|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00162 |
PLN00162 |
transport protein sec23; Provisional |
12-811 |
0e+00 |
|
transport protein sec23; Provisional
Pssm-ID: 215083 [Multi-domain] Cd Length: 761 Bit Score: 1055.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 12 QANDGVQFTWNMWPHSRVDSQKLVVPLTCFFTPLKERPStevaQPPLEYDPVLCqkASCKAILNPLCAVDYRAKIWMCPF 91
Cdd:PLN00162 7 EAIDGVRMSWNVWPSSKIEASKCVIPLAALYTPLKPLPE----LPVLPYDPLRC--RTCRAVLNPYCRVDFQAKIWICPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 92 CNNRNPFPAHYAAIAEDNRPPELYPQFTTIEYTLRKATT---MPPIFVFVVDTCMTAEELKSLKECLQTALSLLPADALV 168
Cdd:PLN00162 81 CFQRNHFPPHYSSISETNLPAELFPQYTTVEYTLPPGSGgapSPPVFVFVVDTCMIEEELGALKSALLQAIALLPENALV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 169 GLITYGRMVQLHELNTQGISRSYVFKGTKEVTAKQIKDVMAGGGLSQRpaagapgapagapgapmamgsgaaplgqlpgs 248
Cdd:PLN00162 161 GLITFGTHVHVHELGFSECSKSYVFRGNKEVSKDQILEQLGLGGKKRR-------------------------------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 249 glpgglprgggpplpgaAQGIVAPGGGAPVPHAPANKFLQPISECDESINDLIDQISIDRWPVPQGHRPLRATGAALAVA 328
Cdd:PLN00162 209 -----------------PAGGGIAGARDGLSSSGVNRFLLPASECEFTLNSALEELQKDPWPVPPGHRPARCTGAALSVA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 329 VTLLESCFPSTGARIMSFIGGACTHGPGAVVGEELKNPIRSWNSIKEDAAPYMKKAIKFYDGLAARIVKNGHAVDVYSCA 408
Cdd:PLN00162 272 AGLLGACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDAAPYYKKAVKFYEGLAKQLVAQGHVLDVFACS 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 409 LDQTGLLEMKNMFNSSGGHVVMGDSFNSSLFKQTYQRSFDKDSAGNLKMGFNATMEVKVGAGLKIEGVLGCCASGNVRNA 488
Cdd:PLN00162 352 LDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFERDGEGSLGLSFNGTFEVNCSKDVKVQGAIGPCASLEKKGP 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 489 NVSDQEMGIGGTCQWKFGAISPRTTIGVVFEIAAQHGSA-IPQGGRGMVQFVTQYQHADGRKRIRVTTTCRTWADmATQQ 567
Cdd:PLN00162 432 SVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSNpQPPGQQFFLQFLTRYQHSNGQTRLRVTTVTRRWVE-GSSS 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 568 PNIAYGFDQEAAAVAIARLASFRASNEnDTPEALRWLDRSLIRLCQKFGEYSKDDPNSFRLSDKFSLFPQFMFHLRRSQF 647
Cdd:PLN00162 511 EELVAGFDQEAAAVVMARLASHKMETE-EEFDATRWLDRALIRLCSKFGDYRKDDPSSFRLSPNFSLYPQFMFNLRRSQF 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 648 LQVFNNSPDETAYYRHILFSENVLESTTMIQPVLFSYSFNGPPEPVLLDTSSILADRILLMDDYFHVLIYHGQTIAQWRK 727
Cdd:PLN00162 590 VQVFNNSPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLDVASIAADRILLLDSYFSVVIFHGSTIAQWRK 669
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 728 QNFHENPQYATFKQLLEAPVADATSILQERFPMPRYIVTEHEGSQARFLLSKVNPSLTHNNPYANEAGSAVFTDDVSLQV 807
Cdd:PLN00162 670 AGYHNQPEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFLLAKLNPSATYNSANAMGGSDIIFTDDVSLQV 749
|
....
gi 17566436 808 FMEH 811
Cdd:PLN00162 750 FMEH 753
|
|
| SEC23 |
COG5047 |
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]; |
14-811 |
0e+00 |
|
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
Pssm-ID: 227380 [Multi-domain] Cd Length: 755 Bit Score: 854.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 14 NDGVQFTWNMWPHSRVDSQKLVVPLTCFFTPLKERPstevAQPPLEYDPVLCqKASCKAILNPLCAVDYRAKIWMCPFCN 93
Cdd:COG5047 9 NDGIRLTWNVFPATRGDATRTVIPIACLYTPLHEDD----ALTVNYYEPVKC-TAPCKAVLNPYCHIDERNQSWICPFCN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 94 NRNPFPAHYAAIAEDNRPPELYPQFTTIEYTLRKATTMPPIFVFVVDTCMTAEELKSLKECLQTALSLLPADALVGLITY 173
Cdd:COG5047 84 QRNTLPPQYRDISNANLPLELLPQSSTIEYTLSKPVILPPVFFFVVDACCDEEELTALKDSLIVSLSLLPPEALVGLITY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 174 GRMVQLHELNTQGISRSYVFKGTKEVTAKQIKDVmaggglsqrpaagapgapagapgapmamgsGAAPLGQLPGSglpgg 253
Cdd:COG5047 164 GTSIQVHELNAENHRRSYVFSGNKEYTKENLQEL------------------------------LALSKPTKSGG----- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 254 lprgggpplpgAAQGIVAPGGGAPvphapaNKFLQPISECDESINDLIDQISIDRWPVPQGHRPLRATGAALAVAVTLLE 333
Cdd:COG5047 209 -----------FESKISGIGQFAS------SRFLLPTQQCEFKLLNILEQLQPDPWPVPAGKRPLRCTGSALNIASSLLE 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 334 SCFPSTGARIMSFIGGACTHGPGAVVGEELKNPIRSWNSIKEDAAPYMKKAIKFYDGLAARIVKNGHAVDVYSCALDQTG 413
Cdd:COG5047 272 QCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEPMRSHHDIESDSAQHSKKATKFYKGLAERVANQGHALDIFAGCLDQIG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 414 LLEMKNMFNSSGGHVVMGDSFNSSLFKQTYQRSFDKDSAGNLKMGFNATMEVKVGAGLKIEGVLGCCASGNVRNANVSDQ 493
Cdd:COG5047 352 IMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFNRDSEGYLKMGFNANMEVKTSKNLKIKGLIGHAVSVKKKANNISDS 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 494 EMGIGGTCQWKFGAISPRTTIGVVFEIAAQHGSAIPQGG-RGMVQFVTQYQHADGRKRIRVTTTCRTWADMATqqPNIAY 572
Cdd:COG5047 432 EIGIGATNSWKMASLSPKSNYALYFEIALGAASGSAQRPaEAYIQFITTYQHSSGTYRIRVTTVARMFTDGGL--PKINR 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 573 GFDQEAAAVAIARLASFRASNEnDTPEALRWLDRSLIRLCQKFGEYSKDDPNSFRLSDKFSLFPQFMFHLRRSQFLQVFN 652
Cdd:COG5047 510 SFDQEAAAVFMARIAAFKAETE-DIIDVFRWIDRNLIRLCQKFADYRKDDPSSFRLDPNFTLYPQFMYHLRRSPFLSVFN 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 653 NSPDETAYYRHILFSENVLESTTMIQPVLFSYSFNGPPEPVLLDTSSILADRILLMDDYFHVLIYHGQTIAQWRKQNFHE 732
Cdd:COG5047 589 NSPDETAFYRHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVLLDSVSVKPDVILLLDTFFHILIFHGSYIAQWRNAGYQE 668
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17566436 733 NPQYATFKQLLEAPVADATSILQERFPMPRYIVTEHEGSQARFLLSKVNPSLTHNNPyANEAGSAVFTDDVSLQVFMEH 811
Cdd:COG5047 669 QPEYLNLKELLEAPRLEAAELLQDRFPIPRFIVTEQGGSQARFLLSKINPSDITNKM-SGGGSETILTDDVNLQKFMNH 746
|
|
| Sec23-like |
cd01478 |
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
130-445 |
1.07e-161 |
|
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: 470.31 E-value: 1.07e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 130 TMPPIFVFVVDTCMTAEELKSLKECLQTALSLLPADALVGLITYGRMVQLHELNTQGISRSYVFKGTKEVTAKQIKDVMA 209
Cdd:cd01478 1 TSPPVFLFVVDTCMDEEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 210 GGGLSQRpaagapgapagapgapmamgsgaaplgqlPGSGlpgglprgggpplpgaaqgiVAPGGGAPVPHAPANKFLQP 289
Cdd:cd01478 81 LGGPAMR-----------------------------PSAS--------------------QHPGAGNPLPSAAASRFLLP 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 290 ISECDESINDLIDQISIDRWPVPQGHRPLRATGAALAVAVTLLESCFPSTGARIMSFIGGACTHGPGAVVGEELKNPIRS 369
Cdd:cd01478 112 VSQCEFTLTDLLEQLQPDPWPVPAGHRPLRCTGVALSIAVGLLEACFPNTGARIMLFAGGPCTVGPGAVVSTELKDPIRS 191
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17566436 370 WNSIKEDAAPYMKKAIKFYDGLAARIVKNGHAVDVYSCALDQTGLLEMKNMFNSSGGHVVMGDSFNSSLFKQTYQR 445
Cdd:cd01478 192 HHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMKVLVNSTGGHVVLSDSFTTSIFKQSFQR 267
|
|
| Sec23_trunk |
pfam04811 |
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
131-447 |
1.42e-66 |
|
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: 221.36 E-value: 1.42e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 131 MPPIFVFVVDTCMTA---EELKSLKECLQTALSLLPAD--ALVGLITYGRMVQLHELntqgisrSYVFKGTKEVTAKQIK 205
Cdd:pfam04811 2 QPPVFLFVIDVSYNAiksGLLAALKESLLQSLDLLPGDprARVGFITFDSTVHFFNL-------GSSLRQPQMLVVSDLQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 206 DVMaggglsqrpaagapgapagapgapmamgsgaaplgqlpgsglpgglprgggpplpgaaqgivapgggapVPhaPANK 285
Cdd:pfam04811 75 DMF---------------------------------------------------------------------LP--LPDR 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 286 FLQPISECDESINDLIDQISiDRWPVPqgHRPLRATGAALAVAVTLLESCFpsTGARIMSFIGGACTHGPGAVVGEELKn 365
Cdd:pfam04811 84 FLVPLSECRFVLEDLLEQLP-PMFPVT--KRPERCLGPALQAAFLLLKAAF--TGGKIMVFQGGLPTVGPGGKLKSRLD- 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 366 piRSWNSIKEDAAPYMKKAIKFYDGLAARIVKNGHAVDVYSCALDQTGLLEMKNMFNSSGGHVVMGDSFN----SSLFKQ 441
Cdd:pfam04811 158 --ESHHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVATLGQLSRLTGGQVYLYPSFQadvdGSKFKQ 235
|
....*.
gi 17566436 442 TYQRSF 447
Cdd:pfam04811 236 DLQRYF 241
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00162 |
PLN00162 |
transport protein sec23; Provisional |
12-811 |
0e+00 |
|
transport protein sec23; Provisional
Pssm-ID: 215083 [Multi-domain] Cd Length: 761 Bit Score: 1055.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 12 QANDGVQFTWNMWPHSRVDSQKLVVPLTCFFTPLKERPStevaQPPLEYDPVLCqkASCKAILNPLCAVDYRAKIWMCPF 91
Cdd:PLN00162 7 EAIDGVRMSWNVWPSSKIEASKCVIPLAALYTPLKPLPE----LPVLPYDPLRC--RTCRAVLNPYCRVDFQAKIWICPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 92 CNNRNPFPAHYAAIAEDNRPPELYPQFTTIEYTLRKATT---MPPIFVFVVDTCMTAEELKSLKECLQTALSLLPADALV 168
Cdd:PLN00162 81 CFQRNHFPPHYSSISETNLPAELFPQYTTVEYTLPPGSGgapSPPVFVFVVDTCMIEEELGALKSALLQAIALLPENALV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 169 GLITYGRMVQLHELNTQGISRSYVFKGTKEVTAKQIKDVMAGGGLSQRpaagapgapagapgapmamgsgaaplgqlpgs 248
Cdd:PLN00162 161 GLITFGTHVHVHELGFSECSKSYVFRGNKEVSKDQILEQLGLGGKKRR-------------------------------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 249 glpgglprgggpplpgaAQGIVAPGGGAPVPHAPANKFLQPISECDESINDLIDQISIDRWPVPQGHRPLRATGAALAVA 328
Cdd:PLN00162 209 -----------------PAGGGIAGARDGLSSSGVNRFLLPASECEFTLNSALEELQKDPWPVPPGHRPARCTGAALSVA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 329 VTLLESCFPSTGARIMSFIGGACTHGPGAVVGEELKNPIRSWNSIKEDAAPYMKKAIKFYDGLAARIVKNGHAVDVYSCA 408
Cdd:PLN00162 272 AGLLGACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDAAPYYKKAVKFYEGLAKQLVAQGHVLDVFACS 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 409 LDQTGLLEMKNMFNSSGGHVVMGDSFNSSLFKQTYQRSFDKDSAGNLKMGFNATMEVKVGAGLKIEGVLGCCASGNVRNA 488
Cdd:PLN00162 352 LDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFERDGEGSLGLSFNGTFEVNCSKDVKVQGAIGPCASLEKKGP 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 489 NVSDQEMGIGGTCQWKFGAISPRTTIGVVFEIAAQHGSA-IPQGGRGMVQFVTQYQHADGRKRIRVTTTCRTWADmATQQ 567
Cdd:PLN00162 432 SVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSNpQPPGQQFFLQFLTRYQHSNGQTRLRVTTVTRRWVE-GSSS 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 568 PNIAYGFDQEAAAVAIARLASFRASNEnDTPEALRWLDRSLIRLCQKFGEYSKDDPNSFRLSDKFSLFPQFMFHLRRSQF 647
Cdd:PLN00162 511 EELVAGFDQEAAAVVMARLASHKMETE-EEFDATRWLDRALIRLCSKFGDYRKDDPSSFRLSPNFSLYPQFMFNLRRSQF 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 648 LQVFNNSPDETAYYRHILFSENVLESTTMIQPVLFSYSFNGPPEPVLLDTSSILADRILLMDDYFHVLIYHGQTIAQWRK 727
Cdd:PLN00162 590 VQVFNNSPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLDVASIAADRILLLDSYFSVVIFHGSTIAQWRK 669
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 728 QNFHENPQYATFKQLLEAPVADATSILQERFPMPRYIVTEHEGSQARFLLSKVNPSLTHNNPYANEAGSAVFTDDVSLQV 807
Cdd:PLN00162 670 AGYHNQPEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFLLAKLNPSATYNSANAMGGSDIIFTDDVSLQV 749
|
....
gi 17566436 808 FMEH 811
Cdd:PLN00162 750 FMEH 753
|
|
| SEC23 |
COG5047 |
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]; |
14-811 |
0e+00 |
|
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
Pssm-ID: 227380 [Multi-domain] Cd Length: 755 Bit Score: 854.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 14 NDGVQFTWNMWPHSRVDSQKLVVPLTCFFTPLKERPstevAQPPLEYDPVLCqKASCKAILNPLCAVDYRAKIWMCPFCN 93
Cdd:COG5047 9 NDGIRLTWNVFPATRGDATRTVIPIACLYTPLHEDD----ALTVNYYEPVKC-TAPCKAVLNPYCHIDERNQSWICPFCN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 94 NRNPFPAHYAAIAEDNRPPELYPQFTTIEYTLRKATTMPPIFVFVVDTCMTAEELKSLKECLQTALSLLPADALVGLITY 173
Cdd:COG5047 84 QRNTLPPQYRDISNANLPLELLPQSSTIEYTLSKPVILPPVFFFVVDACCDEEELTALKDSLIVSLSLLPPEALVGLITY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 174 GRMVQLHELNTQGISRSYVFKGTKEVTAKQIKDVmaggglsqrpaagapgapagapgapmamgsGAAPLGQLPGSglpgg 253
Cdd:COG5047 164 GTSIQVHELNAENHRRSYVFSGNKEYTKENLQEL------------------------------LALSKPTKSGG----- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 254 lprgggpplpgAAQGIVAPGGGAPvphapaNKFLQPISECDESINDLIDQISIDRWPVPQGHRPLRATGAALAVAVTLLE 333
Cdd:COG5047 209 -----------FESKISGIGQFAS------SRFLLPTQQCEFKLLNILEQLQPDPWPVPAGKRPLRCTGSALNIASSLLE 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 334 SCFPSTGARIMSFIGGACTHGPGAVVGEELKNPIRSWNSIKEDAAPYMKKAIKFYDGLAARIVKNGHAVDVYSCALDQTG 413
Cdd:COG5047 272 QCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEPMRSHHDIESDSAQHSKKATKFYKGLAERVANQGHALDIFAGCLDQIG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 414 LLEMKNMFNSSGGHVVMGDSFNSSLFKQTYQRSFDKDSAGNLKMGFNATMEVKVGAGLKIEGVLGCCASGNVRNANVSDQ 493
Cdd:COG5047 352 IMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFNRDSEGYLKMGFNANMEVKTSKNLKIKGLIGHAVSVKKKANNISDS 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 494 EMGIGGTCQWKFGAISPRTTIGVVFEIAAQHGSAIPQGG-RGMVQFVTQYQHADGRKRIRVTTTCRTWADMATqqPNIAY 572
Cdd:COG5047 432 EIGIGATNSWKMASLSPKSNYALYFEIALGAASGSAQRPaEAYIQFITTYQHSSGTYRIRVTTVARMFTDGGL--PKINR 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 573 GFDQEAAAVAIARLASFRASNEnDTPEALRWLDRSLIRLCQKFGEYSKDDPNSFRLSDKFSLFPQFMFHLRRSQFLQVFN 652
Cdd:COG5047 510 SFDQEAAAVFMARIAAFKAETE-DIIDVFRWIDRNLIRLCQKFADYRKDDPSSFRLDPNFTLYPQFMYHLRRSPFLSVFN 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 653 NSPDETAYYRHILFSENVLESTTMIQPVLFSYSFNGPPEPVLLDTSSILADRILLMDDYFHVLIYHGQTIAQWRKQNFHE 732
Cdd:COG5047 589 NSPDETAFYRHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVLLDSVSVKPDVILLLDTFFHILIFHGSYIAQWRNAGYQE 668
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17566436 733 NPQYATFKQLLEAPVADATSILQERFPMPRYIVTEHEGSQARFLLSKVNPSLTHNNPyANEAGSAVFTDDVSLQVFMEH 811
Cdd:COG5047 669 QPEYLNLKELLEAPRLEAAELLQDRFPIPRFIVTEQGGSQARFLLSKINPSDITNKM-SGGGSETILTDDVNLQKFMNH 746
|
|
| Sec23-like |
cd01478 |
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
130-445 |
1.07e-161 |
|
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: 470.31 E-value: 1.07e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 130 TMPPIFVFVVDTCMTAEELKSLKECLQTALSLLPADALVGLITYGRMVQLHELNTQGISRSYVFKGTKEVTAKQIKDVMA 209
Cdd:cd01478 1 TSPPVFLFVVDTCMDEEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 210 GGGLSQRpaagapgapagapgapmamgsgaaplgqlPGSGlpgglprgggpplpgaaqgiVAPGGGAPVPHAPANKFLQP 289
Cdd:cd01478 81 LGGPAMR-----------------------------PSAS--------------------QHPGAGNPLPSAAASRFLLP 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 290 ISECDESINDLIDQISIDRWPVPQGHRPLRATGAALAVAVTLLESCFPSTGARIMSFIGGACTHGPGAVVGEELKNPIRS 369
Cdd:cd01478 112 VSQCEFTLTDLLEQLQPDPWPVPAGHRPLRCTGVALSIAVGLLEACFPNTGARIMLFAGGPCTVGPGAVVSTELKDPIRS 191
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17566436 370 WNSIKEDAAPYMKKAIKFYDGLAARIVKNGHAVDVYSCALDQTGLLEMKNMFNSSGGHVVMGDSFNSSLFKQTYQR 445
Cdd:cd01478 192 HHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMKVLVNSTGGHVVLSDSFTTSIFKQSFQR 267
|
|
| trunk_domain |
cd01468 |
trunk domain. COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi ... |
130-445 |
1.75e-78 |
|
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: 253.32 E-value: 1.75e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 130 TMPPIFVFVVDTCMTA---EELKSLKECLQTALSLLPAD--ALVGLITYGRMVQLHELNTQGI-SRSYVFKGTKEVTakq 203
Cdd:cd01468 1 PQPPVFVFVIDVSYEAikeGLLQALKESLLASLDLLPGDprARVGLITYDSTVHFYNLSSDLAqPKMYVVSDLKDVF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 204 ikdvmaggglsqrpaagapgapagapgapmamgsgaaplgqlpgsglpgglprgggpplpgaaqgivapgggapvpHAPA 283
Cdd:cd01468 78 ----------------------------------------------------------------------------LPLP 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 284 NKFLQPISECDESINDLIDQISIDRWPVPqGHRPLRATGAALAVAVTLLESCFpsTGARIMSFIGGACTHGPGAVVGEEL 363
Cdd:cd01468 82 DRFLVPLSECKKVIHDLLEQLPPMFWPVP-THRPERCLGPALQAAFLLLKGTF--AGGRIIVFQGGLPTVGPGKLKSRED 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 364 KNPIRSWnsikeDAAPYMKKAIKFYDGLAARIVKNGHAVDVYSCALDQTGLLEMKNMFNSSGGHVVMGDSFN----SSLF 439
Cdd:cd01468 159 KEPIRSH-----DEAQLLKPATKFYKSLAKECVKSGICVDLFAFSLDYVDVATLKQLAKSTGGQVYLYDSFQapndGSKF 233
|
....*.
gi 17566436 440 KQTYQR 445
Cdd:cd01468 234 KQDLQR 239
|
|
| Sec23_C |
cd11287 |
C-terminal Actin depolymerization factor-homology domain of Sec23; The C-terminal domain of ... |
668-788 |
9.34e-77 |
|
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: 244.21 E-value: 9.34e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 668 ENVLESTTMIQPVLFSYSFNGPPEPVLLDTSSILADRILLMDDYFHVLIYHGQTIAQWRKQNFHENPQYATFKQLLEAPV 747
Cdd:cd11287 1 EDVSNSLIMIQPTLYSYSFNGPPEPVLLDSSSILPDRILLLDTFFHILIYHGETIAQWRKAGYQDQPEYENFKDLLEAPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 17566436 748 ADATSILQERFPMPRYIVTEHEGSQARFLLSKVNPSLTHNN 788
Cdd:cd11287 81 DDAQELLQDRFPMPRYIVTEQGGSQARFLLSKVNPSQTHNN 121
|
|
| Sec23_trunk |
pfam04811 |
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
131-447 |
1.42e-66 |
|
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: 221.36 E-value: 1.42e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 131 MPPIFVFVVDTCMTA---EELKSLKECLQTALSLLPAD--ALVGLITYGRMVQLHELntqgisrSYVFKGTKEVTAKQIK 205
Cdd:pfam04811 2 QPPVFLFVIDVSYNAiksGLLAALKESLLQSLDLLPGDprARVGFITFDSTVHFFNL-------GSSLRQPQMLVVSDLQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 206 DVMaggglsqrpaagapgapagapgapmamgsgaaplgqlpgsglpgglprgggpplpgaaqgivapgggapVPhaPANK 285
Cdd:pfam04811 75 DMF---------------------------------------------------------------------LP--LPDR 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 286 FLQPISECDESINDLIDQISiDRWPVPqgHRPLRATGAALAVAVTLLESCFpsTGARIMSFIGGACTHGPGAVVGEELKn 365
Cdd:pfam04811 84 FLVPLSECRFVLEDLLEQLP-PMFPVT--KRPERCLGPALQAAFLLLKAAF--TGGKIMVFQGGLPTVGPGGKLKSRLD- 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 366 piRSWNSIKEDAAPYMKKAIKFYDGLAARIVKNGHAVDVYSCALDQTGLLEMKNMFNSSGGHVVMGDSFN----SSLFKQ 441
Cdd:pfam04811 158 --ESHHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVATLGQLSRLTGGQVYLYPSFQadvdGSKFKQ 235
|
....*.
gi 17566436 442 TYQRSF 447
Cdd:pfam04811 236 DLQRYF 241
|
|
| Sec23_BS |
pfam08033 |
Sec23/Sec24 beta-sandwich domain; |
458-561 |
6.19e-24 |
|
Sec23/Sec24 beta-sandwich domain;
Pssm-ID: 429794 [Multi-domain] Cd Length: 86 Bit Score: 96.07 E-value: 6.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 458 GFNATMEVKVGAGLKIEGVLGCCASGNvrnanvsdqemgIGGTcqWKFGAISPRTTIGVVFEIAAQhgsaIPQGGRGMVQ 537
Cdd:pfam08033 1 GFNAVLRVRTSKGLKVSGFIGNFVSRS------------SGDT--WKLPSLDPDTSYAFEFDIDEP----LPNGSNAYIQ 62
|
90 100
....*....|....*....|....
gi 17566436 538 FVTQYQHADGRKRIRVTTTCRTWA 561
Cdd:pfam08033 63 FALLYTHSSGERRIRVTTVALPVT 86
|
|
| Sec23_helical |
pfam04815 |
Sec23/Sec24 helical domain; COPII-coated vesicles carry proteins from the endoplasmic ... |
589-673 |
3.61e-23 |
|
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: 94.49 E-value: 3.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 589 FRASNENDTpEALRWLDRSLIRLCQKFGEYSKD--DPNSFRLSDKFSLFPQFMFHLRRSQFLQVFNNSP-DETAYYRHIL 665
Cdd:pfam04815 15 EKALSSSLS-DAREALDNKLVDILAAYRKYCASssSPGQLILPESLKLLPLYMLALLKSPALRGGNSSPsDERAYARHLL 93
|
....*...
gi 17566436 666 FSENVLES 673
Cdd:pfam04815 94 LSLPVEEL 101
|
|
| COG5028 |
COG5028 |
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ... |
52-810 |
5.94e-15 |
|
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking and secretion];
Pssm-ID: 227361 [Multi-domain] Cd Length: 861 Bit Score: 79.07 E-value: 5.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 52 EVAQPPLEYD--PVLCQKasCKAILNPLCAVDYRAKIWMCPFCNNRNPFPAHYAAIAEDNRP-------PELypQFTTI- 121
Cdd:COG5028 187 EEDPVPLVEDgsIVRCRR--CRSYINPFVQFIEQGRKWRCNICRSKNDVPEGFDNPSGPNDPrsdrysrPEL--KSGVVd 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 122 -----EYTLRkaTTMPPIFVFVVDTCMTAEE-------LKSLKECLQTALSLLPaDALVGLITYGRMVQLHELNTQGISR 189
Cdd:COG5028 263 flapkEYSLR--QPPPPVYVFLIDVSFEAIKnglvkaaIRAILENLDQIPNFDP-RTKIAIICFDSSLHFFKLSPDLDEQ 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 190 SYVFKGTKEVtakqikdvmaggglsqrpaagapgapagapgapmamgsgaaplgQLPgsglpgglprgggpplpgaaqgi 269
Cdd:COG5028 340 MLIVSDLDEP--------------------------------------------FLP----------------------- 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 270 vapgggapvphAPANKFLQPISECDESINDLIDQISidrwPVPQG-HRPLRATGAALAVAVTLLESCfpstGARIMSFIG 348
Cdd:COG5028 353 -----------FPSGLFVLPLKSCKQIIETLLDRVP----RIFQDnKSPKNALGPALKAAKSLIGGT----GGKIIVFLS 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 349 GACTHGPGAVvgeELKNPIRSWNSIKEDaapymkkaiKFYDGLAARIVKNGHAVDVYSCALDQTGLLEMKNMFNSSGGHV 428
Cdd:COG5028 414 TLPNMGIGKL---QLREDKESSLLSCKD---------SFYKEFAIECSKVGISVDLFLTSEDYIDVATLSHLCRYTGGQT 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 429 VMGDSFNSSLFKQTYQRSFDKDSAGNLKMGFNATMEVKVGAGLKIEGVLgccasGNVRNANVSDQEmgiggtcqwkFGAI 508
Cdd:COG5028 482 YFYPNFSATRPNDATKLANDLVSHLSMEIGYEAVMRVRCSTGLRVSSFY-----GNFFNRSSDLCA----------FSTM 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 509 SPRTTIGVVFEIAAqhgsaiPQGGRGM-VQFVTQYQHADGRKRIRVTTTCrtwadMATQQpNIA--YGF-DQEAAAVAIA 584
Cdd:COG5028 547 PRDTSLLVEFSIDE------KLMTSDVyFQVALLYTLNDGERRIRVVNLS-----LPTSS-SIRevYASaDQLAIACILA 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 585 RLASFRASNeNDTPEALRWLDRSLIR-LCQKFGEYSKDDPNS-FRLSDKFSLFPQFMFHLRRSQFLQVFNNSPDETAYYR 662
Cdd:COG5028 615 KKASTKALN-SSLKEARVLINKSMVDiLKAYKKELVKSNTSTqLPLPANLKLLPLLMLALLKSSAFRSGSTPSDIRISAL 693
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 663 HILFSENVLESTTMIQPVLFS----YSFNGPPEPVLLDTSSILADRILLMDDYFHVLIYHGQTIAQWrkqnFHENpqyaT 738
Cdd:COG5028 694 NRLTSLPLKQLMRNIYPTLYAlhdmPIEAGLPDEGLLVLPSPINATSSLLESGGLYLIDTGQKIFLW----FGKD----A 765
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17566436 739 FKQLLEA--PVADATSILQERFPMPryiVTEHEGSQ-ARFLLSK---VNPSLTHnNPYANEAGSAVFTDDVSLQVFME 810
Cdd:COG5028 766 VPSLLQDlfGVDSLSDIPSGKFTLP---PTGNEFNErVRNIIGElrsVNDDSTL-PLVLVRGGGDPSLRLWFFSTLVE 839
|
|
| zf-Sec23_Sec24 |
pfam04810 |
Sec23/Sec24 zinc finger; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
62-101 |
2.55e-14 |
|
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: 67.47 E-value: 2.55e-14
10 20 30 40
....*....|....*....|....*....|....*....|
gi 17566436 62 PVLCQKasCKAILNPLCAVDYRAKIWMCPFCNNRNPFPAH 101
Cdd:pfam04810 1 PVRCRR--CRAYLNPFCQFDFGGKKWTCNFCGTRNPVPPE 38
|
|
| Gelsolin |
pfam00626 |
Gelsolin repeat; |
690-776 |
1.44e-13 |
|
Gelsolin repeat;
Pssm-ID: 395501 [Multi-domain] Cd Length: 76 Bit Score: 66.56 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 690 PEPVLLDTSSILADRILLMDdyfhvliyHGQTIAQWRKQNfhENPQYATFKQLLEAPVADatsilQERFPMPRYIVTEHE 769
Cdd:pfam00626 5 PPPVPLSQESLNSGDCYLLD--------NGFTIFLWVGKG--SSLLEKLFAALLAAQLDD-----DERFPLPEVIRVPQG 69
|
....*..
gi 17566436 770 GSQARFL 776
Cdd:pfam00626 70 KEPARFL 76
|
|
| gelsolin_like |
cd11280 |
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ... |
678-780 |
3.58e-07 |
|
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: 48.52 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 678 QPVLF--SYSFNGPPEPVLLDTSSILADRILLMDDYFHVLIYHGqtiaqwrkqnfhenpqYATFKQLLEAPVADATSILQ 755
Cdd:cd11280 1 PPRLYrvRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQG----------------RASSQAELAAAALLAKELDE 64
|
90 100
....*....|....*....|....*
gi 17566436 756 ERFPMPRYIVtEHEGSQARFLLSKV 780
Cdd:cd11280 65 ERKGKPEIVR-IRQGQEPREFWSLF 88
|
|
| Sec24-like |
cd01479 |
Sec24-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
284-405 |
1.28e-04 |
|
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: 44.57 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566436 284 NKFLQPISECDESINDLIDQIsidrwpvP----QGHRPLRATGAALAVAVTLLESCfpstGARIMSFIGGACTHGPGAVv 359
Cdd:cd01479 83 DGLLVNLKESRQVIEDLLDQI-------PemfqDTKETESALGPALQAAFLLLKET----GGKIIVFQSSLPTLGAGKL- 150
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 17566436 360 geELKNPIRSWNSIKEDAApyMKKAIKFYDGLAARIVKNGHAVDVY 405
Cdd:cd01479 151 --KSREDPKLLSTDKEKQL--LQPQTDFYKKLALECVKSQISVDLF 192
|
|
| |
