|
Name |
Accession |
Description |
Interval |
E-value |
| COG5028 |
COG5028 |
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ... |
491-1196 |
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: 565.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 491 NCSPDSFRCTLTNIPQTQALLNKAKLPLGLLLHPFRDLT----QLPVITSNTIVRCRSCRTYINPFVSFIDQ-RRWKCNL 565
Cdd:COG5028 147 NCSPKYVRSTMYAIPETNDLLKKSKIPFGLVIRPFLELYpeedPVPLVEDGSIVRCRRCRSYINPFVQFIEQgRKWRCNI 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 566 CYRVNDVPEEFmYNPLTRS--YGEPHKRPEVQNSTVEFIASSDYMLRPPQPAVYLFVLDVSHNAVEAGYLTILCQSLLEN 643
Cdd:COG5028 227 CRSKNDVPEGF-DNPSGPNdpRSDRYSRPELKSGVVDFLAPKEYSLRQPPPPVYVFLIDVSFEAIKNGLVKAAIRAILEN 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 644 LDKLPG-DSRTRIGFMTFDSTIHFYNLQEGLSQpQMLIVSDIDDVFLPTP-DSLLVNLYESKELIKDLLNALPNMFTNTR 721
Cdd:COG5028 306 LDQIPNfDPRTKIAIICFDSSLHFFKLSPDLDE-QMLIVSDLDEPFLPFPsGLFVLPLKSCKQIIETLLDRVPRIFQDNK 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 722 ETHSALGPALQAAFKLMSPTGGRVSVFQTQLPSLGAGLLQSREDPNQRsstkvvqHLGPATDFYKKLALDCSGQQTAVDL 801
Cdd:COG5028 385 SPKNALGPALKAAKSLIGGTGGKIIVFLSTLPNMGIGKLQLREDKESS-------LLSCKDSFYKEFAIECSKVGISVDL 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 802 FLLSSQYSDLASLACMSKYSAGCIYYYPSFHYThNPSQAEKLQKDLKRYLTRKIGFEAVMRIRCTKGLSMHTFHGNFFVR 881
Cdd:COG5028 458 FLTSEDYIDVATLSHLCRYTGGQTYFYPNFSAT-RPNDATKLANDLVSHLSMEIGYEAVMRVRCSTGLRVSSFYGNFFNR 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 882 STDLLSLANINPDAGFAVQLSIEESLTdTSLVCFQTALLYTSSKGERRIRVHTLCLPVVSSLADVYAGVDVQAAICLLAN 961
Cdd:COG5028 537 SSDLCAFSTMPRDTSLLVEFSIDEKLM-TSDVYFQVALLYTLNDGERRIRVVNLSLPTSSSIREVYASADQLAIACILAK 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 962 MAVDRSVSSSLSDARDALVNAVVDSLSAY-GSTVSNLQHSALMAPSSLKLFPLYVLALLKQKAFRTGtSTRLDDRVYAMC 1040
Cdd:COG5028 616 KASTKALNSSLKEARVLINKSMVDILKAYkKELVKSNTSTQLPLPANLKLLPLLMLALLKSSAFRSG-STPSDIRISALN 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 1041 QIKSQPLVHLMKMIHPNLYRIDRLTDEGAVHVNDRIVPQPPLqKLSAEKLTREGAFLMDCGSVFYIWVGKGCDNNFIEDV 1120
Cdd:COG5028 695 RLTSLPLKQLMRNIYPTLYALHDMPIEAGLPDEGLLVLPSPI-NATSSLLESGGLYLIDTGQKIFLWFGKDAVPSLLQDL 773
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217348607 1121 LGYTNFASIPQKMTHLPELDTLSSERARSFITWLRDSRP-LSPILHIVKD--ESPAKAEFFQHLIEDRTEAAFSYYEFL 1196
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 ... |
612-855 |
5.63e-132 |
|
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: 402.42 E-value: 5.63e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 612 PQPAVYLFVLDVSHNAVEAGYLTILCQSLLENLDKLPGD-SRTRIGFMTFDSTIHFYNLQEGLSQPQMLIVSDIDDVFLP 690
Cdd:cd01479 1 PQPAVYVFLIDVSYNAIKSGLLATACEALLSNLDNLPGDdPRTRVGFITFDSTLHFFNLKSSLEQPQMMVVSDLDDPFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 691 TPDSLLVNLYESKELIKDLLNALPNMFTNTRETHSALGPALQAAFKLMSPTGGRVSVFQTQLPSLGAGLLQSREDPNQRS 770
Cdd:cd01479 81 LPDGLLVNLKESRQVIEDLLDQIPEMFQDTKETESALGPALQAAFLLLKETGGKIIVFQSSLPTLGAGKLKSREDPKLLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 771 STKVVQHLGPATDFYKKLALDCSGQQTAVDLFLLSSQYSDLASLACMSKYSAGCIYYYPSFHyTHNPSQAEKLQKDLKRY 850
Cdd:cd01479 161 TDKEKQLLQPQTDFYKKLALECVKSQISVDLFLFSNQYVDVATLGCLSRLTGGQVYYYPSFN-FSAPNDVEKLVNELARY 239
|
....*
gi 2217348607 851 LTRKI 855
Cdd:cd01479 240 LTRKI 244
|
|
| Sec23_trunk |
pfam04811 |
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
612-851 |
6.93e-108 |
|
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: 6.93e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 612 PQPAVYLFVLDVSHNAVEAGYLTILCQSLLENLDKLPGDSRTRIGFMTFDSTIHFYNLQEGLSQPQMLIVSDIDDVFLPT 691
Cdd:pfam04811 1 PQPPVFLFVIDVSYNAIKSGLLAALKESLLQSLDLLPGDPRARVGFITFDSTVHFFNLGSSLRQPQMLVVSDLQDMFLPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 692 PDSLLVNLYESKELIKDLLNALPNMFTNTRETHSALGPALQAAFKLM--SPTGGRVSVFQTQLPSLGA-GLLQSREDPNQ 768
Cdd:pfam04811 81 PDRFLVPLSECRFVLEDLLEQLPPMFPVTKRPERCLGPALQAAFLLLkaAFTGGKIMVFQGGLPTVGPgGKLKSRLDESH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 769 RSSTKVVQHLGPATD-FYKKLALDCSGQQTAVDLFLLSSQYSDLASLACMSKYSAGCIYYYPSFHYTHnpsQAEKLQKDL 847
Cdd:pfam04811 161 HGTDKEKAKLVKKADkFYKSLAKECVKQGHSVDLFAFSLDYVDVATLGQLSRLTGGQVYLYPSFQADV---DGSKFKQDL 237
|
....
gi 2217348607 848 KRYL 851
Cdd:pfam04811 238 QRYF 241
|
|
| PTZ00395 |
PTZ00395 |
Sec24-related protein; Provisional |
577-1205 |
1.74e-44 |
|
Sec24-related protein; Provisional
Pssm-ID: 185594 [Multi-domain] Cd Length: 1560 Bit Score: 176.80 E-value: 1.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 577 MYNPLTRSYGEPHKRPEVQNStvefiassdYMLRPPQ-----PAVYLFVLDVSHNAVEAGYLTILCQSL---LENLdKLP 648
Cdd:PTZ00395 919 MKNLICEKNGEPDSAKIRRNS---------FLAKYPQvknmlPPYFVFVVECSYNAIYNNITYTILEGIryaVQNV-KCP 988
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 649 gdsRTRIGFMTFDSTIHFYNLQEGLSQP-------------QMLIVSDIDDVFLPTP-DSLLVNLYESKELIKDLLNALP 714
Cdd:PTZ00395 989 ---QTKIAIITFNSSIYFYHCKGGKGVSgeegdggggsgnhQVIVMSDVDDPFLPLPlEDLFFGCVEEIDKINTLIDTIK 1065
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 715 NMFTNTRETHSALGPALQAAFKLMSPTGG--RVSVFQTQLPSLGAGLLQSREDPNQRSSTKVVQHLgpatdFYKKLALDC 792
Cdd:PTZ00395 1066 SVSTTMQSYGSCGNSALKIAMDMLKERNGlgSICMFYTTTPNCGIGAIKELKKDLQENFLEVKQKI-----FYDSLLLDL 1140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 793 SGQQTAVDLFLLSSQYSDLA--SLACMSKYSAGCIYYYPSFHYthnpsqaeklQKDLKR-YL-------TRKIGFEAVMR 862
Cdd:PTZ00395 1141 YAFNISVDIFIISSNNVRVCvpSLQYVAQNTGGKILFVENFLW----------QKDYKEiYMnimdtltSEDIAYCCELK 1210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 863 IRCTKGLSMHTF---HGNF-FVRSTDLLSLANINPDAGFAVQLSIEESLTDTSLVCFQTALLYTSSKGERRIRVHTLCLP 938
Cdd:PTZ00395 1211 LRYSHHMSVKKLfccNNNFnSIISVDTIKIPKIRHDQTFAFLLNYSDISESKKQIYFQCACIYTNLWGDRFVRLHTTHMN 1290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 939 VVSSLADVYAGVDVQAaiclLANMAVDRSVSSSLSDarDALVNAVVDSLSA----YGSTVSNLQHSA-LMAPSSLKLFPL 1013
Cdd:PTZ00395 1291 LTSSLSTVFRYTDAEA----LMNILIKQLCTNILHN--DNYSKIIIDNLAAilfsYRINCASSAHSGqLILPDTLKLLPL 1364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 1014 YVLALLKQKAfrTGTSTRLDDRVYAMCQIKSQPLVHLMKMIHPNLY--RIDRLTDE-GAVHVNDRIVpQPPLQKLSAEKL 1090
Cdd:PTZ00395 1365 FTSSLLKHNV--TKKEILHDLKVYSLIKLLSMPIISSLLYVYPVMYviHIKGKTNEiDSMDVDDDLF-IPKTIPSSAEKI 1441
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 1091 TREGAFLMDCGSVFYIWVGKGCDNNFIEDVLGytnfaSIP-QKMTHLPEL-DTLSSERARSFItwlrdsRPLSPILH--- 1165
Cdd:PTZ00395 1442 YSNGIYLLDACTHFYLYFGFHSDANFAKEIVG-----DIPtEKNAHELNLtDTPNAQKVQRII------KNLSRIHHfnk 1510
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 2217348607 1166 -----IVKDESPAKAEFFQHLIEDRTEAAFSYYEFLLHVQQQICK 1205
Cdd:PTZ00395 1511 yvplvMVAPKSNEEEHLISLCVEDKADKEYSYVNFLCFIHKLVHK 1555
|
|
| GEL |
smart00262 |
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ... |
1070-1112 |
9.29e-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: 9.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2217348607 1070 VHVNDRIVPQPPLQKLSAEKLTREGAFLMDCGSVFYIWVGKGC 1112
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 ... |
491-1196 |
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: 565.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 491 NCSPDSFRCTLTNIPQTQALLNKAKLPLGLLLHPFRDLT----QLPVITSNTIVRCRSCRTYINPFVSFIDQ-RRWKCNL 565
Cdd:COG5028 147 NCSPKYVRSTMYAIPETNDLLKKSKIPFGLVIRPFLELYpeedPVPLVEDGSIVRCRRCRSYINPFVQFIEQgRKWRCNI 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 566 CYRVNDVPEEFmYNPLTRS--YGEPHKRPEVQNSTVEFIASSDYMLRPPQPAVYLFVLDVSHNAVEAGYLTILCQSLLEN 643
Cdd:COG5028 227 CRSKNDVPEGF-DNPSGPNdpRSDRYSRPELKSGVVDFLAPKEYSLRQPPPPVYVFLIDVSFEAIKNGLVKAAIRAILEN 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 644 LDKLPG-DSRTRIGFMTFDSTIHFYNLQEGLSQpQMLIVSDIDDVFLPTP-DSLLVNLYESKELIKDLLNALPNMFTNTR 721
Cdd:COG5028 306 LDQIPNfDPRTKIAIICFDSSLHFFKLSPDLDE-QMLIVSDLDEPFLPFPsGLFVLPLKSCKQIIETLLDRVPRIFQDNK 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 722 ETHSALGPALQAAFKLMSPTGGRVSVFQTQLPSLGAGLLQSREDPNQRsstkvvqHLGPATDFYKKLALDCSGQQTAVDL 801
Cdd:COG5028 385 SPKNALGPALKAAKSLIGGTGGKIIVFLSTLPNMGIGKLQLREDKESS-------LLSCKDSFYKEFAIECSKVGISVDL 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 802 FLLSSQYSDLASLACMSKYSAGCIYYYPSFHYThNPSQAEKLQKDLKRYLTRKIGFEAVMRIRCTKGLSMHTFHGNFFVR 881
Cdd:COG5028 458 FLTSEDYIDVATLSHLCRYTGGQTYFYPNFSAT-RPNDATKLANDLVSHLSMEIGYEAVMRVRCSTGLRVSSFYGNFFNR 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 882 STDLLSLANINPDAGFAVQLSIEESLTdTSLVCFQTALLYTSSKGERRIRVHTLCLPVVSSLADVYAGVDVQAAICLLAN 961
Cdd:COG5028 537 SSDLCAFSTMPRDTSLLVEFSIDEKLM-TSDVYFQVALLYTLNDGERRIRVVNLSLPTSSSIREVYASADQLAIACILAK 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 962 MAVDRSVSSSLSDARDALVNAVVDSLSAY-GSTVSNLQHSALMAPSSLKLFPLYVLALLKQKAFRTGtSTRLDDRVYAMC 1040
Cdd:COG5028 616 KASTKALNSSLKEARVLINKSMVDILKAYkKELVKSNTSTQLPLPANLKLLPLLMLALLKSSAFRSG-STPSDIRISALN 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 1041 QIKSQPLVHLMKMIHPNLYRIDRLTDEGAVHVNDRIVPQPPLqKLSAEKLTREGAFLMDCGSVFYIWVGKGCDNNFIEDV 1120
Cdd:COG5028 695 RLTSLPLKQLMRNIYPTLYALHDMPIEAGLPDEGLLVLPSPI-NATSSLLESGGLYLIDTGQKIFLWFGKDAVPSLLQDL 773
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217348607 1121 LGYTNFASIPQKMTHLPELDTLSSERARSFITWLRDSRP-LSPILHIVKD--ESPAKAEFFQHLIEDRTEAAFSYYEFL 1196
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 ... |
612-855 |
5.63e-132 |
|
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: 402.42 E-value: 5.63e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 612 PQPAVYLFVLDVSHNAVEAGYLTILCQSLLENLDKLPGD-SRTRIGFMTFDSTIHFYNLQEGLSQPQMLIVSDIDDVFLP 690
Cdd:cd01479 1 PQPAVYVFLIDVSYNAIKSGLLATACEALLSNLDNLPGDdPRTRVGFITFDSTLHFFNLKSSLEQPQMMVVSDLDDPFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 691 TPDSLLVNLYESKELIKDLLNALPNMFTNTRETHSALGPALQAAFKLMSPTGGRVSVFQTQLPSLGAGLLQSREDPNQRS 770
Cdd:cd01479 81 LPDGLLVNLKESRQVIEDLLDQIPEMFQDTKETESALGPALQAAFLLLKETGGKIIVFQSSLPTLGAGKLKSREDPKLLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 771 STKVVQHLGPATDFYKKLALDCSGQQTAVDLFLLSSQYSDLASLACMSKYSAGCIYYYPSFHyTHNPSQAEKLQKDLKRY 850
Cdd:cd01479 161 TDKEKQLLQPQTDFYKKLALECVKSQISVDLFLFSNQYVDVATLGCLSRLTGGQVYYYPSFN-FSAPNDVEKLVNELARY 239
|
....*
gi 2217348607 851 LTRKI 855
Cdd:cd01479 240 LTRKI 244
|
|
| Sec23_trunk |
pfam04811 |
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
612-851 |
6.93e-108 |
|
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: 6.93e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 612 PQPAVYLFVLDVSHNAVEAGYLTILCQSLLENLDKLPGDSRTRIGFMTFDSTIHFYNLQEGLSQPQMLIVSDIDDVFLPT 691
Cdd:pfam04811 1 PQPPVFLFVIDVSYNAIKSGLLAALKESLLQSLDLLPGDPRARVGFITFDSTVHFFNLGSSLRQPQMLVVSDLQDMFLPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 692 PDSLLVNLYESKELIKDLLNALPNMFTNTRETHSALGPALQAAFKLM--SPTGGRVSVFQTQLPSLGA-GLLQSREDPNQ 768
Cdd:pfam04811 81 PDRFLVPLSECRFVLEDLLEQLPPMFPVTKRPERCLGPALQAAFLLLkaAFTGGKIMVFQGGLPTVGPgGKLKSRLDESH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 769 RSSTKVVQHLGPATD-FYKKLALDCSGQQTAVDLFLLSSQYSDLASLACMSKYSAGCIYYYPSFHYTHnpsQAEKLQKDL 847
Cdd:pfam04811 161 HGTDKEKAKLVKKADkFYKSLAKECVKQGHSVDLFAFSLDYVDVATLGQLSRLTGGQVYLYPSFQADV---DGSKFKQDL 237
|
....
gi 2217348607 848 KRYL 851
Cdd:pfam04811 238 QRYF 241
|
|
| trunk_domain |
cd01468 |
trunk domain. COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi ... |
612-849 |
2.85e-105 |
|
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: 331.13 E-value: 2.85e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 612 PQPAVYLFVLDVSHNAVEAGYLTILCQSLLENLDKLPGDSRTRIGFMTFDSTIHFYNLQEGLSQPQMLIVSDIDDVFLPT 691
Cdd:cd01468 1 PQPPVFVFVIDVSYEAIKEGLLQALKESLLASLDLLPGDPRARVGLITYDSTVHFYNLSSDLAQPKMYVVSDLKDVFLPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 692 PDSLLVNLYESKELIKDLLNALPNMFTN--TRETHSALGPALQAAFKLMSPT--GGRVSVFQTQLPSLGAGLLQSREDPN 767
Cdd:cd01468 81 PDRFLVPLSECKKVIHDLLEQLPPMFWPvpTHRPERCLGPALQAAFLLLKGTfaGGRIIVFQGGLPTVGPGKLKSREDKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 768 QRSSTKVVQHLGPATDFYKKLALDCSGQQTAVDLFLLSSQYSDLASLACMSKYSAGCIYYYPSFHYthnPSQAEKLQKDL 847
Cdd:cd01468 161 PIRSHDEAQLLKPATKFYKSLAKECVKSGICVDLFAFSLDYVDVATLKQLAKSTGGQVYLYDSFQA---PNDGSKFKQDL 237
|
..
gi 2217348607 848 KR 849
Cdd:cd01468 238 QR 239
|
|
| PTZ00395 |
PTZ00395 |
Sec24-related protein; Provisional |
577-1205 |
1.74e-44 |
|
Sec24-related protein; Provisional
Pssm-ID: 185594 [Multi-domain] Cd Length: 1560 Bit Score: 176.80 E-value: 1.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 577 MYNPLTRSYGEPHKRPEVQNStvefiassdYMLRPPQ-----PAVYLFVLDVSHNAVEAGYLTILCQSL---LENLdKLP 648
Cdd:PTZ00395 919 MKNLICEKNGEPDSAKIRRNS---------FLAKYPQvknmlPPYFVFVVECSYNAIYNNITYTILEGIryaVQNV-KCP 988
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 649 gdsRTRIGFMTFDSTIHFYNLQEGLSQP-------------QMLIVSDIDDVFLPTP-DSLLVNLYESKELIKDLLNALP 714
Cdd:PTZ00395 989 ---QTKIAIITFNSSIYFYHCKGGKGVSgeegdggggsgnhQVIVMSDVDDPFLPLPlEDLFFGCVEEIDKINTLIDTIK 1065
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 715 NMFTNTRETHSALGPALQAAFKLMSPTGG--RVSVFQTQLPSLGAGLLQSREDPNQRSSTKVVQHLgpatdFYKKLALDC 792
Cdd:PTZ00395 1066 SVSTTMQSYGSCGNSALKIAMDMLKERNGlgSICMFYTTTPNCGIGAIKELKKDLQENFLEVKQKI-----FYDSLLLDL 1140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 793 SGQQTAVDLFLLSSQYSDLA--SLACMSKYSAGCIYYYPSFHYthnpsqaeklQKDLKR-YL-------TRKIGFEAVMR 862
Cdd:PTZ00395 1141 YAFNISVDIFIISSNNVRVCvpSLQYVAQNTGGKILFVENFLW----------QKDYKEiYMnimdtltSEDIAYCCELK 1210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 863 IRCTKGLSMHTF---HGNF-FVRSTDLLSLANINPDAGFAVQLSIEESLTDTSLVCFQTALLYTSSKGERRIRVHTLCLP 938
Cdd:PTZ00395 1211 LRYSHHMSVKKLfccNNNFnSIISVDTIKIPKIRHDQTFAFLLNYSDISESKKQIYFQCACIYTNLWGDRFVRLHTTHMN 1290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 939 VVSSLADVYAGVDVQAaiclLANMAVDRSVSSSLSDarDALVNAVVDSLSA----YGSTVSNLQHSA-LMAPSSLKLFPL 1013
Cdd:PTZ00395 1291 LTSSLSTVFRYTDAEA----LMNILIKQLCTNILHN--DNYSKIIIDNLAAilfsYRINCASSAHSGqLILPDTLKLLPL 1364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 1014 YVLALLKQKAfrTGTSTRLDDRVYAMCQIKSQPLVHLMKMIHPNLY--RIDRLTDE-GAVHVNDRIVpQPPLQKLSAEKL 1090
Cdd:PTZ00395 1365 FTSSLLKHNV--TKKEILHDLKVYSLIKLLSMPIISSLLYVYPVMYviHIKGKTNEiDSMDVDDDLF-IPKTIPSSAEKI 1441
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 1091 TREGAFLMDCGSVFYIWVGKGCDNNFIEDVLGytnfaSIP-QKMTHLPEL-DTLSSERARSFItwlrdsRPLSPILH--- 1165
Cdd:PTZ00395 1442 YSNGIYLLDACTHFYLYFGFHSDANFAKEIVG-----DIPtEKNAHELNLtDTPNAQKVQRII------KNLSRIHHfnk 1510
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 2217348607 1166 -----IVKDESPAKAEFFQHLIEDRTEAAFSYYEFLLHVQQQICK 1205
Cdd:PTZ00395 1511 yvplvMVAPKSNEEEHLISLCVEDKADKEYSYVNFLCFIHKLVHK 1555
|
|
| Sec23_helical |
pfam04815 |
Sec23/Sec24 helical domain; COPII-coated vesicles carry proteins from the endoplasmic ... |
951-1052 |
2.31e-34 |
|
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: 127.23 E-value: 2.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 951 DVQAAICLLANMAVDRSVSSSLSDARDALVNAVVDSLSAYGSTVSNLQHSA-LMAPSSLKLFPLYVLALLKQKAFRTGTS 1029
Cdd:pfam04815 1 DQEAIAVLLAKKAVEKALSSSLSDAREALDNKLVDILAAYRKYCASSSSPGqLILPESLKLLPLYMLALLKSPALRGGNS 80
|
90 100
....*....|....*....|...
gi 2217348607 1030 TRLDDRVYAMCQIKSQPLVHLMK 1052
Cdd:pfam04815 81 SPSDERAYARHLLLSLPVEELLL 103
|
|
| Sec23_BS |
pfam08033 |
Sec23/Sec24 beta-sandwich domain; |
856-940 |
2.79e-32 |
|
Sec23/Sec24 beta-sandwich domain;
Pssm-ID: 429794 [Multi-domain] Cd Length: 86 Bit Score: 120.33 E-value: 2.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 856 GFEAVMRIRCTKGLSMHTFHGNFFVRS-TDLLSLANINPDAGFAVQLSIEESLTDTSLVCFQTALLYTSSKGERRIRVHT 934
Cdd:pfam08033 1 GFNAVLRVRTSKGLKVSGFIGNFVSRSsGDTWKLPSLDPDTSYAFEFDIDEPLPNGSNAYIQFALLYTHSSGERRIRVTT 80
|
....*.
gi 2217348607 935 LCLPVV 940
Cdd:pfam08033 81 VALPVT 86
|
|
| SEC23 |
COG5047 |
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]; |
495-1111 |
3.08e-22 |
|
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
Pssm-ID: 227380 [Multi-domain] Cd Length: 755 Bit Score: 103.42 E-value: 3.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 495 DSFRCTLTNIPQTQALLNKAKLPLGLLLHPFRDLTQLPVITSNTIVRCRSCRTYINPFVSfIDQRR--WKCNLCYRVNDV 572
Cdd:COG5047 10 DGIRLTWNVFPATRGDATRTVIPIACLYTPLHEDDALTVNYYEPVKCTAPCKAVLNPYCH-IDERNqsWICPFCNQRNTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 573 PEEfmYNPLTRSYGEPhkRPEVQNSTVEFIASsdymlRPPQ-PAVYLFVLDVshnAVEAGYLTILCQSLLENLDKLPGDS 651
Cdd:COG5047 89 PPQ--YRDISNANLPL--ELLPQSSTIEYTLS-----KPVIlPPVFFFVVDA---CCDEEELTALKDSLIVSLSLLPPEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 652 rtRIGFMTFDSTIHF----------------------YNLQE--GLSQPQMLIV--SDIDDVFLPTPDSLLVNLYESKEL 705
Cdd:COG5047 157 --LVGLITYGTSIQVhelnaenhrrsyvfsgnkeytkENLQEllALSKPTKSGGfeSKISGIGQFASSRFLLPTQQCEFK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 706 IKDLLNAL-------PNMFTNTRETHSALGPA---LQAAFKLMsptGGRVSVFQTQLPSLGAGLLQSRE--DP---NQRS 770
Cdd:COG5047 235 LLNILEQLqpdpwpvPAGKRPLRCTGSALNIAsslLEQCFPNA---GCHIVLFAGGPCTVGPGTVVSTElkEPmrsHHDI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 771 STKVVQHLGPATDFYKKLALDCSGQQTAVDLFLLSSQYSDLASLACMSKYSAGCIYYYPSFhythnpsQAEKLQKDLKRY 850
Cdd:COG5047 312 ESDSAQHSKKATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSF-------TTSIFKQSFQRI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 851 LTR------KIGFEAVMRIRCTKGLSMHTFHGN---------------FFVRSTDLLSLANINPDAGFAVQLSIEESLTD 909
Cdd:COG5047 385 FNRdsegylKMGFNANMEVKTSKNLKIKGLIGHavsvkkkannisdseIGIGATNSWKMASLSPKSNYALYFEIALGAAS 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 910 TS-------LVCFQTalLYTSSKGERRIRVHTLCLPVVSSLADV-YAGVDVQAAICLLANMAVDRSVSSSLSDArDALVN 981
Cdd:COG5047 465 GSaqrpaeaYIQFIT--TYQHSSGTYRIRVTTVARMFTDGGLPKiNRSFDQEAAAVFMARIAAFKAETEDIIDV-FRWID 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 982 AVVDSLSAYGSTVSNLQHSALMAPSSLKLFPLYVLALLKQKAFRTGtSTRLDDRVYAMCQIKSQPLVHLMKMIHPNLYRI 1061
Cdd:COG5047 542 RNLIRLCQKFADYRKDDPSSFRLDPNFTLYPQFMYHLRRSPFLSVF-NNSPDETAFYRHMLNNADVNDSLIMIQPTLQSY 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 2217348607 1062 DRLTDEGAVHVnDRIVPQPPLQKLSAEKLTregaFLMDCGSVFYIWVGKG 1111
Cdd:COG5047 621 SFEKGGVPVLL-DSVSVKPDVILLLDTFFH----ILIFHGSYIAQWRNAG 665
|
|
| zf-Sec23_Sec24 |
pfam04810 |
Sec23/Sec24 zinc finger; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
539-575 |
8.81e-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: 72.09 E-value: 8.81e-16
10 20 30
....*....|....*....|....*....|....*...
gi 2217348607 539 IVRCRSCRTYINPFVSFIDQ-RRWKCNLCYRVNDVPEE 575
Cdd:pfam04810 1 PVRCRRCRAYLNPFCQFDFGgKKWTCNFCGTRNPVPPE 38
|
|
| PLN00162 |
PLN00162 |
transport protein sec23; Provisional |
495-979 |
6.76e-14 |
|
transport protein sec23; Provisional
Pssm-ID: 215083 [Multi-domain] Cd Length: 761 Bit Score: 76.52 E-value: 6.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 495 DSFRCTLTNIPQTQALLNKAKLPLGLLLHPFRDLTQLPVITSNTIvRCRSCRTYINPF--VSFiDQRRWKCNLCYRVNDV 572
Cdd:PLN00162 10 DGVRMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPL-RCRTCRAVLNPYcrVDF-QAKIWICPFCFQRNHF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 573 PeefmynpltRSY---GEPHKRPEV--QNSTVEFiASSDYMLRPPQPAVYLFVLDVSHNAVEAGYLTilcQSLLENLDKL 647
Cdd:PLN00162 88 P---------PHYssiSETNLPAELfpQYTTVEY-TLPPGSGGAPSPPVFVFVVDTCMIEEELGALK---SALLQAIALL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 648 PGDSrtRIGFMTFDSTIHFYNL------------------------QEGLS----QPQMLIVSDIDDVFLPTP-DSLLVN 698
Cdd:PLN00162 155 PENA--LVGLITFGTHVHVHELgfsecsksyvfrgnkevskdqileQLGLGgkkrRPAGGGIAGARDGLSSSGvNRFLLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 699 LYESKELIKDLLNALPNMFTNTRETHSAL---GPALQAAFKLM---SP-TGGRVSVFqTQLPS-LGAGLLQSREDPNQRS 770
Cdd:PLN00162 233 ASECEFTLNSALEELQKDPWPVPPGHRPArctGAALSVAAGLLgacVPgTGARIMAF-VGGPCtEGPGAIVSKDLSEPIR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 771 STK-----VVQHLGPATDFYKKLALDCSGQQTAVDLFLLSSQYSDLASLACMSKYSAGCIYYYPSFHythnpsqAEKLQK 845
Cdd:PLN00162 312 SHKdldkdAAPYYKKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVAEMKVAVERTGGLVVLAESFG-------HSVFKD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 846 DLKRYLTR------KIGFEAVMRIRCTKGL----------SMH----------TFHGNffvrsTDLLSLANINPDAGFAV 899
Cdd:PLN00162 385 SLRRVFERdgegslGLSFNGTFEVNCSKDVkvqgaigpcaSLEkkgpsvsdteIGEGG-----TTAWKLCGLDKKTSLAV 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217348607 900 --QLSIEESLTDTSL---VCFQTALLYTSSKGERRIRVHTLCLPVV--SSLADVYAGVDVQAAICLLANMAVDRSVSssl 972
Cdd:PLN00162 460 ffEVANSGQSNPQPPgqqFFLQFLTRYQHSNGQTRLRVTTVTRRWVegSSSEELVAGFDQEAAAVVMARLASHKMET--- 536
|
....*..
gi 2217348607 973 SDARDAL 979
Cdd:PLN00162 537 EEEFDAT 543
|
|
| Gelsolin |
pfam00626 |
Gelsolin repeat; |
1077-1151 |
3.03e-11 |
|
Gelsolin repeat;
Pssm-ID: 395501 [Multi-domain] Cd Length: 76 Bit Score: 60.40 E-value: 3.03e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217348607 1077 VPQPPLQKLSAEKLTREGAFLMDCGSVFYIWVGKGcdNNFIEDVLGYTNFASIP-QKMTHLPELDTLS-SERARSFI 1151
Cdd:pfam00626 2 FVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKG--SSLLEKLFAALLAAQLDdDERFPLPEVIRVPqGKEPARFL 76
|
|
| GEL |
smart00262 |
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ... |
1070-1112 |
9.29e-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: 9.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2217348607 1070 VHVNDRIVPQPPLQKLSAEKLTREGAFLMDCGSVFYIWVGKGC 1112
Cdd:smart00262 3 VRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKS 45
|
|
|