|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00162 |
PLN00162 |
transport protein sec23; Provisional |
1-794 |
0e+00 |
|
transport protein sec23; Provisional
Pssm-ID: 215083 [Multi-domain] Cd Length: 761 Bit Score: 1344.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 1 MDFLELEAIEGLRWSWNSWPTTKSDCESLVVPLSIMYTPLMHFSELPTIPYDPLICSRCGAVLNPYARVDYQSRIWSCPF 80
Cdd:PLN00162 1 MDFAELEAIDGVRMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPLRCRTCRAVLNPYCRVDFQAKIWICPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 81 CFHKNLFPRSYSGITETNLPAELFPTYSAVEYSPLPSRQSgsntttptaaaswsngfnqgvrsmpsnssfsslasstvgg 160
Cdd:PLN00162 81 CFQRNHFPPHYSSISETNLPAELFPQYTTVEYTLPPGSGG---------------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 161 gggviSELGPAFVFVVDASMVEDELRAVRSDVLFVIEQLPENCLVALITFDSMVRVYDLGFSECSKVVVFHGERDLSPDQ 240
Cdd:PLN00162 121 -----APSPPVFVFVVDTCMIEEELGALKSALLQAIALLPENALVGLITFGTHVHVHELGFSECSKSYVFRGNKEVSKDQ 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 241 IQQFLGLGYSKQFHHGKM--------SAIRKQSFLLPLVECEFNLTSAFEEIIPLV-DVKPGHRPHRSTGAAISTALGLL 311
Cdd:PLN00162 196 ILEQLGLGGKKRRPAGGGiagardglSSSGVNRFLLPASECEFTLNSALEELQKDPwPVPPGHRPARCTGAALSVAAGLL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 312 EGCSVTTGSRIMVFTSGPATRGPGIIVDSDLSNSIRTHRDIITGHVSYYDKSCGFYKKLAKRLCDSSVVLDVFACSLDQV 391
Cdd:PLN00162 276 GACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDAAPYYKKAVKFYEGLAKQLVAQGHVLDVFACSLDQV 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 392 GAAELRYAVEMSGGFLLLGETFESEQFKKCLRHIFIRDADGNLSMYFDVSLEVVTTKDMRICGALGPVVSLRQKNDIVSE 471
Cdd:PLN00162 356 GVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFERDGEGSLGLSFNGTFEVNCSKDVKVQGAIGPCASLEKKGPSVSD 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 472 TEIGEGGTYMWKTSTVTNKTCVSFFFHVSNEQNRKPQP-GSAFFIQFITRYRYGNGAMRKRVTTVARRWVAG-KSPEISS 549
Cdd:PLN00162 436 TEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSNPQPpGQQFFLQFLTRYQHSNGQTRLRVTTVTRRWVEGsSSEELVA 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 550 SFDQETAASVMARLAINRAEECHARDVITWLDNGLIRFASRFGDYIQEDPSSFRLTPNFSLYPQFMFYLRRSQFLDVFNN 629
Cdd:PLN00162 516 GFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFGDYRKDDPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNN 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 630 SPDETGFFRLMLNREGVVNSIIMIQPTLLRYSFDGPPVPVLLDIRSVTPDVILLFDSYFYVVIHHGSKIAQWRKLEYHKD 709
Cdd:PLN00162 596 SPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLDVASIAADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQ 675
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 710 PSHETFRNLLEAPEIDAAQLVTDRIPMPRIVRCDQHGSQARFLLAKLNPSVTQKTDHT-GGSDIVLTDDMSLQDFLEDLQ 788
Cdd:PLN00162 676 PEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFLLAKLNPSATYNSANAmGGSDIIFTDDVSLQVFMEHLQ 755
|
....*.
gi 18422356 789 SLAVKG 794
Cdd:PLN00162 756 RLAVQS 761
|
|
| SEC23 |
COG5047 |
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]; |
1-794 |
0e+00 |
|
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
Pssm-ID: 227380 [Multi-domain] Cd Length: 755 Bit Score: 718.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 1 MDFLELEAIEGLRWSWNSWPTTKSDCESLVVPLSIMYTPLMHFSELPTIPYDPLIC-SRCGAVLNPYARVDYQSRIWSCP 79
Cdd:COG5047 1 MNFEIIEENDGIRLTWNVFPATRGDATRTVIPIACLYTPLHEDDALTVNYYEPVKCtAPCKAVLNPYCHIDERNQSWICP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 80 FCFHKNLFPRSYSGITETNLPAELFPTYSAVEY-SPLPSRqsgsntttptaaaswsngfnqgvrsmpsnssfsslasstv 158
Cdd:COG5047 81 FCNQRNTLPPQYRDISNANLPLELLPQSSTIEYtLSKPVI---------------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 159 gggggviseLGPAFVFVVDASMVEDELRAVRSDVLFVIEQLPENCLVALITFDSMVRVYDLGFSECSKVVVFHGERDLSP 238
Cdd:COG5047 121 ---------LPPVFFFVVDACCDEEELTALKDSLIVSLSLLPPEALVGLITYGTSIQVHELNAENHRRSYVFSGNKEYTK 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 239 DQIQQFLGLgYSKQFHHGKMSAIRKQS------FLLPLVECEFNLTSAFEEIIP-LVDVKPGHRPHRSTGAAISTALGLL 311
Cdd:COG5047 192 ENLQELLAL-SKPTKSGGFESKISGIGqfassrFLLPTQQCEFKLLNILEQLQPdPWPVPAGKRPLRCTGSALNIASSLL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 312 EGCSVTTGSRIMVFTSGPATRGPGIIVDSDLSNSIRTHRDIITGHVSYYDKSCGFYKKLAKRLCDSSVVLDVFACSLDQV 391
Cdd:COG5047 271 EQCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEPMRSHHDIESDSAQHSKKATKFYKGLAERVANQGHALDIFAGCLDQI 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 392 GAAELRYAVEMSGGFLLLGETFESEQFKKCLRHIFIRDADGNLSMYFDVSLEVVTTKDMRICGALGPVVSLRQKNDIVSE 471
Cdd:COG5047 351 GIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFNRDSEGYLKMGFNANMEVKTSKNLKIKGLIGHAVSVKKKANNISD 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 472 TEIGEGGTYMWKTSTVTNKTCVSFFFHVSNEQNRKPQPGSAF-FIQFITRYRYGNGAMRKRVTTVARRWVAGKSPEISSS 550
Cdd:COG5047 431 SEIGIGATNSWKMASLSPKSNYALYFEIALGAASGSAQRPAEaYIQFITTYQHSSGTYRIRVTTVARMFTDGGLPKINRS 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 551 FDQETAASVMARLAINRAEECHARDVITWLDNGLIRFASRFGDYIQEDPSSFRLTPNFSLYPQFMFYLRRSQFLDVFNNS 630
Cdd:COG5047 511 FDQEAAAVFMARIAAFKAETEDIIDVFRWIDRNLIRLCQKFADYRKDDPSSFRLDPNFTLYPQFMYHLRRSPFLSVFNNS 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 631 PDETGFFRLMLNREGVVNSIIMIQPTLLRYSFDGPPVPVLLDIRSVTPDVILLFDSYFYVVIHHGSKIAQWRKLEYHKDP 710
Cdd:COG5047 591 PDETAFYRHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVLLDSVSVKPDVILLLDTFFHILIFHGSYIAQWRNAGYQEQP 670
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 711 SHETFRNLLEAPEIDAAQLVTDRIPMPRIVRCDQHGSQARFLLAKLNPSVTQKTDHTGGSDIVLTDDMSLQDFLEDLQSL 790
Cdd:COG5047 671 EYLNLKELLEAPRLEAAELLQDRFPIPRFIVTEQGGSQARFLLSKINPSDITNKMSGGGSETILTDDVNLQKFMNHLRKL 750
|
....
gi 18422356 791 AVKG 794
Cdd:COG5047 751 AVSK 754
|
|
| Sec23-like |
cd01478 |
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
170-419 |
5.85e-87 |
|
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: 276.17 E-value: 5.85e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 170 PAFVFVVDASMVEDELRAVRSDVLFVIEQLPENCLVALITFDSMVRVYDLGFSECSKVVVFHGERDLSPDQIQQFLGLGY 249
Cdd:cd01478 4 PVFLFVVDTCMDEEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLGLGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 250 SKQ-----FHHGKMSAIRKQS---FLLPLVECEFNLTSAFEEIIPlvD---VKPGHRPHRSTGAAISTALGLLEGCSVTT 318
Cdd:cd01478 84 PAMrpsasQHPGAGNPLPSAAasrFLLPVSQCEFTLTDLLEQLQP--DpwpVPAGHRPLRCTGVALSIAVGLLEACFPNT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 319 GSRIMVFTSGPATRGPGIIVDSDLSNSIRTHRDIITGHVSYYDKSCGFYKKLAKRLCDSSVVLDVFACSLDQVGAAELRY 398
Cdd:cd01478 162 GARIMLFAGGPCTVGPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMKV 241
|
250 260
....*....|....*....|.
gi 18422356 399 AVEMSGGFLLLGETFESEQFK 419
Cdd:cd01478 242 LVNSTGGHVVLSDSFTTSIFK 262
|
|
| Sec23_trunk |
pfam04811 |
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
170-429 |
3.64e-54 |
|
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: 187.07 E-value: 3.64e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 170 PAFVFVVDASMV---EDELRAVRSDVLFVIEQLP--ENCLVALITFDSMVRVYDLGFSEcskvvvfHGERDLSPDQIQQF 244
Cdd:pfam04811 4 PVFLFVIDVSYNaikSGLLAALKESLLQSLDLLPgdPRARVGFITFDSTVHFFNLGSSL-------RQPQMLVVSDLQDM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 245 LGLGYSkqfhhgkmsairkqSFLLPLVECEFNLTSAFEEIIPLVDVKpgHRPHRSTGAAISTALGLLEGCsvTTGSRIMV 324
Cdd:pfam04811 77 FLPLPD--------------RFLVPLSECRFVLEDLLEQLPPMFPVT--KRPERCLGPALQAAFLLLKAA--FTGGKIMV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 325 FTSGPATRGPGIIVDSDLSNSirtHRDIITGHVSYYDKSCGFYKKLAKRLCDSSVVLDVFACSLDQVGAAELRYAVEMSG 404
Cdd:pfam04811 139 FQGGLPTVGPGGKLKSRLDES---HHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVATLGQLSRLTG 215
|
250 260
....*....|....*....|....*
gi 18422356 405 GFLLLGETFESEQFKKCLRHIFIRD 429
Cdd:pfam04811 216 GQVYLYPSFQADVDGSKFKQDLQRY 240
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00162 |
PLN00162 |
transport protein sec23; Provisional |
1-794 |
0e+00 |
|
transport protein sec23; Provisional
Pssm-ID: 215083 [Multi-domain] Cd Length: 761 Bit Score: 1344.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 1 MDFLELEAIEGLRWSWNSWPTTKSDCESLVVPLSIMYTPLMHFSELPTIPYDPLICSRCGAVLNPYARVDYQSRIWSCPF 80
Cdd:PLN00162 1 MDFAELEAIDGVRMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPLRCRTCRAVLNPYCRVDFQAKIWICPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 81 CFHKNLFPRSYSGITETNLPAELFPTYSAVEYSPLPSRQSgsntttptaaaswsngfnqgvrsmpsnssfsslasstvgg 160
Cdd:PLN00162 81 CFQRNHFPPHYSSISETNLPAELFPQYTTVEYTLPPGSGG---------------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 161 gggviSELGPAFVFVVDASMVEDELRAVRSDVLFVIEQLPENCLVALITFDSMVRVYDLGFSECSKVVVFHGERDLSPDQ 240
Cdd:PLN00162 121 -----APSPPVFVFVVDTCMIEEELGALKSALLQAIALLPENALVGLITFGTHVHVHELGFSECSKSYVFRGNKEVSKDQ 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 241 IQQFLGLGYSKQFHHGKM--------SAIRKQSFLLPLVECEFNLTSAFEEIIPLV-DVKPGHRPHRSTGAAISTALGLL 311
Cdd:PLN00162 196 ILEQLGLGGKKRRPAGGGiagardglSSSGVNRFLLPASECEFTLNSALEELQKDPwPVPPGHRPARCTGAALSVAAGLL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 312 EGCSVTTGSRIMVFTSGPATRGPGIIVDSDLSNSIRTHRDIITGHVSYYDKSCGFYKKLAKRLCDSSVVLDVFACSLDQV 391
Cdd:PLN00162 276 GACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKDAAPYYKKAVKFYEGLAKQLVAQGHVLDVFACSLDQV 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 392 GAAELRYAVEMSGGFLLLGETFESEQFKKCLRHIFIRDADGNLSMYFDVSLEVVTTKDMRICGALGPVVSLRQKNDIVSE 471
Cdd:PLN00162 356 GVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFERDGEGSLGLSFNGTFEVNCSKDVKVQGAIGPCASLEKKGPSVSD 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 472 TEIGEGGTYMWKTSTVTNKTCVSFFFHVSNEQNRKPQP-GSAFFIQFITRYRYGNGAMRKRVTTVARRWVAG-KSPEISS 549
Cdd:PLN00162 436 TEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQSNPQPpGQQFFLQFLTRYQHSNGQTRLRVTTVTRRWVEGsSSEELVA 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 550 SFDQETAASVMARLAINRAEECHARDVITWLDNGLIRFASRFGDYIQEDPSSFRLTPNFSLYPQFMFYLRRSQFLDVFNN 629
Cdd:PLN00162 516 GFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFGDYRKDDPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNN 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 630 SPDETGFFRLMLNREGVVNSIIMIQPTLLRYSFDGPPVPVLLDIRSVTPDVILLFDSYFYVVIHHGSKIAQWRKLEYHKD 709
Cdd:PLN00162 596 SPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLDVASIAADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQ 675
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 710 PSHETFRNLLEAPEIDAAQLVTDRIPMPRIVRCDQHGSQARFLLAKLNPSVTQKTDHT-GGSDIVLTDDMSLQDFLEDLQ 788
Cdd:PLN00162 676 PEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFLLAKLNPSATYNSANAmGGSDIIFTDDVSLQVFMEHLQ 755
|
....*.
gi 18422356 789 SLAVKG 794
Cdd:PLN00162 756 RLAVQS 761
|
|
| SEC23 |
COG5047 |
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]; |
1-794 |
0e+00 |
|
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
Pssm-ID: 227380 [Multi-domain] Cd Length: 755 Bit Score: 718.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 1 MDFLELEAIEGLRWSWNSWPTTKSDCESLVVPLSIMYTPLMHFSELPTIPYDPLIC-SRCGAVLNPYARVDYQSRIWSCP 79
Cdd:COG5047 1 MNFEIIEENDGIRLTWNVFPATRGDATRTVIPIACLYTPLHEDDALTVNYYEPVKCtAPCKAVLNPYCHIDERNQSWICP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 80 FCFHKNLFPRSYSGITETNLPAELFPTYSAVEY-SPLPSRqsgsntttptaaaswsngfnqgvrsmpsnssfsslasstv 158
Cdd:COG5047 81 FCNQRNTLPPQYRDISNANLPLELLPQSSTIEYtLSKPVI---------------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 159 gggggviseLGPAFVFVVDASMVEDELRAVRSDVLFVIEQLPENCLVALITFDSMVRVYDLGFSECSKVVVFHGERDLSP 238
Cdd:COG5047 121 ---------LPPVFFFVVDACCDEEELTALKDSLIVSLSLLPPEALVGLITYGTSIQVHELNAENHRRSYVFSGNKEYTK 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 239 DQIQQFLGLgYSKQFHHGKMSAIRKQS------FLLPLVECEFNLTSAFEEIIP-LVDVKPGHRPHRSTGAAISTALGLL 311
Cdd:COG5047 192 ENLQELLAL-SKPTKSGGFESKISGIGqfassrFLLPTQQCEFKLLNILEQLQPdPWPVPAGKRPLRCTGSALNIASSLL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 312 EGCSVTTGSRIMVFTSGPATRGPGIIVDSDLSNSIRTHRDIITGHVSYYDKSCGFYKKLAKRLCDSSVVLDVFACSLDQV 391
Cdd:COG5047 271 EQCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEPMRSHHDIESDSAQHSKKATKFYKGLAERVANQGHALDIFAGCLDQI 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 392 GAAELRYAVEMSGGFLLLGETFESEQFKKCLRHIFIRDADGNLSMYFDVSLEVVTTKDMRICGALGPVVSLRQKNDIVSE 471
Cdd:COG5047 351 GIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFNRDSEGYLKMGFNANMEVKTSKNLKIKGLIGHAVSVKKKANNISD 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 472 TEIGEGGTYMWKTSTVTNKTCVSFFFHVSNEQNRKPQPGSAF-FIQFITRYRYGNGAMRKRVTTVARRWVAGKSPEISSS 550
Cdd:COG5047 431 SEIGIGATNSWKMASLSPKSNYALYFEIALGAASGSAQRPAEaYIQFITTYQHSSGTYRIRVTTVARMFTDGGLPKINRS 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 551 FDQETAASVMARLAINRAEECHARDVITWLDNGLIRFASRFGDYIQEDPSSFRLTPNFSLYPQFMFYLRRSQFLDVFNNS 630
Cdd:COG5047 511 FDQEAAAVFMARIAAFKAETEDIIDVFRWIDRNLIRLCQKFADYRKDDPSSFRLDPNFTLYPQFMYHLRRSPFLSVFNNS 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 631 PDETGFFRLMLNREGVVNSIIMIQPTLLRYSFDGPPVPVLLDIRSVTPDVILLFDSYFYVVIHHGSKIAQWRKLEYHKDP 710
Cdd:COG5047 591 PDETAFYRHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVLLDSVSVKPDVILLLDTFFHILIFHGSYIAQWRNAGYQEQP 670
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 711 SHETFRNLLEAPEIDAAQLVTDRIPMPRIVRCDQHGSQARFLLAKLNPSVTQKTDHTGGSDIVLTDDMSLQDFLEDLQSL 790
Cdd:COG5047 671 EYLNLKELLEAPRLEAAELLQDRFPIPRFIVTEQGGSQARFLLSKINPSDITNKMSGGGSETILTDDVNLQKFMNHLRKL 750
|
....
gi 18422356 791 AVKG 794
Cdd:COG5047 751 AVSK 754
|
|
| Sec23-like |
cd01478 |
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
170-419 |
5.85e-87 |
|
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: 276.17 E-value: 5.85e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 170 PAFVFVVDASMVEDELRAVRSDVLFVIEQLPENCLVALITFDSMVRVYDLGFSECSKVVVFHGERDLSPDQIQQFLGLGY 249
Cdd:cd01478 4 PVFLFVVDTCMDEEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLGLGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 250 SKQ-----FHHGKMSAIRKQS---FLLPLVECEFNLTSAFEEIIPlvD---VKPGHRPHRSTGAAISTALGLLEGCSVTT 318
Cdd:cd01478 84 PAMrpsasQHPGAGNPLPSAAasrFLLPVSQCEFTLTDLLEQLQP--DpwpVPAGHRPLRCTGVALSIAVGLLEACFPNT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 319 GSRIMVFTSGPATRGPGIIVDSDLSNSIRTHRDIITGHVSYYDKSCGFYKKLAKRLCDSSVVLDVFACSLDQVGAAELRY 398
Cdd:cd01478 162 GARIMLFAGGPCTVGPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMKV 241
|
250 260
....*....|....*....|.
gi 18422356 399 AVEMSGGFLLLGETFESEQFK 419
Cdd:cd01478 242 LVNSTGGHVVLSDSFTTSIFK 262
|
|
| Sec23_C |
cd11287 |
C-terminal Actin depolymerization factor-homology domain of Sec23; The C-terminal domain of ... |
644-764 |
5.96e-71 |
|
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: 228.03 E-value: 5.96e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 644 EGVVNSIIMIQPTLLRYSFDGPPVPVLLDIRSVTPDVILLFDSYFYVVIHHGSKIAQWRKLEYHKDPSHETFRNLLEAPE 723
Cdd:cd11287 1 EDVSNSLIMIQPTLYSYSFNGPPEPVLLDSSSILPDRILLLDTFFHILIYHGETIAQWRKAGYQDQPEYENFKDLLEAPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 18422356 724 IDAAQLVTDRIPMPRIVRCDQHGSQARFLLAKLNPSVTQKT 764
Cdd:cd11287 81 DDAQELLQDRFPMPRYIVTEQGGSQARFLLSKVNPSQTHNN 121
|
|
| Sec23_trunk |
pfam04811 |
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
170-429 |
3.64e-54 |
|
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: 187.07 E-value: 3.64e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 170 PAFVFVVDASMV---EDELRAVRSDVLFVIEQLP--ENCLVALITFDSMVRVYDLGFSEcskvvvfHGERDLSPDQIQQF 244
Cdd:pfam04811 4 PVFLFVIDVSYNaikSGLLAALKESLLQSLDLLPgdPRARVGFITFDSTVHFFNLGSSL-------RQPQMLVVSDLQDM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 245 LGLGYSkqfhhgkmsairkqSFLLPLVECEFNLTSAFEEIIPLVDVKpgHRPHRSTGAAISTALGLLEGCsvTTGSRIMV 324
Cdd:pfam04811 77 FLPLPD--------------RFLVPLSECRFVLEDLLEQLPPMFPVT--KRPERCLGPALQAAFLLLKAA--FTGGKIMV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 325 FTSGPATRGPGIIVDSDLSNSirtHRDIITGHVSYYDKSCGFYKKLAKRLCDSSVVLDVFACSLDQVGAAELRYAVEMSG 404
Cdd:pfam04811 139 FQGGLPTVGPGGKLKSRLDES---HHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVATLGQLSRLTG 215
|
250 260
....*....|....*....|....*
gi 18422356 405 GFLLLGETFESEQFKKCLRHIFIRD 429
Cdd:pfam04811 216 GQVYLYPSFQADVDGSKFKQDLQRY 240
|
|
| trunk_domain |
cd01468 |
trunk domain. COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi ... |
170-428 |
1.33e-53 |
|
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: 185.53 E-value: 1.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 170 PAFVFVVDASMV---EDELRAVRSDVLFVIEQLP--ENCLVALITFDSMVRVYDLGFSEC-SKVVVFHGERDLspdqiqq 243
Cdd:cd01468 4 PVFVFVIDVSYEaikEGLLQALKESLLASLDLLPgdPRARVGLITYDSTVHFYNLSSDLAqPKMYVVSDLKDV------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 244 FLGlgyskqfhhgkmsaiRKQSFLLPLVECEFNLTSAFEEIIPLVDVKPGHRPHRSTGAAISTALGLLEGCsvTTGSRIM 323
Cdd:cd01468 77 FLP---------------LPDRFLVPLSECKKVIHDLLEQLPPMFWPVPTHRPERCLGPALQAAFLLLKGT--FAGGRII 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 324 VFTSGPATRGPGIIVDSDLSNSIRTHRDiitghVSYYDKSCGFYKKLAKRLCDSSVVLDVFACSLDQVGAAELRYAVEMS 403
Cdd:cd01468 140 VFQGGLPTVGPGKLKSREDKEPIRSHDE-----AQLLKPATKFYKSLAKECVKSGICVDLFAFSLDYVDVATLKQLAKST 214
|
250 260
....*....|....*....|....*
gi 18422356 404 GGFLLLGETFESEQFKKCLRHIFIR 428
Cdd:cd01468 215 GGQVYLYDSFQAPNDGSKFKQDLQR 239
|
|
| Sec23_helical |
pfam04815 |
Sec23/Sec24 helical domain; COPII-coated vesicles carry proteins from the endoplasmic ... |
552-651 |
1.07e-25 |
|
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: 101.81 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 552 DQETAASVMARLAINRAEECHARDVITWLDNGLIRFASRFGDYI--QEDPSSFRLTPNFSLYPQFMFYLRRSQFLDVFNN 629
Cdd:pfam04815 1 DQEAIAVLLAKKAVEKALSSSLSDAREALDNKLVDILAAYRKYCasSSSPGQLILPESLKLLPLYMLALLKSPALRGGNS 80
|
90 100
....*....|....*....|...
gi 18422356 630 SP-DETGFFRLMLNREGVVNSII 651
Cdd:pfam04815 81 SPsDERAYARHLLLSLPVEELLL 103
|
|
| COG5028 |
COG5028 |
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ... |
12-701 |
1.45e-19 |
|
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking and secretion];
Pssm-ID: 227361 [Multi-domain] Cd Length: 861 Bit Score: 94.09 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 12 LRWSWNSWPTTKSDCESLVVPLSIMYTPLMH-FSELPTIPYD----PLICSRCGAVLNPYARVDYQSRIWSCPFCFHKNL 86
Cdd:COG5028 153 VRSTMYAIPETNDLLKKSKIPFGLVIRPFLElYPEEDPVPLVedgsIVRCRRCRSYINPFVQFIEQGRKWRCNICRSKND 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 87 FPRSYSGitetnlpaelfPTYSAVEYSPLPSRQSGSNTTTPTAAASwsngfnqgvrsmpsnssfsslasstvggGGGVIS 166
Cdd:COG5028 233 VPEGFDN-----------PSGPNDPRSDRYSRPELKSGVVDFLAPK----------------------------EYSLRQ 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 167 ELGPAFVFVVDASMVEDELRAVRS------DVLFVIEQLPENCLVALITFDSMVRVYDLgfsecskvvvfhgerdlSPDQ 240
Cdd:COG5028 274 PPPPVYVFLIDVSFEAIKNGLVKAairailENLDQIPNFDPRTKIAIICFDSSLHFFKL-----------------SPDL 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 241 IQQFLGLGYSKQFHHGKMSairkQSFLLPLVEC---EFNLTSAFEEIipLVDVkpgHRPHRSTGAAISTALGLLEGCsvt 317
Cdd:COG5028 337 DEQMLIVSDLDEPFLPFPS----GLFVLPLKSCkqiIETLLDRVPRI--FQDN---KSPKNALGPALKAAKSLIGGT--- 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 318 tGSRIMVFTSGPATRGPGiivdsdlsnSIRTHRDIITGHVSYYDkscGFYKKLAKRLCDSSVVLDVFACSLDQVGAAELR 397
Cdd:COG5028 405 -GGKIIVFLSTLPNMGIG---------KLQLREDKESSLLSCKD---SFYKEFAIECSKVGISVDLFLTSEDYIDVATLS 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 398 YAVEMSGGFLLLGETFESEQFKKCLRhiFIRDADGNLSMyfDVSLEVV----TTKDMRICGALGPVVSlRQKNDIVsete 473
Cdd:COG5028 472 HLCRYTGGQTYFYPNFSATRPNDATK--LANDLVSHLSM--EIGYEAVmrvrCSTGLRVSSFYGNFFN-RSSDLCA---- 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 474 igeggtymwkTSTVTNKTCVSFFFHVSNEQNrkpqpGSAFFIQFITRYRYGNGAMRKRVTTVARRwVAGKSPEISSSFDQ 553
Cdd:COG5028 543 ----------FSTMPRDTSLLVEFSIDEKLM-----TSDVYFQVALLYTLNDGERRIRVVNLSLP-TSSSIREVYASADQ 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 554 ETAASVMARLAINRAEECHARDVITWLDNGLIRFASRFGDYIQED--PSSFRLTPNFSLYPQFMFYLRRSQFLDVFNNSP 631
Cdd:COG5028 607 LAIACILAKKASTKALNSSLKEARVLINKSMVDILKAYKKELVKSntSTQLPLPANLKLLPLLMLALLKSSAFRSGSTPS 686
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18422356 632 DETGFFRLMLNREGVVNSIIMIQPTLlrYSF------DGPPVPVLLDIRSVTPDVILLFDSYFYVVIHHGSKIAQW 701
Cdd:COG5028 687 DIRISALNRLTSLPLKQLMRNIYPTL--YALhdmpieAGLPDEGLLVLPSPINATSSLLESGGLYLIDTGQKIFLW 760
|
|
| Sec23_BS |
pfam08033 |
Sec23/Sec24 beta-sandwich domain; |
438-540 |
8.50e-18 |
|
Sec23/Sec24 beta-sandwich domain;
Pssm-ID: 429794 [Multi-domain] Cd Length: 86 Bit Score: 78.73 E-value: 8.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 438 FDVSLEVVTTKDMRICGALGPVVSLrqkndivseteiGEGGTymWKTSTVTNKTCVSFFFhvsnEQNRKPQPGSAFFIQF 517
Cdd:pfam08033 2 FNAVLRVRTSKGLKVSGFIGNFVSR------------SSGDT--WKLPSLDPDTSYAFEF----DIDEPLPNGSNAYIQF 63
|
90 100
....*....|....*....|...
gi 18422356 518 ITRYRYGNGAMRKRVTTVARRWV 540
Cdd:pfam08033 64 ALLYTHSSGERRIRVTTVALPVT 86
|
|
| zf-Sec23_Sec24 |
pfam04810 |
Sec23/Sec24 zinc finger; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
53-88 |
3.21e-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: 67.09 E-value: 3.21e-14
10 20 30
....*....|....*....|....*....|....*.
gi 18422356 53 PLICSRCGAVLNPYARVDYQSRIWSCPFCFHKNLFP 88
Cdd:pfam04810 1 PVRCRRCRAYLNPFCQFDFGGKKWTCNFCGTRNPVP 36
|
|
| Gelsolin |
pfam00626 |
Gelsolin repeat; |
666-752 |
3.19e-11 |
|
Gelsolin repeat;
Pssm-ID: 395501 [Multi-domain] Cd Length: 76 Bit Score: 59.63 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 666 PVPVLLDIRSVTPDVILLFDsyfyvvihHGSKIAQWRKleYHKDPSHETFRNLLEAPEIDaaqlvTDRIPMPRIVRCDQH 745
Cdd:pfam00626 5 PPPVPLSQESLNSGDCYLLD--------NGFTIFLWVG--KGSSLLEKLFAALLAAQLDD-----DERFPLPEVIRVPQG 69
|
....*..
gi 18422356 746 GSQARFL 752
Cdd:pfam00626 70 KEPARFL 76
|
|
| Sec24-like |
cd01479 |
Sec24-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
170-405 |
5.86e-10 |
|
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: 60.36 E-value: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 170 PAFVFVVDASMVEDE---LRAVRSDVLFVIEQLPE---NCLVALITFDSMVRVYDLgfsecskvvvfhgERDLspDQIQQ 243
Cdd:cd01479 4 AVYVFLIDVSYNAIKsglLATACEALLSNLDNLPGddpRTRVGFITFDSTLHFFNL-------------KSSL--EQPQM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 244 FLglgyskqfhhgkMSAI------RKQSFLLPLVECEFNLTSAFEEIiPLV--DVKPghrPHRSTGAAISTALGLLEGCs 315
Cdd:cd01479 69 MV------------VSDLddpflpLPDGLLVNLKESRQVIEDLLDQI-PEMfqDTKE---TESALGPALQAAFLLLKET- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 316 vttGSRIMVFTSGPATRGPGIIVDSDLSNSIRTHRDIItgHVSYYDKscgFYKKLAKRLCDSSVVLDVFACSLDQVGAAE 395
Cdd:cd01479 132 ---GGKIIVFQSSLPTLGAGKLKSREDPKLLSTDKEKQ--LLQPQTD---FYKKLALECVKSQISVDLFLFSNQYVDVAT 203
|
250
....*....|
gi 18422356 396 LRYAVEMSGG 405
Cdd:cd01479 204 LGCLSRLTGG 213
|
|
| gelsolin_like |
cd11280 |
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ... |
657-756 |
4.25e-04 |
|
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: 40.04 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422356 657 LLRYSFDGPPVPVLLDIRSVTPDVILLFDSYFYVVIHHGSKiaqwrkleyhkdpsheTFRNLLEAPEIDAAQLVTDRIPM 736
Cdd:cd11280 6 RVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRA----------------SSQAELAAAALLAKELDEERKGK 69
|
90 100
....*....|....*....|
gi 18422356 737 PRIVRCdQHGSQARFLLAKL 756
Cdd:cd11280 70 PEIVRI-RQGQEPREFWSLF 88
|
|
| YfbK |
COG2304 |
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ... |
172-216 |
2.93e-03 |
|
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only];
Pssm-ID: 441879 [Multi-domain] Cd Length: 289 Bit Score: 40.47 E-value: 2.93e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 18422356 172 FVFVVDA--SMVEDELRAVRSDVLFVIEQLPENCLVALITFDSMVRV 216
Cdd:COG2304 94 LVFVIDVsgSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARV 140
|
|
| |
