|
Name |
Accession |
Description |
Interval |
E-value |
| COG5028 |
COG5028 |
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ... |
19-724 |
0e+00 |
|
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking and secretion];
Pssm-ID: 227361 [Multi-domain] Cd Length: 861 Bit Score: 574.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 19 NCSPDSFRCTLTNIPQTQALLNKAKLPLGLLLHPFRDLT----QLPVITSNTIVRCRSCRTYINPFVSFIDQ-RRWKCNL 93
Cdd:COG5028 147 NCSPKYVRSTMYAIPETNDLLKKSKIPFGLVIRPFLELYpeedPVPLVEDGSIVRCRRCRSYINPFVQFIEQgRKWRCNI 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 94 CYRVNDVPEEFmYNPLTRS--YGEPHKRPEVQNSTVEFIASSDYMLRPPQPAVYLFVLDVSHNAVEAGYLTILCQSLLEN 171
Cdd:COG5028 227 CRSKNDVPEGF-DNPSGPNdpRSDRYSRPELKSGVVDFLAPKEYSLRQPPPPVYVFLIDVSFEAIKNGLVKAAIRAILEN 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 172 LDKLPG-DSRTRIGFMTFDSTIHFYNLQEGLSQpQMLIVSDIDDVFLPTP-DSLLVNLYESKELIKDLLNALPNMFTNTR 249
Cdd:COG5028 306 LDQIPNfDPRTKIAIICFDSSLHFFKLSPDLDE-QMLIVSDLDEPFLPFPsGLFVLPLKSCKQIIETLLDRVPRIFQDNK 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 250 ETHSALGPALQAAFKLMSPTGGRVSVFQTQLPSLGAGLLQSREDPNQRsstkvvqHLGPATDFYKKLALDCSGQQTAVDL 329
Cdd:COG5028 385 SPKNALGPALKAAKSLIGGTGGKIIVFLSTLPNMGIGKLQLREDKESS-------LLSCKDSFYKEFAIECSKVGISVDL 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 330 FLLSSQYSDLASLACMSKYSAGCIYYYPSFHYThNPSQAEKLQKDLKRYLTRKIGFEAVMRIRCTKGLSMHTFHGNFFVR 409
Cdd:COG5028 458 FLTSEDYIDVATLSHLCRYTGGQTYFYPNFSAT-RPNDATKLANDLVSHLSMEIGYEAVMRVRCSTGLRVSSFYGNFFNR 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 410 STDLLSLANINPDAGFAVQLSIEESLTdTSLVCFQTALLYTSSKGERRIRVHTLCLPVVSSLADVYAGVDVQAAICLLAN 489
Cdd:COG5028 537 SSDLCAFSTMPRDTSLLVEFSIDEKLM-TSDVYFQVALLYTLNDGERRIRVVNLSLPTSSSIREVYASADQLAIACILAK 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 490 MAVDRSVSSSLSDARDALVNAVVDSLSAY-GSTVSNLQHSALMAPSSLKLFPLYVLALLKQKAFRTGtSTRLDDRVYAMC 568
Cdd:COG5028 616 KASTKALNSSLKEARVLINKSMVDILKAYkKELVKSNTSTQLPLPANLKLLPLLMLALLKSSAFRSG-STPSDIRISALN 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 569 QIKSQPLVHLMKMIHPNLYRIDRLTDEGAVHVNDRIVPQPPLqKLSAEKLTREGAFLMDCGSVFYIWVGKGCDNNFIEDV 648
Cdd:COG5028 695 RLTSLPLKQLMRNIYPTLYALHDMPIEAGLPDEGLLVLPSPI-NATSSLLESGGLYLIDTGQKIFLWFGKDAVPSLLQDL 773
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767930894 649 LGYTNFASIPQKMTHLPELDTLSSERARSFITWLRDSRP-LSPILHIVKD--ESPAKAEFFQHLIEDRTEAAFSYYEFL 724
Cdd:COG5028 774 FGVDSLSDIPSGKFTLPPTGNEFNERVRNIIGELRSVNDdSTLPLVLVRGggDPSLRLWFFSTLVEDKTLNIPSYLDYL 852
|
|
| Sec24-like |
cd01479 |
Sec24-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
140-383 |
5.88e-137 |
|
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: 403.19 E-value: 5.88e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 140 PQPAVYLFVLDVSHNAVEAGYLTILCQSLLENLDKLPGD-SRTRIGFMTFDSTIHFYNLQEGLSQPQMLIVSDIDDVFLP 218
Cdd:cd01479 1 PQPAVYVFLIDVSYNAIKSGLLATACEALLSNLDNLPGDdPRTRVGFITFDSTLHFFNLKSSLEQPQMMVVSDLDDPFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 219 TPDSLLVNLYESKELIKDLLNALPNMFTNTRETHSALGPALQAAFKLMSPTGGRVSVFQTQLPSLGAGLLQSREDPNQRS 298
Cdd:cd01479 81 LPDGLLVNLKESRQVIEDLLDQIPEMFQDTKETESALGPALQAAFLLLKETGGKIIVFQSSLPTLGAGKLKSREDPKLLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 299 STKVVQHLGPATDFYKKLALDCSGQQTAVDLFLLSSQYSDLASLACMSKYSAGCIYYYPSFHyTHNPSQAEKLQKDLKRY 378
Cdd:cd01479 161 TDKEKQLLQPQTDFYKKLALECVKSQISVDLFLFSNQYVDVATLGCLSRLTGGQVYYYPSFN-FSAPNDVEKLVNELARY 239
|
....*
gi 767930894 379 LTRKI 383
Cdd:cd01479 240 LTRKI 244
|
|
| Sec23_trunk |
pfam04811 |
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
140-379 |
6.36e-112 |
|
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: 338.46 E-value: 6.36e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 140 PQPAVYLFVLDVSHNAVEAGYLTILCQSLLENLDKLPGDSRTRIGFMTFDSTIHFYNLQEGLSQPQMLIVSDIDDVFLPT 219
Cdd:pfam04811 1 PQPPVFLFVIDVSYNAIKSGLLAALKESLLQSLDLLPGDPRARVGFITFDSTVHFFNLGSSLRQPQMLVVSDLQDMFLPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 220 PDSLLVNLYESKELIKDLLNALPNMFTNTRETHSALGPALQAAFKLM--SPTGGRVSVFQTQLPSLGA-GLLQSREDPNQ 296
Cdd:pfam04811 81 PDRFLVPLSECRFVLEDLLEQLPPMFPVTKRPERCLGPALQAAFLLLkaAFTGGKIMVFQGGLPTVGPgGKLKSRLDESH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 297 RSSTKVVQHLGPATD-FYKKLALDCSGQQTAVDLFLLSSQYSDLASLACMSKYSAGCIYYYPSFHYTHnpsQAEKLQKDL 375
Cdd:pfam04811 161 HGTDKEKAKLVKKADkFYKSLAKECVKQGHSVDLFAFSLDYVDVATLGQLSRLTGGQVYLYPSFQADV---DGSKFKQDL 237
|
....
gi 767930894 376 KRYL 379
Cdd:pfam04811 238 QRYF 241
|
|
| PTZ00395 |
PTZ00395 |
Sec24-related protein; Provisional |
105-733 |
2.68e-48 |
|
Sec24-related protein; Provisional
Pssm-ID: 185594 [Multi-domain] Cd Length: 1560 Bit Score: 184.89 E-value: 2.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 105 MYNPLTRSYGEPHKRPEVQNStvefiassdYMLRPPQ-----PAVYLFVLDVSHNAVEAGYLTILCQSL---LENLdKLP 176
Cdd:PTZ00395 919 MKNLICEKNGEPDSAKIRRNS---------FLAKYPQvknmlPPYFVFVVECSYNAIYNNITYTILEGIryaVQNV-KCP 988
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 177 gdsRTRIGFMTFDSTIHFYNLQEGLSQP-------------QMLIVSDIDDVFLPTP-DSLLVNLYESKELIKDLLNALP 242
Cdd:PTZ00395 989 ---QTKIAIITFNSSIYFYHCKGGKGVSgeegdggggsgnhQVIVMSDVDDPFLPLPlEDLFFGCVEEIDKINTLIDTIK 1065
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 243 NMFTNTRETHSALGPALQAAFKLMSPTGG--RVSVFQTQLPSLGAGLLQSREDPNQRSSTKVVQHLgpatdFYKKLALDC 320
Cdd:PTZ00395 1066 SVSTTMQSYGSCGNSALKIAMDMLKERNGlgSICMFYTTTPNCGIGAIKELKKDLQENFLEVKQKI-----FYDSLLLDL 1140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 321 SGQQTAVDLFLLSSQYSDLA--SLACMSKYSAGCIYYYPSFHYthnpsqaeklQKDLKR-YL-------TRKIGFEAVMR 390
Cdd:PTZ00395 1141 YAFNISVDIFIISSNNVRVCvpSLQYVAQNTGGKILFVENFLW----------QKDYKEiYMnimdtltSEDIAYCCELK 1210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 391 IRCTKGLSMHTF---HGNF-FVRSTDLLSLANINPDAGFAVQLSIEESLTDTSLVCFQTALLYTSSKGERRIRVHTLCLP 466
Cdd:PTZ00395 1211 LRYSHHMSVKKLfccNNNFnSIISVDTIKIPKIRHDQTFAFLLNYSDISESKKQIYFQCACIYTNLWGDRFVRLHTTHMN 1290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 467 VVSSLADVYAGVDVQAaiclLANMAVDRSVSSSLSDarDALVNAVVDSLSA----YGSTVSNLQHSA-LMAPSSLKLFPL 541
Cdd:PTZ00395 1291 LTSSLSTVFRYTDAEA----LMNILIKQLCTNILHN--DNYSKIIIDNLAAilfsYRINCASSAHSGqLILPDTLKLLPL 1364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 542 YVLALLKQKAfrTGTSTRLDDRVYAMCQIKSQPLVHLMKMIHPNLY--RIDRLTDE-GAVHVNDRIVpQPPLQKLSAEKL 618
Cdd:PTZ00395 1365 FTSSLLKHNV--TKKEILHDLKVYSLIKLLSMPIISSLLYVYPVMYviHIKGKTNEiDSMDVDDDLF-IPKTIPSSAEKI 1441
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 619 TREGAFLMDCGSVFYIWVGKGCDNNFIEDVLGytnfaSIP-QKMTHLPEL-DTLSSERARSFItwlrdsRPLSPILH--- 693
Cdd:PTZ00395 1442 YSNGIYLLDACTHFYLYFGFHSDANFAKEIVG-----DIPtEKNAHELNLtDTPNAQKVQRII------KNLSRIHHfnk 1510
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 767930894 694 -----IVKDESPAKAEFFQHLIEDRTEAAFSYYEFLLHVQQQICK 733
Cdd:PTZ00395 1511 yvplvMVAPKSNEEEHLISLCVEDKADKEYSYVNFLCFIHKLVHK 1555
|
|
| GEL |
smart00262 |
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ... |
598-640 |
5.53e-03 |
|
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains.
Pssm-ID: 214590 [Multi-domain] Cd Length: 90 Bit Score: 36.50 E-value: 5.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 767930894 598 VHVNDRIVPQPPLQKLSAEKLTREGAFLMDCGSVFYIWVGKGC 640
Cdd:smart00262 3 VRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKS 45
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5028 |
COG5028 |
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ... |
19-724 |
0e+00 |
|
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking and secretion];
Pssm-ID: 227361 [Multi-domain] Cd Length: 861 Bit Score: 574.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 19 NCSPDSFRCTLTNIPQTQALLNKAKLPLGLLLHPFRDLT----QLPVITSNTIVRCRSCRTYINPFVSFIDQ-RRWKCNL 93
Cdd:COG5028 147 NCSPKYVRSTMYAIPETNDLLKKSKIPFGLVIRPFLELYpeedPVPLVEDGSIVRCRRCRSYINPFVQFIEQgRKWRCNI 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 94 CYRVNDVPEEFmYNPLTRS--YGEPHKRPEVQNSTVEFIASSDYMLRPPQPAVYLFVLDVSHNAVEAGYLTILCQSLLEN 171
Cdd:COG5028 227 CRSKNDVPEGF-DNPSGPNdpRSDRYSRPELKSGVVDFLAPKEYSLRQPPPPVYVFLIDVSFEAIKNGLVKAAIRAILEN 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 172 LDKLPG-DSRTRIGFMTFDSTIHFYNLQEGLSQpQMLIVSDIDDVFLPTP-DSLLVNLYESKELIKDLLNALPNMFTNTR 249
Cdd:COG5028 306 LDQIPNfDPRTKIAIICFDSSLHFFKLSPDLDE-QMLIVSDLDEPFLPFPsGLFVLPLKSCKQIIETLLDRVPRIFQDNK 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 250 ETHSALGPALQAAFKLMSPTGGRVSVFQTQLPSLGAGLLQSREDPNQRsstkvvqHLGPATDFYKKLALDCSGQQTAVDL 329
Cdd:COG5028 385 SPKNALGPALKAAKSLIGGTGGKIIVFLSTLPNMGIGKLQLREDKESS-------LLSCKDSFYKEFAIECSKVGISVDL 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 330 FLLSSQYSDLASLACMSKYSAGCIYYYPSFHYThNPSQAEKLQKDLKRYLTRKIGFEAVMRIRCTKGLSMHTFHGNFFVR 409
Cdd:COG5028 458 FLTSEDYIDVATLSHLCRYTGGQTYFYPNFSAT-RPNDATKLANDLVSHLSMEIGYEAVMRVRCSTGLRVSSFYGNFFNR 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 410 STDLLSLANINPDAGFAVQLSIEESLTdTSLVCFQTALLYTSSKGERRIRVHTLCLPVVSSLADVYAGVDVQAAICLLAN 489
Cdd:COG5028 537 SSDLCAFSTMPRDTSLLVEFSIDEKLM-TSDVYFQVALLYTLNDGERRIRVVNLSLPTSSSIREVYASADQLAIACILAK 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 490 MAVDRSVSSSLSDARDALVNAVVDSLSAY-GSTVSNLQHSALMAPSSLKLFPLYVLALLKQKAFRTGtSTRLDDRVYAMC 568
Cdd:COG5028 616 KASTKALNSSLKEARVLINKSMVDILKAYkKELVKSNTSTQLPLPANLKLLPLLMLALLKSSAFRSG-STPSDIRISALN 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 569 QIKSQPLVHLMKMIHPNLYRIDRLTDEGAVHVNDRIVPQPPLqKLSAEKLTREGAFLMDCGSVFYIWVGKGCDNNFIEDV 648
Cdd:COG5028 695 RLTSLPLKQLMRNIYPTLYALHDMPIEAGLPDEGLLVLPSPI-NATSSLLESGGLYLIDTGQKIFLWFGKDAVPSLLQDL 773
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767930894 649 LGYTNFASIPQKMTHLPELDTLSSERARSFITWLRDSRP-LSPILHIVKD--ESPAKAEFFQHLIEDRTEAAFSYYEFL 724
Cdd:COG5028 774 FGVDSLSDIPSGKFTLPPTGNEFNERVRNIIGELRSVNDdSTLPLVLVRGggDPSLRLWFFSTLVEDKTLNIPSYLDYL 852
|
|
| Sec24-like |
cd01479 |
Sec24-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
140-383 |
5.88e-137 |
|
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: 403.19 E-value: 5.88e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 140 PQPAVYLFVLDVSHNAVEAGYLTILCQSLLENLDKLPGD-SRTRIGFMTFDSTIHFYNLQEGLSQPQMLIVSDIDDVFLP 218
Cdd:cd01479 1 PQPAVYVFLIDVSYNAIKSGLLATACEALLSNLDNLPGDdPRTRVGFITFDSTLHFFNLKSSLEQPQMMVVSDLDDPFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 219 TPDSLLVNLYESKELIKDLLNALPNMFTNTRETHSALGPALQAAFKLMSPTGGRVSVFQTQLPSLGAGLLQSREDPNQRS 298
Cdd:cd01479 81 LPDGLLVNLKESRQVIEDLLDQIPEMFQDTKETESALGPALQAAFLLLKETGGKIIVFQSSLPTLGAGKLKSREDPKLLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 299 STKVVQHLGPATDFYKKLALDCSGQQTAVDLFLLSSQYSDLASLACMSKYSAGCIYYYPSFHyTHNPSQAEKLQKDLKRY 378
Cdd:cd01479 161 TDKEKQLLQPQTDFYKKLALECVKSQISVDLFLFSNQYVDVATLGCLSRLTGGQVYYYPSFN-FSAPNDVEKLVNELARY 239
|
....*
gi 767930894 379 LTRKI 383
Cdd:cd01479 240 LTRKI 244
|
|
| Sec23_trunk |
pfam04811 |
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
140-379 |
6.36e-112 |
|
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: 338.46 E-value: 6.36e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 140 PQPAVYLFVLDVSHNAVEAGYLTILCQSLLENLDKLPGDSRTRIGFMTFDSTIHFYNLQEGLSQPQMLIVSDIDDVFLPT 219
Cdd:pfam04811 1 PQPPVFLFVIDVSYNAIKSGLLAALKESLLQSLDLLPGDPRARVGFITFDSTVHFFNLGSSLRQPQMLVVSDLQDMFLPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 220 PDSLLVNLYESKELIKDLLNALPNMFTNTRETHSALGPALQAAFKLM--SPTGGRVSVFQTQLPSLGA-GLLQSREDPNQ 296
Cdd:pfam04811 81 PDRFLVPLSECRFVLEDLLEQLPPMFPVTKRPERCLGPALQAAFLLLkaAFTGGKIMVFQGGLPTVGPgGKLKSRLDESH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 297 RSSTKVVQHLGPATD-FYKKLALDCSGQQTAVDLFLLSSQYSDLASLACMSKYSAGCIYYYPSFHYTHnpsQAEKLQKDL 375
Cdd:pfam04811 161 HGTDKEKAKLVKKADkFYKSLAKECVKQGHSVDLFAFSLDYVDVATLGQLSRLTGGQVYLYPSFQADV---DGSKFKQDL 237
|
....
gi 767930894 376 KRYL 379
Cdd:pfam04811 238 QRYF 241
|
|
| trunk_domain |
cd01468 |
trunk domain. COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi ... |
140-377 |
1.05e-109 |
|
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: 332.67 E-value: 1.05e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 140 PQPAVYLFVLDVSHNAVEAGYLTILCQSLLENLDKLPGDSRTRIGFMTFDSTIHFYNLQEGLSQPQMLIVSDIDDVFLPT 219
Cdd:cd01468 1 PQPPVFVFVIDVSYEAIKEGLLQALKESLLASLDLLPGDPRARVGLITYDSTVHFYNLSSDLAQPKMYVVSDLKDVFLPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 220 PDSLLVNLYESKELIKDLLNALPNMFTN--TRETHSALGPALQAAFKLMSPT--GGRVSVFQTQLPSLGAGLLQSREDPN 295
Cdd:cd01468 81 PDRFLVPLSECKKVIHDLLEQLPPMFWPvpTHRPERCLGPALQAAFLLLKGTfaGGRIIVFQGGLPTVGPGKLKSREDKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 296 QRSSTKVVQHLGPATDFYKKLALDCSGQQTAVDLFLLSSQYSDLASLACMSKYSAGCIYYYPSFHYthnPSQAEKLQKDL 375
Cdd:cd01468 161 PIRSHDEAQLLKPATKFYKSLAKECVKSGICVDLFAFSLDYVDVATLKQLAKSTGGQVYLYDSFQA---PNDGSKFKQDL 237
|
..
gi 767930894 376 KR 377
Cdd:cd01468 238 QR 239
|
|
| PTZ00395 |
PTZ00395 |
Sec24-related protein; Provisional |
105-733 |
2.68e-48 |
|
Sec24-related protein; Provisional
Pssm-ID: 185594 [Multi-domain] Cd Length: 1560 Bit Score: 184.89 E-value: 2.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 105 MYNPLTRSYGEPHKRPEVQNStvefiassdYMLRPPQ-----PAVYLFVLDVSHNAVEAGYLTILCQSL---LENLdKLP 176
Cdd:PTZ00395 919 MKNLICEKNGEPDSAKIRRNS---------FLAKYPQvknmlPPYFVFVVECSYNAIYNNITYTILEGIryaVQNV-KCP 988
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 177 gdsRTRIGFMTFDSTIHFYNLQEGLSQP-------------QMLIVSDIDDVFLPTP-DSLLVNLYESKELIKDLLNALP 242
Cdd:PTZ00395 989 ---QTKIAIITFNSSIYFYHCKGGKGVSgeegdggggsgnhQVIVMSDVDDPFLPLPlEDLFFGCVEEIDKINTLIDTIK 1065
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 243 NMFTNTRETHSALGPALQAAFKLMSPTGG--RVSVFQTQLPSLGAGLLQSREDPNQRSSTKVVQHLgpatdFYKKLALDC 320
Cdd:PTZ00395 1066 SVSTTMQSYGSCGNSALKIAMDMLKERNGlgSICMFYTTTPNCGIGAIKELKKDLQENFLEVKQKI-----FYDSLLLDL 1140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 321 SGQQTAVDLFLLSSQYSDLA--SLACMSKYSAGCIYYYPSFHYthnpsqaeklQKDLKR-YL-------TRKIGFEAVMR 390
Cdd:PTZ00395 1141 YAFNISVDIFIISSNNVRVCvpSLQYVAQNTGGKILFVENFLW----------QKDYKEiYMnimdtltSEDIAYCCELK 1210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 391 IRCTKGLSMHTF---HGNF-FVRSTDLLSLANINPDAGFAVQLSIEESLTDTSLVCFQTALLYTSSKGERRIRVHTLCLP 466
Cdd:PTZ00395 1211 LRYSHHMSVKKLfccNNNFnSIISVDTIKIPKIRHDQTFAFLLNYSDISESKKQIYFQCACIYTNLWGDRFVRLHTTHMN 1290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 467 VVSSLADVYAGVDVQAaiclLANMAVDRSVSSSLSDarDALVNAVVDSLSA----YGSTVSNLQHSA-LMAPSSLKLFPL 541
Cdd:PTZ00395 1291 LTSSLSTVFRYTDAEA----LMNILIKQLCTNILHN--DNYSKIIIDNLAAilfsYRINCASSAHSGqLILPDTLKLLPL 1364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 542 YVLALLKQKAfrTGTSTRLDDRVYAMCQIKSQPLVHLMKMIHPNLY--RIDRLTDE-GAVHVNDRIVpQPPLQKLSAEKL 618
Cdd:PTZ00395 1365 FTSSLLKHNV--TKKEILHDLKVYSLIKLLSMPIISSLLYVYPVMYviHIKGKTNEiDSMDVDDDLF-IPKTIPSSAEKI 1441
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 619 TREGAFLMDCGSVFYIWVGKGCDNNFIEDVLGytnfaSIP-QKMTHLPEL-DTLSSERARSFItwlrdsRPLSPILH--- 693
Cdd:PTZ00395 1442 YSNGIYLLDACTHFYLYFGFHSDANFAKEIVG-----DIPtEKNAHELNLtDTPNAQKVQRII------KNLSRIHHfnk 1510
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 767930894 694 -----IVKDESPAKAEFFQHLIEDRTEAAFSYYEFLLHVQQQICK 733
Cdd:PTZ00395 1511 yvplvMVAPKSNEEEHLISLCVEDKADKEYSYVNFLCFIHKLVHK 1555
|
|
| Sec23_helical |
pfam04815 |
Sec23/Sec24 helical domain; COPII-coated vesicles carry proteins from the endoplasmic ... |
479-580 |
2.58e-33 |
|
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: 123.38 E-value: 2.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 479 DVQAAICLLANMAVDRSVSSSLSDARDALVNAVVDSLSAYGSTV-SNLQHSALMAPSSLKLFPLYVLALLKQKAFRTGTS 557
Cdd:pfam04815 1 DQEAIAVLLAKKAVEKALSSSLSDAREALDNKLVDILAAYRKYCaSSSSPGQLILPESLKLLPLYMLALLKSPALRGGNS 80
|
90 100
....*....|....*....|...
gi 767930894 558 TRLDDRVYAMCQIKSQPLVHLMK 580
Cdd:pfam04815 81 SPSDERAYARHLLLSLPVEELLL 103
|
|
| Sec23_BS |
pfam08033 |
Sec23/Sec24 beta-sandwich domain; |
384-468 |
1.49e-32 |
|
Sec23/Sec24 beta-sandwich domain;
Pssm-ID: 429794 [Multi-domain] Cd Length: 86 Bit Score: 120.72 E-value: 1.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 384 GFEAVMRIRCTKGLSMHTFHGNFFVRS-TDLLSLANINPDAGFAVQLSIEESLTDTSLVCFQTALLYTSSKGERRIRVHT 462
Cdd:pfam08033 1 GFNAVLRVRTSKGLKVSGFIGNFVSRSsGDTWKLPSLDPDTSYAFEFDIDEPLPNGSNAYIQFALLYTHSSGERRIRVTT 80
|
....*.
gi 767930894 463 LCLPVV 468
Cdd:pfam08033 81 VALPVT 86
|
|
| SEC23 |
COG5047 |
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]; |
23-639 |
4.52e-23 |
|
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
Pssm-ID: 227380 [Multi-domain] Cd Length: 755 Bit Score: 104.96 E-value: 4.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 23 DSFRCTLTNIPQTQALLNKAKLPLGLLLHPFRDLTQLPVITSNTIVRCRSCRTYINPFVSfIDQRR--WKCNLCYRVNDV 100
Cdd:COG5047 10 DGIRLTWNVFPATRGDATRTVIPIACLYTPLHEDDALTVNYYEPVKCTAPCKAVLNPYCH-IDERNqsWICPFCNQRNTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 101 PEEfmYNPLTRSYGEPhkRPEVQNSTVEFIASsdymlRPPQ-PAVYLFVLDVshnAVEAGYLTILCQSLLENLDKLPGDS 179
Cdd:COG5047 89 PPQ--YRDISNANLPL--ELLPQSSTIEYTLS-----KPVIlPPVFFFVVDA---CCDEEELTALKDSLIVSLSLLPPEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 180 rtRIGFMTFDSTIHF----------------------YNLQE--GLSQPQMLIV--SDIDDVFLPTPDSLLVNLYESKEL 233
Cdd:COG5047 157 --LVGLITYGTSIQVhelnaenhrrsyvfsgnkeytkENLQEllALSKPTKSGGfeSKISGIGQFASSRFLLPTQQCEFK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 234 IKDLLNAL-------PNMFTNTRETHSALGPA---LQAAFKLMsptGGRVSVFQTQLPSLGAGLLQSRE--DP---NQRS 298
Cdd:COG5047 235 LLNILEQLqpdpwpvPAGKRPLRCTGSALNIAsslLEQCFPNA---GCHIVLFAGGPCTVGPGTVVSTElkEPmrsHHDI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 299 STKVVQHLGPATDFYKKLALDCSGQQTAVDLFLLSSQYSDLASLACMSKYSAGCIYYYPSFhythnpsQAEKLQKDLKRY 378
Cdd:COG5047 312 ESDSAQHSKKATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSF-------TTSIFKQSFQRI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 379 LTR------KIGFEAVMRIRCTKGLSMHTFHGN---------------FFVRSTDLLSLANINPDAGFAVQLSIEESLTD 437
Cdd:COG5047 385 FNRdsegylKMGFNANMEVKTSKNLKIKGLIGHavsvkkkannisdseIGIGATNSWKMASLSPKSNYALYFEIALGAAS 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 438 TS-------LVCFQTalLYTSSKGERRIRVHTLCLPVVSSLADV-YAGVDVQAAICLLANMAVDRSVSSSLSDArDALVN 509
Cdd:COG5047 465 GSaqrpaeaYIQFIT--TYQHSSGTYRIRVTTVARMFTDGGLPKiNRSFDQEAAAVFMARIAAFKAETEDIIDV-FRWID 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 510 AVVDSLSAYGSTVSNLQHSALMAPSSLKLFPLYVLALLKQKAFRTGtSTRLDDRVYAMCQIKSQPLVHLMKMIHPNLYRI 589
Cdd:COG5047 542 RNLIRLCQKFADYRKDDPSSFRLDPNFTLYPQFMYHLRRSPFLSVF-NNSPDETAFYRHMLNNADVNDSLIMIQPTLQSY 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 767930894 590 DRLTDEGAVHVnDRIVPQPPLQKLSAEKLTregaFLMDCGSVFYIWVGKG 639
Cdd:COG5047 621 SFEKGGVPVLL-DSVSVKPDVILLLDTFFH----ILIFHGSYIAQWRNAG 665
|
|
| zf-Sec23_Sec24 |
pfam04810 |
Sec23/Sec24 zinc finger; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
67-103 |
7.01e-16 |
|
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: 71.71 E-value: 7.01e-16
10 20 30
....*....|....*....|....*....|....*...
gi 767930894 67 IVRCRSCRTYINPFVSFIDQ-RRWKCNLCYRVNDVPEE 103
Cdd:pfam04810 1 PVRCRRCRAYLNPFCQFDFGgKKWTCNFCGTRNPVPPE 38
|
|
| PLN00162 |
PLN00162 |
transport protein sec23; Provisional |
23-507 |
1.35e-14 |
|
transport protein sec23; Provisional
Pssm-ID: 215083 [Multi-domain] Cd Length: 761 Bit Score: 77.67 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 23 DSFRCTLTNIPQTQALLNKAKLPLGLLLHPFRDLTQLPVITSNTIvRCRSCRTYINPF--VSFiDQRRWKCNLCYRVNDV 100
Cdd:PLN00162 10 DGVRMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPL-RCRTCRAVLNPYcrVDF-QAKIWICPFCFQRNHF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 101 PeefmynpltRSY---GEPHKRPEV--QNSTVEFiASSDYMLRPPQPAVYLFVLDVSHNAVEAGYLTilcQSLLENLDKL 175
Cdd:PLN00162 88 P---------PHYssiSETNLPAELfpQYTTVEY-TLPPGSGGAPSPPVFVFVVDTCMIEEELGALK---SALLQAIALL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 176 PGDSrtRIGFMTFDSTIHFYNL------------------------QEGLS----QPQMLIVSDIDDVFLPTP-DSLLVN 226
Cdd:PLN00162 155 PENA--LVGLITFGTHVHVHELgfsecsksyvfrgnkevskdqileQLGLGgkkrRPAGGGIAGARDGLSSSGvNRFLLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 227 LYESKELIKDLLNALPNMFTNTRETHSAL---GPALQAAFKLM---SP-TGGRVSVFqTQLPS-LGAGLLQSREDPNQRS 298
Cdd:PLN00162 233 ASECEFTLNSALEELQKDPWPVPPGHRPArctGAALSVAAGLLgacVPgTGARIMAF-VGGPCtEGPGAIVSKDLSEPIR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 299 STK-----VVQHLGPATDFYKKLALDCSGQQTAVDLFLLSSQYSDLASLACMSKYSAGCIYYYPSFHythnpsqAEKLQK 373
Cdd:PLN00162 312 SHKdldkdAAPYYKKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVAEMKVAVERTGGLVVLAESFG-------HSVFKD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 374 DLKRYLTR------KIGFEAVMRIRCTKGL----------SMH----------TFHGNffvrsTDLLSLANINPDAGFAV 427
Cdd:PLN00162 385 SLRRVFERdgegslGLSFNGTFEVNCSKDVkvqgaigpcaSLEkkgpsvsdteIGEGG-----TTAWKLCGLDKKTSLAV 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767930894 428 --QLSIEESLTDTSL---VCFQTALLYTSSKGERRIRVHTLCLPVV--SSLADVYAGVDVQAAICLLANMAVDRSVSssl 500
Cdd:PLN00162 460 ffEVANSGQSNPQPPgqqFFLQFLTRYQHSNGQTRLRVTTVTRRWVegSSSEELVAGFDQEAAAVVMARLASHKMET--- 536
|
....*..
gi 767930894 501 SDARDAL 507
Cdd:PLN00162 537 EEEFDAT 543
|
|
| Gelsolin |
pfam00626 |
Gelsolin repeat; |
605-679 |
3.14e-11 |
|
Gelsolin repeat;
Pssm-ID: 395501 [Multi-domain] Cd Length: 76 Bit Score: 59.63 E-value: 3.14e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767930894 605 VPQPPLQKLSAEKLTREGAFLMDCGSVFYIWVGKGcdNNFIEDVLGYTNFASIP-QKMTHLPELDTLS-SERARSFI 679
Cdd:pfam00626 2 FVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKG--SSLLEKLFAALLAAQLDdDERFPLPEVIRVPqGKEPARFL 76
|
|
| GEL |
smart00262 |
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ... |
598-640 |
5.53e-03 |
|
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains.
Pssm-ID: 214590 [Multi-domain] Cd Length: 90 Bit Score: 36.50 E-value: 5.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 767930894 598 VHVNDRIVPQPPLQKLSAEKLTREGAFLMDCGSVFYIWVGKGC 640
Cdd:smart00262 3 VRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKS 45
|
|
|