|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00162 |
PLN00162 |
transport protein sec23; Provisional |
2-761 |
0e+00 |
|
transport protein sec23; Provisional
Pssm-ID: 215083 [Multi-domain] Cd Length: 761 Bit Score: 1430.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 2 AEFGELEAQDGVRMPWNIIPvaTKKEQSIDSEVPVSAIYTPLKPLrSQSLLLPYSPLRCRTCRSVLNPYSVVDFSACNWG 81
Cdd:PLN00162 1 MDFAELEAIDGVRMSWNVWP--SSKIEASKCVIPLAALYTPLKPL-PELPVLPYDPLRCRTCRAVLNPYCRVDFQAKIWI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 82 CPFCFNRNPFPLNYSSVADNNLPPELFPHSTTVEYLCD--SFSSPSPPVFLFVVDTCLISEELDFLKSSLFQALDLLPDT 159
Cdd:PLN00162 78 CPFCFQRNHFPPHYSSISETNLPAELFPQYTTVEYTLPpgSGGAPSPPVFVFVVDTCMIEEELGALKSALLQAIALLPEN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 160 SILGLITFDSLVRVYELGFPHCTKSYFFHGNKDCTKDQLLDQLSFFVKNPKPSSGVIAGARDGLSSDDIARFLLPASDCH 239
Cdd:PLN00162 158 ALVGLITFGTHVHVHELGFSECSKSYVFRGNKEVSKDQILEQLGLGGKKRRPAGGGIAGARDGLSSSGVNRFLLPASECE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 240 FTLHSVLEELGNSPWPVAADHRPARCTGVALRIAASLLGACFPGSAARIMAFIGGPSTQGPGAIVSRELSDPIRSHKDID 319
Cdd:PLN00162 238 FTLNSALEELQKDPWPVPPGHRPARCTGAALSVAAGLLGACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 320 KDSAMYYHKAVEFYEMLAKQLVHQGHVLDVFASSVDQVGIAELKVAVEQTGGFVVLAESFGHSVFRDSLKRVCQ-SGEND 398
Cdd:PLN00162 318 KDAAPYYKKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFErDGEGS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 399 LGLSSCGIFEINCSKDIKVQGIIGPCASLEKKGPLCSDTAIGQGHTSAWKMCGLDNNTSICLVFEIAKIDTAdvVLQSQS 478
Cdd:PLN00162 398 LGLSFNGTFEVNCSKDVKVQGAIGPCASLEKKGPSVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQS--NPQPPG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 479 NQFYFQFLTYYQHSNGQTRLRVTTLSRRWVMGTeSLQELSNGFDQEAAAVVMARLISSKMETQPEFNPQRWVDKALINLC 558
Cdd:PLN00162 476 QQFFLQFLTRYQHSNGQTRLRVTTVTRRWVEGS-SSEELVAGFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLC 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 559 TWFGDYQKGNPSSFSLSSQLSIFPQFVFHLRRSQFVQVFNNSPDETAYFRMILYRENVSNSVVMIQPSLISFSFHSPPEP 638
Cdd:PLN00162 555 SKFGDYRKDDPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNNSPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEP 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 639 ILLDVASIAADRILLLDSYFTLVIFHGSTIAQWRKAGYHNQPEHQAFGHLLQSPRDYADTIMSERFPTPRLVICDQYGSQ 718
Cdd:PLN00162 635 VLLDVASIAADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQ 714
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 15226602 719 ARFLLAKLNPC---DGDAHFSGQSNVFTDDVSLSVFLDHLRRLIVH 761
Cdd:PLN00162 715 ARFLLAKLNPSatyNSANAMGGSDIIFTDDVSLQVFMEHLQRLAVQ 760
|
|
| SEC23 |
COG5047 |
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]; |
3-760 |
0e+00 |
|
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
Pssm-ID: 227380 [Multi-domain] Cd Length: 755 Bit Score: 750.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 3 EFGELEAQDGVRMPWNIIPvATKKEQSiDSEVPVSAIYTPLKPlRSQSLLLPYSPLRCR-TCRSVLNPYSVVDFSACNWG 81
Cdd:COG5047 2 NFEIIEENDGIRLTWNVFP-ATRGDAT-RTVIPIACLYTPLHE-DDALTVNYYEPVKCTaPCKAVLNPYCHIDERNQSWI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 82 CPFCFNRNPFPLNYSSVADNNLPPELFPHSTTVEYLCdSFSSPSPPVFLFVVDTCLISEELDFLKSSLFQALDLLPDTSI 161
Cdd:COG5047 79 CPFCNQRNTLPPQYRDISNANLPLELLPQSSTIEYTL-SKPVILPPVFFFVVDACCDEEELTALKDSLIVSLSLLPPEAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 162 LGLITFDSLVRVYELGFPHCTKSYFFHGNKDCTKDQLlDQLSFFVKNPKPSSgvIAGARDGLSSDDIARFLLPASDCHFT 241
Cdd:COG5047 158 VGLITYGTSIQVHELNAENHRRSYVFSGNKEYTKENL-QELLALSKPTKSGG--FESKISGIGQFASSRFLLPTQQCEFK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 242 LHSVLEELGNSPWPVAADHRPARCTGVALRIAASLLGACFPGSAARIMAFIGGPSTQGPGAIVSRELSDPIRSHKDIDKD 321
Cdd:COG5047 235 LLNILEQLQPDPWPVPAGKRPLRCTGSALNIASSLLEQCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEPMRSHHDIESD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 322 SAMYYHKAVEFYEMLAKQLVHQGHVLDVFASSVDQVGIAELKVAVEQTGGFVVLAESFGHSVFRDSLKRVC-QSGENDLG 400
Cdd:COG5047 315 SAQHSKKATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFnRDSEGYLK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 401 LSSCGIFEINCSKDIKVQGIIGPCASLEKKGPLCSDTAIGQGHTSAWKMCGLDNNTSICLVFEIAKidTADVVLQSQSNQ 480
Cdd:COG5047 395 MGFNANMEVKTSKNLKIKGLIGHAVSVKKKANNISDSEIGIGATNSWKMASLSPKSNYALYFEIAL--GAASGSAQRPAE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 481 FYFQFLTYYQHSNGQTRLRVTTLSRRWVMGTESLqeLSNGFDQEAAAVVMARLISSKMETQPEFNPQRWVDKALINLCTW 560
Cdd:COG5047 473 AYIQFITTYQHSSGTYRIRVTTVARMFTDGGLPK--INRSFDQEAAAVFMARIAAFKAETEDIIDVFRWIDRNLIRLCQK 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 561 FGDYQKGNPSSFSLSSQLSIFPQFVFHLRRSQFVQVFNNSPDETAYFRMILYRENVSNSVVMIQPSLISFSFHSPPEPIL 640
Cdd:COG5047 551 FADYRKDDPSSFRLDPNFTLYPQFMYHLRRSPFLSVFNNSPDETAFYRHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVL 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 641 LDVASIAADRILLLDSYFTLVIFHGSTIAQWRKAGYHNQPEHQAFGHLLQSPRDYADTIMSERFPTPRLVICDQYGSQAR 720
Cdd:COG5047 631 LDSVSVKPDVILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKELLEAPRLEAAELLQDRFPIPRFIVTEQGGSQAR 710
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 15226602 721 FLLAKLNPCD--GDAHFSGQSNVFTDDVSLSVFLDHLRRLIV 760
Cdd:COG5047 711 FLLSKINPSDitNKMSGGGSETILTDDVNLQKFMNHLRKLAV 752
|
|
| Sec23-like |
cd01478 |
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
124-390 |
9.05e-165 |
|
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: 476.09 E-value: 9.05e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 124 PSPPVFLFVVDTCLISEELDFLKSSLFQALDLLPDTSILGLITFDSLVRVYELGFPHCTKSYFFHGNKDCTKDQLLDQLS 203
Cdd:cd01478 1 TSPPVFLFVVDTCMDEEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 204 FFVKNPKPSSGVIAGARDGLSSDDIARFLLPASDCHFTLHSVLEELGNSPWPVAADHRPARCTGVALRIAASLLGACFPG 283
Cdd:cd01478 81 LGGPAMRPSASQHPGAGNPLPSAAASRFLLPVSQCEFTLTDLLEQLQPDPWPVPAGHRPLRCTGVALSIAVGLLEACFPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 284 SAARIMAFIGGPSTQGPGAIVSRELSDPIRSHKDIDKDSAMYYHKAVEFYEMLAKQLVHQGHVLDVFASSVDQVGIAELK 363
Cdd:cd01478 161 TGARIMLFAGGPCTVGPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMK 240
|
250 260
....*....|....*....|....*..
gi 15226602 364 VAVEQTGGFVVLAESFGHSVFRDSLKR 390
Cdd:cd01478 241 VLVNSTGGHVVLSDSFTTSIFKQSFQR 267
|
|
| Sec23_trunk |
pfam04811 |
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
124-392 |
5.97e-84 |
|
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: 266.42 E-value: 5.97e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 124 PSPPVFLFVVDTCLI---SEELDFLKSSLFQALDLLPDTS--ILGLITFDSLVRVYELGFPHctksyffHGNKDCTKDQL 198
Cdd:pfam04811 1 PQPPVFLFVIDVSYNaikSGLLAALKESLLQSLDLLPGDPraRVGFITFDSTVHFFNLGSSL-------RQPQMLVVSDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 199 LDQLSffvknPKPSsgviagardglssddiaRFLLPASDCHFTLHSVLEELGNsPWPVAadHRPARCTGVALRIAASLLG 278
Cdd:pfam04811 74 QDMFL-----PLPD-----------------RFLVPLSECRFVLEDLLEQLPP-MFPVT--KRPERCLGPALQAAFLLLK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 279 ACFpgSAARIMAFIGGPSTQGPGAIVSRELSDpirSHKDIDKDSAMYYHKAVEFYEMLAKQLVHQGHVLDVFASSVDQVG 358
Cdd:pfam04811 129 AAF--TGGKIMVFQGGLPTVGPGGKLKSRLDE---SHHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVD 203
|
250 260 270
....*....|....*....|....*....|....*...
gi 15226602 359 IAELKVAVEQTGGFVVLAESFG----HSVFRDSLKRVC 392
Cdd:pfam04811 204 VATLGQLSRLTGGQVYLYPSFQadvdGSKFKQDLQRYF 241
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00162 |
PLN00162 |
transport protein sec23; Provisional |
2-761 |
0e+00 |
|
transport protein sec23; Provisional
Pssm-ID: 215083 [Multi-domain] Cd Length: 761 Bit Score: 1430.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 2 AEFGELEAQDGVRMPWNIIPvaTKKEQSIDSEVPVSAIYTPLKPLrSQSLLLPYSPLRCRTCRSVLNPYSVVDFSACNWG 81
Cdd:PLN00162 1 MDFAELEAIDGVRMSWNVWP--SSKIEASKCVIPLAALYTPLKPL-PELPVLPYDPLRCRTCRAVLNPYCRVDFQAKIWI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 82 CPFCFNRNPFPLNYSSVADNNLPPELFPHSTTVEYLCD--SFSSPSPPVFLFVVDTCLISEELDFLKSSLFQALDLLPDT 159
Cdd:PLN00162 78 CPFCFQRNHFPPHYSSISETNLPAELFPQYTTVEYTLPpgSGGAPSPPVFVFVVDTCMIEEELGALKSALLQAIALLPEN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 160 SILGLITFDSLVRVYELGFPHCTKSYFFHGNKDCTKDQLLDQLSFFVKNPKPSSGVIAGARDGLSSDDIARFLLPASDCH 239
Cdd:PLN00162 158 ALVGLITFGTHVHVHELGFSECSKSYVFRGNKEVSKDQILEQLGLGGKKRRPAGGGIAGARDGLSSSGVNRFLLPASECE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 240 FTLHSVLEELGNSPWPVAADHRPARCTGVALRIAASLLGACFPGSAARIMAFIGGPSTQGPGAIVSRELSDPIRSHKDID 319
Cdd:PLN00162 238 FTLNSALEELQKDPWPVPPGHRPARCTGAALSVAAGLLGACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 320 KDSAMYYHKAVEFYEMLAKQLVHQGHVLDVFASSVDQVGIAELKVAVEQTGGFVVLAESFGHSVFRDSLKRVCQ-SGEND 398
Cdd:PLN00162 318 KDAAPYYKKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFErDGEGS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 399 LGLSSCGIFEINCSKDIKVQGIIGPCASLEKKGPLCSDTAIGQGHTSAWKMCGLDNNTSICLVFEIAKIDTAdvVLQSQS 478
Cdd:PLN00162 398 LGLSFNGTFEVNCSKDVKVQGAIGPCASLEKKGPSVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVANSGQS--NPQPPG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 479 NQFYFQFLTYYQHSNGQTRLRVTTLSRRWVMGTeSLQELSNGFDQEAAAVVMARLISSKMETQPEFNPQRWVDKALINLC 558
Cdd:PLN00162 476 QQFFLQFLTRYQHSNGQTRLRVTTVTRRWVEGS-SSEELVAGFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLC 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 559 TWFGDYQKGNPSSFSLSSQLSIFPQFVFHLRRSQFVQVFNNSPDETAYFRMILYRENVSNSVVMIQPSLISFSFHSPPEP 638
Cdd:PLN00162 555 SKFGDYRKDDPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNNSPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEP 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 639 ILLDVASIAADRILLLDSYFTLVIFHGSTIAQWRKAGYHNQPEHQAFGHLLQSPRDYADTIMSERFPTPRLVICDQYGSQ 718
Cdd:PLN00162 635 VLLDVASIAADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQ 714
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 15226602 719 ARFLLAKLNPC---DGDAHFSGQSNVFTDDVSLSVFLDHLRRLIVH 761
Cdd:PLN00162 715 ARFLLAKLNPSatyNSANAMGGSDIIFTDDVSLQVFMEHLQRLAVQ 760
|
|
| SEC23 |
COG5047 |
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]; |
3-760 |
0e+00 |
|
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
Pssm-ID: 227380 [Multi-domain] Cd Length: 755 Bit Score: 750.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 3 EFGELEAQDGVRMPWNIIPvATKKEQSiDSEVPVSAIYTPLKPlRSQSLLLPYSPLRCR-TCRSVLNPYSVVDFSACNWG 81
Cdd:COG5047 2 NFEIIEENDGIRLTWNVFP-ATRGDAT-RTVIPIACLYTPLHE-DDALTVNYYEPVKCTaPCKAVLNPYCHIDERNQSWI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 82 CPFCFNRNPFPLNYSSVADNNLPPELFPHSTTVEYLCdSFSSPSPPVFLFVVDTCLISEELDFLKSSLFQALDLLPDTSI 161
Cdd:COG5047 79 CPFCNQRNTLPPQYRDISNANLPLELLPQSSTIEYTL-SKPVILPPVFFFVVDACCDEEELTALKDSLIVSLSLLPPEAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 162 LGLITFDSLVRVYELGFPHCTKSYFFHGNKDCTKDQLlDQLSFFVKNPKPSSgvIAGARDGLSSDDIARFLLPASDCHFT 241
Cdd:COG5047 158 VGLITYGTSIQVHELNAENHRRSYVFSGNKEYTKENL-QELLALSKPTKSGG--FESKISGIGQFASSRFLLPTQQCEFK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 242 LHSVLEELGNSPWPVAADHRPARCTGVALRIAASLLGACFPGSAARIMAFIGGPSTQGPGAIVSRELSDPIRSHKDIDKD 321
Cdd:COG5047 235 LLNILEQLQPDPWPVPAGKRPLRCTGSALNIASSLLEQCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEPMRSHHDIESD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 322 SAMYYHKAVEFYEMLAKQLVHQGHVLDVFASSVDQVGIAELKVAVEQTGGFVVLAESFGHSVFRDSLKRVC-QSGENDLG 400
Cdd:COG5047 315 SAQHSKKATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFnRDSEGYLK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 401 LSSCGIFEINCSKDIKVQGIIGPCASLEKKGPLCSDTAIGQGHTSAWKMCGLDNNTSICLVFEIAKidTADVVLQSQSNQ 480
Cdd:COG5047 395 MGFNANMEVKTSKNLKIKGLIGHAVSVKKKANNISDSEIGIGATNSWKMASLSPKSNYALYFEIAL--GAASGSAQRPAE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 481 FYFQFLTYYQHSNGQTRLRVTTLSRRWVMGTESLqeLSNGFDQEAAAVVMARLISSKMETQPEFNPQRWVDKALINLCTW 560
Cdd:COG5047 473 AYIQFITTYQHSSGTYRIRVTTVARMFTDGGLPK--INRSFDQEAAAVFMARIAAFKAETEDIIDVFRWIDRNLIRLCQK 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 561 FGDYQKGNPSSFSLSSQLSIFPQFVFHLRRSQFVQVFNNSPDETAYFRMILYRENVSNSVVMIQPSLISFSFHSPPEPIL 640
Cdd:COG5047 551 FADYRKDDPSSFRLDPNFTLYPQFMYHLRRSPFLSVFNNSPDETAFYRHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVL 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 641 LDVASIAADRILLLDSYFTLVIFHGSTIAQWRKAGYHNQPEHQAFGHLLQSPRDYADTIMSERFPTPRLVICDQYGSQAR 720
Cdd:COG5047 631 LDSVSVKPDVILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKELLEAPRLEAAELLQDRFPIPRFIVTEQGGSQAR 710
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 15226602 721 FLLAKLNPCD--GDAHFSGQSNVFTDDVSLSVFLDHLRRLIV 760
Cdd:COG5047 711 FLLSKINPSDitNKMSGGGSETILTDDVNLQKFMNHLRKLAV 752
|
|
| Sec23-like |
cd01478 |
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
124-390 |
9.05e-165 |
|
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: 476.09 E-value: 9.05e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 124 PSPPVFLFVVDTCLISEELDFLKSSLFQALDLLPDTSILGLITFDSLVRVYELGFPHCTKSYFFHGNKDCTKDQLLDQLS 203
Cdd:cd01478 1 TSPPVFLFVVDTCMDEEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 204 FFVKNPKPSSGVIAGARDGLSSDDIARFLLPASDCHFTLHSVLEELGNSPWPVAADHRPARCTGVALRIAASLLGACFPG 283
Cdd:cd01478 81 LGGPAMRPSASQHPGAGNPLPSAAASRFLLPVSQCEFTLTDLLEQLQPDPWPVPAGHRPLRCTGVALSIAVGLLEACFPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 284 SAARIMAFIGGPSTQGPGAIVSRELSDPIRSHKDIDKDSAMYYHKAVEFYEMLAKQLVHQGHVLDVFASSVDQVGIAELK 363
Cdd:cd01478 161 TGARIMLFAGGPCTVGPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMK 240
|
250 260
....*....|....*....|....*..
gi 15226602 364 VAVEQTGGFVVLAESFGHSVFRDSLKR 390
Cdd:cd01478 241 VLVNSTGGHVVLSDSFTTSIFKQSFQR 267
|
|
| Sec23_trunk |
pfam04811 |
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
124-392 |
5.97e-84 |
|
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: 266.42 E-value: 5.97e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 124 PSPPVFLFVVDTCLI---SEELDFLKSSLFQALDLLPDTS--ILGLITFDSLVRVYELGFPHctksyffHGNKDCTKDQL 198
Cdd:pfam04811 1 PQPPVFLFVIDVSYNaikSGLLAALKESLLQSLDLLPGDPraRVGFITFDSTVHFFNLGSSL-------RQPQMLVVSDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 199 LDQLSffvknPKPSsgviagardglssddiaRFLLPASDCHFTLHSVLEELGNsPWPVAadHRPARCTGVALRIAASLLG 278
Cdd:pfam04811 74 QDMFL-----PLPD-----------------RFLVPLSECRFVLEDLLEQLPP-MFPVT--KRPERCLGPALQAAFLLLK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 279 ACFpgSAARIMAFIGGPSTQGPGAIVSRELSDpirSHKDIDKDSAMYYHKAVEFYEMLAKQLVHQGHVLDVFASSVDQVG 358
Cdd:pfam04811 129 AAF--TGGKIMVFQGGLPTVGPGGKLKSRLDE---SHHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVD 203
|
250 260 270
....*....|....*....|....*....|....*...
gi 15226602 359 IAELKVAVEQTGGFVVLAESFG----HSVFRDSLKRVC 392
Cdd:pfam04811 204 VATLGQLSRLTGGQVYLYPSFQadvdGSKFKQDLQRYF 241
|
|
| trunk_domain |
cd01468 |
trunk domain. COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi ... |
124-390 |
2.92e-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: 251.40 E-value: 2.92e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 124 PSPPVFLFVVDTCLI---SEELDFLKSSLFQALDLLPD--TSILGLITFDSLVRVYELGFPHCT-KSYFFHGNKDCTkdq 197
Cdd:cd01468 1 PQPPVFVFVIDVSYEaikEGLLQALKESLLASLDLLPGdpRARVGLITYDSTVHFYNLSSDLAQpKMYVVSDLKDVF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 198 lldqlsffvknpkpssgviagardglsSDDIARFLLPASDCHFTLHSVLEELGNSPWPVaADHRPARCTGVALRIAASLL 277
Cdd:cd01468 78 ---------------------------LPLPDRFLVPLSECKKVIHDLLEQLPPMFWPV-PTHRPERCLGPALQAAFLLL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 278 GACFPGsaARIMAFIGGPSTQGPGAIVSRELSDPIRSHkdidkDSAMYYHKAVEFYEMLAKQLVHQGHVLDVFASSVDQV 357
Cdd:cd01468 130 KGTFAG--GRIIVFQGGLPTVGPGKLKSREDKEPIRSH-----DEAQLLKPATKFYKSLAKECVKSGICVDLFAFSLDYV 202
|
250 260 270
....*....|....*....|....*....|....*..
gi 15226602 358 GIAELKVAVEQTGGFVVLAESF----GHSVFRDSLKR 390
Cdd:cd01468 203 DVATLKQLAKSTGGQVYLYDSFqapnDGSKFKQDLQR 239
|
|
| Sec23_C |
cd11287 |
C-terminal Actin depolymerization factor-homology domain of Sec23; The C-terminal domain of ... |
614-731 |
3.76e-63 |
|
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: 206.84 E-value: 3.76e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 614 ENVSNSVVMIQPSLISFSFHSPPEPILLDVASIAADRILLLDSYFTLVIFHGSTIAQWRKAGYHNQPEHQAFGHLLQSPR 693
Cdd:cd11287 1 EDVSNSLIMIQPTLYSYSFNGPPEPVLLDSSSILPDRILLLDTFFHILIYHGETIAQWRKAGYQDQPEYENFKDLLEAPV 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 15226602 694 DYADTIMSERFPTPRLVICDQYGSQARFLLAKLNPCDG 731
Cdd:cd11287 81 DDAQELLQDRFPMPRYIVTEQGGSQARFLLSKVNPSQT 118
|
|
| Sec23_BS |
pfam08033 |
Sec23/Sec24 beta-sandwich domain; |
404-508 |
6.18e-24 |
|
Sec23/Sec24 beta-sandwich domain;
Pssm-ID: 429794 [Multi-domain] Cd Length: 86 Bit Score: 96.07 E-value: 6.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 404 CGIFEINCSKDIKVQGIIGPCASLEkkgplCSDTaigqghtsaWKMCGLDNNTSICLVFEI-AKIDTAdvvlqsqsNQFY 482
Cdd:pfam08033 3 NAVLRVRTSKGLKVSGFIGNFVSRS-----SGDT---------WKLPSLDPDTSYAFEFDIdEPLPNG--------SNAY 60
|
90 100
....*....|....*....|....*.
gi 15226602 483 FQFLTYYQHSNGQTRLRVTTLSRRWV 508
Cdd:pfam08033 61 IQFALLYTHSSGERRIRVTTVALPVT 86
|
|
| COG5028 |
COG5028 |
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ... |
56-537 |
2.72e-22 |
|
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking and secretion];
Pssm-ID: 227361 [Multi-domain] Cd Length: 861 Bit Score: 102.56 E-value: 2.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 56 SPLRCRTCRSVLNPYSVVDFSACNWGCPFCFNRNPFPLNYSSVADNNLP-------PELfpHSTTVEYLCD---SFSSPS 125
Cdd:COG5028 198 SIVRCRRCRSYINPFVQFIEQGRKWRCNICRSKNDVPEGFDNPSGPNDPrsdrysrPEL--KSGVVDFLAPkeySLRQPP 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 126 PPVFLFVVDTCLISeeldfLKSSLFQALDLLPDTSILGLITFDSLVRVYELGFPHctKSYFFHGNKDCTKDQL--LDQLS 203
Cdd:COG5028 276 PPVYVFLIDVSFEA-----IKNGLVKAAIRAILENLDQIPNFDPRTKIAIICFDS--SLHFFKLSPDLDEQMLivSDLDE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 204 FFVKNPKPSsgviagardglssddiarFLLPASDCHFTLHSVLEELGNSPwpvAADHRPARCTGVALRIAASLLGACfpg 283
Cdd:COG5028 349 PFLPFPSGL------------------FVLPLKSCKQIIETLLDRVPRIF---QDNKSPKNALGPALKAAKSLIGGT--- 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 284 sAARIMAFIGGPSTQGPGAIVSRElsDPIRSHkDIDKDSamyyhkaveFYEMLAKQLVHQGHVLDVFASSVDQVGIAELK 363
Cdd:COG5028 405 -GGKIIVFLSTLPNMGIGKLQLRE--DKESSL-LSCKDS---------FYKEFAIECSKVGISVDLFLTSEDYIDVATLS 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 364 VAVEQTGGFVVLAESFGHSVFRDSLKRV---CQSGENDLGLSscGIFEINCSKDIKVQGIIGpcASLEKKGPLCsdtAIG 440
Cdd:COG5028 472 HLCRYTGGQTYFYPNFSATRPNDATKLAndlVSHLSMEIGYE--AVMRVRCSTGLRVSSFYG--NFFNRSSDLC---AFS 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 441 QghtsawkmcgLDNNTSicLVFEIA---KIDTADVvlqsqsnqfYFQFLTYYQHSNGQTRLRVTTLSrrwVMGTESLQEL 517
Cdd:COG5028 545 T----------MPRDTS--LLVEFSideKLMTSDV---------YFQVALLYTLNDGERRIRVVNLS---LPTSSSIREV 600
|
490 500
....*....|....*....|
gi 15226602 518 SNGFDQEAAAVVMARLISSK 537
Cdd:COG5028 601 YASADQLAIACILAKKASTK 620
|
|
| Sec23_helical |
pfam04815 |
Sec23/Sec24 helical domain; COPII-coated vesicles carry proteins from the endoplasmic ... |
522-621 |
5.87e-19 |
|
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: 82.55 E-value: 5.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 522 DQEAAAVVMARLISSKMETQPEFNPQRWVDKALINLCTWFGDYQKGN--PSSFSLSSQLSIFPQFVFHLRRSQFVQVFNN 599
Cdd:pfam04815 1 DQEAIAVLLAKKAVEKALSSSLSDAREALDNKLVDILAAYRKYCASSssPGQLILPESLKLLPLYMLALLKSPALRGGNS 80
|
90 100
....*....|....*....|...
gi 15226602 600 SP-DETAYFRMILYRENVSNSVV 621
Cdd:pfam04815 81 SPsDERAYARHLLLSLPVEELLL 103
|
|
| zf-Sec23_Sec24 |
pfam04810 |
Sec23/Sec24 zinc finger; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
57-92 |
1.60e-13 |
|
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: 64.77 E-value: 1.60e-13
10 20 30
....*....|....*....|....*....|....*.
gi 15226602 57 PLRCRTCRSVLNPYSVVDFSACNWGCPFCFNRNPFP 92
Cdd:pfam04810 1 PVRCRRCRAYLNPFCQFDFGGKKWTCNFCGTRNPVP 36
|
|
| Gelsolin |
pfam00626 |
Gelsolin repeat; |
636-722 |
2.41e-13 |
|
Gelsolin repeat;
Pssm-ID: 395501 [Multi-domain] Cd Length: 76 Bit Score: 65.79 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 636 PEPILLDVASIAADRILLLDsyftlvifHGSTIAQWRkaGYHNQPEHQAFGHLLQSPRDyadtiMSERFPTPRLVICDQY 715
Cdd:pfam00626 5 PPPVPLSQESLNSGDCYLLD--------NGFTIFLWV--GKGSSLLEKLFAALLAAQLD-----DDERFPLPEVIRVPQG 69
|
....*..
gi 15226602 716 GSQARFL 722
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 ... |
124-389 |
5.77e-07 |
|
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: 51.50 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 124 PSPPVFLFVVDTCLISEELDFLK---SSLFQALDLLPD----TSIlGLITFDSLVRvyelgfphctksyFFHGNKDCTKD 196
Cdd:cd01479 1 PQPAVYVFLIDVSYNAIKSGLLAtacEALLSNLDNLPGddprTRV-GFITFDSTLH-------------FFNLKSSLEQP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 197 QLL---DQLSFFVknPKPSSgviagardglssddiarFLLPASDCHFTLHSVLEELgnsPWPVAADHRPARCTGVALRIA 273
Cdd:cd01479 67 QMMvvsDLDDPFL--PLPDG-----------------LLVNLKESRQVIEDLLDQI---PEMFQDTKETESALGPALQAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 274 ASLLGACfpgsAARIMAFIGGPSTQGPGAIVSRElsDPirSHKDIDKDSAMYyHKAVEFYEMLAKQLVHQGHVLDVFASS 353
Cdd:cd01479 125 FLLLKET----GGKIIVFQSSLPTLGAGKLKSRE--DP--KLLSTDKEKQLL-QPQTDFYKKLALECVKSQISVDLFLFS 195
|
250 260 270
....*....|....*....|....*....|....*.
gi 15226602 354 VDQVGIAELKVAVEQTGGFVVLAESFGHSVFRDSLK 389
Cdd:cd01479 196 NQYVDVATLGCLSRLTGGQVYYYPSFNFSAPNDVEK 231
|
|
| gelsolin_like |
cd11280 |
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ... |
627-726 |
4.15e-06 |
|
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: 45.44 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226602 627 LISFSFHSPPEPILLDVASIAADRILLLDSYFTLVIFHGStiaqwrkagyhnqpehQAFGHLLQSPRDYADTIMSERFPT 706
Cdd:cd11280 6 RVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGR----------------ASSQAELAAAALLAKELDEERKGK 69
|
90 100
....*....|....*....|
gi 15226602 707 PRLVICDQyGSQARFLLAKL 726
Cdd:cd11280 70 PEIVRIRQ-GQEPREFWSLF 88
|
|
| vWA_subgroup |
cd01465 |
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
129-173 |
6.53e-03 |
|
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Not much is known about the function of the VWA domain in these proteins. The members do have a conserved MIDAS motif. The biochemical function however is not known.
Pssm-ID: 238742 [Multi-domain] Cd Length: 170 Bit Score: 38.41 E-value: 6.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 15226602 129 FLFVVDTC--LISEELDFLKSSLFQALDLLPDTSILGLITFDSLVRV 173
Cdd:cd01465 3 LVFVIDRSgsMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAAET 49
|
|
| |
