|
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
|
|
| |
