|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00162 |
PLN00162 |
transport protein sec23; Provisional |
1-730 |
0e+00 |
|
transport protein sec23; Provisional
Pssm-ID: 215083 [Multi-domain] Cd Length: 761 Bit Score: 1118.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 1 MDLVELEAVEGLRWAWNSW---AADGTNMIIPLSIMCTPLMLLnSEVPLLPYDPLLCSRCGAVLNPYARLDYQSRIWHCP 77
Cdd:PLN00162 1 MDFAELEAIDGVRMSWNVWpssKIEASKCVIPLAALYTPLKPL-PELPVLPYDPLRCRTCRAVLNPYCRVDFQAKIWICP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 78 FCSLRNPFPR---PIADTNLPAELFPTYSTVEYSSPSPSPPPPPP-AFVFLLDLSTPQDELPPLKNQLLHLLHHLPDHSL 153
Cdd:PLN00162 80 FCFQRNHFPPhysSISETNLPAELFPQYTTVEYTLPPGSGGAPSPpVFVFVVDTCMIEEELGALKSALLQAIALLPENAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 154 VSLITFDSMVYLHHLSSSHFSSLLVFHGNRHLSSNQIRHFLN----PHRHQA-----------------FLLPISECQFS 212
Cdd:PLN00162 160 VGLITFGTHVHVHELGFSECSKSYVFRGNKEVSKDQILEQLGlggkKRRPAGggiagardglsssgvnrFLLPASECEFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 213 ITTAIEEIHSTSNSTISASRPPRCTGSAISVALGLLESCPINTGSRILVFTSGPATLGPGIVVDSDRRQPIRTHHHIFNA 292
Cdd:PLN00162 240 LNSALEELQKDPWPVPPGHRPARCTGAALSVAAGLLGACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 293 QATHYAKSSAFYNQLSKRLSGASVVLDLFACSLDQVGAAELRGPVEHSGGFIVLSESFDSDQFKNCLRQMFRCDDQGHLR 372
Cdd:PLN00162 320 AAPYYKKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFERDGEGSLG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 373 MNFDATIEIVTTKDVKICGALGPCVSLERNNCLVSEAEVGEGGTSVWKLNTLTHKTCIAFFFQV-NQEQKMKIQPGSAFL 451
Cdd:PLN00162 400 LSFNGTFEVNCSKDVKVQGAIGPCASLEKKGPSVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVaNSGQSNPQPPGQQFF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 452 IQFITRYRQGNM-IRKRVTTAARRWVA-SHSADIGAGFDQEAAAAVMARLAILRAETCHARDVIRWLDDTLIRFTSKFGD 529
Cdd:PLN00162 480 LQFLTRYQHSNGqTRLRVTTVTRRWVEgSSSEELVAGFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFGD 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 530 YVPEDPSSFRLSSNFSLYPQFMYHLRRSQFIDVSNTTPDETAFFRLVLNREGVVGSLIMIQPTLFQYSFDGPPVPVLLDI 609
Cdd:PLN00162 560 YRKDDPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNNSPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLDV 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 610 RSISPDFILLFDSFFCVVIHYGSKIAQWRKLGYDKDPNHESLRKLLEAPELDAEQLVADRLPVPRIIRCDQHSSQARFLL 689
Cdd:PLN00162 640 ASIAADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFLL 719
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 356567478 690 AKLNPSVTQNSTYT-EGSDIIFTDDLSLEVFLDQLQVLAVQS 730
Cdd:PLN00162 720 AKLNPSATYNSANAmGGSDIIFTDDVSLQVFMEHLQRLAVQS 761
|
|
| SEC23 |
COG5047 |
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]; |
1-728 |
0e+00 |
|
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
Pssm-ID: 227380 [Multi-domain] Cd Length: 755 Bit Score: 638.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 1 MDLVELEAVEGLRWAWNSWAA---DGTNMIIPLSIMCTPLMLlNSEVPLLPYDPLLC-SRCGAVLNPYARLDYQSRIWHC 76
Cdd:COG5047 1 MNFEIIEENDGIRLTWNVFPAtrgDATRTVIPIACLYTPLHE-DDALTVNYYEPVKCtAPCKAVLNPYCHIDERNQSWIC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 77 PFCSLRNPFP---RPIADTNLPAELFPTYSTVEYSSPSPSPPPPPpaFVFLLDLSTPQDELPPLKNQLLHLLHHLPDHSL 153
Cdd:COG5047 80 PFCNQRNTLPpqyRDISNANLPLELLPQSSTIEYTLSKPVILPPV--FFFVVDACCDEEELTALKDSLIVSLSLLPPEAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 154 VSLITFDSMVYLHHLSSSHFSSLLVFHGNRHLSSNQIRHFL---NPHRHQA---------------FLLPISECQFSITT 215
Cdd:COG5047 158 VGLITYGTSIQVHELNAENHRRSYVFSGNKEYTKENLQELLalsKPTKSGGfeskisgigqfassrFLLPTQQCEFKLLN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 216 AIEEIHSTSNSTISASRPPRCTGSAISVALGLLESCPINTGSRILVFTSGPATLGPGIVVDSDRRQPIRTHHHIFNAQAT 295
Cdd:COG5047 238 ILEQLQPDPWPVPAGKRPLRCTGSALNIASSLLEQCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEPMRSHHDIESDSAQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 296 HYAKSSAFYNQLSKRLSGASVVLDLFACSLDQVGAAELRGPVEHSGGFIVLSESFDSDQFKNCLRQMFRCDDQGHLRMNF 375
Cdd:COG5047 318 HSKKATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFNRDSEGYLKMGF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 376 DATIEIVTTKDVKICGALGPCVSLERNNCLVSEAEVGEGGTSVWKLNTLTHKTCIAFFFQVNQEQKMKIQPGSAF-LIQF 454
Cdd:COG5047 398 NANMEVKTSKNLKIKGLIGHAVSVKKKANNISDSEIGIGATNSWKMASLSPKSNYALYFEIALGAASGSAQRPAEaYIQF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 455 ITRY-RQGNMIRKRVTTAARRWVASHSADIGAGFDQEAAAAVMARLAILRAETCHARDVIRWLDDTLIRFTSKFGDYVPE 533
Cdd:COG5047 478 ITTYqHSSGTYRIRVTTVARMFTDGGLPKINRSFDQEAAAVFMARIAAFKAETEDIIDVFRWIDRNLIRLCQKFADYRKD 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 534 DPSSFRLSSNFSLYPQFMYHLRRSQFIDVSNTTPDETAFFRLVLNREGVVGSLIMIQPTLFQYSFDGPPVPVLLDIRSIS 613
Cdd:COG5047 558 DPSSFRLDPNFTLYPQFMYHLRRSPFLSVFNNSPDETAFYRHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVLLDSVSVK 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 614 PDFILLFDSFFCVVIHYGSKIAQWRKLGYDKDPNHESLRKLLEAPELDAEQLVADRLPVPRIIRCDQHSSQARFLLAKLN 693
Cdd:COG5047 638 PDVILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKELLEAPRLEAAELLQDRFPIPRFIVTEQGGSQARFLLSKIN 717
|
730 740 750
....*....|....*....|....*....|....*
gi 356567478 694 PSVTQNSTYTEGSDIIFTDDLSLEVFLDQLQVLAV 728
Cdd:COG5047 718 PSDITNKMSGGGSETILTDDVNLQKFMNHLRKLAV 752
|
|
| Sec23-like |
cd01478 |
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
121-356 |
1.68e-65 |
|
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: 218.01 E-value: 1.68e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 121 FVFLLDLSTPQDELPPLKNQLLHLLHHLPDHSLVSLITFDSMVYLHHLSSSHFSSLLVFHGNRHLSSNQIRHFL------ 194
Cdd:cd01478 6 FLFVVDTCMDEEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLglggpa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 195 ------------NPHRHQA---FLLPISECQFSITTAIEEIHSTSNSTISASRPPRCTGSAISVALGLLESCPINTGSRI 259
Cdd:cd01478 86 mrpsasqhpgagNPLPSAAasrFLLPVSQCEFTLTDLLEQLQPDPWPVPAGHRPLRCTGVALSIAVGLLEACFPNTGARI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 260 LVFTSGPATLGPGIVVDSDRRQPIRTHHHIFNAQATHYAKSSAFYNQLSKRLSGASVVLDLFACSLDQVGAAELRGPVEH 339
Cdd:cd01478 166 MLFAGGPCTVGPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMKVLVNS 245
|
250
....*....|....*..
gi 356567478 340 SGGFIVLSESFDSDQFK 356
Cdd:cd01478 246 TGGHVVLSDSFTTSIFK 262
|
|
| Sec23_trunk |
pfam04811 |
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
120-363 |
6.09e-43 |
|
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: 155.49 E-value: 6.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 120 AFVFLLDLS---TPQDELPPLKNQLLHLLHHLP--DHSLVSLITFDSMVYlhhlssshfssllvFH-------GNRHLSS 187
Cdd:pfam04811 5 VFLFVIDVSynaIKSGLLAALKESLLQSLDLLPgdPRARVGFITFDSTVH--------------FFnlgsslrQPQMLVV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 188 NQIRHFLNPhRHQAFLLPISECQFSITTAIEEIHSTSNSTisaSRPPRCTGSAISVALGLLESCPinTGSRILVFTSGPA 267
Cdd:pfam04811 71 SDLQDMFLP-LPDRFLVPLSECRFVLEDLLEQLPPMFPVT---KRPERCLGPALQAAFLLLKAAF--TGGKIMVFQGGLP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 268 TLGPGIVVDSDRRqpiRTHHHIFNAQATHYAKSSAFYNQLSKRLSGASVVLDLFACSLDQVGAAELRGPVEHSGGFIVLS 347
Cdd:pfam04811 145 TVGPGGKLKSRLD---ESHHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVATLGQLSRLTGGQVYLY 221
|
250 260
....*....|....*....|
gi 356567478 348 ESF----DSDQFKNCLRQMF 363
Cdd:pfam04811 222 PSFqadvDGSKFKQDLQRYF 241
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00162 |
PLN00162 |
transport protein sec23; Provisional |
1-730 |
0e+00 |
|
transport protein sec23; Provisional
Pssm-ID: 215083 [Multi-domain] Cd Length: 761 Bit Score: 1118.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 1 MDLVELEAVEGLRWAWNSW---AADGTNMIIPLSIMCTPLMLLnSEVPLLPYDPLLCSRCGAVLNPYARLDYQSRIWHCP 77
Cdd:PLN00162 1 MDFAELEAIDGVRMSWNVWpssKIEASKCVIPLAALYTPLKPL-PELPVLPYDPLRCRTCRAVLNPYCRVDFQAKIWICP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 78 FCSLRNPFPR---PIADTNLPAELFPTYSTVEYSSPSPSPPPPPP-AFVFLLDLSTPQDELPPLKNQLLHLLHHLPDHSL 153
Cdd:PLN00162 80 FCFQRNHFPPhysSISETNLPAELFPQYTTVEYTLPPGSGGAPSPpVFVFVVDTCMIEEELGALKSALLQAIALLPENAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 154 VSLITFDSMVYLHHLSSSHFSSLLVFHGNRHLSSNQIRHFLN----PHRHQA-----------------FLLPISECQFS 212
Cdd:PLN00162 160 VGLITFGTHVHVHELGFSECSKSYVFRGNKEVSKDQILEQLGlggkKRRPAGggiagardglsssgvnrFLLPASECEFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 213 ITTAIEEIHSTSNSTISASRPPRCTGSAISVALGLLESCPINTGSRILVFTSGPATLGPGIVVDSDRRQPIRTHHHIFNA 292
Cdd:PLN00162 240 LNSALEELQKDPWPVPPGHRPARCTGAALSVAAGLLGACVPGTGARIMAFVGGPCTEGPGAIVSKDLSEPIRSHKDLDKD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 293 QATHYAKSSAFYNQLSKRLSGASVVLDLFACSLDQVGAAELRGPVEHSGGFIVLSESFDSDQFKNCLRQMFRCDDQGHLR 372
Cdd:PLN00162 320 AAPYYKKAVKFYEGLAKQLVAQGHVLDVFACSLDQVGVAEMKVAVERTGGLVVLAESFGHSVFKDSLRRVFERDGEGSLG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 373 MNFDATIEIVTTKDVKICGALGPCVSLERNNCLVSEAEVGEGGTSVWKLNTLTHKTCIAFFFQV-NQEQKMKIQPGSAFL 451
Cdd:PLN00162 400 LSFNGTFEVNCSKDVKVQGAIGPCASLEKKGPSVSDTEIGEGGTTAWKLCGLDKKTSLAVFFEVaNSGQSNPQPPGQQFF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 452 IQFITRYRQGNM-IRKRVTTAARRWVA-SHSADIGAGFDQEAAAAVMARLAILRAETCHARDVIRWLDDTLIRFTSKFGD 529
Cdd:PLN00162 480 LQFLTRYQHSNGqTRLRVTTVTRRWVEgSSSEELVAGFDQEAAAVVMARLASHKMETEEEFDATRWLDRALIRLCSKFGD 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 530 YVPEDPSSFRLSSNFSLYPQFMYHLRRSQFIDVSNTTPDETAFFRLVLNREGVVGSLIMIQPTLFQYSFDGPPVPVLLDI 609
Cdd:PLN00162 560 YRKDDPSSFRLSPNFSLYPQFMFNLRRSQFVQVFNNSPDETAYFRMMLNRENVTNSLVMIQPTLISYSFNGPPEPVLLDV 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 610 RSISPDFILLFDSFFCVVIHYGSKIAQWRKLGYDKDPNHESLRKLLEAPELDAEQLVADRLPVPRIIRCDQHSSQARFLL 689
Cdd:PLN00162 640 ASIAADRILLLDSYFSVVIFHGSTIAQWRKAGYHNQPEHEAFAQLLEAPQADAQAIIKERFPVPRLVVCDQHGSQARFLL 719
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 356567478 690 AKLNPSVTQNSTYT-EGSDIIFTDDLSLEVFLDQLQVLAVQS 730
Cdd:PLN00162 720 AKLNPSATYNSANAmGGSDIIFTDDVSLQVFMEHLQRLAVQS 761
|
|
| SEC23 |
COG5047 |
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]; |
1-728 |
0e+00 |
|
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
Pssm-ID: 227380 [Multi-domain] Cd Length: 755 Bit Score: 638.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 1 MDLVELEAVEGLRWAWNSWAA---DGTNMIIPLSIMCTPLMLlNSEVPLLPYDPLLC-SRCGAVLNPYARLDYQSRIWHC 76
Cdd:COG5047 1 MNFEIIEENDGIRLTWNVFPAtrgDATRTVIPIACLYTPLHE-DDALTVNYYEPVKCtAPCKAVLNPYCHIDERNQSWIC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 77 PFCSLRNPFP---RPIADTNLPAELFPTYSTVEYSSPSPSPPPPPpaFVFLLDLSTPQDELPPLKNQLLHLLHHLPDHSL 153
Cdd:COG5047 80 PFCNQRNTLPpqyRDISNANLPLELLPQSSTIEYTLSKPVILPPV--FFFVVDACCDEEELTALKDSLIVSLSLLPPEAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 154 VSLITFDSMVYLHHLSSSHFSSLLVFHGNRHLSSNQIRHFL---NPHRHQA---------------FLLPISECQFSITT 215
Cdd:COG5047 158 VGLITYGTSIQVHELNAENHRRSYVFSGNKEYTKENLQELLalsKPTKSGGfeskisgigqfassrFLLPTQQCEFKLLN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 216 AIEEIHSTSNSTISASRPPRCTGSAISVALGLLESCPINTGSRILVFTSGPATLGPGIVVDSDRRQPIRTHHHIFNAQAT 295
Cdd:COG5047 238 ILEQLQPDPWPVPAGKRPLRCTGSALNIASSLLEQCFPNAGCHIVLFAGGPCTVGPGTVVSTELKEPMRSHHDIESDSAQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 296 HYAKSSAFYNQLSKRLSGASVVLDLFACSLDQVGAAELRGPVEHSGGFIVLSESFDSDQFKNCLRQMFRCDDQGHLRMNF 375
Cdd:COG5047 318 HSKKATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRIFNRDSEGYLKMGF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 376 DATIEIVTTKDVKICGALGPCVSLERNNCLVSEAEVGEGGTSVWKLNTLTHKTCIAFFFQVNQEQKMKIQPGSAF-LIQF 454
Cdd:COG5047 398 NANMEVKTSKNLKIKGLIGHAVSVKKKANNISDSEIGIGATNSWKMASLSPKSNYALYFEIALGAASGSAQRPAEaYIQF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 455 ITRY-RQGNMIRKRVTTAARRWVASHSADIGAGFDQEAAAAVMARLAILRAETCHARDVIRWLDDTLIRFTSKFGDYVPE 533
Cdd:COG5047 478 ITTYqHSSGTYRIRVTTVARMFTDGGLPKINRSFDQEAAAVFMARIAAFKAETEDIIDVFRWIDRNLIRLCQKFADYRKD 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 534 DPSSFRLSSNFSLYPQFMYHLRRSQFIDVSNTTPDETAFFRLVLNREGVVGSLIMIQPTLFQYSFDGPPVPVLLDIRSIS 613
Cdd:COG5047 558 DPSSFRLDPNFTLYPQFMYHLRRSPFLSVFNNSPDETAFYRHMLNNADVNDSLIMIQPTLQSYSFEKGGVPVLLDSVSVK 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 614 PDFILLFDSFFCVVIHYGSKIAQWRKLGYDKDPNHESLRKLLEAPELDAEQLVADRLPVPRIIRCDQHSSQARFLLAKLN 693
Cdd:COG5047 638 PDVILLLDTFFHILIFHGSYIAQWRNAGYQEQPEYLNLKELLEAPRLEAAELLQDRFPIPRFIVTEQGGSQARFLLSKIN 717
|
730 740 750
....*....|....*....|....*....|....*
gi 356567478 694 PSVTQNSTYTEGSDIIFTDDLSLEVFLDQLQVLAV 728
Cdd:COG5047 718 PSDITNKMSGGGSETILTDDVNLQKFMNHLRKLAV 752
|
|
| Sec23-like |
cd01478 |
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
121-356 |
1.68e-65 |
|
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: 218.01 E-value: 1.68e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 121 FVFLLDLSTPQDELPPLKNQLLHLLHHLPDHSLVSLITFDSMVYLHHLSSSHFSSLLVFHGNRHLSSNQIRHFL------ 194
Cdd:cd01478 6 FLFVVDTCMDEEELDALKESLIMSLSLLPPNALVGLITFGTMVQVHELGFEECSKSYVFRGNKDYTAKQIQDMLglggpa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 195 ------------NPHRHQA---FLLPISECQFSITTAIEEIHSTSNSTISASRPPRCTGSAISVALGLLESCPINTGSRI 259
Cdd:cd01478 86 mrpsasqhpgagNPLPSAAasrFLLPVSQCEFTLTDLLEQLQPDPWPVPAGHRPLRCTGVALSIAVGLLEACFPNTGARI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 260 LVFTSGPATLGPGIVVDSDRRQPIRTHHHIFNAQATHYAKSSAFYNQLSKRLSGASVVLDLFACSLDQVGAAELRGPVEH 339
Cdd:cd01478 166 MLFAGGPCTVGPGAVVSTELKDPIRSHHDIDKDNAKYYKKAVKFYDSLAKRLAANGHAVDIFAGCLDQVGLLEMKVLVNS 245
|
250
....*....|....*..
gi 356567478 340 SGGFIVLSESFDSDQFK 356
Cdd:cd01478 246 TGGHVVLSDSFTTSIFK 262
|
|
| Sec23_C |
cd11287 |
C-terminal Actin depolymerization factor-homology domain of Sec23; The C-terminal domain of ... |
580-700 |
4.30e-64 |
|
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: 208.77 E-value: 4.30e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 580 EGVVGSLIMIQPTLFQYSFDGPPVPVLLDIRSISPDFILLFDSFFCVVIHYGSKIAQWRKLGYDKDPNHESLRKLLEAPE 659
Cdd:cd11287 1 EDVSNSLIMIQPTLYSYSFNGPPEPVLLDSSSILPDRILLLDTFFHILIYHGETIAQWRKAGYQDQPEYENFKDLLEAPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 356567478 660 LDAEQLVADRLPVPRIIRCDQHSSQARFLLAKLNPSVTQNS 700
Cdd:cd11287 81 DDAQELLQDRFPMPRYIVTEQGGSQARFLLSKVNPSQTHNN 121
|
|
| Sec23_trunk |
pfam04811 |
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
120-363 |
6.09e-43 |
|
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: 155.49 E-value: 6.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 120 AFVFLLDLS---TPQDELPPLKNQLLHLLHHLP--DHSLVSLITFDSMVYlhhlssshfssllvFH-------GNRHLSS 187
Cdd:pfam04811 5 VFLFVIDVSynaIKSGLLAALKESLLQSLDLLPgdPRARVGFITFDSTVH--------------FFnlgsslrQPQMLVV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 188 NQIRHFLNPhRHQAFLLPISECQFSITTAIEEIHSTSNSTisaSRPPRCTGSAISVALGLLESCPinTGSRILVFTSGPA 267
Cdd:pfam04811 71 SDLQDMFLP-LPDRFLVPLSECRFVLEDLLEQLPPMFPVT---KRPERCLGPALQAAFLLLKAAF--TGGKIMVFQGGLP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 268 TLGPGIVVDSDRRqpiRTHHHIFNAQATHYAKSSAFYNQLSKRLSGASVVLDLFACSLDQVGAAELRGPVEHSGGFIVLS 347
Cdd:pfam04811 145 TVGPGGKLKSRLD---ESHHGTDKEKAKLVKKADKFYKSLAKECVKQGHSVDLFAFSLDYVDVATLGQLSRLTGGQVYLY 221
|
250 260
....*....|....*....|
gi 356567478 348 ESF----DSDQFKNCLRQMF 363
Cdd:pfam04811 222 PSFqadvDGSKFKQDLQRYF 241
|
|
| trunk_domain |
cd01468 |
trunk domain. COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi ... |
120-359 |
2.16e-40 |
|
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: 148.16 E-value: 2.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 120 AFVFLLDLS---TPQDELPPLKNQLLHLLHHLPD--HSLVSLITFDSMV-YLHHLSSSHFSSLLVFHGNRHLSsnqirhf 193
Cdd:cd01468 5 VFVFVIDVSyeaIKEGLLQALKESLLASLDLLPGdpRARVGLITYDSTVhFYNLSSDLAQPKMYVVSDLKDVF------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 194 lnPHRHQAFLLPISECQFSITTAIEEIhSTSNSTISASRPPRCTGSAISVALGLLESCpiNTGSRILVFTSGPATLGPGI 273
Cdd:cd01468 78 --LPLPDRFLVPLSECKKVIHDLLEQL-PPMFWPVPTHRPERCLGPALQAAFLLLKGT--FAGGRIIVFQGGLPTVGPGK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 274 VVDSDRRQPIRTHhhifnAQATHYAKSSAFYNQLSKRLSGASVVLDLFACSLDQVGAAELRGPVEHSGGFIVLSESF--- 350
Cdd:cd01468 153 LKSREDKEPIRSH-----DEAQLLKPATKFYKSLAKECVKSGICVDLFAFSLDYVDVATLKQLAKSTGGQVYLYDSFqap 227
|
250
....*....|
gi 356567478 351 -DSDQFKNCL 359
Cdd:cd01468 228 nDGSKFKQDL 237
|
|
| Sec23_helical |
pfam04815 |
Sec23/Sec24 helical domain; COPII-coated vesicles carry proteins from the endoplasmic ... |
488-587 |
6.18e-20 |
|
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: 85.25 E-value: 6.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 488 DQEAAAAVMARLAILRAETCHARDVIRWLDDTLIRFTSKFGDYVPE--DPSSFRLSSNFSLYPQFMYHLRRSQ-FIDVSN 564
Cdd:pfam04815 1 DQEAIAVLLAKKAVEKALSSSLSDAREALDNKLVDILAAYRKYCASssSPGQLILPESLKLLPLYMLALLKSPaLRGGNS 80
|
90 100
....*....|....*....|...
gi 356567478 565 TTPDETAFFRLVLNREGVVGSLI 587
Cdd:pfam04815 81 SPSDERAYARHLLLSLPVEELLL 103
|
|
| Sec23_BS |
pfam08033 |
Sec23/Sec24 beta-sandwich domain; |
375-476 |
1.24e-15 |
|
Sec23/Sec24 beta-sandwich domain;
Pssm-ID: 429794 [Multi-domain] Cd Length: 86 Bit Score: 72.57 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 375 FDATIEIVTTKDVKICGALGPCVSleRNNclvseaevgeGGTsvWKLNTLTHKTCIAFFFQVNQeqkmKIQPGSAFLIQF 454
Cdd:pfam08033 2 FNAVLRVRTSKGLKVSGFIGNFVS--RSS----------GDT--WKLPSLDPDTSYAFEFDIDE----PLPNGSNAYIQF 63
|
90 100
....*....|....*....|...
gi 356567478 455 ITRYRQGNMIRK-RVTTAARRWV 476
Cdd:pfam08033 64 ALLYTHSSGERRiRVTTVALPVT 86
|
|
| zf-Sec23_Sec24 |
pfam04810 |
Sec23/Sec24 zinc finger; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
51-86 |
2.00e-14 |
|
Sec23/Sec24 zinc finger; COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi complex. This vesicular transport can be reconstituted by using three cytosolic components containing five proteins: the small GTPase Sar1p, the Sec23p/24p complex, and the Sec13p/Sec31p complex. This domain is found to be zinc binding domain.
Pssm-ID: 461437 [Multi-domain] Cd Length: 38 Bit Score: 67.47 E-value: 2.00e-14
10 20 30
....*....|....*....|....*....|....*.
gi 356567478 51 PLLCSRCGAVLNPYARLDYQSRIWHCPFCSLRNPFP 86
Cdd:pfam04810 1 PVRCRRCRAYLNPFCQFDFGGKKWTCNFCGTRNPVP 36
|
|
| COG5028 |
COG5028 |
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ... |
28-357 |
1.93e-13 |
|
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking and secretion];
Pssm-ID: 227361 [Multi-domain] Cd Length: 861 Bit Score: 74.06 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 28 IPLSIMCTPLMLLNSEVPLLPYD----PLLCSRCGAVLNPYARLDYQSRIWHCPFCSLRNPFPR----------PIADTN 93
Cdd:COG5028 172 IPFGLVIRPFLELYPEEDPVPLVedgsIVRCRRCRSYINPFVQFIEQGRKWRCNICRSKNDVPEgfdnpsgpndPRSDRY 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 94 LPAELfpTYSTVEYSSPSPSPPPPP--PAFVFLLDLSTPQDELPPLK---NQLLHLLHHLPDHSL---VSLITFDSMVYL 165
Cdd:COG5028 252 SRPEL--KSGVVDFLAPKEYSLRQPppPVYVFLIDVSFEAIKNGLVKaaiRAILENLDQIPNFDPrtkIAIICFDSSLHF 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 166 HHLSSShfssllvFHGNRHLSSNQIRHFLnPHRHQAFLLPISECQFSITTAIEEIHSTSNSTISasrPPRCTGSAISVAL 245
Cdd:COG5028 330 FKLSPD-------LDEQMLIVSDLDEPFL-PFPSGLFVLPLKSCKQIIETLLDRVPRIFQDNKS---PKNALGPALKAAK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 246 GLLESCpintGSRILVFTSGPATLGPGIVvdSDRRQPIRTHHHIfnaqathyakSSAFYNQLSKRLSGASVVLDLFACSL 325
Cdd:COG5028 399 SLIGGT----GGKIIVFLSTLPNMGIGKL--QLREDKESSLLSC----------KDSFYKEFAIECSKVGISVDLFLTSE 462
|
330 340 350
....*....|....*....|....*....|....*...
gi 356567478 326 DQVGAAELRGPVEHSGGFI------VLSESFDSDQFKN 357
Cdd:COG5028 463 DYIDVATLSHLCRYTGGQTyfypnfSATRPNDATKLAN 500
|
|
| Gelsolin |
pfam00626 |
Gelsolin repeat; |
602-688 |
4.35e-09 |
|
Gelsolin repeat;
Pssm-ID: 395501 [Multi-domain] Cd Length: 76 Bit Score: 53.47 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 602 PVPVLLDIRSISPDFILLFDsffcvvihYGSKIAQWRklGYDKDPNhESLRKLLEAPELDAEqlvaDRLPVPRIIRCDQH 681
Cdd:pfam00626 5 PPPVPLSQESLNSGDCYLLD--------NGFTIFLWV--GKGSSLL-EKLFAALLAAQLDDD----ERFPLPEVIRVPQG 69
|
....*..
gi 356567478 682 SSQARFL 688
Cdd:pfam00626 70 KEPARFL 76
|
|
| gelsolin_like |
cd11280 |
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ... |
590-688 |
5.97e-07 |
|
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.
Pssm-ID: 200436 Cd Length: 88 Bit Score: 47.75 E-value: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 590 QPTLFQYSFDG--PPVPVLLDIRSISPDFILLFDsffcvvihYGSKIAQWrkLGYdkdpnhESLRKLLEAPELDAEQLVA 667
Cdd:cd11280 1 PPRLYRVRGSKaiEIEEVPLASSSLDSDDVFVLD--------TGSEIYIW--QGR------ASSQAELAAAALLAKELDE 64
|
90 100
....*....|....*....|.
gi 356567478 668 DRLPVPRIIRCDQHSSQARFL 688
Cdd:cd11280 65 ERKGKPEIVRIRQGQEPREFW 85
|
|
| Sec24-like |
cd01479 |
Sec24-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
202-342 |
4.63e-06 |
|
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: 48.42 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356567478 202 FLLPISECQFSITTAIEEI---HSTSNSTISasrpprCTGSAISVALGLLESCpintGSRILVFTSGPATLGPGIVVDSD 278
Cdd:cd01479 85 LLVNLKESRQVIEDLLDQIpemFQDTKETES------ALGPALQAAFLLLKET----GGKIIVFQSSLPTLGAGKLKSRE 154
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 356567478 279 RRQPIRTHhhifnAQATHYAKSSAFYNQLSKRLSGASVVLDLFACSLDQVGAAELRGPVEHSGG 342
Cdd:cd01479 155 DPKLLSTD-----KEKQLLQPQTDFYKKLALECVKSQISVDLFLFSNQYVDVATLGCLSRLTGG 213
|
|
| |
