|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00162 |
PLN00162 |
transport protein sec23; Provisional |
2-655 |
0e+00 |
|
transport protein sec23; Provisional
Pssm-ID: 215083 [Multi-domain] Cd Length: 761 Bit Score: 984.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 2 PQFSTIEYMIQRGAR---SPLIFLYVVDTCLEEDDLQALKESLQMSLSLLPPDALVGLITFGRMVQVHELSCEGISKSYV 78
Cdd:PLN00162 105 PQYTTVEYTLPPGSGgapSPPVFVFVVDTCMIEEELGALKSALLQAIALLPENALVGLITFGTHVHVHELGFSECSKSYV 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 79 FRGTKDLTAKQIQEMLGLTKSAMPVQQARPAQPQEQPFVSS--RFLQPIHKIDMNLTDLLGELQRDPWPVTQGKRPLRST 156
Cdd:PLN00162 185 FRGNKEVSKDQILEQLGLGGKKRRPAGGGIAGARDGLSSSGvnRFLLPASECEFTLNSALEELQKDPWPVPPGHRPARCT 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 157 GVALSIAVGLLEGTFPNTGARIMLFTGGPPTQGPGMVVGDELKTPIRSWHDIEKDNARFMKKATKHYEMLANRTATNGHC 236
Cdd:PLN00162 265 GAALSVAAGLLGACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDAAPYYKKAVKFYEGLAKQLVAQGHV 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 237 IDIYACALDQTGLLEMKCCPNLTGGHMVMGDSFNTSLFKQTFQRIFSKDFNGDFRMAFGATLDVKTSRELKIAGAIGPCV 316
Cdd:PLN00162 345 LDVFACSLDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFERDGEGSLGLSFNGTFEVNCSKDVKVQGAIGPCA 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 317 SLNVKGPCVSENELGVGGTSQWKICGLDPSSTLGIYFEVVNQHNA-PVPQGGRGAIQFVTQYQHSSTQKRIRVTTIARNW 395
Cdd:PLN00162 425 SLEKKGPSVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSnPQPPGQQFFLQFLTRYQHSNGQTRLRVTTVTRRW 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 396 ADAqSQLRHIEAAFDQEAAAVLMARLGVFRAESEEGPDVLRWLDRQLIRLCQKFGQYNKEDPTSFRLSDSFSLYPQFMFH 475
Cdd:PLN00162 505 VEG-SSSEELVAGFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFGDYRKDDPSSFRLSPNFSLYPQFMFN 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 476 LRRSPFLQVFNNSPDESSYYRHHFARQDLTQSLIMIQPILYSYSFHGPPEPVLLDSSSILADRILLMDTFFQIVIYLGET 555
Cdd:PLN00162 584 LRRSQFVQVFNNSPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLDVASIAADRILLLDSYFSVVIFHGST 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 556 IAQWRKAGYQDMPEYENFKHLLQAPLDDAQEILQARFPMPRYINTEHGGSQARFLLSKVNPSQTHNNLYAWGqeTGAPIL 635
Cdd:PLN00162 664 IAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFLLAKLNPSATYNSANAMG--GSDIIF 741
|
650 660
....*....|....*....|
gi 1907140069 636 TDDVSLQVFMDHLKKLAVSS 655
Cdd:PLN00162 742 TDDVSLQVFMEHLQRLAVQS 761
|
|
| SEC23 |
COG5047 |
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]; |
1-656 |
0e+00 |
|
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
Pssm-ID: 227380 [Multi-domain] Cd Length: 755 Bit Score: 809.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 1 MPQFSTIEYMIQRGARSPLIFLYVVDTCLEEDDLQALKESLQMSLSLLPPDALVGLITFGRMVQVHELSCEGISKSYVFR 80
Cdd:COG5047 105 LPQSSTIEYTLSKPVILPPVFFFVVDACCDEEELTALKDSLIVSLSLLPPEALVGLITYGTSIQVHELNAENHRRSYVFS 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 81 GTKDLTAKQIQEMLGLTKSAMPV--QQARPAQPQeqpFVSSRFLQPIHKIDMNLTDLLGELQRDPWPVTQGKRPLRSTGV 158
Cdd:COG5047 185 GNKEYTKENLQELLALSKPTKSGgfESKISGIGQ---FASSRFLLPTQQCEFKLLNILEQLQPDPWPVPAGKRPLRCTGS 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 159 ALSIAVGLLEGTFPNTGARIMLFTGGPPTQGPGMVVGDELKTPIRSWHDIEKDNARFMKKATKHYEMLANRTATNGHCID 238
Cdd:COG5047 262 ALNIASSLLEQCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEPMRSHHDIESDSAQHSKKATKFYKGLAERVANQGHALD 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 239 IYACALDQTGLLEMKCCPNLTGGHMVMGDSFNTSLFKQTFQRIFSKDFNGDFRMAFGATLDVKTSRELKIAGAIGPCVSL 318
Cdd:COG5047 342 IFAGCLDQIGIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFNRDSEGYLKMGFNANMEVKTSKNLKIKGLIGHAVSV 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 319 NVKGPCVSENELGVGGTSQWKICGLDPSSTLGIYFEVVNQHNAPVPQGG-RGAIQFVTQYQHSSTQKRIRVTTIARNWAD 397
Cdd:COG5047 422 KKKANNISDSEIGIGATNSWKMASLSPKSNYALYFEIALGAASGSAQRPaEAYIQFITTYQHSSGTYRIRVTTVARMFTD 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 398 AQSQLrhIEAAFDQEAAAVLMARLGVFRAESEEGPDVLRWLDRQLIRLCQKFGQYNKEDPTSFRLSDSFSLYPQFMFHLR 477
Cdd:COG5047 502 GGLPK--INRSFDQEAAAVFMARIAAFKAETEDIIDVFRWIDRNLIRLCQKFADYRKDDPSSFRLDPNFTLYPQFMYHLR 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 478 RSPFLQVFNNSPDESSYYRHHFARQDLTQSLIMIQPILYSYSFHGPPEPVLLDSSSILADRILLMDTFFQIVIYLGETIA 557
Cdd:COG5047 580 RSPFLSVFNNSPDETAFYRHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVLLDSVSVKPDVILLLDTFFHILIFHGSYIA 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 558 QWRKAGYQDMPEYENFKHLLQAPLDDAQEILQARFPMPRYINTEHGGSQARFLLSKVNPSQTHNNLYAWGQETgapILTD 637
Cdd:COG5047 660 QWRNAGYQEQPEYLNLKELLEAPRLEAAELLQDRFPIPRFIVTEQGGSQARFLLSKINPSDITNKMSGGGSET---ILTD 736
|
650
....*....|....*....
gi 1907140069 638 DVSLQVFMDHLKKLAVSSA 656
Cdd:COG5047 737 DVNLQKFMNHLRKLAVSKS 755
|
|
| Sec23-like |
cd01478 |
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
17-280 |
1.76e-174 |
|
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: 497.28 E-value: 1.76e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 17 SPLIFLYVVDTCLEEDDLQALKESLQMSLSLLPPDALVGLITFGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQEMLGL 96
Cdd:cd01478 2 SPPVFLFVVDTCMDEEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 97 TKSAMPVQQARPAQPQ--EQPFVSSRFLQPIHKIDMNLTDLLGELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNT 174
Cdd:cd01478 82 GGPAMRPSASQHPGAGnpLPSAAASRFLLPVSQCEFTLTDLLEQLQPDPWPVPAGHRPLRCTGVALSIAVGLLEACFPNT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 175 GARIMLFTGGPPTQGPGMVVGDELKTPIRSWHDIEKDNARFMKKATKHYEMLANRTATNGHCIDIYACALDQTGLLEMKC 254
Cdd:cd01478 162 GARIMLFAGGPCTVGPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMKV 241
|
250 260
....*....|....*....|....*.
gi 1907140069 255 CPNLTGGHMVMGDSFNTSLFKQTFQR 280
Cdd:cd01478 242 LVNSTGGHVVLSDSFTTSIFKQSFQR 267
|
|
| Sec23_trunk |
pfam04811 |
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
17-282 |
3.30e-91 |
|
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: 282.60 E-value: 3.30e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 17 SPLIFLYVVDTCLE---EDDLQALKESLQMSLSLLP--PDALVGLITFGRMVQVHELSCEGisksyvfRGTKDLTAKQIQ 91
Cdd:pfam04811 2 QPPVFLFVIDVSYNaikSGLLAALKESLLQSLDLLPgdPRARVGFITFDSTVHFFNLGSSL-------RQPQMLVVSDLQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 92 EMLGltksampvqqarpaqpqeqPFVSsRFLQPIHKIDMNLTDLLGELQRdPWPVTqgKRPLRSTGVALSIAVGLLEGTF 171
Cdd:pfam04811 75 DMFL-------------------PLPD-RFLVPLSECRFVLEDLLEQLPP-MFPVT--KRPERCLGPALQAAFLLLKAAF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 172 pnTGARIMLFTGGPPTQGPGMVVGDELKtpiRSWHDIEKDNARFMKKATKHYEMLANRTATNGHCIDIYACALDQTGLLE 251
Cdd:pfam04811 132 --TGGKIMVFQGGLPTVGPGGKLKSRLD---ESHHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVAT 206
|
250 260 270
....*....|....*....|....*....|....*
gi 1907140069 252 MKCCPNLTGGHMVMGDSFN----TSLFKQTFQRIF 282
Cdd:pfam04811 207 LGQLSRLTGGQVYLYPSFQadvdGSKFKQDLQRYF 241
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00162 |
PLN00162 |
transport protein sec23; Provisional |
2-655 |
0e+00 |
|
transport protein sec23; Provisional
Pssm-ID: 215083 [Multi-domain] Cd Length: 761 Bit Score: 984.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 2 PQFSTIEYMIQRGAR---SPLIFLYVVDTCLEEDDLQALKESLQMSLSLLPPDALVGLITFGRMVQVHELSCEGISKSYV 78
Cdd:PLN00162 105 PQYTTVEYTLPPGSGgapSPPVFVFVVDTCMIEEELGALKSALLQAIALLPENALVGLITFGTHVHVHELGFSECSKSYV 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 79 FRGTKDLTAKQIQEMLGLTKSAMPVQQARPAQPQEQPFVSS--RFLQPIHKIDMNLTDLLGELQRDPWPVTQGKRPLRST 156
Cdd:PLN00162 185 FRGNKEVSKDQILEQLGLGGKKRRPAGGGIAGARDGLSSSGvnRFLLPASECEFTLNSALEELQKDPWPVPPGHRPARCT 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 157 GVALSIAVGLLEGTFPNTGARIMLFTGGPPTQGPGMVVGDELKTPIRSWHDIEKDNARFMKKATKHYEMLANRTATNGHC 236
Cdd:PLN00162 265 GAALSVAAGLLGACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDAAPYYKKAVKFYEGLAKQLVAQGHV 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 237 IDIYACALDQTGLLEMKCCPNLTGGHMVMGDSFNTSLFKQTFQRIFSKDFNGDFRMAFGATLDVKTSRELKIAGAIGPCV 316
Cdd:PLN00162 345 LDVFACSLDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFERDGEGSLGLSFNGTFEVNCSKDVKVQGAIGPCA 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 317 SLNVKGPCVSENELGVGGTSQWKICGLDPSSTLGIYFEVVNQHNA-PVPQGGRGAIQFVTQYQHSSTQKRIRVTTIARNW 395
Cdd:PLN00162 425 SLEKKGPSVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSnPQPPGQQFFLQFLTRYQHSNGQTRLRVTTVTRRW 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 396 ADAqSQLRHIEAAFDQEAAAVLMARLGVFRAESEEGPDVLRWLDRQLIRLCQKFGQYNKEDPTSFRLSDSFSLYPQFMFH 475
Cdd:PLN00162 505 VEG-SSSEELVAGFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFGDYRKDDPSSFRLSPNFSLYPQFMFN 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 476 LRRSPFLQVFNNSPDESSYYRHHFARQDLTQSLIMIQPILYSYSFHGPPEPVLLDSSSILADRILLMDTFFQIVIYLGET 555
Cdd:PLN00162 584 LRRSQFVQVFNNSPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLDVASIAADRILLLDSYFSVVIFHGST 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 556 IAQWRKAGYQDMPEYENFKHLLQAPLDDAQEILQARFPMPRYINTEHGGSQARFLLSKVNPSQTHNNLYAWGqeTGAPIL 635
Cdd:PLN00162 664 IAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFLLAKLNPSATYNSANAMG--GSDIIF 741
|
650 660
....*....|....*....|
gi 1907140069 636 TDDVSLQVFMDHLKKLAVSS 655
Cdd:PLN00162 742 TDDVSLQVFMEHLQRLAVQS 761
|
|
| SEC23 |
COG5047 |
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]; |
1-656 |
0e+00 |
|
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
Pssm-ID: 227380 [Multi-domain] Cd Length: 755 Bit Score: 809.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 1 MPQFSTIEYMIQRGARSPLIFLYVVDTCLEEDDLQALKESLQMSLSLLPPDALVGLITFGRMVQVHELSCEGISKSYVFR 80
Cdd:COG5047 105 LPQSSTIEYTLSKPVILPPVFFFVVDACCDEEELTALKDSLIVSLSLLPPEALVGLITYGTSIQVHELNAENHRRSYVFS 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 81 GTKDLTAKQIQEMLGLTKSAMPV--QQARPAQPQeqpFVSSRFLQPIHKIDMNLTDLLGELQRDPWPVTQGKRPLRSTGV 158
Cdd:COG5047 185 GNKEYTKENLQELLALSKPTKSGgfESKISGIGQ---FASSRFLLPTQQCEFKLLNILEQLQPDPWPVPAGKRPLRCTGS 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 159 ALSIAVGLLEGTFPNTGARIMLFTGGPPTQGPGMVVGDELKTPIRSWHDIEKDNARFMKKATKHYEMLANRTATNGHCID 238
Cdd:COG5047 262 ALNIASSLLEQCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEPMRSHHDIESDSAQHSKKATKFYKGLAERVANQGHALD 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 239 IYACALDQTGLLEMKCCPNLTGGHMVMGDSFNTSLFKQTFQRIFSKDFNGDFRMAFGATLDVKTSRELKIAGAIGPCVSL 318
Cdd:COG5047 342 IFAGCLDQIGIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFNRDSEGYLKMGFNANMEVKTSKNLKIKGLIGHAVSV 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 319 NVKGPCVSENELGVGGTSQWKICGLDPSSTLGIYFEVVNQHNAPVPQGG-RGAIQFVTQYQHSSTQKRIRVTTIARNWAD 397
Cdd:COG5047 422 KKKANNISDSEIGIGATNSWKMASLSPKSNYALYFEIALGAASGSAQRPaEAYIQFITTYQHSSGTYRIRVTTVARMFTD 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 398 AQSQLrhIEAAFDQEAAAVLMARLGVFRAESEEGPDVLRWLDRQLIRLCQKFGQYNKEDPTSFRLSDSFSLYPQFMFHLR 477
Cdd:COG5047 502 GGLPK--INRSFDQEAAAVFMARIAAFKAETEDIIDVFRWIDRNLIRLCQKFADYRKDDPSSFRLDPNFTLYPQFMYHLR 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 478 RSPFLQVFNNSPDESSYYRHHFARQDLTQSLIMIQPILYSYSFHGPPEPVLLDSSSILADRILLMDTFFQIVIYLGETIA 557
Cdd:COG5047 580 RSPFLSVFNNSPDETAFYRHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVLLDSVSVKPDVILLLDTFFHILIFHGSYIA 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 558 QWRKAGYQDMPEYENFKHLLQAPLDDAQEILQARFPMPRYINTEHGGSQARFLLSKVNPSQTHNNLYAWGQETgapILTD 637
Cdd:COG5047 660 QWRNAGYQEQPEYLNLKELLEAPRLEAAELLQDRFPIPRFIVTEQGGSQARFLLSKINPSDITNKMSGGGSET---ILTD 736
|
650
....*....|....*....
gi 1907140069 638 DVSLQVFMDHLKKLAVSSA 656
Cdd:COG5047 737 DVNLQKFMNHLRKLAVSKS 755
|
|
| Sec23-like |
cd01478 |
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
17-280 |
1.76e-174 |
|
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: 497.28 E-value: 1.76e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 17 SPLIFLYVVDTCLEEDDLQALKESLQMSLSLLPPDALVGLITFGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQEMLGL 96
Cdd:cd01478 2 SPPVFLFVVDTCMDEEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 97 TKSAMPVQQARPAQPQ--EQPFVSSRFLQPIHKIDMNLTDLLGELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNT 174
Cdd:cd01478 82 GGPAMRPSASQHPGAGnpLPSAAASRFLLPVSQCEFTLTDLLEQLQPDPWPVPAGHRPLRCTGVALSIAVGLLEACFPNT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 175 GARIMLFTGGPPTQGPGMVVGDELKTPIRSWHDIEKDNARFMKKATKHYEMLANRTATNGHCIDIYACALDQTGLLEMKC 254
Cdd:cd01478 162 GARIMLFAGGPCTVGPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMKV 241
|
250 260
....*....|....*....|....*.
gi 1907140069 255 CPNLTGGHMVMGDSFNTSLFKQTFQR 280
Cdd:cd01478 242 LVNSTGGHVVLSDSFTTSIFKQSFQR 267
|
|
| Sec23_trunk |
pfam04811 |
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
17-282 |
3.30e-91 |
|
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: 282.60 E-value: 3.30e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 17 SPLIFLYVVDTCLE---EDDLQALKESLQMSLSLLP--PDALVGLITFGRMVQVHELSCEGisksyvfRGTKDLTAKQIQ 91
Cdd:pfam04811 2 QPPVFLFVIDVSYNaikSGLLAALKESLLQSLDLLPgdPRARVGFITFDSTVHFFNLGSSL-------RQPQMLVVSDLQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 92 EMLGltksampvqqarpaqpqeqPFVSsRFLQPIHKIDMNLTDLLGELQRdPWPVTqgKRPLRSTGVALSIAVGLLEGTF 171
Cdd:pfam04811 75 DMFL-------------------PLPD-RFLVPLSECRFVLEDLLEQLPP-MFPVT--KRPERCLGPALQAAFLLLKAAF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 172 pnTGARIMLFTGGPPTQGPGMVVGDELKtpiRSWHDIEKDNARFMKKATKHYEMLANRTATNGHCIDIYACALDQTGLLE 251
Cdd:pfam04811 132 --TGGKIMVFQGGLPTVGPGGKLKSRLD---ESHHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVAT 206
|
250 260 270
....*....|....*....|....*....|....*
gi 1907140069 252 MKCCPNLTGGHMVMGDSFN----TSLFKQTFQRIF 282
Cdd:pfam04811 207 LGQLSRLTGGQVYLYPSFQadvdGSKFKQDLQRYF 241
|
|
| trunk_domain |
cd01468 |
trunk domain. COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi ... |
17-280 |
1.26e-87 |
|
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: 273.35 E-value: 1.26e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 17 SPLIFLYVVDTCLE---EDDLQALKESLQMSLSLLP--PDALVGLITFGRMVQVHELSCEGI-SKSYVFRGTKDLTAkqi 90
Cdd:cd01468 2 QPPVFVFVIDVSYEaikEGLLQALKESLLASLDLLPgdPRARVGLITYDSTVHFYNLSSDLAqPKMYVVSDLKDVFL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 91 qemlgltksampvqqarpaqpqeqPFVSsRFLQPIHKIDMNLTDLLGELQRDPWPVtQGKRPLRSTGVALSIAVGLLEGT 170
Cdd:cd01468 79 ------------------------PLPD-RFLVPLSECKKVIHDLLEQLPPMFWPV-PTHRPERCLGPALQAAFLLLKGT 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 171 FpnTGARIMLFTGGPPTQGPGMVVGDELKTPIRSWhdiekDNARFMKKATKHYEMLANRTATNGHCIDIYACALDQTGLL 250
Cdd:cd01468 133 F--AGGRIIVFQGGLPTVGPGKLKSREDKEPIRSH-----DEAQLLKPATKFYKSLAKECVKSGICVDLFAFSLDYVDVA 205
|
250 260 270
....*....|....*....|....*....|....
gi 1907140069 251 EMKCCPNLTGGHMVMGDSFN----TSLFKQTFQR 280
Cdd:cd01468 206 TLKQLAKSTGGQVYLYDSFQapndGSKFKQDLQR 239
|
|
| Sec23_C |
cd11287 |
C-terminal Actin depolymerization factor-homology domain of Sec23; The C-terminal domain of ... |
502-622 |
4.21e-83 |
|
C-terminal Actin depolymerization factor-homology domain of Sec23; The C-terminal domain of the Sec23 subunit of the coat protein complex II (COPII) is distantly related to gelsolin-like repeats and the actin depolymerizing domains found in cofilin and similar proteins. Sec23 forms a tight complex with Sec24. The cytoplasmic Sec23/24 complex is recruited together with Sar1-GTP and Sec13/31 to induce coat polymerization and membrane deformation in the forming of COPII-coated endoplasmic reticulum vesicles. The function of the Sec23 C-terminal domain is unclear.
Pssm-ID: 200443 [Multi-domain] Cd Length: 121 Bit Score: 257.30 E-value: 4.21e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 502 QDLTQSLIMIQPILYSYSFHGPPEPVLLDSSSILADRILLMDTFFQIVIYLGETIAQWRKAGYQDMPEYENFKHLLQAPL 581
Cdd:cd11287 1 EDVSNSLIMIQPTLYSYSFNGPPEPVLLDSSSILPDRILLLDTFFHILIYHGETIAQWRKAGYQDQPEYENFKDLLEAPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1907140069 582 DDAQEILQARFPMPRYINTEHGGSQARFLLSKVNPSQTHNN 622
Cdd:cd11287 81 DDAQELLQDRFPMPRYIVTEQGGSQARFLLSKVNPSQTHNN 121
|
|
| Sec23_helical |
pfam04815 |
Sec23/Sec24 helical domain; COPII-coated vesicles carry proteins from the endoplasmic ... |
410-509 |
4.83e-32 |
|
Sec23/Sec24 helical domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi complex. This vesicular transport can be reconstituted by using three cytosolic components containing five proteins: the small GTPase Sar1p, the Sec23p/24p complex, and the Sec13p/Sec31p complex. This domain is composed of five alpha helices.
Pssm-ID: 461441 [Multi-domain] Cd Length: 103 Bit Score: 119.53 E-value: 4.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 410 DQEAAAVLMARLGVFRAESEEGPDVLRWLDRQLIRLCQKFGQYNKE--DPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNN 487
Cdd:pfam04815 1 DQEAIAVLLAKKAVEKALSSSLSDAREALDNKLVDILAAYRKYCASssSPGQLILPESLKLLPLYMLALLKSPALRGGNS 80
|
90 100
....*....|....*....|...
gi 1907140069 488 SP-DESSYYRHHFARQDLTQSLI 509
Cdd:pfam04815 81 SPsDERAYARHLLLSLPVEELLL 103
|
|
| Sec23_BS |
pfam08033 |
Sec23/Sec24 beta-sandwich domain; |
293-396 |
5.25e-28 |
|
Sec23/Sec24 beta-sandwich domain;
Pssm-ID: 429794 [Multi-domain] Cd Length: 86 Bit Score: 107.62 E-value: 5.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 293 AFGATLDVKTSRELKIAGAIGPCVSLNVkgpcvsenelgvGGTsqWKICGLDPSSTLGIYFEvvnqHNAPVPQGGRGAIQ 372
Cdd:pfam08033 1 GFNAVLRVRTSKGLKVSGFIGNFVSRSS------------GDT--WKLPSLDPDTSYAFEFD----IDEPLPNGSNAYIQ 62
|
90 100
....*....|....*....|....
gi 1907140069 373 FVTQYQHSSTQKRIRVTTIARNWA 396
Cdd:pfam08033 63 FALLYTHSSGERRIRVTTVALPVT 86
|
|
| Gelsolin |
pfam00626 |
Gelsolin repeat; |
524-610 |
3.21e-15 |
|
Gelsolin repeat;
Pssm-ID: 395501 [Multi-domain] Cd Length: 76 Bit Score: 70.80 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 524 PEPVLLDSSSILADRILLMDTFFqiviylgeTIAQWRkaGYQDMPEYENFKHLLQAPLDDaqeilQARFPMPRYINTEHG 603
Cdd:pfam00626 5 PPPVPLSQESLNSGDCYLLDNGF--------TIFLWV--GKGSSLLEKLFAALLAAQLDD-----DERFPLPEVIRVPQG 69
|
....*..
gi 1907140069 604 GSQARFL 610
Cdd:pfam00626 70 KEPARFL 76
|
|
| gelsolin_like |
cd11280 |
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ... |
512-610 |
2.36e-10 |
|
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.
Pssm-ID: 200436 Cd Length: 88 Bit Score: 57.38 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 512 QPILY--SYSFHGPPEPVLLDSSSILADRILLMDTFFQIVIYLGEtiaqwrkagyqdmpeyENFKHLLQAPLDDAQEILQ 589
Cdd:cd11280 1 PPRLYrvRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGR----------------ASSQAELAAAALLAKELDE 64
|
90 100
....*....|....*....|.
gi 1907140069 590 ARFPMPRYINTEHGGSQARFL 610
Cdd:cd11280 65 ERKGKPEIVRIRQGQEPREFW 85
|
|
| COG5028 |
COG5028 |
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ... |
115-554 |
6.54e-09 |
|
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking and secretion];
Pssm-ID: 227361 [Multi-domain] Cd Length: 861 Bit Score: 59.03 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 115 PFVSSRFLQPI-HKIDMNLTdLLGELQRDPwpvTQGKRPLRSTGVALSIAVGLLEGTfpntGARIMLFTGGPPTQGPGMV 193
Cdd:COG5028 352 PFPSGLFVLPLkSCKQIIET-LLDRVPRIF---QDNKSPKNALGPALKAAKSLIGGT----GGKIIVFLSTLPNMGIGKL 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 194 vgdELKTPIRSWHDIEKDNarFMKKATKHYemlanrtATNGHCIDIYACALDQTGLLEMKCCPNLTGGHMVMGDSFNTSL 273
Cdd:COG5028 424 ---QLREDKESSLLSCKDS--FYKEFAIEC-------SKVGISVDLFLTSEDYIDVATLSHLCRYTGGQTYFYPNFSATR 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 274 FKQTFQriFSKDF--NGDFRMAFGATLDVKTSRELKIAGAIGPcvslnvkgpcVSENELGVGGTSQwkicgLDPSSTLGI 351
Cdd:COG5028 492 PNDATK--LANDLvsHLSMEIGYEAVMRVRCSTGLRVSSFYGN----------FFNRSSDLCAFST-----MPRDTSLLV 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 352 YFEVVNQHNAPvpqggRGAIQFVTQYQHSSTQKRIRVTTIArnwADAQSQLRHIEAAFDQEAAAVLMARLGVFRAESEEG 431
Cdd:COG5028 555 EFSIDEKLMTS-----DVYFQVALLYTLNDGERRIRVVNLS---LPTSSSIREVYASADQLAIACILAKKASTKALNSSL 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140069 432 PDVLRWLDRQLIRLCQkfgQYNKE-----DPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFARQDLTQ 506
Cdd:COG5028 627 KEARVLINKSMVDILK---AYKKElvksnTSTQLPLPANLKLLPLLMLALLKSSAFRSGSTPSDIRISALNRLTSLPLKQ 703
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907140069 507 SLIMIQPILysYSFHGP--------------PEPVLLDSSSILADRILLMDTFFQIVIYLGE 554
Cdd:COG5028 704 LMRNIYPTL--YALHDMpieaglpdegllvlPSPINATSSLLESGGLYLIDTGQKIFLWFGK 763
|
|
| |
