|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00162 |
PLN00162 |
transport protein sec23; Provisional |
12-747 |
0e+00 |
|
transport protein sec23; Provisional
Pssm-ID: 215083 [Multi-domain] Cd Length: 761 Bit Score: 1122.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 12 EERDGVRFSWNVWPSSRLEATRMVVPLACLLTPLKERPDLPPVQYEPVLCSrpTCKAVLNPLCQVDYRAKLWACNFCFQR 91
Cdd:PLN00162 7 EAIDGVRMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPLRCR--TCRAVLNPYCRVDFQAKIWICPFCFQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 92 NQFPPAYGGISEVNQPAELMPQFSTIEYVIQ---------------------EDDLQALKESLQMSLSLLPPDALVGLIT 150
Cdd:PLN00162 85 NHFPPHYSSISETNLPAELFPQYTTVEYTLPpgsggapsppvfvfvvdtcmiEEELGALKSALLQAIALLPENALVGLIT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 151 FGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQDMLGLTKPAMPMQQARPAQPQEHPFASS--RFLQPVHKIDMNLTDLL 228
Cdd:PLN00162 165 FGTHVHVHELGFSECSKSYVFRGNKEVSKDQILEQLGLGGKKRRPAGGGIAGARDGLSSSGvnRFLLPASECEFTLNSAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 229 GELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNTGARIMLFTGGPPTQGPGMVVGDELKIPIRSWHDIEKDNARFM 308
Cdd:PLN00162 245 EELQKDPWPVPPGHRPARCTGAALSVAAGLLGACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDAAPYY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 309 KKATKHYEMLANRTAANGHCIDIYACALDQTGLLEMKCCANLTGGYMVMGDSFNTSLFKQTFQRIFTKDFNGDFRMAFGA 388
Cdd:PLN00162 325 KKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFERDGEGSLGLSFNG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 389 TLDVKTSRELKIAGAIGPCVSLNVKGPCVSENELGVGGTSQWKICGLDPTSTLGIYFEVVNQHNT-PIPQGGRGAIQFVT 467
Cdd:PLN00162 405 TFEVNCSKDVKVQGAIGPCASLEKKGPSVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSnPQPPGQQFFLQFLT 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 468 HYQHSSTQRRIRVTTIARNWADvQSQLRHIEAAFDQEAAAVLMARLGVFRAESEEGPDVLRWLDRQLIRLCQKFGQYNKE 547
Cdd:PLN00162 485 RYQHSNGQTRLRVTTVTRRWVE-GSSSEELVAGFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFGDYRKD 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 548 DPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFARQDLTQSLIMIQPILYSYSFHGPPEPVLLDSSSIL 627
Cdd:PLN00162 564 DPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNNSPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLDVASIA 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 628 ADRILLMDTFFQIVIYLGETIAQWRKAGYQDMPEYENFKHLLQAPLDDAQEILQARFPMPRYINTEHGGSQARFLLSKVN 707
Cdd:PLN00162 644 ADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFLLAKLN 723
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 289629267 708 PSQTHNNLYAWGqeTGAPILTDDVSLQVFMDHLKKLAVSS 747
Cdd:PLN00162 724 PSATYNSANAMG--GSDIIFTDDVSLQVFMEHLQRLAVQS 761
|
|
| SEC23 |
COG5047 |
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]; |
9-748 |
0e+00 |
|
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
Pssm-ID: 227380 [Multi-domain] Cd Length: 755 Bit Score: 931.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 9 QQNEERDGVRFSWNVWPSSRLEATRMVVPLACLLTPLKERPDLPPVQYEPVLCSRPtCKAVLNPLCQVDYRAKLWACNFC 88
Cdd:COG5047 4 EIIEENDGIRLTWNVFPATRGDATRTVIPIACLYTPLHEDDALTVNYYEPVKCTAP-CKAVLNPYCHIDERNQSWICPFC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 89 FQRNQFPPAYGGISEVNQPAELMPQFSTIEYVI------------------QEDDLQALKESLQMSLSLLPPDALVGLIT 150
Cdd:COG5047 83 NQRNTLPPQYRDISNANLPLELLPQSSTIEYTLskpvilppvfffvvdaccDEEELTALKDSLIVSLSLLPPEALVGLIT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 151 FGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQDMLGLTKPAMP--MQQARPAQPQehpFASSRFLQPVHKIDMNLTDLL 228
Cdd:COG5047 163 YGTSIQVHELNAENHRRSYVFSGNKEYTKENLQELLALSKPTKSggFESKISGIGQ---FASSRFLLPTQQCEFKLLNIL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 229 GELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNTGARIMLFTGGPPTQGPGMVVGDELKIPIRSWHDIEKDNARFM 308
Cdd:COG5047 240 EQLQPDPWPVPAGKRPLRCTGSALNIASSLLEQCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEPMRSHHDIESDSAQHS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 309 KKATKHYEMLANRTAANGHCIDIYACALDQTGLLEMKCCANLTGGYMVMGDSFNTSLFKQTFQRIFTKDFNGDFRMAFGA 388
Cdd:COG5047 320 KKATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFNRDSEGYLKMGFNA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 389 TLDVKTSRELKIAGAIGPCVSLNVKGPCVSENELGVGGTSQWKICGLDPTSTLGIYFEVVNQHNTPIPQGG-RGAIQFVT 467
Cdd:COG5047 400 NMEVKTSKNLKIKGLIGHAVSVKKKANNISDSEIGIGATNSWKMASLSPKSNYALYFEIALGAASGSAQRPaEAYIQFIT 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 468 HYQHSSTQRRIRVTTIARNWADvqSQLRHIEAAFDQEAAAVLMARLGVFRAESEEGPDVLRWLDRQLIRLCQKFGQYNKE 547
Cdd:COG5047 480 TYQHSSGTYRIRVTTVARMFTD--GGLPKINRSFDQEAAAVFMARIAAFKAETEDIIDVFRWIDRNLIRLCQKFADYRKD 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 548 DPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFARQDLTQSLIMIQPILYSYSFHGPPEPVLLDSSSIL 627
Cdd:COG5047 558 DPSSFRLDPNFTLYPQFMYHLRRSPFLSVFNNSPDETAFYRHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVLLDSVSVK 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 628 ADRILLMDTFFQIVIYLGETIAQWRKAGYQDMPEYENFKHLLQAPLDDAQEILQARFPMPRYINTEHGGSQARFLLSKVN 707
Cdd:COG5047 638 PDVILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKELLEAPRLEAAELLQDRFPIPRFIVTEQGGSQARFLLSKIN 717
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 289629267 708 PSQTHNNLYAWGQETgapILTDDVSLQVFMDHLKKLAVSSA 748
Cdd:COG5047 718 PSDITNKMSGGGSET---ILTDDVNLQKFMNHLRKLAVSKS 755
|
|
| Sec23-like |
cd01478 |
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
123-372 |
9.90e-167 |
|
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: 480.71 E-value: 9.90e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 123 EDDLQALKESLQMSLSLLPPDALVGLITFGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQDMLGLTKPAMPMQQARPAQ 202
Cdd:cd01478 16 EEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLGLGGPAMRPSASQHPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 203 PQ--EHPFASSRFLQPVHKIDMNLTDLLGELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNTGARIMLFTGGPPTQ 280
Cdd:cd01478 96 AGnpLPSAAASRFLLPVSQCEFTLTDLLEQLQPDPWPVPAGHRPLRCTGVALSIAVGLLEACFPNTGARIMLFAGGPCTV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 281 GPGMVVGDELKIPIRSWHDIEKDNARFMKKATKHYEMLANRTAANGHCIDIYACALDQTGLLEMKCCANLTGGYMVMGDS 360
Cdd:cd01478 176 GPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMKVLVNSTGGHVVLSDS 255
|
250
....*....|..
gi 289629267 361 FNTSLFKQTFQR 372
Cdd:cd01478 256 FTTSIFKQSFQR 267
|
|
| Sec23_trunk |
pfam04811 |
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
121-374 |
1.19e-85 |
|
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: 270.66 E-value: 1.19e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 121 IQEDDLQALKESLQMSLSLLP--PDALVGLITFGRMVQVHELSCEGisksyvfRGTKDLTAKQIQDMLgltkpaMPMqqa 198
Cdd:pfam04811 17 IKSGLLAALKESLLQSLDLLPgdPRARVGFITFDSTVHFFNLGSSL-------RQPQMLVVSDLQDMF------LPL--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 199 rpaqpqehpfaSSRFLQPVHKIDMNLTDLLGELQRdPWPVTqgKRPLRSTGVALSIAVGLLEGTFpnTGARIMLFTGGPP 278
Cdd:pfam04811 81 -----------PDRFLVPLSECRFVLEDLLEQLPP-MFPVT--KRPERCLGPALQAAFLLLKAAF--TGGKIMVFQGGLP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 279 TQGPGMVVGDELKipiRSWHDIEKDNARFMKKATKHYEMLANRTAANGHCIDIYACALDQTGLLEMKCCANLTGGYMVMG 358
Cdd:pfam04811 145 TVGPGGKLKSRLD---ESHHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVATLGQLSRLTGGQVYLY 221
|
250 260
....*....|....*....|
gi 289629267 359 DSFN----TSLFKQTFQRIF 374
Cdd:pfam04811 222 PSFQadvdGSKFKQDLQRYF 241
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00162 |
PLN00162 |
transport protein sec23; Provisional |
12-747 |
0e+00 |
|
transport protein sec23; Provisional
Pssm-ID: 215083 [Multi-domain] Cd Length: 761 Bit Score: 1122.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 12 EERDGVRFSWNVWPSSRLEATRMVVPLACLLTPLKERPDLPPVQYEPVLCSrpTCKAVLNPLCQVDYRAKLWACNFCFQR 91
Cdd:PLN00162 7 EAIDGVRMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPLRCR--TCRAVLNPYCRVDFQAKIWICPFCFQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 92 NQFPPAYGGISEVNQPAELMPQFSTIEYVIQ---------------------EDDLQALKESLQMSLSLLPPDALVGLIT 150
Cdd:PLN00162 85 NHFPPHYSSISETNLPAELFPQYTTVEYTLPpgsggapsppvfvfvvdtcmiEEELGALKSALLQAIALLPENALVGLIT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 151 FGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQDMLGLTKPAMPMQQARPAQPQEHPFASS--RFLQPVHKIDMNLTDLL 228
Cdd:PLN00162 165 FGTHVHVHELGFSECSKSYVFRGNKEVSKDQILEQLGLGGKKRRPAGGGIAGARDGLSSSGvnRFLLPASECEFTLNSAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 229 GELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNTGARIMLFTGGPPTQGPGMVVGDELKIPIRSWHDIEKDNARFM 308
Cdd:PLN00162 245 EELQKDPWPVPPGHRPARCTGAALSVAAGLLGACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDAAPYY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 309 KKATKHYEMLANRTAANGHCIDIYACALDQTGLLEMKCCANLTGGYMVMGDSFNTSLFKQTFQRIFTKDFNGDFRMAFGA 388
Cdd:PLN00162 325 KKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFERDGEGSLGLSFNG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 389 TLDVKTSRELKIAGAIGPCVSLNVKGPCVSENELGVGGTSQWKICGLDPTSTLGIYFEVVNQHNT-PIPQGGRGAIQFVT 467
Cdd:PLN00162 405 TFEVNCSKDVKVQGAIGPCASLEKKGPSVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSnPQPPGQQFFLQFLT 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 468 HYQHSSTQRRIRVTTIARNWADvQSQLRHIEAAFDQEAAAVLMARLGVFRAESEEGPDVLRWLDRQLIRLCQKFGQYNKE 547
Cdd:PLN00162 485 RYQHSNGQTRLRVTTVTRRWVE-GSSSEELVAGFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFGDYRKD 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 548 DPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFARQDLTQSLIMIQPILYSYSFHGPPEPVLLDSSSIL 627
Cdd:PLN00162 564 DPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNNSPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLDVASIA 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 628 ADRILLMDTFFQIVIYLGETIAQWRKAGYQDMPEYENFKHLLQAPLDDAQEILQARFPMPRYINTEHGGSQARFLLSKVN 707
Cdd:PLN00162 644 ADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFLLAKLN 723
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 289629267 708 PSQTHNNLYAWGqeTGAPILTDDVSLQVFMDHLKKLAVSS 747
Cdd:PLN00162 724 PSATYNSANAMG--GSDIIFTDDVSLQVFMEHLQRLAVQS 761
|
|
| SEC23 |
COG5047 |
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]; |
9-748 |
0e+00 |
|
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
Pssm-ID: 227380 [Multi-domain] Cd Length: 755 Bit Score: 931.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 9 QQNEERDGVRFSWNVWPSSRLEATRMVVPLACLLTPLKERPDLPPVQYEPVLCSRPtCKAVLNPLCQVDYRAKLWACNFC 88
Cdd:COG5047 4 EIIEENDGIRLTWNVFPATRGDATRTVIPIACLYTPLHEDDALTVNYYEPVKCTAP-CKAVLNPYCHIDERNQSWICPFC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 89 FQRNQFPPAYGGISEVNQPAELMPQFSTIEYVI------------------QEDDLQALKESLQMSLSLLPPDALVGLIT 150
Cdd:COG5047 83 NQRNTLPPQYRDISNANLPLELLPQSSTIEYTLskpvilppvfffvvdaccDEEELTALKDSLIVSLSLLPPEALVGLIT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 151 FGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQDMLGLTKPAMP--MQQARPAQPQehpFASSRFLQPVHKIDMNLTDLL 228
Cdd:COG5047 163 YGTSIQVHELNAENHRRSYVFSGNKEYTKENLQELLALSKPTKSggFESKISGIGQ---FASSRFLLPTQQCEFKLLNIL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 229 GELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNTGARIMLFTGGPPTQGPGMVVGDELKIPIRSWHDIEKDNARFM 308
Cdd:COG5047 240 EQLQPDPWPVPAGKRPLRCTGSALNIASSLLEQCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEPMRSHHDIESDSAQHS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 309 KKATKHYEMLANRTAANGHCIDIYACALDQTGLLEMKCCANLTGGYMVMGDSFNTSLFKQTFQRIFTKDFNGDFRMAFGA 388
Cdd:COG5047 320 KKATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFNRDSEGYLKMGFNA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 389 TLDVKTSRELKIAGAIGPCVSLNVKGPCVSENELGVGGTSQWKICGLDPTSTLGIYFEVVNQHNTPIPQGG-RGAIQFVT 467
Cdd:COG5047 400 NMEVKTSKNLKIKGLIGHAVSVKKKANNISDSEIGIGATNSWKMASLSPKSNYALYFEIALGAASGSAQRPaEAYIQFIT 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 468 HYQHSSTQRRIRVTTIARNWADvqSQLRHIEAAFDQEAAAVLMARLGVFRAESEEGPDVLRWLDRQLIRLCQKFGQYNKE 547
Cdd:COG5047 480 TYQHSSGTYRIRVTTVARMFTD--GGLPKINRSFDQEAAAVFMARIAAFKAETEDIIDVFRWIDRNLIRLCQKFADYRKD 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 548 DPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFARQDLTQSLIMIQPILYSYSFHGPPEPVLLDSSSIL 627
Cdd:COG5047 558 DPSSFRLDPNFTLYPQFMYHLRRSPFLSVFNNSPDETAFYRHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVLLDSVSVK 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 628 ADRILLMDTFFQIVIYLGETIAQWRKAGYQDMPEYENFKHLLQAPLDDAQEILQARFPMPRYINTEHGGSQARFLLSKVN 707
Cdd:COG5047 638 PDVILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKELLEAPRLEAAELLQDRFPIPRFIVTEQGGSQARFLLSKIN 717
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 289629267 708 PSQTHNNLYAWGQETgapILTDDVSLQVFMDHLKKLAVSSA 748
Cdd:COG5047 718 PSDITNKMSGGGSET---ILTDDVNLQKFMNHLRKLAVSKS 755
|
|
| Sec23-like |
cd01478 |
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
123-372 |
9.90e-167 |
|
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: 480.71 E-value: 9.90e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 123 EDDLQALKESLQMSLSLLPPDALVGLITFGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQDMLGLTKPAMPMQQARPAQ 202
Cdd:cd01478 16 EEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLGLGGPAMRPSASQHPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 203 PQ--EHPFASSRFLQPVHKIDMNLTDLLGELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNTGARIMLFTGGPPTQ 280
Cdd:cd01478 96 AGnpLPSAAASRFLLPVSQCEFTLTDLLEQLQPDPWPVPAGHRPLRCTGVALSIAVGLLEACFPNTGARIMLFAGGPCTV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 281 GPGMVVGDELKIPIRSWHDIEKDNARFMKKATKHYEMLANRTAANGHCIDIYACALDQTGLLEMKCCANLTGGYMVMGDS 360
Cdd:cd01478 176 GPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMKVLVNSTGGHVVLSDS 255
|
250
....*....|..
gi 289629267 361 FNTSLFKQTFQR 372
Cdd:cd01478 256 FTTSIFKQSFQR 267
|
|
| Sec23_trunk |
pfam04811 |
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
121-374 |
1.19e-85 |
|
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: 270.66 E-value: 1.19e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 121 IQEDDLQALKESLQMSLSLLP--PDALVGLITFGRMVQVHELSCEGisksyvfRGTKDLTAKQIQDMLgltkpaMPMqqa 198
Cdd:pfam04811 17 IKSGLLAALKESLLQSLDLLPgdPRARVGFITFDSTVHFFNLGSSL-------RQPQMLVVSDLQDMF------LPL--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 199 rpaqpqehpfaSSRFLQPVHKIDMNLTDLLGELQRdPWPVTqgKRPLRSTGVALSIAVGLLEGTFpnTGARIMLFTGGPP 278
Cdd:pfam04811 81 -----------PDRFLVPLSECRFVLEDLLEQLPP-MFPVT--KRPERCLGPALQAAFLLLKAAF--TGGKIMVFQGGLP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 279 TQGPGMVVGDELKipiRSWHDIEKDNARFMKKATKHYEMLANRTAANGHCIDIYACALDQTGLLEMKCCANLTGGYMVMG 358
Cdd:pfam04811 145 TVGPGGKLKSRLD---ESHHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVATLGQLSRLTGGQVYLY 221
|
250 260
....*....|....*....|
gi 289629267 359 DSFN----TSLFKQTFQRIF 374
Cdd:pfam04811 222 PSFQadvdGSKFKQDLQRYF 241
|
|
| trunk_domain |
cd01468 |
trunk domain. COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi ... |
121-372 |
8.30e-83 |
|
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: 262.95 E-value: 8.30e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 121 IQEDDLQALKESLQMSLSLLP--PDALVGLITFGRMVQVHELSCEGI-SKSYVFRGTKDLTakqiqdmlgltkpampmqq 197
Cdd:cd01468 17 IKEGLLQALKESLLASLDLLPgdPRARVGLITYDSTVHFYNLSSDLAqPKMYVVSDLKDVF------------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 198 arpaqpqehPFASSRFLQPVHKIDMNLTDLLGELQRDPWPVtQGKRPLRSTGVALSIAVGLLEGTFpnTGARIMLFTGGP 277
Cdd:cd01468 78 ---------LPLPDRFLVPLSECKKVIHDLLEQLPPMFWPV-PTHRPERCLGPALQAAFLLLKGTF--AGGRIIVFQGGL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 278 PTQGPGMVVGDELKIPIRSWhdiekDNARFMKKATKHYEMLANRTAANGHCIDIYACALDQTGLLEMKCCANLTGGYMVM 357
Cdd:cd01468 146 PTVGPGKLKSREDKEPIRSH-----DEAQLLKPATKFYKSLAKECVKSGICVDLFAFSLDYVDVATLKQLAKSTGGQVYL 220
|
250
....*....|....*....
gi 289629267 358 GDSFN----TSLFKQTFQR 372
Cdd:cd01468 221 YDSFQapndGSKFKQDLQR 239
|
|
| Sec23_C |
cd11287 |
C-terminal Actin depolymerization factor-homology domain of Sec23; The C-terminal domain of ... |
594-714 |
1.93e-82 |
|
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: 257.69 E-value: 1.93e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 594 QDLTQSLIMIQPILYSYSFHGPPEPVLLDSSSILADRILLMDTFFQIVIYLGETIAQWRKAGYQDMPEYENFKHLLQAPL 673
Cdd:cd11287 1 EDVSNSLIMIQPTLYSYSFNGPPEPVLLDSSSILPDRILLLDTFFHILIYHGETIAQWRKAGYQDQPEYENFKDLLEAPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 289629267 674 DDAQEILQARFPMPRYINTEHGGSQARFLLSKVNPSQTHNN 714
Cdd:cd11287 81 DDAQELLQDRFPMPRYIVTEQGGSQARFLLSKVNPSQTHNN 121
|
|
| Sec23_helical |
pfam04815 |
Sec23/Sec24 helical domain; COPII-coated vesicles carry proteins from the endoplasmic ... |
502-601 |
3.58e-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: 120.30 E-value: 3.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 502 DQEAAAVLMARLGVFRAESEEGPDVLRWLDRQLIRLCQKFGQYNKE--DPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNN 579
Cdd:pfam04815 1 DQEAIAVLLAKKAVEKALSSSLSDAREALDNKLVDILAAYRKYCASssSPGQLILPESLKLLPLYMLALLKSPALRGGNS 80
|
90 100
....*....|....*....|...
gi 289629267 580 SP-DESSYYRHHFARQDLTQSLI 601
Cdd:pfam04815 81 SPsDERAYARHLLLSLPVEELLL 103
|
|
| Sec23_BS |
pfam08033 |
Sec23/Sec24 beta-sandwich domain; |
385-488 |
5.22e-30 |
|
Sec23/Sec24 beta-sandwich domain;
Pssm-ID: 429794 [Multi-domain] Cd Length: 86 Bit Score: 113.40 E-value: 5.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 385 AFGATLDVKTSRELKIAGAIGPCVSLNVkgpcvsenelgvGGTsqWKICGLDPTSTLGIYFEvvnqHNTPIPQGGRGAIQ 464
Cdd:pfam08033 1 GFNAVLRVRTSKGLKVSGFIGNFVSRSS------------GDT--WKLPSLDPDTSYAFEFD----IDEPLPNGSNAYIQ 62
|
90 100
....*....|....*....|....
gi 289629267 465 FVTHYQHSSTQRRIRVTTIARNWA 488
Cdd:pfam08033 63 FALLYTHSSGERRIRVTTVALPVT 86
|
|
| COG5028 |
COG5028 |
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ... |
9-646 |
6.45e-16 |
|
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking and secretion];
Pssm-ID: 227361 [Multi-domain] Cd Length: 861 Bit Score: 82.15 E-value: 6.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 9 QQNEERDGVRFSWNVWP--SSRLEATRmvVPLACLLTPLKE-RPDLPPVQYE----PVLCSRptCKAVLNPLCQVDYRAK 81
Cdd:COG5028 145 QSNCSPKYVRSTMYAIPetNDLLKKSK--IPFGLVIRPFLElYPEEDPVPLVedgsIVRCRR--CRSYINPFVQFIEQGR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 82 LWACNFCFQRNQFP-----PAYGGI--SEVNQPAELmpQFSTIEYVIQEDdlqalkeslqMSLSLLPPDALVGLITfgrm 154
Cdd:COG5028 221 KWRCNICRSKNDVPegfdnPSGPNDprSDRYSRPEL--KSGVVDFLAPKE----------YSLRQPPPPVYVFLID---- 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 155 VQVHELSC-------EGISKSYVFRGTKDLTAKQ----IQDMLGLTK--PAMPMQQARPAQPQEH--PFASSRFLQPV-H 218
Cdd:COG5028 285 VSFEAIKNglvkaaiRAILENLDQIPNFDPRTKIaiicFDSSLHFFKlsPDLDEQMLIVSDLDEPflPFPSGLFVLPLkS 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 219 KIDMNLTdLLGELQRDPwpvTQGKRPLRSTGVALSIAVGLLEGtfpnTGARIMLFTGGPPTQGPGMVvgdELKIPIRSWH 298
Cdd:COG5028 365 CKQIIET-LLDRVPRIF---QDNKSPKNALGPALKAAKSLIGG----TGGKIIVFLSTLPNMGIGKL---QLREDKESSL 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 299 DIEKDNarFMKKATKHYEMLanrtaanGHCIDIYACALDQTGLLEMKCCANLTGGYMVMGDSFNTSLFKQTFQriFTKDF 378
Cdd:COG5028 434 LSCKDS--FYKEFAIECSKV-------GISVDLFLTSEDYIDVATLSHLCRYTGGQTYFYPNFSATRPNDATK--LANDL 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 379 --NGDFRMAFGATLDVKTSRELKIAGAIGPcvslnvkgpcVSENELGVGGTSQwkicgLDPTSTLGIYFEVVNQHNTPip 456
Cdd:COG5028 503 vsHLSMEIGYEAVMRVRCSTGLRVSSFYGN----------FFNRSSDLCAFST-----MPRDTSLLVEFSIDEKLMTS-- 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 457 qggRGAIQFVTHYQHSSTQRRIRVTTIArnwADVQSQLRHIEAAFDQEAAAVLMARLGVFRAESEEGPDVLRWLDRQLIR 536
Cdd:COG5028 566 ---DVYFQVALLYTLNDGERRIRVVNLS---LPTSSSIREVYASADQLAIACILAKKASTKALNSSLKEARVLINKSMVD 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 537 LCQkfgQYNKE-----DPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFARQDLTQSLIMIQPILysYS 611
Cdd:COG5028 640 ILK---AYKKElvksnTSTQLPLPANLKLLPLLMLALLKSSAFRSGSTPSDIRISALNRLTSLPLKQLMRNIYPTL--YA 714
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 289629267 612 FHGP--------------PEPVLLDSSSILADRILLMDTFFQIVIYLGE 646
Cdd:COG5028 715 LHDMpieaglpdegllvlPSPINATSSLLESGGLYLIDTGQKIFLWFGK 763
|
|
| Gelsolin |
pfam00626 |
Gelsolin repeat; |
616-702 |
2.97e-15 |
|
Gelsolin repeat;
Pssm-ID: 395501 [Multi-domain] Cd Length: 76 Bit Score: 71.18 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 616 PEPVLLDSSSILADRILLMDTFFqiviylgeTIAQWRkaGYQDMPEYENFKHLLQAPLDDaqeilQARFPMPRYINTEHG 695
Cdd:pfam00626 5 PPPVPLSQESLNSGDCYLLDNGF--------TIFLWV--GKGSSLLEKLFAALLAAQLDD-----DERFPLPEVIRVPQG 69
|
....*..
gi 289629267 696 GSQARFL 702
Cdd:pfam00626 70 KEPARFL 76
|
|
| zf-Sec23_Sec24 |
pfam04810 |
Sec23/Sec24 zinc finger; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
58-97 |
4.52e-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: 4.52e-15
10 20 30 40
....*....|....*....|....*....|....*....|
gi 289629267 58 PVLCSRptCKAVLNPLCQVDYRAKLWACNFCFQRNQFPPA 97
Cdd:pfam04810 1 PVRCRR--CRAYLNPFCQFDFGGKKWTCNFCGTRNPVPPE 38
|
|
| gelsolin_like |
cd11280 |
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ... |
604-702 |
2.71e-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: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289629267 604 QPILY--SYSFHGPPEPVLLDSSSILADRILLMDTFFQIVIYLGEtiaqwrkagyqdmpeyENFKHLLQAPLDDAQEILQ 681
Cdd:cd11280 1 PPRLYrvRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGR----------------ASSQAELAAAALLAKELDE 64
|
90 100
....*....|....*....|.
gi 289629267 682 ARFPMPRYINTEHGGSQARFL 702
Cdd:cd11280 65 ERKGKPEIVRIRQGQEPREFW 85
|
|
|