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Conserved domains on  [gi|578810097|ref|XP_006714586|]
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protein transport protein Sec24A isoform X2 [Homo sapiens]

Protein Classification

SEC24 family transport protein( domain architecture ID 1001573)

SEC24 family transport protein is a component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5028 super family cl34873
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ...
 172-1035 7.91e-179

Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking and secretion];


The actual alignment was detected with superfamily member COG5028:

Pssm-ID: 227361 [Multi-domain]  Cd Length: 861  Bit Score: 543.23  E-value: 7.91e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  172 QYVSSGYPSLQNSFIKSGITSNtnnGSMVVHSSYDEIEGGGLLATPQLTNKNPKMSRSV--GYSYPSLPPGYQNTTPPGA 249
Cdd:COG5028     3 QHKKGVYPQAQSQVHTGAASSK---KSARPHRAYANFSAGQMGMPPYTTPPLQQQSRRQidQAATAMHNTGANNPAPSVM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  250 TGVPPSSLNYPS---GPQAFTQTPLGANHLTTSMSGLSLQPEglrvvnllQERNMLPSTPLKPPVPNLHEDIQKLNCNPE 326
Cdd:COG5028    80 SPAFQSQQKFSSpygGSMADGTAPKPTNPLVPVDLFEDQPPP--------ISDLFLPPPPIVPPLTTNFVGSEQSNCSPK 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  327 LFRCTLTSIPQTQALLNKAKLPLGLLLHPFKDLV----QLPVVTSSTIVRCRSCRTYINPFVSFLDQ-RRWKCNLCYRVN 401
Cdd:COG5028   152 YVRSTMYAIPETNDLLKKSKIPFGLVIRPFLELYpeedPVPLVEDGSIVRCRRCRSYINPFVQFIEQgRKWRCNICRSKN 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  402 DVPEEFlYNPLTRV--YGEPHRRPEVQNATIEFMAPSEYMLRPPQPPVYLFVFDVSHNAVETGYLNSVCQSLLDNLDLLP 479
Cdd:COG5028   232 DVPEGF-DNPSGPNdpRSDRYSRPELKSGVVDFLAPKEYSLRQPPPPVYVFLIDVSFEAIKNGLVKAAIRAILENLDQIP 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  480 G-NTRTKIGFITFDSTIHFYGLQESLSQpQMLIVSDIEDVFIPMPENLLV-NLNESKELVQDLLKTLPQMFTKTLETQSA 557
Cdd:COG5028   311 NfDPRTKIAIICFDSSLHFFKLSPDLDE-QMLIVSDLDEPFLPFPSGLFVlPLKSCKQIIETLLDRVPRIFQDNKSPKNA 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  558 LGPALQAAFKLMSPTGGRMSVFQTQLPTLGVGALKPREEPNHRssakdiHMTPSTDFYKKLALDCSGQQVAVDLFLLSGQ 637
Cdd:COG5028   390 LGPALKAAKSLIGGTGGKIIVFLSTLPNMGIGKLQLREDKESS------LLSCKDSFYKEFAIECSKVGISVDLFLTSED 463

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  638 YSDLASLGCISRYSAGSVYYYPSYHhQHNPVQVQKLQKELQRYLTRKIGFEAVMRIRCTKGLSIHTFHGNFFVRSTDLLS 717
Cdd:COG5028   464 YIDVATLSHLCRYTGGQTYFYPNFS-ATRPNDATKLANDLVSHLSMEIGYEAVMRVRCSTGLRVSSFYGNFFNRSSDLCA 542

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  718 LPNVNPDAGYAVQMSVEESLTdTQLVSFQSALLYTSSKGERRIRVHTLCLPVVSTLNDVFLGADVQAISGLLANMAVDRS 797
Cdd:COG5028   543 FSTMPRDTSLLVEFSIDEKLM-TSDVYFQVALLYTLNDGERRIRVVNLSLPTSSSIREVYASADQLAIACILAKKASTKA 621

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  798 MTASLSDARDALVNAVIDSLSAYRSS-VLSNQQPGLMVPFSLRLFPLFVLALLKQKSFQTGTNaRLDERIFAMCQVKNQP 876
Cdd:COG5028   622 LNSSLKEARVLINKSMVDILKAYKKElVKSNTSTQLPLPANLKLLPLLMLALLKSSAFRSGST-PSDIRISALNRLTSLP 700

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  877 LVYLMLTTHPSLYRVDNLSDEGALNISDRTI-PQPpiLQLSVEKLSRDGAFLMDAGSVLMLWVGKNCTQNFLSQVLGVQN 955
Cdd:COG5028   701 LKQLMRNIYPTLYALHDMPIEAGLPDEGLLVlPSP--INATSSLLESGGLYLIDTGQKIFLWFGKDAVPSLLQDLFGVDS 778

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  956 YASIPQPMTDLPELDTPESARIIAFISWLREQRPFFPI-LYVIRD--ESPMKANFLQNMIEDRTESALSYYEFLLHIQQQ 1032
Cdd:COG5028   779 LSDIPSGKFTLPPTGNEFNERVRNIIGELRSVNDDSTLpLVLVRGggDPSLRLWFFSTLVEDKTLNIPSYLDYLQILHEK 858


                  ...
gi 578810097 1033 VNK 1035
Cdd:COG5028   859 IKS 861
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 26-311 4.58e-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.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.91  E-value: 4.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097    26 SGSPYTNGPVQN---ALLSSQESVSQGYNFQLPGSYPHPIPAKTLNPVSGQSNYGGSQGSGQTLN---RPPVASNPVTPS 99
Cdd:pfam03154  143 STSPSIPSPQDNesdSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPpqgSPATSQPPNQTQ 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097   100 LHSGPAPRMPLPASQNPATTPMPSSSFLPEANLPPPlnwqynypstaSQTnhCPRASSQPTVSGntSLTTNHQYVSSGYP 179
Cdd:pfam03154  223 STAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPP-----------SQV--SPQPLPQPSLHG--QMPPMPHSLQTGPS 287

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097   180 SLQNSFIKSGITSNTNNGSMVVHSSYDEIEGGGLLATPQLTNKNPKMSRSVGYSYPSLPPG---YQNTTPPGATGVP--- 253
Cdd:pfam03154  288 HMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAplsMPHIKPPPTTPIPqlp 367

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578810097   254 -PSSLNYP---SGPQAFTQT----PLGANHLTTSMSGL---SLQPEGLRvvnLLQERNMLPSTPLKPPV 311
Cdd:pfam03154  368 nPQSHKHPphlSGPSPFQMNsnlpPPPALKPLSSLSTHhppSAHPPPLQ---LMPQSQQLPPPPAQPPV 433
 
Name Accession Description Interval E-value
COG5028 COG5028
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ...
 172-1035 7.91e-179

Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking and secretion];


Pssm-ID: 227361 [Multi-domain]  Cd Length: 861  Bit Score: 543.23  E-value: 7.91e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  172 QYVSSGYPSLQNSFIKSGITSNtnnGSMVVHSSYDEIEGGGLLATPQLTNKNPKMSRSV--GYSYPSLPPGYQNTTPPGA 249
Cdd:COG5028     3 QHKKGVYPQAQSQVHTGAASSK---KSARPHRAYANFSAGQMGMPPYTTPPLQQQSRRQidQAATAMHNTGANNPAPSVM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  250 TGVPPSSLNYPS---GPQAFTQTPLGANHLTTSMSGLSLQPEglrvvnllQERNMLPSTPLKPPVPNLHEDIQKLNCNPE 326
Cdd:COG5028    80 SPAFQSQQKFSSpygGSMADGTAPKPTNPLVPVDLFEDQPPP--------ISDLFLPPPPIVPPLTTNFVGSEQSNCSPK 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  327 LFRCTLTSIPQTQALLNKAKLPLGLLLHPFKDLV----QLPVVTSSTIVRCRSCRTYINPFVSFLDQ-RRWKCNLCYRVN 401
Cdd:COG5028   152 YVRSTMYAIPETNDLLKKSKIPFGLVIRPFLELYpeedPVPLVEDGSIVRCRRCRSYINPFVQFIEQgRKWRCNICRSKN 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  402 DVPEEFlYNPLTRV--YGEPHRRPEVQNATIEFMAPSEYMLRPPQPPVYLFVFDVSHNAVETGYLNSVCQSLLDNLDLLP 479
Cdd:COG5028   232 DVPEGF-DNPSGPNdpRSDRYSRPELKSGVVDFLAPKEYSLRQPPPPVYVFLIDVSFEAIKNGLVKAAIRAILENLDQIP 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  480 G-NTRTKIGFITFDSTIHFYGLQESLSQpQMLIVSDIEDVFIPMPENLLV-NLNESKELVQDLLKTLPQMFTKTLETQSA 557
Cdd:COG5028   311 NfDPRTKIAIICFDSSLHFFKLSPDLDE-QMLIVSDLDEPFLPFPSGLFVlPLKSCKQIIETLLDRVPRIFQDNKSPKNA 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  558 LGPALQAAFKLMSPTGGRMSVFQTQLPTLGVGALKPREEPNHRssakdiHMTPSTDFYKKLALDCSGQQVAVDLFLLSGQ 637
Cdd:COG5028   390 LGPALKAAKSLIGGTGGKIIVFLSTLPNMGIGKLQLREDKESS------LLSCKDSFYKEFAIECSKVGISVDLFLTSED 463

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  638 YSDLASLGCISRYSAGSVYYYPSYHhQHNPVQVQKLQKELQRYLTRKIGFEAVMRIRCTKGLSIHTFHGNFFVRSTDLLS 717
Cdd:COG5028   464 YIDVATLSHLCRYTGGQTYFYPNFS-ATRPNDATKLANDLVSHLSMEIGYEAVMRVRCSTGLRVSSFYGNFFNRSSDLCA 542

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  718 LPNVNPDAGYAVQMSVEESLTdTQLVSFQSALLYTSSKGERRIRVHTLCLPVVSTLNDVFLGADVQAISGLLANMAVDRS 797
Cdd:COG5028   543 FSTMPRDTSLLVEFSIDEKLM-TSDVYFQVALLYTLNDGERRIRVVNLSLPTSSSIREVYASADQLAIACILAKKASTKA 621

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  798 MTASLSDARDALVNAVIDSLSAYRSS-VLSNQQPGLMVPFSLRLFPLFVLALLKQKSFQTGTNaRLDERIFAMCQVKNQP 876
Cdd:COG5028   622 LNSSLKEARVLINKSMVDILKAYKKElVKSNTSTQLPLPANLKLLPLLMLALLKSSAFRSGST-PSDIRISALNRLTSLP 700

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  877 LVYLMLTTHPSLYRVDNLSDEGALNISDRTI-PQPpiLQLSVEKLSRDGAFLMDAGSVLMLWVGKNCTQNFLSQVLGVQN 955
Cdd:COG5028   701 LKQLMRNIYPTLYALHDMPIEAGLPDEGLLVlPSP--INATSSLLESGGLYLIDTGQKIFLWFGKDAVPSLLQDLFGVDS 778

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  956 YASIPQPMTDLPELDTPESARIIAFISWLREQRPFFPI-LYVIRD--ESPMKANFLQNMIEDRTESALSYYEFLLHIQQQ 1032
Cdd:COG5028   779 LSDIPSGKFTLPPTGNEFNERVRNIIGELRSVNDDSTLpLVLVRGggDPSLRLWFFSTLVEDKTLNIPSYLDYLQILHEK 858


                  ...
gi 578810097 1033 VNK 1035
Cdd:COG5028   859 IKS 861
Sec24-like cd01479
Sec24-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ...
 443-685 5.87e-129

Sec24-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the budding and fusion of intracellular transport vesicles that selectively carry cargo proteins and lipids from donor to acceptor organelles. The two main classes of vesicular carriers within the endocytic and the biosynthetic pathways are COP- and clathrin-coated vesicles. Formation of COPII vesicles requires the ordered assembly of the coat built from several cytosolic components GTPase Sar1, complexes of Sec23-Sec24 and Sec13-Sec31. The process is initiated by the conversion of GDP to GTP by the GTPase Sar1 which then recruits the heterodimeric complex of Sec23 and Sec24. This heterodimeric complex generates the pre-budding complex. The final step leading to membrane deformation and budding of COPII-coated vesicles is carried by the heterodimeric complex Sec13-Sec31. The members of this CD belong to the Sec23-like family. Sec 24 is very similar to Sec23. The Sec23 and Sec24 polypeptides fold into five distinct domains: a beta-barrel, a zinc finger, a vWA or trunk, an all helical region and a carboxy Gelsolin domain. The members of this subgroup carry a partial MIDAS motif and have the overall Para-Rossmann type fold that is characteristic of this superfamily.


Pssm-ID: 238756 [Multi-domain]  Cd Length: 244  Bit Score: 390.87  E-value: 5.87e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  443 PQPPVYLFVFDVSHNAVETGYLNSVCQSLLDNLDLLPGN-TRTKIGFITFDSTIHFYGLQESLSQPQMLIVSDIEDVFIP 521
Cdd:cd01479     1 PQPAVYVFLIDVSYNAIKSGLLATACEALLSNLDNLPGDdPRTRVGFITFDSTLHFFNLKSSLEQPQMMVVSDLDDPFLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  522 MPENLLVNLNESKELVQDLLKTLPQMFTKTLETQSALGPALQAAFKLMSPTGGRMSVFQTQLPTLGVGALKPREEPNHRS 601
Cdd:cd01479    81 LPDGLLVNLKESRQVIEDLLDQIPEMFQDTKETESALGPALQAAFLLLKETGGKIIVFQSSLPTLGAGKLKSREDPKLLS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  602 SAKD-IHMTPSTDFYKKLALDCSGQQVAVDLFLLSGQYSDLASLGCISRYSAGSVYYYPSyHHQHNPVQVQKLQKELQRY 680
Cdd:cd01479   161 TDKEkQLLQPQTDFYKKLALECVKSQISVDLFLFSNQYVDVATLGCLSRLTGGQVYYYPS-FNFSAPNDVEKLVNELARY 239


                  ....*
gi 578810097  681 LTRKI 685
Cdd:cd01479   240 LTRKI 244
Sec23_trunk pfam04811
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ...
 443-681 1.24e-107

Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi complex. This vesicular transport can be reconstituted by using three cytosolic components containing five proteins: the small GTPase Sar1p, the Sec23p/24p complex, and the Sec13p/Sec31p complex. This domain is known as the trunk domain and has an alpha/beta vWA fold and forms the dimer interface.


Pssm-ID: 398467 [Multi-domain]  Cd Length: 241  Bit Score: 334.60  E-value: 1.24e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097   443 PQPPVYLFVFDVSHNAVETGYLNSVCQSLLDNLDLLPGNTRTKIGFITFDSTIHFYGLQESLSQPQMLIVSDIEDVFIPM 522
Cdd:pfam04811    1 PQPPVFLFVIDVSYNAIKSGLLAALKESLLQSLDLLPGDPRARVGFITFDSTVHFFNLGSSLRQPQMLVVSDLQDMFLPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097   523 PENLLVNLNESKELVQDLLKTLPQMFTKTLETQSALGPALQAAFKLM--SPTGGRMSVFQTQLPTLGV-GALKPREEPNH 599
Cdd:pfam04811   81 PDRFLVPLSECRFVLEDLLEQLPPMFPVTKRPERCLGPALQAAFLLLkaAFTGGKIMVFQGGLPTVGPgGKLKSRLDESH 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097   600 RSSAKD-IHMTPSTD-FYKKLALDCSGQQVAVDLFLLSGQYSDLASLGCISRYSAGSVYYYPSYHHQHnpvQVQKLQKEL 677
Cdd:pfam04811  161 HGTDKEkAKLVKKADkFYKSLAKECVKQGHSVDLFAFSLDYVDVATLGQLSRLTGGQVYLYPSFQADV---DGSKFKQDL 237


                   ....
gi 578810097   678 QRYL 681
Cdd:pfam04811  238 QRYF 241
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 433-1035 4.26e-45

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 177.96  E-value: 4.26e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  433 MAPSEYMLRPPQ-----PPVYLFVFDVSHNAVetgyLNSVCQSLLDNLDLLPGNTR---TKIGFITFDSTIHFYGLQESL 504
Cdd:PTZ00395  935 IRRNSFLAKYPQvknmlPPYFVFVVECSYNAI----YNNITYTILEGIRYAVQNVKcpqTKIAIITFNSSIYFYHCKGGK 1010

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  505 SQP-------------QMLIVSDIEDVFIPMP-ENLLVNLNESKELVQDLLKTLPQMFTKTLETQSALGPALQAAFKLMS 570
Cdd:PTZ00395 1011 GVSgeegdggggsgnhQVIVMSDVDDPFLPLPlEDLFFGCVEEIDKINTLIDTIKSVSTTMQSYGSCGNSALKIAMDMLK 1090

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  571 PTGGRMSV--FQTQLPTLGVGALKPREepnhRSSAKDIHMTPSTDFYKKLALDCSGQQVAVDLFLLSGQYSDLA--SLGC 646
Cdd:PTZ00395 1091 ERNGLGSIcmFYTTTPNCGIGAIKELK----KDLQENFLEVKQKIFYDSLLLDLYAFNISVDIFIISSNNVRVCvpSLQY 1166

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  647 ISRYSAGSVYYYPSYHHQHNpvqVQKLQKELQRYLTRK-IGFEAVMRIRCTKGLSIHTF---HGNF-FVRSTDLLSLPNV 721
Cdd:PTZ00395 1167 VAQNTGGKILFVENFLWQKD---YKEIYMNIMDTLTSEdIAYCCELKLRYSHHMSVKKLfccNNNFnSIISVDTIKIPKI 1243

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  722 NPDAGYAVQMSVEESLTDTQLVSFQSALLYTSSKGERRIRVHTLCLPVVSTLNDVFLGADVQAisglLANMAVDRSMTAS 801
Cdd:PTZ00395 1244 RHDQTFAFLLNYSDISESKKQIYFQCACIYTNLWGDRFVRLHTTHMNLTSSLSTVFRYTDAEA----LMNILIKQLCTNI 1319

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  802 LSDarDALVNAVIDSLSA----YRSSVLSNQQPG-LMVPFSLRLFPLFVLALLKQKSfqTGTNARLDERIFAMCQVKNQP 876
Cdd:PTZ00395 1320 LHN--DNYSKIIIDNLAAilfsYRINCASSAHSGqLILPDTLKLLPLFTSSLLKHNV--TKKEILHDLKVYSLIKLLSMP 1395

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  877 LVYLMLTTHPSLY---------RVDNLSDEGALNISdRTIPQppilqlSVEKLSRDGAFLMDAGSVLMLWVGKNCTQNFL 947
Cdd:PTZ00395 1396 IISSLLYVYPVMYvihikgktnEIDSMDVDDDLFIP-KTIPS------SAEKIYSNGIYLLDACTHFYLYFGFHSDANFA 1468

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  948 SQVLGvqnyaSIPQPMT--DLPELDTPES---ARIIAFISWLREQRPFFPiLYVIRDESPMKANFLQNMIEDRTESALSY 1022
Cdd:PTZ00395 1469 KEIVG-----DIPTEKNahELNLTDTPNAqkvQRIIKNLSRIHHFNKYVP-LVMVAPKSNEEEHLISLCVEDKADKEYSY 1542

                         650
                  ....*....|...
gi 578810097 1023 YEFLLHIQQQVNK 1035
Cdd:PTZ00395 1543 VNFLCFIHKLVHK 1555
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 26-311 4.58e-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: 40.91  E-value: 4.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097    26 SGSPYTNGPVQN---ALLSSQESVSQGYNFQLPGSYPHPIPAKTLNPVSGQSNYGGSQGSGQTLN---RPPVASNPVTPS 99
Cdd:pfam03154  143 STSPSIPSPQDNesdSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPpqgSPATSQPPNQTQ 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097   100 LHSGPAPRMPLPASQNPATTPMPSSSFLPEANLPPPlnwqynypstaSQTnhCPRASSQPTVSGntSLTTNHQYVSSGYP 179
Cdd:pfam03154  223 STAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPP-----------SQV--SPQPLPQPSLHG--QMPPMPHSLQTGPS 287

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097   180 SLQNSFIKSGITSNTNNGSMVVHSSYDEIEGGGLLATPQLTNKNPKMSRSVGYSYPSLPPG---YQNTTPPGATGVP--- 253
Cdd:pfam03154  288 HMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAplsMPHIKPPPTTPIPqlp 367

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578810097   254 -PSSLNYP---SGPQAFTQT----PLGANHLTTSMSGL---SLQPEGLRvvnLLQERNMLPSTPLKPPV 311
Cdd:pfam03154  368 nPQSHKHPphlSGPSPFQMNsnlpPPPALKPLSSLSTHhppSAHPPPLQ---LMPQSQQLPPPPAQPPV 433
 
Name Accession Description Interval E-value
COG5028 COG5028
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ...
 172-1035 7.91e-179

Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking and secretion];


Pssm-ID: 227361 [Multi-domain]  Cd Length: 861  Bit Score: 543.23  E-value: 7.91e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  172 QYVSSGYPSLQNSFIKSGITSNtnnGSMVVHSSYDEIEGGGLLATPQLTNKNPKMSRSV--GYSYPSLPPGYQNTTPPGA 249
Cdd:COG5028     3 QHKKGVYPQAQSQVHTGAASSK---KSARPHRAYANFSAGQMGMPPYTTPPLQQQSRRQidQAATAMHNTGANNPAPSVM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  250 TGVPPSSLNYPS---GPQAFTQTPLGANHLTTSMSGLSLQPEglrvvnllQERNMLPSTPLKPPVPNLHEDIQKLNCNPE 326
Cdd:COG5028    80 SPAFQSQQKFSSpygGSMADGTAPKPTNPLVPVDLFEDQPPP--------ISDLFLPPPPIVPPLTTNFVGSEQSNCSPK 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  327 LFRCTLTSIPQTQALLNKAKLPLGLLLHPFKDLV----QLPVVTSSTIVRCRSCRTYINPFVSFLDQ-RRWKCNLCYRVN 401
Cdd:COG5028   152 YVRSTMYAIPETNDLLKKSKIPFGLVIRPFLELYpeedPVPLVEDGSIVRCRRCRSYINPFVQFIEQgRKWRCNICRSKN 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  402 DVPEEFlYNPLTRV--YGEPHRRPEVQNATIEFMAPSEYMLRPPQPPVYLFVFDVSHNAVETGYLNSVCQSLLDNLDLLP 479
Cdd:COG5028   232 DVPEGF-DNPSGPNdpRSDRYSRPELKSGVVDFLAPKEYSLRQPPPPVYVFLIDVSFEAIKNGLVKAAIRAILENLDQIP 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  480 G-NTRTKIGFITFDSTIHFYGLQESLSQpQMLIVSDIEDVFIPMPENLLV-NLNESKELVQDLLKTLPQMFTKTLETQSA 557
Cdd:COG5028   311 NfDPRTKIAIICFDSSLHFFKLSPDLDE-QMLIVSDLDEPFLPFPSGLFVlPLKSCKQIIETLLDRVPRIFQDNKSPKNA 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  558 LGPALQAAFKLMSPTGGRMSVFQTQLPTLGVGALKPREEPNHRssakdiHMTPSTDFYKKLALDCSGQQVAVDLFLLSGQ 637
Cdd:COG5028   390 LGPALKAAKSLIGGTGGKIIVFLSTLPNMGIGKLQLREDKESS------LLSCKDSFYKEFAIECSKVGISVDLFLTSED 463

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  638 YSDLASLGCISRYSAGSVYYYPSYHhQHNPVQVQKLQKELQRYLTRKIGFEAVMRIRCTKGLSIHTFHGNFFVRSTDLLS 717
Cdd:COG5028   464 YIDVATLSHLCRYTGGQTYFYPNFS-ATRPNDATKLANDLVSHLSMEIGYEAVMRVRCSTGLRVSSFYGNFFNRSSDLCA 542

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  718 LPNVNPDAGYAVQMSVEESLTdTQLVSFQSALLYTSSKGERRIRVHTLCLPVVSTLNDVFLGADVQAISGLLANMAVDRS 797
Cdd:COG5028   543 FSTMPRDTSLLVEFSIDEKLM-TSDVYFQVALLYTLNDGERRIRVVNLSLPTSSSIREVYASADQLAIACILAKKASTKA 621

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  798 MTASLSDARDALVNAVIDSLSAYRSS-VLSNQQPGLMVPFSLRLFPLFVLALLKQKSFQTGTNaRLDERIFAMCQVKNQP 876
Cdd:COG5028   622 LNSSLKEARVLINKSMVDILKAYKKElVKSNTSTQLPLPANLKLLPLLMLALLKSSAFRSGST-PSDIRISALNRLTSLP 700

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  877 LVYLMLTTHPSLYRVDNLSDEGALNISDRTI-PQPpiLQLSVEKLSRDGAFLMDAGSVLMLWVGKNCTQNFLSQVLGVQN 955
Cdd:COG5028   701 LKQLMRNIYPTLYALHDMPIEAGLPDEGLLVlPSP--INATSSLLESGGLYLIDTGQKIFLWFGKDAVPSLLQDLFGVDS 778

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  956 YASIPQPMTDLPELDTPESARIIAFISWLREQRPFFPI-LYVIRD--ESPMKANFLQNMIEDRTESALSYYEFLLHIQQQ 1032
Cdd:COG5028   779 LSDIPSGKFTLPPTGNEFNERVRNIIGELRSVNDDSTLpLVLVRGggDPSLRLWFFSTLVEDKTLNIPSYLDYLQILHEK 858


                  ...
gi 578810097 1033 VNK 1035
Cdd:COG5028   859 IKS 861
Sec24-like cd01479
Sec24-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ...
 443-685 5.87e-129

Sec24-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the budding and fusion of intracellular transport vesicles that selectively carry cargo proteins and lipids from donor to acceptor organelles. The two main classes of vesicular carriers within the endocytic and the biosynthetic pathways are COP- and clathrin-coated vesicles. Formation of COPII vesicles requires the ordered assembly of the coat built from several cytosolic components GTPase Sar1, complexes of Sec23-Sec24 and Sec13-Sec31. The process is initiated by the conversion of GDP to GTP by the GTPase Sar1 which then recruits the heterodimeric complex of Sec23 and Sec24. This heterodimeric complex generates the pre-budding complex. The final step leading to membrane deformation and budding of COPII-coated vesicles is carried by the heterodimeric complex Sec13-Sec31. The members of this CD belong to the Sec23-like family. Sec 24 is very similar to Sec23. The Sec23 and Sec24 polypeptides fold into five distinct domains: a beta-barrel, a zinc finger, a vWA or trunk, an all helical region and a carboxy Gelsolin domain. The members of this subgroup carry a partial MIDAS motif and have the overall Para-Rossmann type fold that is characteristic of this superfamily.


Pssm-ID: 238756 [Multi-domain]  Cd Length: 244  Bit Score: 390.87  E-value: 5.87e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  443 PQPPVYLFVFDVSHNAVETGYLNSVCQSLLDNLDLLPGN-TRTKIGFITFDSTIHFYGLQESLSQPQMLIVSDIEDVFIP 521
Cdd:cd01479     1 PQPAVYVFLIDVSYNAIKSGLLATACEALLSNLDNLPGDdPRTRVGFITFDSTLHFFNLKSSLEQPQMMVVSDLDDPFLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  522 MPENLLVNLNESKELVQDLLKTLPQMFTKTLETQSALGPALQAAFKLMSPTGGRMSVFQTQLPTLGVGALKPREEPNHRS 601
Cdd:cd01479    81 LPDGLLVNLKESRQVIEDLLDQIPEMFQDTKETESALGPALQAAFLLLKETGGKIIVFQSSLPTLGAGKLKSREDPKLLS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  602 SAKD-IHMTPSTDFYKKLALDCSGQQVAVDLFLLSGQYSDLASLGCISRYSAGSVYYYPSyHHQHNPVQVQKLQKELQRY 680
Cdd:cd01479   161 TDKEkQLLQPQTDFYKKLALECVKSQISVDLFLFSNQYVDVATLGCLSRLTGGQVYYYPS-FNFSAPNDVEKLVNELARY 239


                  ....*
gi 578810097  681 LTRKI 685
Cdd:cd01479   240 LTRKI 244
Sec23_trunk pfam04811
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ...
 443-681 1.24e-107

Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi complex. This vesicular transport can be reconstituted by using three cytosolic components containing five proteins: the small GTPase Sar1p, the Sec23p/24p complex, and the Sec13p/Sec31p complex. This domain is known as the trunk domain and has an alpha/beta vWA fold and forms the dimer interface.


Pssm-ID: 398467 [Multi-domain]  Cd Length: 241  Bit Score: 334.60  E-value: 1.24e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097   443 PQPPVYLFVFDVSHNAVETGYLNSVCQSLLDNLDLLPGNTRTKIGFITFDSTIHFYGLQESLSQPQMLIVSDIEDVFIPM 522
Cdd:pfam04811    1 PQPPVFLFVIDVSYNAIKSGLLAALKESLLQSLDLLPGDPRARVGFITFDSTVHFFNLGSSLRQPQMLVVSDLQDMFLPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097   523 PENLLVNLNESKELVQDLLKTLPQMFTKTLETQSALGPALQAAFKLM--SPTGGRMSVFQTQLPTLGV-GALKPREEPNH 599
Cdd:pfam04811   81 PDRFLVPLSECRFVLEDLLEQLPPMFPVTKRPERCLGPALQAAFLLLkaAFTGGKIMVFQGGLPTVGPgGKLKSRLDESH 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097   600 RSSAKD-IHMTPSTD-FYKKLALDCSGQQVAVDLFLLSGQYSDLASLGCISRYSAGSVYYYPSYHHQHnpvQVQKLQKEL 677
Cdd:pfam04811  161 HGTDKEkAKLVKKADkFYKSLAKECVKQGHSVDLFAFSLDYVDVATLGQLSRLTGGQVYLYPSFQADV---DGSKFKQDL 237


                   ....
gi 578810097   678 QRYL 681
Cdd:pfam04811  238 QRYF 241
trunk_domain cd01468
trunk domain. COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi ...
 443-679 7.45e-103

trunk domain. COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi complex. This vesicular transport can be reconstituted by using three cytosolic components containing five proteins: the small GTPase Sar1p, the Sec23p/24p complex, and the Sec13p/Sec31p complex. This domain is known as the trunk domain and has an alpha/beta vWA fold and forms the dimer interface. Some members of this family possess a partial MIDAS motif that is a characteristic feature of most vWA domain proteins.


Pssm-ID: 238745 [Multi-domain]  Cd Length: 239  Bit Score: 321.89  E-value: 7.45e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  443 PQPPVYLFVFDVSHNAVETGYLNSVCQSLLDNLDLLPGNTRTKIGFITFDSTIHFYGLQESLSQPQMLIVSDIEDVFIPM 522
Cdd:cd01468     1 PQPPVFVFVIDVSYEAIKEGLLQALKESLLASLDLLPGDPRARVGLITYDSTVHFYNLSSDLAQPKMYVVSDLKDVFLPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  523 PENLLVNLNESKELVQDLLKTLPQMFTK--TLETQSALGPALQAAFKLMSPT--GGRMSVFQTQLPTLGVGALKPREEPN 598
Cdd:cd01468    81 PDRFLVPLSECKKVIHDLLEQLPPMFWPvpTHRPERCLGPALQAAFLLLKGTfaGGRIIVFQGGLPTVGPGKLKSREDKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  599 HRSSAKD-IHMTPSTDFYKKLALDCSGQQVAVDLFLLSGQYSDLASLGCISRYSAGSVYYYPSYHHqhnPVQVQKLQKEL 677
Cdd:cd01468   161 PIRSHDEaQLLKPATKFYKSLAKECVKSGICVDLFAFSLDYVDVATLKQLAKSTGGQVYLYDSFQA---PNDGSKFKQDL 237


                  ..
gi 578810097  678 QR 679
Cdd:cd01468   238 QR 239
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 433-1035 4.26e-45

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 177.96  E-value: 4.26e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  433 MAPSEYMLRPPQ-----PPVYLFVFDVSHNAVetgyLNSVCQSLLDNLDLLPGNTR---TKIGFITFDSTIHFYGLQESL 504
Cdd:PTZ00395  935 IRRNSFLAKYPQvknmlPPYFVFVVECSYNAI----YNNITYTILEGIRYAVQNVKcpqTKIAIITFNSSIYFYHCKGGK 1010

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  505 SQP-------------QMLIVSDIEDVFIPMP-ENLLVNLNESKELVQDLLKTLPQMFTKTLETQSALGPALQAAFKLMS 570
Cdd:PTZ00395 1011 GVSgeegdggggsgnhQVIVMSDVDDPFLPLPlEDLFFGCVEEIDKINTLIDTIKSVSTTMQSYGSCGNSALKIAMDMLK 1090

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  571 PTGGRMSV--FQTQLPTLGVGALKPREepnhRSSAKDIHMTPSTDFYKKLALDCSGQQVAVDLFLLSGQYSDLA--SLGC 646
Cdd:PTZ00395 1091 ERNGLGSIcmFYTTTPNCGIGAIKELK----KDLQENFLEVKQKIFYDSLLLDLYAFNISVDIFIISSNNVRVCvpSLQY 1166

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  647 ISRYSAGSVYYYPSYHHQHNpvqVQKLQKELQRYLTRK-IGFEAVMRIRCTKGLSIHTF---HGNF-FVRSTDLLSLPNV 721
Cdd:PTZ00395 1167 VAQNTGGKILFVENFLWQKD---YKEIYMNIMDTLTSEdIAYCCELKLRYSHHMSVKKLfccNNNFnSIISVDTIKIPKI 1243

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  722 NPDAGYAVQMSVEESLTDTQLVSFQSALLYTSSKGERRIRVHTLCLPVVSTLNDVFLGADVQAisglLANMAVDRSMTAS 801
Cdd:PTZ00395 1244 RHDQTFAFLLNYSDISESKKQIYFQCACIYTNLWGDRFVRLHTTHMNLTSSLSTVFRYTDAEA----LMNILIKQLCTNI 1319

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  802 LSDarDALVNAVIDSLSA----YRSSVLSNQQPG-LMVPFSLRLFPLFVLALLKQKSfqTGTNARLDERIFAMCQVKNQP 876
Cdd:PTZ00395 1320 LHN--DNYSKIIIDNLAAilfsYRINCASSAHSGqLILPDTLKLLPLFTSSLLKHNV--TKKEILHDLKVYSLIKLLSMP 1395

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  877 LVYLMLTTHPSLY---------RVDNLSDEGALNISdRTIPQppilqlSVEKLSRDGAFLMDAGSVLMLWVGKNCTQNFL 947
Cdd:PTZ00395 1396 IISSLLYVYPVMYvihikgktnEIDSMDVDDDLFIP-KTIPS------SAEKIYSNGIYLLDACTHFYLYFGFHSDANFA 1468

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  948 SQVLGvqnyaSIPQPMT--DLPELDTPES---ARIIAFISWLREQRPFFPiLYVIRDESPMKANFLQNMIEDRTESALSY 1022
Cdd:PTZ00395 1469 KEIVG-----DIPTEKNahELNLTDTPNAqkvQRIIKNLSRIHHFNKYVP-LVMVAPKSNEEEHLISLCVEDKADKEYSY 1542

                         650
                  ....*....|...
gi 578810097 1023 YEFLLHIQQQVNK 1035
Cdd:PTZ00395 1543 VNFLCFIHKLVHK 1555
Sec23_BS pfam08033
Sec23/Sec24 beta-sandwich domain;
686-770 5.45e-32

Sec23/Sec24 beta-sandwich domain;


Pssm-ID: 429794 [Multi-domain]  Cd Length: 86  Bit Score: 119.56  E-value: 5.45e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097   686 GFEAVMRIRCTKGLSIHTFHGNFFVRS-TDLLSLPNVNPDAGYAVQMSVEESLTDTQLVSFQSALLYTSSKGERRIRVHT 764
Cdd:pfam08033    1 GFNAVLRVRTSKGLKVSGFIGNFVSRSsGDTWKLPSLDPDTSYAFEFDIDEPLPNGSNAYIQFALLYTHSSGERRIRVTT 80


                   ....*.
gi 578810097   765 LCLPVV 770
Cdd:pfam08033   81 VALPVT 86
Sec23_helical pfam04815
Sec23/Sec24 helical domain; COPII-coated vesicles carry proteins from the endoplasmic ...
 781-882 1.17e-31

Sec23/Sec24 helical domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi complex. This vesicular transport can be reconstituted by using three cytosolic components containing five proteins: the small GTPase Sar1p, the Sec23p/24p complex, and the Sec13p/Sec31p complex. This domain is composed of five alpha helices.


Pssm-ID: 461441 [Multi-domain]  Cd Length: 103  Bit Score: 119.14  E-value: 1.17e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097   781 DVQAISGLLANMAVDRSMTASLSDARDALVNAVIDSLSAYRSSVLSNQQPG-LMVPFSLRLFPLFVLALLKQKSFQTGTN 859
Cdd:pfam04815    1 DQEAIAVLLAKKAVEKALSSSLSDAREALDNKLVDILAAYRKYCASSSSPGqLILPESLKLLPLYMLALLKSPALRGGNS 80

                           90       100
                   ....*....|....*....|...
gi 578810097   860 ARLDERIFAMCQVKNQPLVYLML 882
Cdd:pfam04815   81 SPSDERAYARHLLLSLPVEELLL 103
PLN00162 PLN00162
transport protein sec23; Provisional
 329-632 2.96e-18

transport protein sec23; Provisional


Pssm-ID: 215083 [Multi-domain]  Cd Length: 761  Bit Score: 90.38  E-value: 2.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  329 RCTLTSIPQTQALLNKAKLPLGLLLHPFKDLVQLPVVTSSTIvRCRSCRTYINPF--VSFlDQRRWKCNLCYRVNDVPEE 406
Cdd:PLN00162   13 RMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPL-RCRTCRAVLNPYcrVDF-QAKIWICPFCFQRNHFPPH 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  407 FLYNPLTRVYGE--PhrrpevQNATIEFMAPSEYMLRPPqPPVYLFVFDVSHNAVETGYLNSvcqSLLDNLDLLPGNTRt 484
Cdd:PLN00162   91 YSSISETNLPAElfP------QYTTVEYTLPPGSGGAPS-PPVFVFVVDTCMIEEELGALKS---ALLQAIALLPENAL- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  485 kIGFITFDSTIHFYGL----------------------QESLS------QPQMLIVSDIEDVFIPMPEN-LLVNLNESK- 534
Cdd:PLN00162  160 -VGLITFGTHVHVHELgfsecsksyvfrgnkevskdqiLEQLGlggkkrRPAGGGIAGARDGLSSSGVNrFLLPASECEf 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  535 --ELVQDLLKTLPQMFTKTLETQSALGPALQAAFKLM---SP-TGGRMSVFQTQLPTLGVGAL--KPREEP--NHRSSAK 604
Cdd:PLN00162  239 tlNSALEELQKDPWPVPPGHRPARCTGAALSVAAGLLgacVPgTGARIMAFVGGPCTEGPGAIvsKDLSEPirSHKDLDK 318

                         330       340       350
                  ....*....|....*....|....*....|
gi 578810097  605 DI--HMTPSTDFYKKLALDCSGQQVAVDLF 632
Cdd:PLN00162  319 DAapYYKKAVKFYEGLAKQLVAQGHVLDVF 348
SEC23 COG5047
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
329-804 9.39e-17

Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];


Pssm-ID: 227380 [Multi-domain]  Cd Length: 755  Bit Score: 85.32  E-value: 9.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  329 RCTLTSIPQTQALLNKAKLPLGLLLHPFKDLVQLPVVTSSTIVRCRSCRTYINPFVSFLDQRR-WKCNLCYRVNDVPEEf 407
Cdd:COG5047    13 RLTWNVFPATRGDATRTVIPIACLYTPLHEDDALTVNYYEPVKCTAPCKAVLNPYCHIDERNQsWICPFCNQRNTLPPQ- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  408 lYNPLTRVYGEPhrRPEVQNATIEFMAPseymlRPPQ-PPVYLFVFDVshnAVETGYLNSVCQSLLDNLDLLPGNTRtkI 486
Cdd:COG5047    92 -YRDISNANLPL--ELLPQSSTIEYTLS-----KPVIlPPVFFFVVDA---CCDEEELTALKDSLIVSLSLLPPEAL--V 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  487 GFITFDSTIHF----------------------YGLQESLSQPQML----IVSDIEDVFIPMPENLLVNLNESKELVQDL 540
Cdd:COG5047   159 GLITYGTSIQVhelnaenhrrsyvfsgnkeytkENLQELLALSKPTksggFESKISGIGQFASSRFLLPTQQCEFKLLNI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  541 LKTL---PQMFTKTLETQSALGPALQAAFKLMS----PTGGRMSVFQTQLPTLGVGALKPRE--EP----NHRSSAKDIH 607
Cdd:COG5047   239 LEQLqpdPWPVPAGKRPLRCTGSALNIASSLLEqcfpNAGCHIVLFAGGPCTVGPGTVVSTElkEPmrshHDIESDSAQH 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  608 MTPSTDFYKKLALDCSGQQVAVDLFLLSGQYSDLASLGCISRYSAGSVYYYPSYhhqhnpvQVQKLQKELQRYLTR---- 683
Cdd:COG5047   319 SKKATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSF-------TTSIFKQSFQRIFNRdseg 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  684 --KIGFEAVMRIRCTKGLSIHTFHGN---------------FFVRSTDLLSLPNVNPDAGYAV------QMSVEESLTDT 740
Cdd:COG5047   392 ylKMGFNANMEVKTSKNLKIKGLIGHavsvkkkannisdseIGIGATNSWKMASLSPKSNYALyfeialGAASGSAQRPA 471

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578810097  741 Q-LVSFQSalLYTSSKGERRIRVHTLCLPVVSTLNDVFLGA-DVQAISGLLANMAVDRSMTASLSD 804
Cdd:COG5047   472 EaYIQFIT--TYQHSSGTYRIRVTTVARMFTDGGLPKINRSfDQEAAAVFMARIAAFKAETEDIID 535
zf-Sec23_Sec24 pfam04810
Sec23/Sec24 zinc finger; COPII-coated vesicles carry proteins from the endoplasmic reticulum ...
 370-406 6.74e-16

Sec23/Sec24 zinc finger; COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi complex. This vesicular transport can be reconstituted by using three cytosolic components containing five proteins: the small GTPase Sar1p, the Sec23p/24p complex, and the Sec13p/Sec31p complex. This domain is found to be zinc binding domain.


Pssm-ID: 461437 [Multi-domain]  Cd Length: 38  Bit Score: 72.09  E-value: 6.74e-16
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 578810097   370 IVRCRSCRTYINPFVSFLDQ-RRWKCNLCYRVNDVPEE 406
Cdd:pfam04810    1 PVRCRRCRAYLNPFCQFDFGgKKWTCNFCGTRNPVPPE 38
Gelsolin pfam00626
Gelsolin repeat;
906-981 6.50e-11

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 59.24  E-value: 6.50e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578810097   906 TIPQPPILQLSVEKLSRDGAFLMDAGSVLMLWVGKNctQNFLSQVLGVQNYASIPQPM-TDLPELDT-PESARIIAFI 981
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKG--SSLLEKLFAALLAAQLDDDErFPLPEVIRvPQGKEPARFL 76
Sec23-like cd01478
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ...
 443-632 7.51e-07

Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the budding and fusion of intracellular transport vesicles that selectively carry cargo proteins and lipids from donor to acceptor organelles. The two main classes of vesicular carriers within the endocytic and the biosynthetic pathways are COP- and clathrin-coated vesicles. Formation of COPII vesicles requires the ordered assembly of the coat built from several cytosolic components GTPase Sar1, complexes of Sec23-Sec24 and Sec13-Sec31. The process is initiated by the conversion of GDP to GTP by the GTPase Sar1 which then recruits the heterodimeric complex of Sec23 and Sec24. This heterodimeric complex generates the pre-budding complex. The final step leading to membrane deformation and budding of COPII-coated vesicles is carried by the heterodimeric complex Sec13-Sec31. The members of this CD belong to the Sec23-like family. Sec 23 is very similar to Sec24. The Sec23 and Sec24 polypeptides fold into five distinct domains: a beta-barrel, a zinc finger, a vWA or trunk, an all helical region and a carboxy Gelsolin domain. The members of this subgroup lack the consensus MIDAS motif but have the overall Para-Rossmann type fold that is characteristic of this superfamily.


Pssm-ID: 238755 [Multi-domain]  Cd Length: 267  Bit Score: 51.99  E-value: 7.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  443 PQPPVYLFVFDVSHNAVETGYLNSvcqSLLDNLDLLPGNTRtkIGFITFDSTIHFY------------------------ 498
Cdd:cd01478     1 TSPPVFLFVVDTCMDEEELDALKE---SLIMSLSLLPPNAL--VGLITFGTMVQVHelgfeecsksyvfrgnkdytakqi 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097  499 ----GLQESLSQPQMLIVSDIEDVFIPMPEN-LLVNLNESKELVQDLLKTL---PQMFTKTLETQSALGPALQAAFKLMS 570
Cdd:cd01478    76 qdmlGLGGPAMRPSASQHPGAGNPLPSAAASrFLLPVSQCEFTLTDLLEQLqpdPWPVPAGHRPLRCTGVALSIAVGLLE 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578810097  571 P----TGGRMSVFQTQLPTLGVGALKPREEPNHRSSAKDI------HMTPSTDFYKKLALDCSGQQVAVDLF 632
Cdd:cd01478   156 AcfpnTGARIMLFAGGPCTVGPGAVVSTELKDPIRSHHDIdkdnakYYKKAVKFYDSLAKRLAANGHAVDIF 227
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 55-312 1.22e-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: 42.83  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097    55 PGSYPHPIPAK--TLNPVSGQSNY---GGSQGSGQTLNRPpvASNPVTPSLHSGPAPR--------MPLPASQNPATTPM 121
Cdd:pfam03154  286 PSHMQHPVPPQpfPLTPQSSQSQVppgPSPAAPGQSQQRI--HTPPSQSQLQSQQPPReqplppapLSMPHIKPPPTTPI 363

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097   122 PS----------------SSFLPEANLPPPLNWQynyPSTASQTNHCPRASSQPTvsgntslttnhQYVSSGYPsLQNSF 185
Cdd:pfam03154  364 PQlpnpqshkhpphlsgpSPFQMNSNLPPPPALK---PLSSLSTHHPPSAHPPPL-----------QLMPQSQQ-LPPPP 428

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097   186 IKSGITSNTNNGSMVVHSSydeiegggllatPQLTNKNPKMSRSVGYSYPSLPPGYQNTTPPgaTGVPPSSLNYPSGPQA 265
Cdd:pfam03154  429 AQPPVLTQSQSLPPPAASH------------PPTSGLHQVPSQSPFPQHPFVPGGPPPITPP--SGPPTSTSSAMPGIQP 494

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 578810097   266 FTQTPLGANHLTTSMSGLSLQPeglrvVNLLQERNMLPSTPLKPPVP 312
Cdd:pfam03154  495 PSSASVSSSGPVPAAVSCPLPP-----VQIKEEALDEAEEPESPPPP 536
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 26-311 4.58e-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: 40.91  E-value: 4.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097    26 SGSPYTNGPVQN---ALLSSQESVSQGYNFQLPGSYPHPIPAKTLNPVSGQSNYGGSQGSGQTLN---RPPVASNPVTPS 99
Cdd:pfam03154  143 STSPSIPSPQDNesdSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPpqgSPATSQPPNQTQ 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097   100 LHSGPAPRMPLPASQNPATTPMPSSSFLPEANLPPPlnwqynypstaSQTnhCPRASSQPTVSGntSLTTNHQYVSSGYP 179
Cdd:pfam03154  223 STAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPP-----------SQV--SPQPLPQPSLHG--QMPPMPHSLQTGPS 287

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810097   180 SLQNSFIKSGITSNTNNGSMVVHSSYDEIEGGGLLATPQLTNKNPKMSRSVGYSYPSLPPG---YQNTTPPGATGVP--- 253
Cdd:pfam03154  288 HMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAplsMPHIKPPPTTPIPqlp 367

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578810097   254 -PSSLNYP---SGPQAFTQT----PLGANHLTTSMSGL---SLQPEGLRvvnLLQERNMLPSTPLKPPV 311
Cdd:pfam03154  368 nPQSHKHPphlSGPSPFQMNsnlpPPPALKPLSSLSTHhppSAHPPPLQ---LMPQSQQLPPPPAQPPV 433
 
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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