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Conserved domains on  [gi|356582355|ref|NP_001239160|]
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protein transport protein Sec24A isoform 2 [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 ...
 255-592 6.69e-54

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: 197.32  E-value: 6.69e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582355 255 GSMVVHSSYDEIEGGGLLATPQLTNKNPKMSRSV--GYSYPSLPPGYQNTTPPGATGVPPSSLNYPS---GPQAFTQTPL 329
Cdd:COG5028   25 KSARPHRAYANFSAGQMGMPPYTTPPLQQQSRRQidQAATAMHNTGANNPAPSVMSPAFQSQQKFSSpygGSMADGTAPK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582355 330 GANHLTTSMSGLSLQPEGLRVVNllqernmlPSTPLKPPVPNLHEDIQKLNCNPELFRCTLTSIPQTQALLNKAKLPLGL 409
Cdd:COG5028  105 PTNPLVPVDLFEDQPPPISDLFL--------PPPPIVPPLTTNFVGSEQSNCSPKYVRSTMYAIPETNDLLKKSKIPFGL 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582355 410 LLHPFKDLV----QLPVVTSSTIVRCRSCRTYINPFVSFLDQ-RRWKCNLCYRVNDVPEEFlYNPLTRV--YGEPHRRPE 482
Cdd:COG5028  177 VIRPFLELYpeedPVPLVEDGSIVRCRRCRSYINPFVQFIEQgRKWRCNICRSKNDVPEGF-DNPSGPNdpRSDRYSRPE 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582355 483 VQNATIEFMAPSEYMLRPPQPPVYLFVFDVSHNAVETGYLNSVCQSLLDNLDLLPG-NTRTKIGFITFDSTIHFYGLQES 561
Cdd:COG5028  256 LKSGVVDFLAPKEYSLRQPPPPVYVFLIDVSFEAIKNGLVKAAIRAILENLDQIPNfDPRTKIAIICFDSSLHFFKLSPD 335

                        330       340       350
                 ....*....|....*....|....*....|..
gi 356582355 562 LSQpQMLIVSDIEDVFIPMPENLLV-NLNESK 592
Cdd:COG5028  336 LDE-QMLIVSDLDEPFLPFPSGLFVlPLKSCK 366
 
Name Accession Description Interval E-value
COG5028 COG5028
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ...
 255-592 6.69e-54

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


Pssm-ID: 227361 [Multi-domain]  Cd Length: 861  Bit Score: 197.32  E-value: 6.69e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582355 255 GSMVVHSSYDEIEGGGLLATPQLTNKNPKMSRSV--GYSYPSLPPGYQNTTPPGATGVPPSSLNYPS---GPQAFTQTPL 329
Cdd:COG5028   25 KSARPHRAYANFSAGQMGMPPYTTPPLQQQSRRQidQAATAMHNTGANNPAPSVMSPAFQSQQKFSSpygGSMADGTAPK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582355 330 GANHLTTSMSGLSLQPEGLRVVNllqernmlPSTPLKPPVPNLHEDIQKLNCNPELFRCTLTSIPQTQALLNKAKLPLGL 409
Cdd:COG5028  105 PTNPLVPVDLFEDQPPPISDLFL--------PPPPIVPPLTTNFVGSEQSNCSPKYVRSTMYAIPETNDLLKKSKIPFGL 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582355 410 LLHPFKDLV----QLPVVTSSTIVRCRSCRTYINPFVSFLDQ-RRWKCNLCYRVNDVPEEFlYNPLTRV--YGEPHRRPE 482
Cdd:COG5028  177 VIRPFLELYpeedPVPLVEDGSIVRCRRCRSYINPFVQFIEQgRKWRCNICRSKNDVPEGF-DNPSGPNdpRSDRYSRPE 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582355 483 VQNATIEFMAPSEYMLRPPQPPVYLFVFDVSHNAVETGYLNSVCQSLLDNLDLLPG-NTRTKIGFITFDSTIHFYGLQES 561
Cdd:COG5028  256 LKSGVVDFLAPKEYSLRQPPPPVYVFLIDVSFEAIKNGLVKAAIRAILENLDQIPNfDPRTKIAIICFDSSLHFFKLSPD 335

                        330       340       350
                 ....*....|....*....|....*....|..
gi 356582355 562 LSQpQMLIVSDIEDVFIPMPENLLV-NLNESK 592
Cdd:COG5028  336 LDE-QMLIVSDLDEPFLPFPSGLFVlPLKSCK 366
Sec24-like cd01479
Sec24-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ...
 501-595 6.56e-46

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: 162.44  E-value: 6.56e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582355 501 PQPPVYLFVFDVSHNAVETGYLNSVCQSLLDNLDLLPGN-TRTKIGFITFDSTIHFYGLQESLSQPQMLIVSDIEDVFIP 579
Cdd:cd01479    1 PQPAVYVFLIDVSYNAIKSGLLATACEALLSNLDNLPGDdPRTRVGFITFDSTLHFFNLKSSLEQPQMMVVSDLDDPFLP 80

                         90
                 ....*....|....*.
gi 356582355 580 MPENLLVNLNESKESV 595
Cdd:cd01479   81 LPDGLLVNLKESRQVI 96
Sec23_trunk pfam04811
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ...
 501-593 4.12e-43

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: 154.72  E-value: 4.12e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582355  501 PQPPVYLFVFDVSHNAVETGYLNSVCQSLLDNLDLLPGNTRTKIGFITFDSTIHFYGLQESLSQPQMLIVSDIEDVFIPM 580
Cdd:pfam04811   1 PQPPVFLFVIDVSYNAIKSGLLAALKESLLQSLDLLPGDPRARVGFITFDSTVHFFNLGSSLRQPQMLVVSDLQDMFLPL 80

                          90
                  ....*....|...
gi 356582355  581 PENLLVNLNESKE 593
Cdd:pfam04811  81 PDRFLVPLSECRF 93
PLN00162 PLN00162
transport protein sec23; Provisional
 387-558 3.34e-16

transport protein sec23; Provisional


Pssm-ID: 215083 [Multi-domain]  Cd Length: 761  Bit Score: 82.30  E-value: 3.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582355 387 RCTLTSIPQTQALLNKAKLPLGLLLHPFKDLVQLPVVTSSTIvRCRSCRTYINPF--VSFlDQRRWKCNLCYRVNDVPEE 464
Cdd:PLN00162  13 RMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPL-RCRTCRAVLNPYcrVDF-QAKIWICPFCFQRNHFPPH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582355 465 FLYNPLTRVYGE--PhrrpevQNATIEFMAPSEYMLRPPqPPVYLFVFDVSHNAVETGYLNSvcqSLLDNLDLLPGNTRt 542
Cdd:PLN00162  91 YSSISETNLPAElfP------QYTTVEYTLPPGSGGAPS-PPVFVFVVDTCMIEEELGALKS---ALLQAIALLPENAL- 159

                        170
                 ....*....|....*.
gi 356582355 543 kIGFITFDSTIHFYGL 558
Cdd:PLN00162 160 -VGLITFGTHVHVHEL 174
 
Name Accession Description Interval E-value
COG5028 COG5028
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ...
 255-592 6.69e-54

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


Pssm-ID: 227361 [Multi-domain]  Cd Length: 861  Bit Score: 197.32  E-value: 6.69e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582355 255 GSMVVHSSYDEIEGGGLLATPQLTNKNPKMSRSV--GYSYPSLPPGYQNTTPPGATGVPPSSLNYPS---GPQAFTQTPL 329
Cdd:COG5028   25 KSARPHRAYANFSAGQMGMPPYTTPPLQQQSRRQidQAATAMHNTGANNPAPSVMSPAFQSQQKFSSpygGSMADGTAPK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582355 330 GANHLTTSMSGLSLQPEGLRVVNllqernmlPSTPLKPPVPNLHEDIQKLNCNPELFRCTLTSIPQTQALLNKAKLPLGL 409
Cdd:COG5028  105 PTNPLVPVDLFEDQPPPISDLFL--------PPPPIVPPLTTNFVGSEQSNCSPKYVRSTMYAIPETNDLLKKSKIPFGL 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582355 410 LLHPFKDLV----QLPVVTSSTIVRCRSCRTYINPFVSFLDQ-RRWKCNLCYRVNDVPEEFlYNPLTRV--YGEPHRRPE 482
Cdd:COG5028  177 VIRPFLELYpeedPVPLVEDGSIVRCRRCRSYINPFVQFIEQgRKWRCNICRSKNDVPEGF-DNPSGPNdpRSDRYSRPE 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582355 483 VQNATIEFMAPSEYMLRPPQPPVYLFVFDVSHNAVETGYLNSVCQSLLDNLDLLPG-NTRTKIGFITFDSTIHFYGLQES 561
Cdd:COG5028  256 LKSGVVDFLAPKEYSLRQPPPPVYVFLIDVSFEAIKNGLVKAAIRAILENLDQIPNfDPRTKIAIICFDSSLHFFKLSPD 335

                        330       340       350
                 ....*....|....*....|....*....|..
gi 356582355 562 LSQpQMLIVSDIEDVFIPMPENLLV-NLNESK 592
Cdd:COG5028  336 LDE-QMLIVSDLDEPFLPFPSGLFVlPLKSCK 366
Sec24-like cd01479
Sec24-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ...
 501-595 6.56e-46

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: 162.44  E-value: 6.56e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582355 501 PQPPVYLFVFDVSHNAVETGYLNSVCQSLLDNLDLLPGN-TRTKIGFITFDSTIHFYGLQESLSQPQMLIVSDIEDVFIP 579
Cdd:cd01479    1 PQPAVYVFLIDVSYNAIKSGLLATACEALLSNLDNLPGDdPRTRVGFITFDSTLHFFNLKSSLEQPQMMVVSDLDDPFLP 80

                         90
                 ....*....|....*.
gi 356582355 580 MPENLLVNLNESKESV 595
Cdd:cd01479   81 LPDGLLVNLKESRQVI 96
Sec23_trunk pfam04811
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ...
 501-593 4.12e-43

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: 154.72  E-value: 4.12e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582355  501 PQPPVYLFVFDVSHNAVETGYLNSVCQSLLDNLDLLPGNTRTKIGFITFDSTIHFYGLQESLSQPQMLIVSDIEDVFIPM 580
Cdd:pfam04811   1 PQPPVFLFVIDVSYNAIKSGLLAALKESLLQSLDLLPGDPRARVGFITFDSTVHFFNLGSSLRQPQMLVVSDLQDMFLPL 80

                          90
                  ....*....|...
gi 356582355  581 PENLLVNLNESKE 593
Cdd:pfam04811  81 PDRFLVPLSECRF 93
trunk_domain cd01468
trunk domain. COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi ...
 501-595 2.54e-41

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: 149.70  E-value: 2.54e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582355 501 PQPPVYLFVFDVSHNAVETGYLNSVCQSLLDNLDLLPGNTRTKIGFITFDSTIHFYGLQESLSQPQMLIVSDIEDVFIPM 580
Cdd:cd01468    1 PQPPVFVFVIDVSYEAIKEGLLQALKESLLASLDLLPGDPRARVGLITYDSTVHFYNLSSDLAQPKMYVVSDLKDVFLPL 80

                         90
                 ....*....|....*
gi 356582355 581 PENLLVNLNESKESV 595
Cdd:cd01468   81 PDRFLVPLSECKKVI 95
PLN00162 PLN00162
transport protein sec23; Provisional
 387-558 3.34e-16

transport protein sec23; Provisional


Pssm-ID: 215083 [Multi-domain]  Cd Length: 761  Bit Score: 82.30  E-value: 3.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582355 387 RCTLTSIPQTQALLNKAKLPLGLLLHPFKDLVQLPVVTSSTIvRCRSCRTYINPF--VSFlDQRRWKCNLCYRVNDVPEE 464
Cdd:PLN00162  13 RMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPL-RCRTCRAVLNPYcrVDF-QAKIWICPFCFQRNHFPPH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582355 465 FLYNPLTRVYGE--PhrrpevQNATIEFMAPSEYMLRPPqPPVYLFVFDVSHNAVETGYLNSvcqSLLDNLDLLPGNTRt 542
Cdd:PLN00162  91 YSSISETNLPAElfP------QYTTVEYTLPPGSGGAPS-PPVFVFVVDTCMIEEELGALKS---ALLQAIALLPENAL- 159

                        170
                 ....*....|....*.
gi 356582355 543 kIGFITFDSTIHFYGL 558
Cdd:PLN00162 160 -VGLITFGTHVHVHEL 174
zf-Sec23_Sec24 pfam04810
Sec23/Sec24 zinc finger; COPII-coated vesicles carry proteins from the endoplasmic reticulum ...
 428-464 3.05e-15

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: 69.40  E-value: 3.05e-15
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 356582355  428 IVRCRSCRTYINPFVSFLDQ-RRWKCNLCYRVNDVPEE 464
Cdd:pfam04810   1 PVRCRRCRAYLNPFCQFDFGgKKWTCNFCGTRNPVPPE 38
SEC23 COG5047
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
387-558 8.33e-12

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


Pssm-ID: 227380 [Multi-domain]  Cd Length: 755  Bit Score: 68.37  E-value: 8.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582355 387 RCTLTSIPQTQALLNKAKLPLGLLLHPFKDLVQLPVVTSSTIVRCRSCRTYINPFVSFLDQRR-WKCNLCYRVNDVPEEf 465
Cdd:COG5047   13 RLTWNVFPATRGDATRTVIPIACLYTPLHEDDALTVNYYEPVKCTAPCKAVLNPYCHIDERNQsWICPFCNQRNTLPPQ- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582355 466 lYNPLTRVYGEPhrRPEVQNATIEFMAPseymlRPPQ-PPVYLFVFDVshnAVETGYLNSVCQSLLDNLDLLPGNTRtkI 544
Cdd:COG5047   92 -YRDISNANLPL--ELLPQSSTIEYTLS-----KPVIlPPVFFFVVDA---CCDEEELTALKDSLIVSLSLLPPEAL--V 158

                        170
                 ....*....|....
gi 356582355 545 GFITFDSTIHFYGL 558
Cdd:COG5047  159 GLITYGTSIQVHEL 172
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 491-595 1.40e-06

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 51.61  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582355  491 MAPSEYMLRPPQ-----PPVYLFVFDVSHNAVetgyLNSVCQSLLDNLDLLPGNTR---TKIGFITFDSTIHFYGLQESL 562
Cdd:PTZ00395  935 IRRNSFLAKYPQvknmlPPYFVFVVECSYNAI----YNNITYTILEGIRYAVQNVKcpqTKIAIITFNSSIYFYHCKGGK 1010

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 356582355  563 SQP-------------QMLIVSDIEDVFIPMP-ENLLVNLNESKESV 595
Cdd:PTZ00395 1011 GVSgeegdggggsgnhQVIVMSDVDDPFLPLPlEDLFFGCVEEIDKI 1057
Sec23-like cd01478
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ...
 501-558 3.26e-04

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: 42.74  E-value: 3.26e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 356582355 501 PQPPVYLFVFDVSHNAVETGYLNSvcqSLLDNLDLLPGNTRtkIGFITFDSTIHFYGL 558
Cdd:cd01478    1 TSPPVFLFVVDTCMDEEELDALKE---SLIMSLSLLPPNAL--VGLITFGTMVQVHEL 53
 
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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