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Conserved domains on  [gi|1039738669|ref|XP_017170322|]
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protein transport protein Sec24A isoform X1 [Mus musculus]

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 ...
 297-589 3.95e-55

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: 200.79  E-value: 3.95e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669 297 YQNSAPPVAGMPPPSLSYPSgpQAFTQTPLGANHLTASMSglslhpeglrvvnllqernmlpstPLQPPVPNLLEDIQKL 376
Cdd:COG5028    93 YGGSMADGTAPKPTNPLVPV--DLFEDQPPPISDLFLPPP------------------------PIVPPLTTNFVGSEQS 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669 377 NCNPELFRCTLTSVPQTQALLNKAKLPLGLLLHPFKDLV----QLPVVTSSTIVRCRSCRTYINPFVNFLDQ-RRWKCNL 451
Cdd:COG5028   147 NCSPKYVRSTMYAIPETNDLLKKSKIPFGLVIRPFLELYpeedPVPLVEDGSIVRCRRCRSYINPFVQFIEQgRKWRCNI 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669 452 CYRVNDVPEEFmYNPLTRV--YGEPHKRPEVQNATIEFMAPSEYMLRPPQPPVYLFVFDVSHNAIETGYLNSVCQSLLDN 529
Cdd:COG5028   227 CRSKNDVPEGF-DNPSGPNdpRSDRYSRPELKSGVVDFLAPKEYSLRQPPPPVYVFLIDVSFEAIKNGLVKAAIRAILEN 305

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039738669 530 LDLLPG-NTRTKIGFITFDSTIHFYSLQEGLSQpQMLIVSDIDDVFIPMPENLLV-NLNESK 589
Cdd:COG5028   306 LDQIPNfDPRTKIAIICFDSSLHFFKLSPDLDE-QMLIVSDLDEPFLPFPSGLFVlPLKSCK 366
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 5-367 4.29e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 4.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669    5 RIPAARGAAASLQAQNGAASASGSPYTNGPVHNTLMSPQVSSSQGYDSQPPGsyPRPMPAKTlnpfsaqsnyggsqgsgq 84
Cdd:PHA03247  2654 DDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPP--PTPEPAPH------------------ 2713

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669   85 tlnsPLVTSGPVLPSLHSGPVPRMPLPTSqnPAATPMPSGSFLPGANPPPPlnwqynypsTGPQTNHFPHVAPPTLP-GN 163
Cdd:PHA03247  2714 ----ALVSATPLPPGPAAARQASPALPAA--PAPPAVPAGPATPGGPARPA---------RPPTTAGPPAPAPPAAPaAG 2778

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669  164 PNLTADHQYVSSGDPALQTSFKKPGSALPLQNPPLPPTFQPGAPPGPPPAGGPPPSRGPAPQKTPPRAAPPPSFNSAVNQ 243
Cdd:PHA03247  2779 PPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAP 2858

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669  244 EG-ITSNANNGSTAAHNTYDEIEGGGFLATPQLVNQ-NPKTSRSVGSAYPSLPPGYQNSAPPVAGMPPPSLSYPSGPQAF 321
Cdd:PHA03247  2859 GGdVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRStESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR 2938

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1039738669  322 TQTPLGANHLTASMSGLSLHPEGLRVVNLLQERNMLPSTPLQPPVP 367
Cdd:PHA03247  2939 PQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
 
Name Accession Description Interval E-value
COG5028 COG5028
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ...
 297-589 3.95e-55

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


Pssm-ID: 227361 [Multi-domain]  Cd Length: 861  Bit Score: 200.79  E-value: 3.95e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669 297 YQNSAPPVAGMPPPSLSYPSgpQAFTQTPLGANHLTASMSglslhpeglrvvnllqernmlpstPLQPPVPNLLEDIQKL 376
Cdd:COG5028    93 YGGSMADGTAPKPTNPLVPV--DLFEDQPPPISDLFLPPP------------------------PIVPPLTTNFVGSEQS 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669 377 NCNPELFRCTLTSVPQTQALLNKAKLPLGLLLHPFKDLV----QLPVVTSSTIVRCRSCRTYINPFVNFLDQ-RRWKCNL 451
Cdd:COG5028   147 NCSPKYVRSTMYAIPETNDLLKKSKIPFGLVIRPFLELYpeedPVPLVEDGSIVRCRRCRSYINPFVQFIEQgRKWRCNI 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669 452 CYRVNDVPEEFmYNPLTRV--YGEPHKRPEVQNATIEFMAPSEYMLRPPQPPVYLFVFDVSHNAIETGYLNSVCQSLLDN 529
Cdd:COG5028   227 CRSKNDVPEGF-DNPSGPNdpRSDRYSRPELKSGVVDFLAPKEYSLRQPPPPVYVFLIDVSFEAIKNGLVKAAIRAILEN 305

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039738669 530 LDLLPG-NTRTKIGFITFDSTIHFYSLQEGLSQpQMLIVSDIDDVFIPMPENLLV-NLNESK 589
Cdd:COG5028   306 LDQIPNfDPRTKIAIICFDSSLHFFKLSPDLDE-QMLIVSDLDEPFLPFPSGLFVlPLKSCK 366
Sec24-like cd01479
Sec24-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ...
 498-592 1.23e-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: 164.37  E-value: 1.23e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669 498 PQPPVYLFVFDVSHNAIETGYLNSVCQSLLDNLDLLPGN-TRTKIGFITFDSTIHFYSLQEGLSQPQMLIVSDIDDVFIP 576
Cdd:cd01479     1 PQPAVYVFLIDVSYNAIKSGLLATACEALLSNLDNLPGDdPRTRVGFITFDSTLHFFNLKSSLEQPQMMVVSDLDDPFLP 80

                          90
                  ....*....|....*.
gi 1039738669 577 MPENLLVNLNESKESV 592
Cdd:cd01479    81 LPDGLLVNLKESRQVI 96
Sec23_trunk pfam04811
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ...
 498-590 1.33e-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: 155.87  E-value: 1.33e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669 498 PQPPVYLFVFDVSHNAIETGYLNSVCQSLLDNLDLLPGNTRTKIGFITFDSTIHFYSLQEGLSQPQMLIVSDIDDVFIPM 577
Cdd:pfam04811   1 PQPPVFLFVIDVSYNAIKSGLLAALKESLLQSLDLLPGDPRARVGFITFDSTVHFFNLGSSLRQPQMLVVSDLQDMFLPL 80

                          90
                  ....*....|...
gi 1039738669 578 PENLLVNLNESKE 590
Cdd:pfam04811  81 PDRFLVPLSECRF 93
PLN00162 PLN00162
transport protein sec23; Provisional
 384-555 3.60e-16

transport protein sec23; Provisional


Pssm-ID: 215083 [Multi-domain]  Cd Length: 761  Bit Score: 82.30  E-value: 3.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669 384 RCTLTSVPQTQALLNKAKLPLGLLLHPFKDLVQLPVVTSSTIvRCRSCRTYINPF--VNFlDQRRWKCNLCYRVNDVPEE 461
Cdd:PLN00162   13 RMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPL-RCRTCRAVLNPYcrVDF-QAKIWICPFCFQRNHFPPH 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669 462 FMYNPLTRVYGE--PhkrpevQNATIEFMAPSEYMLRPPqPPVYLFVFDVSHNAIETGYLNSvcqSLLDNLDLLPGNTRt 539
Cdd:PLN00162   91 YSSISETNLPAElfP------QYTTVEYTLPPGSGGAPS-PPVFVFVVDTCMIEEELGALKS---ALLQAIALLPENAL- 159

                         170
                  ....*....|....*.
gi 1039738669 540 kIGFITFDSTIHFYSL 555
Cdd:PLN00162  160 -VGLITFGTHVHVHEL 174
PHA03247 PHA03247
large tegument protein UL36; Provisional
 5-367 4.29e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 4.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669    5 RIPAARGAAASLQAQNGAASASGSPYTNGPVHNTLMSPQVSSSQGYDSQPPGsyPRPMPAKTlnpfsaqsnyggsqgsgq 84
Cdd:PHA03247  2654 DDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPP--PTPEPAPH------------------ 2713

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669   85 tlnsPLVTSGPVLPSLHSGPVPRMPLPTSqnPAATPMPSGSFLPGANPPPPlnwqynypsTGPQTNHFPHVAPPTLP-GN 163
Cdd:PHA03247  2714 ----ALVSATPLPPGPAAARQASPALPAA--PAPPAVPAGPATPGGPARPA---------RPPTTAGPPAPAPPAAPaAG 2778

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669  164 PNLTADHQYVSSGDPALQTSFKKPGSALPLQNPPLPPTFQPGAPPGPPPAGGPPPSRGPAPQKTPPRAAPPPSFNSAVNQ 243
Cdd:PHA03247  2779 PPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAP 2858

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669  244 EG-ITSNANNGSTAAHNTYDEIEGGGFLATPQLVNQ-NPKTSRSVGSAYPSLPPGYQNSAPPVAGMPPPSLSYPSGPQAF 321
Cdd:PHA03247  2859 GGdVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRStESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR 2938

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1039738669  322 TQTPLGANHLTASMSGLSLHPEGLRVVNLLQERNMLPSTPLQPPVP 367
Cdd:PHA03247  2939 PQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
 
Name Accession Description Interval E-value
COG5028 COG5028
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ...
 297-589 3.95e-55

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


Pssm-ID: 227361 [Multi-domain]  Cd Length: 861  Bit Score: 200.79  E-value: 3.95e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669 297 YQNSAPPVAGMPPPSLSYPSgpQAFTQTPLGANHLTASMSglslhpeglrvvnllqernmlpstPLQPPVPNLLEDIQKL 376
Cdd:COG5028    93 YGGSMADGTAPKPTNPLVPV--DLFEDQPPPISDLFLPPP------------------------PIVPPLTTNFVGSEQS 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669 377 NCNPELFRCTLTSVPQTQALLNKAKLPLGLLLHPFKDLV----QLPVVTSSTIVRCRSCRTYINPFVNFLDQ-RRWKCNL 451
Cdd:COG5028   147 NCSPKYVRSTMYAIPETNDLLKKSKIPFGLVIRPFLELYpeedPVPLVEDGSIVRCRRCRSYINPFVQFIEQgRKWRCNI 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669 452 CYRVNDVPEEFmYNPLTRV--YGEPHKRPEVQNATIEFMAPSEYMLRPPQPPVYLFVFDVSHNAIETGYLNSVCQSLLDN 529
Cdd:COG5028   227 CRSKNDVPEGF-DNPSGPNdpRSDRYSRPELKSGVVDFLAPKEYSLRQPPPPVYVFLIDVSFEAIKNGLVKAAIRAILEN 305

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039738669 530 LDLLPG-NTRTKIGFITFDSTIHFYSLQEGLSQpQMLIVSDIDDVFIPMPENLLV-NLNESK 589
Cdd:COG5028   306 LDQIPNfDPRTKIAIICFDSSLHFFKLSPDLDE-QMLIVSDLDEPFLPFPSGLFVlPLKSCK 366
Sec24-like cd01479
Sec24-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ...
 498-592 1.23e-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: 164.37  E-value: 1.23e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669 498 PQPPVYLFVFDVSHNAIETGYLNSVCQSLLDNLDLLPGN-TRTKIGFITFDSTIHFYSLQEGLSQPQMLIVSDIDDVFIP 576
Cdd:cd01479     1 PQPAVYVFLIDVSYNAIKSGLLATACEALLSNLDNLPGDdPRTRVGFITFDSTLHFFNLKSSLEQPQMMVVSDLDDPFLP 80

                          90
                  ....*....|....*.
gi 1039738669 577 MPENLLVNLNESKESV 592
Cdd:cd01479    81 LPDGLLVNLKESRQVI 96
Sec23_trunk pfam04811
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ...
 498-590 1.33e-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: 155.87  E-value: 1.33e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669 498 PQPPVYLFVFDVSHNAIETGYLNSVCQSLLDNLDLLPGNTRTKIGFITFDSTIHFYSLQEGLSQPQMLIVSDIDDVFIPM 577
Cdd:pfam04811   1 PQPPVFLFVIDVSYNAIKSGLLAALKESLLQSLDLLPGDPRARVGFITFDSTVHFFNLGSSLRQPQMLVVSDLQDMFLPL 80

                          90
                  ....*....|...
gi 1039738669 578 PENLLVNLNESKE 590
Cdd:pfam04811  81 PDRFLVPLSECRF 93
trunk_domain cd01468
trunk domain. COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi ...
 498-592 6.14e-42

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: 151.24  E-value: 6.14e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669 498 PQPPVYLFVFDVSHNAIETGYLNSVCQSLLDNLDLLPGNTRTKIGFITFDSTIHFYSLQEGLSQPQMLIVSDIDDVFIPM 577
Cdd:cd01468     1 PQPPVFVFVIDVSYEAIKEGLLQALKESLLASLDLLPGDPRARVGLITYDSTVHFYNLSSDLAQPKMYVVSDLKDVFLPL 80

                          90
                  ....*....|....*
gi 1039738669 578 PENLLVNLNESKESV 592
Cdd:cd01468    81 PDRFLVPLSECKKVI 95
PLN00162 PLN00162
transport protein sec23; Provisional
 384-555 3.60e-16

transport protein sec23; Provisional


Pssm-ID: 215083 [Multi-domain]  Cd Length: 761  Bit Score: 82.30  E-value: 3.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669 384 RCTLTSVPQTQALLNKAKLPLGLLLHPFKDLVQLPVVTSSTIvRCRSCRTYINPF--VNFlDQRRWKCNLCYRVNDVPEE 461
Cdd:PLN00162   13 RMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPL-RCRTCRAVLNPYcrVDF-QAKIWICPFCFQRNHFPPH 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669 462 FMYNPLTRVYGE--PhkrpevQNATIEFMAPSEYMLRPPqPPVYLFVFDVSHNAIETGYLNSvcqSLLDNLDLLPGNTRt 539
Cdd:PLN00162   91 YSSISETNLPAElfP------QYTTVEYTLPPGSGGAPS-PPVFVFVVDTCMIEEELGALKS---ALLQAIALLPENAL- 159

                         170
                  ....*....|....*.
gi 1039738669 540 kIGFITFDSTIHFYSL 555
Cdd:PLN00162  160 -VGLITFGTHVHVHEL 174
zf-Sec23_Sec24 pfam04810
Sec23/Sec24 zinc finger; COPII-coated vesicles carry proteins from the endoplasmic reticulum ...
 425-461 2.33e-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: 69.78  E-value: 2.33e-15
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1039738669 425 IVRCRSCRTYINPFVNFLDQ-RRWKCNLCYRVNDVPEE 461
Cdd:pfam04810   1 PVRCRRCRAYLNPFCQFDFGgKKWTCNFCGTRNPVPPE 38
SEC23 COG5047
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
384-555 4.56e-12

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


Pssm-ID: 227380 [Multi-domain]  Cd Length: 755  Bit Score: 69.14  E-value: 4.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669 384 RCTLTSVPQTQALLNKAKLPLGLLLHPFKDLVQLPVVTSSTIVRCRSCRTYINPFVNFLDQRR-WKCNLCYRVNDVPEEF 462
Cdd:COG5047    13 RLTWNVFPATRGDATRTVIPIACLYTPLHEDDALTVNYYEPVKCTAPCKAVLNPYCHIDERNQsWICPFCNQRNTLPPQY 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669 463 MYNPLTRVYGEPHKrpevQNATIEFMAPseymlRPPQ-PPVYLFVFDVshnAIETGYLNSVCQSLLDNLDLLPGNTRtkI 541
Cdd:COG5047    93 RDISNANLPLELLP----QSSTIEYTLS-----KPVIlPPVFFFVVDA---CCDEEELTALKDSLIVSLSLLPPEAL--V 158

                         170
                  ....*....|....
gi 1039738669 542 GFITFDSTIHFYSL 555
Cdd:COG5047   159 GLITYGTSIQVHEL 172
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 463-592 1.37e-08

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 58.16  E-value: 1.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669  463 MYNPLTRVYGEPHKRPEVQNATIEFMAPSEYMLrppqPPVYLFVFDVSHNAIetgyLNSVCQSLLDNLDLLPGNTR---T 539
Cdd:PTZ00395   919 MKNLICEKNGEPDSAKIRRNSFLAKYPQVKNML----PPYFVFVVECSYNAI----YNNITYTILEGIRYAVQNVKcpqT 990

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039738669  540 KIGFITFDSTIHFYSLQEGLSQP-------------QMLIVSDIDDVFIPMP-ENLLVNLNESKESV 592
Cdd:PTZ00395   991 KIAIITFNSSIYFYHCKGGKGVSgeegdggggsgnhQVIVMSDVDDPFLPLPlEDLFFGCVEEIDKI 1057
Sec23-like cd01478
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ...
 498-555 3.12e-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: 3.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738669 498 PQPPVYLFVFDVSHNAIETGYLNSvcqSLLDNLDLLPGNTRtkIGFITFDSTIHFYSL 555
Cdd:cd01478     1 TSPPVFLFVVDTCMDEEELDALKE---SLIMSLSLLPPNAL--VGLITFGTMVQVHEL 53
PHA03247 PHA03247
large tegument protein UL36; Provisional
 5-367 4.29e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 4.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669    5 RIPAARGAAASLQAQNGAASASGSPYTNGPVHNTLMSPQVSSSQGYDSQPPGsyPRPMPAKTlnpfsaqsnyggsqgsgq 84
Cdd:PHA03247  2654 DDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPP--PTPEPAPH------------------ 2713

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669   85 tlnsPLVTSGPVLPSLHSGPVPRMPLPTSqnPAATPMPSGSFLPGANPPPPlnwqynypsTGPQTNHFPHVAPPTLP-GN 163
Cdd:PHA03247  2714 ----ALVSATPLPPGPAAARQASPALPAA--PAPPAVPAGPATPGGPARPA---------RPPTTAGPPAPAPPAAPaAG 2778

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669  164 PNLTADHQYVSSGDPALQTSFKKPGSALPLQNPPLPPTFQPGAPPGPPPAGGPPPSRGPAPQKTPPRAAPPPSFNSAVNQ 243
Cdd:PHA03247  2779 PPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAP 2858

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669  244 EG-ITSNANNGSTAAHNTYDEIEGGGFLATPQLVNQ-NPKTSRSVGSAYPSLPPGYQNSAPPVAGMPPPSLSYPSGPQAF 321
Cdd:PHA03247  2859 GGdVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRStESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR 2938

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1039738669  322 TQTPLGANHLTASMSGLSLHPEGLRVVNLLQERNMLPSTPLQPPVP 367
Cdd:PHA03247  2939 PQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
PHA03247 PHA03247
large tegument protein UL36; Provisional
 2-305 1.59e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 1.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669    2 AQPRIPAARGAAASLQAQNGAASASGSPYTNGPVHNTlmSPQVsssqgydsqPPGSYPRPMPAKTLNPFSAQSNYGGSQG 81
Cdd:PHA03247  2734 ALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPA--PPAA---------PAAGPPRRLTRPAVASLSESRESLPSPW 2802

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669   82 SGQTLNSPLVTSGPVLPSlHSGPVPRMPLPTSQNPAATPMPSGSflpganPPPPLNWQYNYPSTGPQTNHFPHVAPPTLP 161
Cdd:PHA03247  2803 DPADPPAAVLAPAAALPP-AASPAGPLPPPTSAQPTAPPPPPGP------PPPSLPLGGSVAPGGDVRRRPPSRSPAAKP 2875

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669  162 GNPNltadHQYVSS-GDPALQTSFKKpgSALPLQNPPLPPTFQPGAPPGPPPAGGPPPSRGPAPQkTPPRAAPPPSFNSA 240
Cdd:PHA03247  2876 AAPA----RPPVRRlARPAVSRSTES--FALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPP-PPPRPQPPLAPTTD 2948

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039738669  241 vnqegiTSNANNGSTAAHNTYDEIEGGGFLATPQLVNQNPKTSRSVGSayPSLPPGYQNSAPPVA 305
Cdd:PHA03247  2949 ------PAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPA--SSTPPLTGHSLSRVS 3005
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 7-135 4.42e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.15  E-value: 4.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738669    7 PAARGAAASLQAQNGAASASGSPYTNGPVHNTLMSPQVSSSQGYDSQPPGSYPRPMPAKTLNPFSAQSNYGGSQGSGQTL 86
Cdd:PHA03307   334 ESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPR 413

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1039738669   87 NSPLVTSGPvlpslHSGPVPRMPLPtsqnpaatpMPSGSFLPGANPPPP 135
Cdd:PHA03307   414 PSPLDAGAA-----SGAFYARYPLL---------TPSGEPWPGSPPPPP 448
 
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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