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Conserved domains on  [gi|193785341|dbj|BAG54494|]
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unnamed protein product [Homo sapiens]

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
 1-561 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: 879.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341   1 MLGLSKVPLTQATRGPQVQQPPPS----NRFLQPVQKIDMNLTDLLGELQRDPWPVPQGKRPLRSSGVALSIAVGLLECT 76
Cdd:PLN00162 199 QLGLGGKKRRPAGGGIAGARDGLSssgvNRFLLPASECEFTLNSALEELQKDPWPVPPGHRPARCTGAALSVAAGLLGAC 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341  77 FPNTGARIMMFIGGPATQGPGMVVGDELKTPIRSWHDIDKDNAKYVKKGTKHFEALANRAATTGHVIDIYACALDQTGLL 156
Cdd:PLN00162 279 VPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDAAPYYKKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVA 358

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 157 EMKCCPNLTGGYMVMGDSFNTSLFKQTFQRVFTKDMHGQFKMGFGGTLEIKTSREIKISGAIGPCVSLNSKGPCVSENEI 236
Cdd:PLN00162 359 EMKVAVERTGGLVVLAESFGHSVFKDSLRRVFERDGEGSLGLSFNGTFEVNCSKDVKVQGAIGPCASLEKKGPSVSDTEI 438

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 237 GTGGTCQWKICGLSPTTTLAIYFEVVNQHNA-PIPQGGRGAIQFVTQYQHSSGQRRIRVTTIARNWADAqTQIQNIAASF 315
Cdd:PLN00162 439 GEGGTTAWKLCGLDKKTSLAVFFEVANSGQSnPQPPGQQFFLQFLTRYQHSNGQTRLRVTTVTRRWVEG-SSSEELVAGF 517

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 316 DQEAAAILMARLAIYRAETEEGPDVLRWLDRQLIRLCQKFGEYHKDDPSSFRFSETFSLYPQFMFHLRRSSFLQVFNNSP 395
Cdd:PLN00162 518 DQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFGDYRKDDPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNNSP 597

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 396 DESSYYRHHFMRQDLTQSLIMIQPILYAYSFSGPPEPVLLDSSSILADRILLMDTFFQILIYHGETIAQWRKSGYQDMPE 475
Cdd:PLN00162 598 DETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLDVASIAADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPE 677

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 476 YENFRHLLQAPVDDAQEILHSRFPMPRYIDTEHGGSQARFLLSKVNPSQTHNNMYAWGqeSGAPILTDDVSLQVFMDHLK 555
Cdd:PLN00162 678 HEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFLLAKLNPSATYNSANAMG--GSDIIFTDDVSLQVFMEHLQ 755


                 ....*.
gi 193785341 556 KLAVSS 561
Cdd:PLN00162 756 RLAVQS 761
 
Name Accession Description Interval E-value
PLN00162 PLN00162
transport protein sec23; Provisional
 1-561 0e+00

transport protein sec23; Provisional


Pssm-ID: 215083 [Multi-domain]  Cd Length: 761  Bit Score: 879.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341   1 MLGLSKVPLTQATRGPQVQQPPPS----NRFLQPVQKIDMNLTDLLGELQRDPWPVPQGKRPLRSSGVALSIAVGLLECT 76
Cdd:PLN00162 199 QLGLGGKKRRPAGGGIAGARDGLSssgvNRFLLPASECEFTLNSALEELQKDPWPVPPGHRPARCTGAALSVAAGLLGAC 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341  77 FPNTGARIMMFIGGPATQGPGMVVGDELKTPIRSWHDIDKDNAKYVKKGTKHFEALANRAATTGHVIDIYACALDQTGLL 156
Cdd:PLN00162 279 VPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDAAPYYKKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVA 358

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 157 EMKCCPNLTGGYMVMGDSFNTSLFKQTFQRVFTKDMHGQFKMGFGGTLEIKTSREIKISGAIGPCVSLNSKGPCVSENEI 236
Cdd:PLN00162 359 EMKVAVERTGGLVVLAESFGHSVFKDSLRRVFERDGEGSLGLSFNGTFEVNCSKDVKVQGAIGPCASLEKKGPSVSDTEI 438

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 237 GTGGTCQWKICGLSPTTTLAIYFEVVNQHNA-PIPQGGRGAIQFVTQYQHSSGQRRIRVTTIARNWADAqTQIQNIAASF 315
Cdd:PLN00162 439 GEGGTTAWKLCGLDKKTSLAVFFEVANSGQSnPQPPGQQFFLQFLTRYQHSNGQTRLRVTTVTRRWVEG-SSSEELVAGF 517

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 316 DQEAAAILMARLAIYRAETEEGPDVLRWLDRQLIRLCQKFGEYHKDDPSSFRFSETFSLYPQFMFHLRRSSFLQVFNNSP 395
Cdd:PLN00162 518 DQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFGDYRKDDPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNNSP 597

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 396 DESSYYRHHFMRQDLTQSLIMIQPILYAYSFSGPPEPVLLDSSSILADRILLMDTFFQILIYHGETIAQWRKSGYQDMPE 475
Cdd:PLN00162 598 DETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLDVASIAADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPE 677

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 476 YENFRHLLQAPVDDAQEILHSRFPMPRYIDTEHGGSQARFLLSKVNPSQTHNNMYAWGqeSGAPILTDDVSLQVFMDHLK 555
Cdd:PLN00162 678 HEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFLLAKLNPSATYNSANAMG--GSDIIFTDDVSLQVFMEHLQ 755


                 ....*.
gi 193785341 556 KLAVSS 561
Cdd:PLN00162 756 RLAVQS 761
SEC23 COG5047
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
24-562 0e+00

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


Pssm-ID: 227380 [Multi-domain]  Cd Length: 755  Bit Score: 697.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341  24 SNRFLQPVQKIDMNLTDLLGELQRDPWPVPQGKRPLRSSGVALSIAVGLLECTFPNTGARIMMFIGGPATQGPGMVVGDE 103
Cdd:COG5047  221 SSRFLLPTQQCEFKLLNILEQLQPDPWPVPAGKRPLRCTGSALNIASSLLEQCFPNAGCHIVLFAGGPCTVGPGTVVSTE 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 104 LKTPIRSWHDIDKDNAKYVKKGTKHFEALANRAATTGHVIDIYACALDQTGLLEMKCCPNLTGGYMVMGDSFNTSLFKQT 183
Cdd:COG5047  301 LKEPMRSHHDIESDSAQHSKKATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSFTTSIFKQS 380

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 184 FQRVFTKDMHGQFKMGFGGTLEIKTSREIKISGAIGPCVSLNSKGPCVSENEIGTGGTCQWKICGLSPTTTLAIYFEVVN 263
Cdd:COG5047  381 FQRIFNRDSEGYLKMGFNANMEVKTSKNLKIKGLIGHAVSVKKKANNISDSEIGIGATNSWKMASLSPKSNYALYFEIAL 460

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 264 QHNAPIPQGG-RGAIQFVTQYQHSSGQRRIRVTTIARNWADAQTQIqnIAASFDQEAAAILMARLAIYRAETEEGPDVLR 342
Cdd:COG5047  461 GAASGSAQRPaEAYIQFITTYQHSSGTYRIRVTTVARMFTDGGLPK--INRSFDQEAAAVFMARIAAFKAETEDIIDVFR 538

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 343 WLDRQLIRLCQKFGEYHKDDPSSFRFSETFSLYPQFMFHLRRSSFLQVFNNSPDESSYYRHHFMRQDLTQSLIMIQPILY 422
Cdd:COG5047  539 WIDRNLIRLCQKFADYRKDDPSSFRLDPNFTLYPQFMYHLRRSPFLSVFNNSPDETAFYRHMLNNADVNDSLIMIQPTLQ 618

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 423 AYSFSGPPEPVLLDSSSILADRILLMDTFFQILIYHGETIAQWRKSGYQDMPEYENFRHLLQAPVDDAQEILHSRFPMPR 502
Cdd:COG5047  619 SYSFEKGGVPVLLDSVSVKPDVILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKELLEAPRLEAAELLQDRFPIPR 698

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 503 YIDTEHGGSQARFLLSKVNPSQTHNNMYAWGQESgapILTDDVSLQVFMDHLKKLAVSSA 562
Cdd:COG5047  699 FIVTEQGGSQARFLLSKINPSDITNKMSGGGSET---ILTDDVNLQKFMNHLRKLAVSKS 755
Sec23-like cd01478
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ...
 1-186 6.61e-108

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: 323.94  E-value: 6.61e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341   1 MLGLSKV---PLTQATRGPQVQQPP-PSNRFLQPVQKIDMNLTDLLGELQRDPWPVPQGKRPLRSSGVALSIAVGLLECT 76
Cdd:cd01478   78 MLGLGGPamrPSASQHPGAGNPLPSaAASRFLLPVSQCEFTLTDLLEQLQPDPWPVPAGHRPLRCTGVALSIAVGLLEAC 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341  77 FPNTGARIMMFIGGPATQGPGMVVGDELKTPIRSWHDIDKDNAKYVKKGTKHFEALANRAATTGHVIDIYACALDQTGLL 156
Cdd:cd01478  158 FPNTGARIMLFAGGPCTVGPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLL 237

                        170       180       190
                 ....*....|....*....|....*....|
gi 193785341 157 EMKCCPNLTGGYMVMGDSFNTSLFKQTFQR 186
Cdd:cd01478  238 EMKVLVNSTGGHVVLSDSFTTSIFKQSFQR 267
Sec23_trunk pfam04811
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ...
 16-188 6.07e-65

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: 212.11  E-value: 6.07e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341   16 PQVQQP--PPSNRFLQPVQKIDMNLTDLLGELQRdPWPVPqgKRPLRSSGVALSIAVGLLECTFpnTGARIMMFIGGPAT 93
Cdd:pfam04811  71 SDLQDMflPLPDRFLVPLSECRFVLEDLLEQLPP-MFPVT--KRPERCLGPALQAAFLLLKAAF--TGGKIMVFQGGLPT 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341   94 QGPGMVVGDELKtpiRSWHDIDKDNAKYVKKGTKHFEALANRAATTGHVIDIYACALDQTGLLEMKCCPNLTGGYMVMGD 173
Cdd:pfam04811 146 VGPGGKLKSRLD---ESHHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVATLGQLSRLTGGQVYLYP 222

                         170
                  ....*....|....*....
gi 193785341  174 SFN----TSLFKQTFQRVF 188
Cdd:pfam04811 223 SFQadvdGSKFKQDLQRYF 241
 
Name Accession Description Interval E-value
PLN00162 PLN00162
transport protein sec23; Provisional
 1-561 0e+00

transport protein sec23; Provisional


Pssm-ID: 215083 [Multi-domain]  Cd Length: 761  Bit Score: 879.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341   1 MLGLSKVPLTQATRGPQVQQPPPS----NRFLQPVQKIDMNLTDLLGELQRDPWPVPQGKRPLRSSGVALSIAVGLLECT 76
Cdd:PLN00162 199 QLGLGGKKRRPAGGGIAGARDGLSssgvNRFLLPASECEFTLNSALEELQKDPWPVPPGHRPARCTGAALSVAAGLLGAC 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341  77 FPNTGARIMMFIGGPATQGPGMVVGDELKTPIRSWHDIDKDNAKYVKKGTKHFEALANRAATTGHVIDIYACALDQTGLL 156
Cdd:PLN00162 279 VPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDAAPYYKKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVA 358

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 157 EMKCCPNLTGGYMVMGDSFNTSLFKQTFQRVFTKDMHGQFKMGFGGTLEIKTSREIKISGAIGPCVSLNSKGPCVSENEI 236
Cdd:PLN00162 359 EMKVAVERTGGLVVLAESFGHSVFKDSLRRVFERDGEGSLGLSFNGTFEVNCSKDVKVQGAIGPCASLEKKGPSVSDTEI 438

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 237 GTGGTCQWKICGLSPTTTLAIYFEVVNQHNA-PIPQGGRGAIQFVTQYQHSSGQRRIRVTTIARNWADAqTQIQNIAASF 315
Cdd:PLN00162 439 GEGGTTAWKLCGLDKKTSLAVFFEVANSGQSnPQPPGQQFFLQFLTRYQHSNGQTRLRVTTVTRRWVEG-SSSEELVAGF 517

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 316 DQEAAAILMARLAIYRAETEEGPDVLRWLDRQLIRLCQKFGEYHKDDPSSFRFSETFSLYPQFMFHLRRSSFLQVFNNSP 395
Cdd:PLN00162 518 DQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFGDYRKDDPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNNSP 597

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 396 DESSYYRHHFMRQDLTQSLIMIQPILYAYSFSGPPEPVLLDSSSILADRILLMDTFFQILIYHGETIAQWRKSGYQDMPE 475
Cdd:PLN00162 598 DETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLDVASIAADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPE 677

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 476 YENFRHLLQAPVDDAQEILHSRFPMPRYIDTEHGGSQARFLLSKVNPSQTHNNMYAWGqeSGAPILTDDVSLQVFMDHLK 555
Cdd:PLN00162 678 HEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFLLAKLNPSATYNSANAMG--GSDIIFTDDVSLQVFMEHLQ 755


                 ....*.
gi 193785341 556 KLAVSS 561
Cdd:PLN00162 756 RLAVQS 761
SEC23 COG5047
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
24-562 0e+00

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


Pssm-ID: 227380 [Multi-domain]  Cd Length: 755  Bit Score: 697.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341  24 SNRFLQPVQKIDMNLTDLLGELQRDPWPVPQGKRPLRSSGVALSIAVGLLECTFPNTGARIMMFIGGPATQGPGMVVGDE 103
Cdd:COG5047  221 SSRFLLPTQQCEFKLLNILEQLQPDPWPVPAGKRPLRCTGSALNIASSLLEQCFPNAGCHIVLFAGGPCTVGPGTVVSTE 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 104 LKTPIRSWHDIDKDNAKYVKKGTKHFEALANRAATTGHVIDIYACALDQTGLLEMKCCPNLTGGYMVMGDSFNTSLFKQT 183
Cdd:COG5047  301 LKEPMRSHHDIESDSAQHSKKATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSFTTSIFKQS 380

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 184 FQRVFTKDMHGQFKMGFGGTLEIKTSREIKISGAIGPCVSLNSKGPCVSENEIGTGGTCQWKICGLSPTTTLAIYFEVVN 263
Cdd:COG5047  381 FQRIFNRDSEGYLKMGFNANMEVKTSKNLKIKGLIGHAVSVKKKANNISDSEIGIGATNSWKMASLSPKSNYALYFEIAL 460

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 264 QHNAPIPQGG-RGAIQFVTQYQHSSGQRRIRVTTIARNWADAQTQIqnIAASFDQEAAAILMARLAIYRAETEEGPDVLR 342
Cdd:COG5047  461 GAASGSAQRPaEAYIQFITTYQHSSGTYRIRVTTVARMFTDGGLPK--INRSFDQEAAAVFMARIAAFKAETEDIIDVFR 538

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 343 WLDRQLIRLCQKFGEYHKDDPSSFRFSETFSLYPQFMFHLRRSSFLQVFNNSPDESSYYRHHFMRQDLTQSLIMIQPILY 422
Cdd:COG5047  539 WIDRNLIRLCQKFADYRKDDPSSFRLDPNFTLYPQFMYHLRRSPFLSVFNNSPDETAFYRHMLNNADVNDSLIMIQPTLQ 618

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 423 AYSFSGPPEPVLLDSSSILADRILLMDTFFQILIYHGETIAQWRKSGYQDMPEYENFRHLLQAPVDDAQEILHSRFPMPR 502
Cdd:COG5047  619 SYSFEKGGVPVLLDSVSVKPDVILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKELLEAPRLEAAELLQDRFPIPR 698

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 503 YIDTEHGGSQARFLLSKVNPSQTHNNMYAWGQESgapILTDDVSLQVFMDHLKKLAVSSA 562
Cdd:COG5047  699 FIVTEQGGSQARFLLSKINPSDITNKMSGGGSET---ILTDDVNLQKFMNHLRKLAVSKS 755
Sec23-like cd01478
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ...
 1-186 6.61e-108

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: 323.94  E-value: 6.61e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341   1 MLGLSKV---PLTQATRGPQVQQPP-PSNRFLQPVQKIDMNLTDLLGELQRDPWPVPQGKRPLRSSGVALSIAVGLLECT 76
Cdd:cd01478   78 MLGLGGPamrPSASQHPGAGNPLPSaAASRFLLPVSQCEFTLTDLLEQLQPDPWPVPAGHRPLRCTGVALSIAVGLLEAC 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341  77 FPNTGARIMMFIGGPATQGPGMVVGDELKTPIRSWHDIDKDNAKYVKKGTKHFEALANRAATTGHVIDIYACALDQTGLL 156
Cdd:cd01478  158 FPNTGARIMLFAGGPCTVGPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLL 237

                        170       180       190
                 ....*....|....*....|....*....|
gi 193785341 157 EMKCCPNLTGGYMVMGDSFNTSLFKQTFQR 186
Cdd:cd01478  238 EMKVLVNSTGGHVVLSDSFTTSIFKQSFQR 267
Sec23_C cd11287
C-terminal Actin depolymerization factor-homology domain of Sec23; The C-terminal domain of ...
 408-528 1.89e-86

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: 263.08  E-value: 1.89e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 408 QDLTQSLIMIQPILYAYSFSGPPEPVLLDSSSILADRILLMDTFFQILIYHGETIAQWRKSGYQDMPEYENFRHLLQAPV 487
Cdd:cd11287    1 EDVSNSLIMIQPTLYSYSFNGPPEPVLLDSSSILPDRILLLDTFFHILIYHGETIAQWRKAGYQDQPEYENFKDLLEAPV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 193785341 488 DDAQEILHSRFPMPRYIDTEHGGSQARFLLSKVNPSQTHNN 528
Cdd:cd11287   81 DDAQELLQDRFPMPRYIVTEQGGSQARFLLSKVNPSQTHNN 121
Sec23_trunk pfam04811
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ...
 16-188 6.07e-65

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: 212.11  E-value: 6.07e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341   16 PQVQQP--PPSNRFLQPVQKIDMNLTDLLGELQRdPWPVPqgKRPLRSSGVALSIAVGLLECTFpnTGARIMMFIGGPAT 93
Cdd:pfam04811  71 SDLQDMflPLPDRFLVPLSECRFVLEDLLEQLPP-MFPVT--KRPERCLGPALQAAFLLLKAAF--TGGKIMVFQGGLPT 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341   94 QGPGMVVGDELKtpiRSWHDIDKDNAKYVKKGTKHFEALANRAATTGHVIDIYACALDQTGLLEMKCCPNLTGGYMVMGD 173
Cdd:pfam04811 146 VGPGGKLKSRLD---ESHHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVATLGQLSRLTGGQVYLYP 222

                         170
                  ....*....|....*....
gi 193785341  174 SFN----TSLFKQTFQRVF 188
Cdd:pfam04811 223 SFQadvdGSKFKQDLQRYF 241
trunk_domain cd01468
trunk domain. COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi ...
 21-186 1.19e-56

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: 190.15  E-value: 1.19e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341  21 PPPSNRFLQPVQKIDMNLTDLLGELQRDPWPVPqGKRPLRSSGVALSIAVGLLECTFpnTGARIMMFIGGPATQGPGMVV 100
Cdd:cd01468   78 LPLPDRFLVPLSECKKVIHDLLEQLPPMFWPVP-THRPERCLGPALQAAFLLLKGTF--AGGRIIVFQGGLPTVGPGKLK 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 101 GDELKTPIRSWhdidkDNAKYVKKGTKHFEALANRAATTGHVIDIYACALDQTGLLEMKCCPNLTGGYMVMGDSFN---- 176
Cdd:cd01468  155 SREDKEPIRSH-----DEAQLLKPATKFYKSLAKECVKSGICVDLFAFSLDYVDVATLKQLAKSTGGQVYLYDSFQapnd 229

                        170
                 ....*....|
gi 193785341 177 TSLFKQTFQR 186
Cdd:cd01468  230 GSKFKQDLQR 239
Sec23_helical pfam04815
Sec23/Sec24 helical domain; COPII-coated vesicles carry proteins from the endoplasmic ...
 316-415 2.33e-34

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: 125.31  E-value: 2.33e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341  316 DQEAAAILMARLAIYRAETEEGPDVLRWLDRQLIRLCQKFGEYHKD--DPSSFRFSETFSLYPQFMFHLRRSSFLQVFNN 393
Cdd:pfam04815   1 DQEAIAVLLAKKAVEKALSSSLSDAREALDNKLVDILAAYRKYCASssSPGQLILPESLKLLPLYMLALLKSPALRGGNS 80

                          90       100
                  ....*....|....*....|...
gi 193785341  394 SP-DESSYYRHHFMRQDLTQSLI 415
Cdd:pfam04815  81 SPsDERAYARHLLLSLPVEELLL 103
Sec23_BS pfam08033
Sec23/Sec24 beta-sandwich domain;
199-302 4.65e-32

Sec23/Sec24 beta-sandwich domain;


Pssm-ID: 429794 [Multi-domain]  Cd Length: 86  Bit Score: 118.41  E-value: 4.65e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341  199 GFGGTLEIKTSREIKISGAIGPCVSLNSkgpcvseneigtGGTcqWKICGLSPTTTLAIYFEvvnqHNAPIPQGGRGAIQ 278
Cdd:pfam08033   1 GFNAVLRVRTSKGLKVSGFIGNFVSRSS------------GDT--WKLPSLDPDTSYAFEFD----IDEPLPNGSNAYIQ 62

                          90       100
                  ....*....|....*....|....
gi 193785341  279 FVTQYQHSSGQRRIRVTTIARNWA 302
Cdd:pfam08033  63 FALLYTHSSGERRIRVTTVALPVT 86
Gelsolin pfam00626
Gelsolin repeat;
430-516 5.15e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 67.33  E-value: 5.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341  430 PEPVLLDSSSILADRILLMDTFFqiliyhgeTIAQWRksGYQDMPEYENFRHLLQAPVDDAQeilhsRFPMPRYIDTEHG 509
Cdd:pfam00626   5 PPPVPLSQESLNSGDCYLLDNGF--------TIFLWV--GKGSSLLEKLFAALLAAQLDDDE-----RFPLPEVIRVPQG 69


                  ....*..
gi 193785341  510 GSQARFL 516
Cdd:pfam00626  70 KEPARFL 76
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 418-516 6.69e-14

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: 67.39  E-value: 6.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 418 QPILYAYSFSG--PPEPVLLDSSSILADRILLMDTFFQILIYHGEtiaqwrksgyqdmpeyENFRHLLQAPVDDAQEILH 495
Cdd:cd11280    1 PPRLYRVRGSKaiEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGR----------------ASSQAELAAAALLAKELDE 64

                         90       100
                 ....*....|....*....|.
gi 193785341 496 SRFPMPRYIDTEHGGSQARFL 516
Cdd:cd11280   65 ERKGKPEIVRIRQGQEPREFW 85
COG5028 COG5028
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ...
 18-465 3.11e-10

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


Pssm-ID: 227361 [Multi-domain]  Cd Length: 861  Bit Score: 62.89  E-value: 3.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341  18 VQQPPPSNRFLQPVQKIDMNLTDLLGELQRdpwpVPQGKR-PLRSSGVALSIAVGLLEctfpNTGARIMMFIGGPATQGP 96
Cdd:COG5028  349 PFLPFPSGLFVLPLKSCKQIIETLLDRVPR----IFQDNKsPKNALGPALKAAKSLIG----GTGGKIIVFLSTLPNMGI 420

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341  97 GMVvgdELKTPIRSWHDIDKDnaKYVKKGTKHFealanraATTGHVIDIYACALDQTGLLEMKCCPNLTGGYMVMGDSFN 176
Cdd:COG5028  421 GKL---QLREDKESSLLSCKD--SFYKEFAIEC-------SKVGISVDLFLTSEDYIDVATLSHLCRYTGGQTYFYPNFS 488

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 177 TSLFKQTFQrvFTKDM--HGQFKMGFGGTLEIKTSREIKISGAIGPCVSlNSKGPCvsenEIGTggtcqwkicgLSPTTT 254
Cdd:COG5028  489 ATRPNDATK--LANDLvsHLSMEIGYEAVMRVRCSTGLRVSSFYGNFFN-RSSDLC----AFST----------MPRDTS 551

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 255 LAIYFEVVNQHNAPipqggRGAIQFVTQYQHSSGQRRIRVTTIArnwADAQTQIQNIAASFDQEAAAILMARLAIyraeT 334
Cdd:COG5028  552 LLVEFSIDEKLMTS-----DVYFQVALLYTLNDGERRIRVVNLS---LPTSSSIREVYASADQLAIACILAKKAS----T 619

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785341 335 EEGPDVLRWLDRQLIRLCQKFGEYHKDD------PSSFRFSETFSLYPQFMFHLRRSSFLQVFNNSPDESSYYRHHFMRQ 408
Cdd:COG5028  620 KALNSSLKEARVLINKSMVDILKAYKKElvksntSTQLPLPANLKLLPLLMLALLKSSAFRSGSTPSDIRISALNRLTSL 699

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193785341 409 DLTQSLIMIQPILYA----YSFSGPPEPVLLDSSSILADRILLMDTFFQILIYHGETIAQW 465
Cdd:COG5028  700 PLKQLMRNIYPTLYAlhdmPIEAGLPDEGLLVLPSPINATSSLLESGGLYLIDTGQKIFLW 760
 
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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