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Conserved domains on  [gi|529250183|ref|NP_001268745|]
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protein transport protein Sec23B isoform 2 [Mus musculus]

Protein Classification

protein transport protein sec23( domain architecture ID 1004043)

protein transport protein sec23 is a component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER)

CATH:  1.20.120.730
Gene Ontology:  GO:0006886|GO:0008270|GO:0005096
PubMed:  8898360|18534853

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PLN00162 super family cl33419
transport protein sec23; Provisional
 3-613 0e+00

transport protein sec23; Provisional


The actual alignment was detected with superfamily member PLN00162:

Pssm-ID: 215083 [Multi-domain]  Cd Length: 761  Bit Score: 932.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183   3 LSLLPPDALVGLITFGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQEMLGLTKSAMPVQQARPAQPQEQPFVSS--RFL 80
Cdd:PLN00162 151 IALLPENALVGLITFGTHVHVHELGFSECSKSYVFRGNKEVSKDQILEQLGLGGKKRRPAGGGIAGARDGLSSSGvnRFL 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183  81 QPIHKIDMNLTDLLGELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNTGARIMLFTGGPPTQGPGMVVGDELKTPI 160
Cdd:PLN00162 231 LPASECEFTLNSALEELQKDPWPVPPGHRPARCTGAALSVAAGLLGACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPI 310

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 161 RSWHDIEKDNARFMKKATKHYEMLANRTATNGHCIDIYACALDQTGLLEMKCCPNLTGGHMVMGDSFNTSLFKQTFQRIF 240
Cdd:PLN00162 311 RSHKDLDKDAAPYYKKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVF 390

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 241 SKDFNGDFRMAFGATLDVKTSRELKIAGAIGPCVSLNVKGPCVSENELGVGGTSQWKICGLDPSSTLGIYFEVVNQHNA- 319
Cdd:PLN00162 391 ERDGEGSLGLSFNGTFEVNCSKDVKVQGAIGPCASLEKKGPSVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSn 470

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 320 PVPQGGRGAIQFVTQYQHSSTQKRIRVTTIARNWADAqSQLRHIEAAFDQEAAAVLMARLGVFRAESEEGPDVLRWLDRQ 399
Cdd:PLN00162 471 PQPPGQQFFLQFLTRYQHSNGQTRLRVTTVTRRWVEG-SSSEELVAGFDQEAAAVVMARLASHKMETEEEFDATRWLDRA 549

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 400 LIRLCQKFGQYNKEDPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFARQDLTQSLIMIQPILYSYSFH 479
Cdd:PLN00162 550 LIRLCSKFGDYRKDDPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNNSPDETAYFRMMLNRENVTNSLVMIQPTLISYSFN 629

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 480 GPPEPVLLDSSSILADRILLMDTFFQIVIYLGETIAQWRKAGYQDMPEYENFKHLLQAPLDDAQEILQARFPMPRYINTE 559
Cdd:PLN00162 630 GPPEPVLLDVASIAADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCD 709

                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....
gi 529250183 560 HGGSQARFLLSKVNPSQTHNNLYAWGqeTGAPILTDDVSLQVFMDHLKKLAVSS 613
Cdd:PLN00162 710 QHGSQARFLLAKLNPSATYNSANAMG--GSDIIFTDDVSLQVFMEHLQRLAVQS 761
 
Name Accession Description Interval E-value
PLN00162 PLN00162
transport protein sec23; Provisional
 3-613 0e+00

transport protein sec23; Provisional


Pssm-ID: 215083 [Multi-domain]  Cd Length: 761  Bit Score: 932.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183   3 LSLLPPDALVGLITFGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQEMLGLTKSAMPVQQARPAQPQEQPFVSS--RFL 80
Cdd:PLN00162 151 IALLPENALVGLITFGTHVHVHELGFSECSKSYVFRGNKEVSKDQILEQLGLGGKKRRPAGGGIAGARDGLSSSGvnRFL 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183  81 QPIHKIDMNLTDLLGELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNTGARIMLFTGGPPTQGPGMVVGDELKTPI 160
Cdd:PLN00162 231 LPASECEFTLNSALEELQKDPWPVPPGHRPARCTGAALSVAAGLLGACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPI 310

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 161 RSWHDIEKDNARFMKKATKHYEMLANRTATNGHCIDIYACALDQTGLLEMKCCPNLTGGHMVMGDSFNTSLFKQTFQRIF 240
Cdd:PLN00162 311 RSHKDLDKDAAPYYKKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVF 390

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 241 SKDFNGDFRMAFGATLDVKTSRELKIAGAIGPCVSLNVKGPCVSENELGVGGTSQWKICGLDPSSTLGIYFEVVNQHNA- 319
Cdd:PLN00162 391 ERDGEGSLGLSFNGTFEVNCSKDVKVQGAIGPCASLEKKGPSVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSn 470

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 320 PVPQGGRGAIQFVTQYQHSSTQKRIRVTTIARNWADAqSQLRHIEAAFDQEAAAVLMARLGVFRAESEEGPDVLRWLDRQ 399
Cdd:PLN00162 471 PQPPGQQFFLQFLTRYQHSNGQTRLRVTTVTRRWVEG-SSSEELVAGFDQEAAAVVMARLASHKMETEEEFDATRWLDRA 549

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 400 LIRLCQKFGQYNKEDPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFARQDLTQSLIMIQPILYSYSFH 479
Cdd:PLN00162 550 LIRLCSKFGDYRKDDPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNNSPDETAYFRMMLNRENVTNSLVMIQPTLISYSFN 629

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 480 GPPEPVLLDSSSILADRILLMDTFFQIVIYLGETIAQWRKAGYQDMPEYENFKHLLQAPLDDAQEILQARFPMPRYINTE 559
Cdd:PLN00162 630 GPPEPVLLDVASIAADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCD 709

                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....
gi 529250183 560 HGGSQARFLLSKVNPSQTHNNLYAWGqeTGAPILTDDVSLQVFMDHLKKLAVSS 613
Cdd:PLN00162 710 QHGSQARFLLAKLNPSATYNSANAMG--GSDIIFTDDVSLQVFMEHLQRLAVQS 761
SEC23 COG5047
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
2-614 0e+00

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


Pssm-ID: 227380 [Multi-domain]  Cd Length: 755  Bit Score: 767.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183   2 SLSLLPPDALVGLITFGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQEMLGLTKSAMPV--QQARPAQPQeqpFVSSRF 79
Cdd:COG5047  148 SLSLLPPEALVGLITYGTSIQVHELNAENHRRSYVFSGNKEYTKENLQELLALSKPTKSGgfESKISGIGQ---FASSRF 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183  80 LQPIHKIDMNLTDLLGELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNTGARIMLFTGGPPTQGPGMVVGDELKTP 159
Cdd:COG5047  225 LLPTQQCEFKLLNILEQLQPDPWPVPAGKRPLRCTGSALNIASSLLEQCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEP 304

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 160 IRSWHDIEKDNARFMKKATKHYEMLANRTATNGHCIDIYACALDQTGLLEMKCCPNLTGGHMVMGDSFNTSLFKQTFQRI 239
Cdd:COG5047  305 MRSHHDIESDSAQHSKKATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRI 384

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 240 FSKDFNGDFRMAFGATLDVKTSRELKIAGAIGPCVSLNVKGPCVSENELGVGGTSQWKICGLDPSSTLGIYFEVVNQHNA 319
Cdd:COG5047  385 FNRDSEGYLKMGFNANMEVKTSKNLKIKGLIGHAVSVKKKANNISDSEIGIGATNSWKMASLSPKSNYALYFEIALGAAS 464

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 320 PVPQGG-RGAIQFVTQYQHSSTQKRIRVTTIARNWADAQSQLrhIEAAFDQEAAAVLMARLGVFRAESEEGPDVLRWLDR 398
Cdd:COG5047  465 GSAQRPaEAYIQFITTYQHSSGTYRIRVTTVARMFTDGGLPK--INRSFDQEAAAVFMARIAAFKAETEDIIDVFRWIDR 542

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 399 QLIRLCQKFGQYNKEDPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFARQDLTQSLIMIQPILYSYSF 478
Cdd:COG5047  543 NLIRLCQKFADYRKDDPSSFRLDPNFTLYPQFMYHLRRSPFLSVFNNSPDETAFYRHMLNNADVNDSLIMIQPTLQSYSF 622

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 479 HGPPEPVLLDSSSILADRILLMDTFFQIVIYLGETIAQWRKAGYQDMPEYENFKHLLQAPLDDAQEILQARFPMPRYINT 558
Cdd:COG5047  623 EKGGVPVLLDSVSVKPDVILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKELLEAPRLEAAELLQDRFPIPRFIVT 702

                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 529250183 559 EHGGSQARFLLSKVNPSQTHNNLYAWGQETgapILTDDVSLQVFMDHLKKLAVSSA 614
Cdd:COG5047  703 EQGGSQARFLLSKINPSDITNKMSGGGSET---ILTDDVNLQKFMNHLRKLAVSKS 755
Sec23-like cd01478
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ...
 1-238 3.71e-156

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: 449.13  E-value: 3.71e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183   1 MSLSLLPPDALVGLITFGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQEMLGLTKSAMPVQQARPAQPQ--EQPFVSSR 78
Cdd:cd01478   28 MSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLGLGGPAMRPSASQHPGAGnpLPSAAASR 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183  79 FLQPIHKIDMNLTDLLGELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNTGARIMLFTGGPPTQGPGMVVGDELKT 158
Cdd:cd01478  108 FLLPVSQCEFTLTDLLEQLQPDPWPVPAGHRPLRCTGVALSIAVGLLEACFPNTGARIMLFAGGPCTVGPGAVVSTELKD 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 159 PIRSWHDIEKDNARFMKKATKHYEMLANRTATNGHCIDIYACALDQTGLLEMKCCPNLTGGHMVMGDSFNTSLFKQTFQR 238
Cdd:cd01478  188 PIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMKVLVNSTGGHVVLSDSFTTSIFKQSFQR 267
Sec23_trunk pfam04811
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ...
 1-240 8.63e-80

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: 252.17  E-value: 8.63e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183    1 MSLSLLP--PDALVGLITFGRMVQVHELSCEGisksyvfRGTKDLTAKQIQEMLGltksampvqqarpaqpqeqPFVSsR 78
Cdd:pfam04811  31 QSLDLLPgdPRARVGFITFDSTVHFFNLGSSL-------RQPQMLVVSDLQDMFL-------------------PLPD-R 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183   79 FLQPIHKIDMNLTDLLGELQRdPWPVTqgKRPLRSTGVALSIAVGLLEGTFpnTGARIMLFTGGPPTQGPGMVVGDELKt 158
Cdd:pfam04811  84 FLVPLSECRFVLEDLLEQLPP-MFPVT--KRPERCLGPALQAAFLLLKAAF--TGGKIMVFQGGLPTVGPGGKLKSRLD- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183  159 piRSWHDIEKDNARFMKKATKHYEMLANRTATNGHCIDIYACALDQTGLLEMKCCPNLTGGHMVMGDSFN----TSLFKQ 234
Cdd:pfam04811 158 --ESHHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVATLGQLSRLTGGQVYLYPSFQadvdGSKFKQ 235


                  ....*.
gi 529250183  235 TFQRIF 240
Cdd:pfam04811 236 DLQRYF 241
 
Name Accession Description Interval E-value
PLN00162 PLN00162
transport protein sec23; Provisional
 3-613 0e+00

transport protein sec23; Provisional


Pssm-ID: 215083 [Multi-domain]  Cd Length: 761  Bit Score: 932.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183   3 LSLLPPDALVGLITFGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQEMLGLTKSAMPVQQARPAQPQEQPFVSS--RFL 80
Cdd:PLN00162 151 IALLPENALVGLITFGTHVHVHELGFSECSKSYVFRGNKEVSKDQILEQLGLGGKKRRPAGGGIAGARDGLSSSGvnRFL 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183  81 QPIHKIDMNLTDLLGELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNTGARIMLFTGGPPTQGPGMVVGDELKTPI 160
Cdd:PLN00162 231 LPASECEFTLNSALEELQKDPWPVPPGHRPARCTGAALSVAAGLLGACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPI 310

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 161 RSWHDIEKDNARFMKKATKHYEMLANRTATNGHCIDIYACALDQTGLLEMKCCPNLTGGHMVMGDSFNTSLFKQTFQRIF 240
Cdd:PLN00162 311 RSHKDLDKDAAPYYKKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVF 390

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 241 SKDFNGDFRMAFGATLDVKTSRELKIAGAIGPCVSLNVKGPCVSENELGVGGTSQWKICGLDPSSTLGIYFEVVNQHNA- 319
Cdd:PLN00162 391 ERDGEGSLGLSFNGTFEVNCSKDVKVQGAIGPCASLEKKGPSVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSn 470

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 320 PVPQGGRGAIQFVTQYQHSSTQKRIRVTTIARNWADAqSQLRHIEAAFDQEAAAVLMARLGVFRAESEEGPDVLRWLDRQ 399
Cdd:PLN00162 471 PQPPGQQFFLQFLTRYQHSNGQTRLRVTTVTRRWVEG-SSSEELVAGFDQEAAAVVMARLASHKMETEEEFDATRWLDRA 549

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 400 LIRLCQKFGQYNKEDPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFARQDLTQSLIMIQPILYSYSFH 479
Cdd:PLN00162 550 LIRLCSKFGDYRKDDPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNNSPDETAYFRMMLNRENVTNSLVMIQPTLISYSFN 629

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 480 GPPEPVLLDSSSILADRILLMDTFFQIVIYLGETIAQWRKAGYQDMPEYENFKHLLQAPLDDAQEILQARFPMPRYINTE 559
Cdd:PLN00162 630 GPPEPVLLDVASIAADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCD 709

                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....
gi 529250183 560 HGGSQARFLLSKVNPSQTHNNLYAWGqeTGAPILTDDVSLQVFMDHLKKLAVSS 613
Cdd:PLN00162 710 QHGSQARFLLAKLNPSATYNSANAMG--GSDIIFTDDVSLQVFMEHLQRLAVQS 761
SEC23 COG5047
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
2-614 0e+00

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


Pssm-ID: 227380 [Multi-domain]  Cd Length: 755  Bit Score: 767.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183   2 SLSLLPPDALVGLITFGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQEMLGLTKSAMPV--QQARPAQPQeqpFVSSRF 79
Cdd:COG5047  148 SLSLLPPEALVGLITYGTSIQVHELNAENHRRSYVFSGNKEYTKENLQELLALSKPTKSGgfESKISGIGQ---FASSRF 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183  80 LQPIHKIDMNLTDLLGELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNTGARIMLFTGGPPTQGPGMVVGDELKTP 159
Cdd:COG5047  225 LLPTQQCEFKLLNILEQLQPDPWPVPAGKRPLRCTGSALNIASSLLEQCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEP 304

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 160 IRSWHDIEKDNARFMKKATKHYEMLANRTATNGHCIDIYACALDQTGLLEMKCCPNLTGGHMVMGDSFNTSLFKQTFQRI 239
Cdd:COG5047  305 MRSHHDIESDSAQHSKKATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRI 384

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 240 FSKDFNGDFRMAFGATLDVKTSRELKIAGAIGPCVSLNVKGPCVSENELGVGGTSQWKICGLDPSSTLGIYFEVVNQHNA 319
Cdd:COG5047  385 FNRDSEGYLKMGFNANMEVKTSKNLKIKGLIGHAVSVKKKANNISDSEIGIGATNSWKMASLSPKSNYALYFEIALGAAS 464

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 320 PVPQGG-RGAIQFVTQYQHSSTQKRIRVTTIARNWADAQSQLrhIEAAFDQEAAAVLMARLGVFRAESEEGPDVLRWLDR 398
Cdd:COG5047  465 GSAQRPaEAYIQFITTYQHSSGTYRIRVTTVARMFTDGGLPK--INRSFDQEAAAVFMARIAAFKAETEDIIDVFRWIDR 542

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 399 QLIRLCQKFGQYNKEDPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFARQDLTQSLIMIQPILYSYSF 478
Cdd:COG5047  543 NLIRLCQKFADYRKDDPSSFRLDPNFTLYPQFMYHLRRSPFLSVFNNSPDETAFYRHMLNNADVNDSLIMIQPTLQSYSF 622

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 479 HGPPEPVLLDSSSILADRILLMDTFFQIVIYLGETIAQWRKAGYQDMPEYENFKHLLQAPLDDAQEILQARFPMPRYINT 558
Cdd:COG5047  623 EKGGVPVLLDSVSVKPDVILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKELLEAPRLEAAELLQDRFPIPRFIVT 702

                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 529250183 559 EHGGSQARFLLSKVNPSQTHNNLYAWGQETgapILTDDVSLQVFMDHLKKLAVSSA 614
Cdd:COG5047  703 EQGGSQARFLLSKINPSDITNKMSGGGSET---ILTDDVNLQKFMNHLRKLAVSKS 755
Sec23-like cd01478
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ...
 1-238 3.71e-156

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: 449.13  E-value: 3.71e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183   1 MSLSLLPPDALVGLITFGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQEMLGLTKSAMPVQQARPAQPQ--EQPFVSSR 78
Cdd:cd01478   28 MSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLGLGGPAMRPSASQHPGAGnpLPSAAASR 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183  79 FLQPIHKIDMNLTDLLGELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNTGARIMLFTGGPPTQGPGMVVGDELKT 158
Cdd:cd01478  108 FLLPVSQCEFTLTDLLEQLQPDPWPVPAGHRPLRCTGVALSIAVGLLEACFPNTGARIMLFAGGPCTVGPGAVVSTELKD 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 159 PIRSWHDIEKDNARFMKKATKHYEMLANRTATNGHCIDIYACALDQTGLLEMKCCPNLTGGHMVMGDSFNTSLFKQTFQR 238
Cdd:cd01478  188 PIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMKVLVNSTGGHVVLSDSFTTSIFKQSFQR 267
Sec23_C cd11287
C-terminal Actin depolymerization factor-homology domain of Sec23; The C-terminal domain of ...
 460-580 8.82e-84

C-terminal Actin depolymerization factor-homology domain of Sec23; The C-terminal domain of the Sec23 subunit of the coat protein complex II (COPII) is distantly related to gelsolin-like repeats and the actin depolymerizing domains found in cofilin and similar proteins. Sec23 forms a tight complex with Sec24. The cytoplasmic Sec23/24 complex is recruited together with Sar1-GTP and Sec13/31 to induce coat polymerization and membrane deformation in the forming of COPII-coated endoplasmic reticulum vesicles. The function of the Sec23 C-terminal domain is unclear.


Pssm-ID: 200443 [Multi-domain]  Cd Length: 121  Bit Score: 257.69  E-value: 8.82e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 460 QDLTQSLIMIQPILYSYSFHGPPEPVLLDSSSILADRILLMDTFFQIVIYLGETIAQWRKAGYQDMPEYENFKHLLQAPL 539
Cdd:cd11287    1 EDVSNSLIMIQPTLYSYSFNGPPEPVLLDSSSILPDRILLLDTFFHILIYHGETIAQWRKAGYQDQPEYENFKDLLEAPV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 529250183 540 DDAQEILQARFPMPRYINTEHGGSQARFLLSKVNPSQTHNN 580
Cdd:cd11287   81 DDAQELLQDRFPMPRYIVTEQGGSQARFLLSKVNPSQTHNN 121
Sec23_trunk pfam04811
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ...
 1-240 8.63e-80

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: 252.17  E-value: 8.63e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183    1 MSLSLLP--PDALVGLITFGRMVQVHELSCEGisksyvfRGTKDLTAKQIQEMLGltksampvqqarpaqpqeqPFVSsR 78
Cdd:pfam04811  31 QSLDLLPgdPRARVGFITFDSTVHFFNLGSSL-------RQPQMLVVSDLQDMFL-------------------PLPD-R 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183   79 FLQPIHKIDMNLTDLLGELQRdPWPVTqgKRPLRSTGVALSIAVGLLEGTFpnTGARIMLFTGGPPTQGPGMVVGDELKt 158
Cdd:pfam04811  84 FLVPLSECRFVLEDLLEQLPP-MFPVT--KRPERCLGPALQAAFLLLKAAF--TGGKIMVFQGGLPTVGPGGKLKSRLD- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183  159 piRSWHDIEKDNARFMKKATKHYEMLANRTATNGHCIDIYACALDQTGLLEMKCCPNLTGGHMVMGDSFN----TSLFKQ 234
Cdd:pfam04811 158 --ESHHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVATLGQLSRLTGGQVYLYPSFQadvdGSKFKQ 235


                  ....*.
gi 529250183  235 TFQRIF 240
Cdd:pfam04811 236 DLQRYF 241
trunk_domain cd01468
trunk domain. COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi ...
 1-238 2.38e-76

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: 242.92  E-value: 2.38e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183   1 MSLSLLP--PDALVGLITFGRMVQVHELSCEGI-SKSYVFRGTKDLTAkqiqemlgltksampvqqarpaqpqeqPFVSs 77
Cdd:cd01468   31 ASLDLLPgdPRARVGLITYDSTVHFYNLSSDLAqPKMYVVSDLKDVFL---------------------------PLPD- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183  78 RFLQPIHKIDMNLTDLLGELQRDPWPVtQGKRPLRSTGVALSIAVGLLEGTFpnTGARIMLFTGGPPTQGPGMVVGDELK 157
Cdd:cd01468   83 RFLVPLSECKKVIHDLLEQLPPMFWPV-PTHRPERCLGPALQAAFLLLKGTF--AGGRIIVFQGGLPTVGPGKLKSREDK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 158 TPIRSWhdiekDNARFMKKATKHYEMLANRTATNGHCIDIYACALDQTGLLEMKCCPNLTGGHMVMGDSFN----TSLFK 233
Cdd:cd01468  160 EPIRSH-----DEAQLLKPATKFYKSLAKECVKSGICVDLFAFSLDYVDVATLKQLAKSTGGQVYLYDSFQapndGSKFK 234


                 ....*
gi 529250183 234 QTFQR 238
Cdd:cd01468  235 QDLQR 239
Sec23_helical pfam04815
Sec23/Sec24 helical domain; COPII-coated vesicles carry proteins from the endoplasmic ...
 368-467 2.62e-32

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: 119.91  E-value: 2.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183  368 DQEAAAVLMARLGVFRAESEEGPDVLRWLDRQLIRLCQKFGQYNKE--DPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNN 445
Cdd:pfam04815   1 DQEAIAVLLAKKAVEKALSSSLSDAREALDNKLVDILAAYRKYCASssSPGQLILPESLKLLPLYMLALLKSPALRGGNS 80

                          90       100
                  ....*....|....*....|...
gi 529250183  446 SP-DESSYYRHHFARQDLTQSLI 467
Cdd:pfam04815  81 SPsDERAYARHLLLSLPVEELLL 103
Sec23_BS pfam08033
Sec23/Sec24 beta-sandwich domain;
251-354 4.93e-28

Sec23/Sec24 beta-sandwich domain;


Pssm-ID: 429794 [Multi-domain]  Cd Length: 86  Bit Score: 107.62  E-value: 4.93e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183  251 AFGATLDVKTSRELKIAGAIGPCVSLNVkgpcvsenelgvGGTsqWKICGLDPSSTLGIYFEvvnqHNAPVPQGGRGAIQ 330
Cdd:pfam08033   1 GFNAVLRVRTSKGLKVSGFIGNFVSRSS------------GDT--WKLPSLDPDTSYAFEFD----IDEPLPNGSNAYIQ 62

                          90       100
                  ....*....|....*....|....
gi 529250183  331 FVTQYQHSSTQKRIRVTTIARNWA 354
Cdd:pfam08033  63 FALLYTHSSGERRIRVTTVALPVT 86
Gelsolin pfam00626
Gelsolin repeat;
482-568 2.42e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 71.18  E-value: 2.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183  482 PEPVLLDSSSILADRILLMDTFFqiviylgeTIAQWRkaGYQDMPEYENFKHLLQAPLDDaqeilQARFPMPRYINTEHG 561
Cdd:pfam00626   5 PPPVPLSQESLNSGDCYLLDNGF--------TIFLWV--GKGSSLLEKLFAALLAAQLDD-----DERFPLPEVIRVPQG 69


                  ....*..
gi 529250183  562 GSQARFL 568
Cdd:pfam00626  70 KEPARFL 76
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 470-568 2.20e-10

Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200436  Cd Length: 88  Bit Score: 57.38  E-value: 2.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 470 QPILY--SYSFHGPPEPVLLDSSSILADRILLMDTFFQIVIYLGEtiaqwrkagyqdmpeyENFKHLLQAPLDDAQEILQ 547
Cdd:cd11280    1 PPRLYrvRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGR----------------ASSQAELAAAALLAKELDE 64

                         90       100
                 ....*....|....*....|.
gi 529250183 548 ARFPMPRYINTEHGGSQARFL 568
Cdd:cd11280   65 ERKGKPEIVRIRQGQEPREFW 85
COG5028 COG5028
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ...
 73-512 4.43e-09

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


Pssm-ID: 227361 [Multi-domain]  Cd Length: 861  Bit Score: 59.42  E-value: 4.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183  73 PFVSSRFLQPI-HKIDMNLTdLLGELQRDPwpvTQGKRPLRSTGVALSIAVGLLEGTfpntGARIMLFTGGPPTQGPGMV 151
Cdd:COG5028  352 PFPSGLFVLPLkSCKQIIET-LLDRVPRIF---QDNKSPKNALGPALKAAKSLIGGT----GGKIIVFLSTLPNMGIGKL 423

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 152 vgdELKTPIRSWHDIEKDNarFMKKATKHYemlanrtATNGHCIDIYACALDQTGLLEMKCCPNLTGGHMVMGDSFNTSL 231
Cdd:COG5028  424 ---QLREDKESSLLSCKDS--FYKEFAIEC-------SKVGISVDLFLTSEDYIDVATLSHLCRYTGGQTYFYPNFSATR 491

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 232 FKQTFQriFSKDF--NGDFRMAFGATLDVKTSRELKIAGAIGPcvslnvkgpcVSENELGVGGTSQwkicgLDPSSTLGI 309
Cdd:COG5028  492 PNDATK--LANDLvsHLSMEIGYEAVMRVRCSTGLRVSSFYGN----------FFNRSSDLCAFST-----MPRDTSLLV 554

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 310 YFEVVNQHNAPvpqggRGAIQFVTQYQHSSTQKRIRVTTIArnwADAQSQLRHIEAAFDQEAAAVLMARLGVFRAESEEG 389
Cdd:COG5028  555 EFSIDEKLMTS-----DVYFQVALLYTLNDGERRIRVVNLS---LPTSSSIREVYASADQLAIACILAKKASTKALNSSL 626

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250183 390 PDVLRWLDRQLIRLCQkfgQYNKE-----DPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFARQDLTQ 464
Cdd:COG5028  627 KEARVLINKSMVDILK---AYKKElvksnTSTQLPLPANLKLLPLLMLALLKSSAFRSGSTPSDIRISALNRLTSLPLKQ 703

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 529250183 465 SLIMIQPILysYSFHGP--------------PEPVLLDSSSILADRILLMDTFFQIVIYLGE 512
Cdd:COG5028  704 LMRNIYPTL--YALHDMpieaglpdegllvlPSPINATSSLLESGGLYLIDTGQKIFLWFGK 763
 
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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