPTWTQIGhipyqpsptGANTMLPIQWAPGTMQPPPRAPTP---MRPPAAPPGRAQRPAAATGRARPPAAAPGR 733

                        170
                 ....*....|....*...
gi 119570208 488 LQLQHLPPEKMERKELPP 505
Cdd:PHA03378 734 ARPPAAAPGRARPPAAAP 751
dnaA PRK14086
chromosomal replication initiator protein DnaA;
327-490 8.45e-03

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 39.04  E-value: 8.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208 327 GQQSPPFPFPRIVVGATLHSKETSSY-----------RLGSQPSHQVPTPSPRPRVFTPQSSPAMPLAPSHPSPYQGPRT 395
Cdd:PRK14086  93 GEPAPPPPHARRTSEPELPRPGRRPYegyggpraddrPPGLPRQDQLPTARPAYPAYQQRPEPGAWPRAADDYGWQQQRL 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119570208 396 QNISdyRAPGPQAIQPLPLSPGVRPGPQDSWKEAPAPRG------------NLQRNKLPETF-----------MPPAPIT 452
Cdd:PRK14086 173 GFPP--RAPYASPASYAPEQERDREPYDAGRPEYDQRRRdydhprpdwdrpRRDRTDRPEPPpgaghvhrggpGPPERDD 250

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 119570208 453 APVMSLTPELQGILPSQPpvssvshAPPGVPGELSLQL 490
Cdd:PRK14086 251 APVVPIRPSAPGPLAAQP-------APAPGPGEPTARL 281
 
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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