FAS2_CANAX
ID FAS2_CANAX Reviewed; 1885 AA.
AC P43098;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Fatty acid synthase subunit alpha;
DE EC=2.3.1.86;
DE Includes:
DE RecName: Full=Acyl carrier;
DE Includes:
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase;
DE EC=1.1.1.100;
DE AltName: Full=Beta-ketoacyl reductase;
DE Includes:
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase;
DE EC=2.3.1.41;
DE AltName: Full=Beta-ketoacyl synthase;
GN Name=FAS2;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=4918;
RX PubMed=7737507; DOI=10.1016/0378-1119(95)00033-3;
RA Southard S.B., Cihlar R.L.;
RT "Analysis and expression of the Candida albicans FAS2 gene.";
RL Gene 156:133-138(1995).
CC -!- FUNCTION: Fatty acid synthetase catalyzes the formation of long-chain
CC fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit
CC contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-
CC protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain
CC fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+);
CC Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:83139; EC=2.3.1.86;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP]
CC + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
CC EC=2.3.1.41;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+)
CC + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
CC -!- SUBUNIT: [Alpha(6)beta(6)] hexamers of two multifunctional subunits
CC (alpha and beta).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Fungal fatty acid
CC synthetase subunit alpha family. {ECO:0000305}.
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DR EMBL; L29063; AAA34345.1; -; Genomic_DNA.
DR PIR; JC4086; JC4086.
DR PDB; 6U5V; EM; 2.80 A; A=1-1885.
DR PDB; 6U5W; EM; 3.30 A; A=1-1885.
DR PDBsum; 6U5V; -.
DR PDBsum; 6U5W; -.
DR AlphaFoldDB; P43098; -.
DR SMR; P43098; -.
DR PRIDE; P43098; -.
DR VEuPathDB; FungiDB:C3_04830C_A; -.
DR VEuPathDB; FungiDB:CAWG_02796; -.
DR PHI-base; PHI:96; -.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:EnsemblFungi.
DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:EnsemblFungi.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IEA:EnsemblFungi.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.90.470.20; -; 1.
DR HAMAP; MF_00101; AcpS; 1.
DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR InterPro; IPR002582; ACPS.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR040899; Fas_alpha_ACP.
DR InterPro; IPR026025; FAS_alpha_yeast.
DR InterPro; IPR041550; FASI_helical.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR004568; Ppantetheine-prot_Trfase_dom.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF01648; ACPS; 1.
DR Pfam; PF18325; Fas_alpha_ACP; 1.
DR Pfam; PF18314; FAS_I_H; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR PIRSF; PIRSF000454; FAS_yeast_alpha; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR SUPFAM; SSF56214; SSF56214; 1.
DR TIGRFAMs; TIGR00556; pantethn_trn; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
KW Multifunctional enzyme; NAD; NADP; Oxidoreductase; Phosphopantetheine;
KW Phosphoprotein; Transferase.
FT CHAIN 1..1885
FT /note="Fatty acid synthase subunit alpha"
FT /id="PRO_0000180284"
FT DOMAIN 146..221
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 92..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1157..1885
FT /note="Beta-ketoacyl synthase"
FT ACT_SITE 1304
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000250"
FT BINDING 1771..1773
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 1771
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1772
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1773
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1797
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 1807
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 1816..1826
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 1840..1843
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 1870..1872
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 1871
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1872
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 181
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT HELIX 5..21
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 28..35
FT /evidence="ECO:0007829|PDB:6U5V"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 42..50
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 66..71
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:6U5V"
FT TURN 86..90
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 148..160
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 173..177
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 181..194
FT /evidence="ECO:0007829|PDB:6U5V"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 208..213
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 223..236
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 244..251
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 259..263
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 267..271
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 281..299
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 326..347
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 357..364
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 366..381
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 383..388
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 404..420
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 430..439
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 444..455
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 464..482
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 499..502
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:6U5W"
FT STRAND 508..511
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 521..529
FT /evidence="ECO:0007829|PDB:6U5V"
FT TURN 580..582
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 630..632
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 641..648
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 651..654
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 656..671
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 680..684
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 691..694
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 696..700
FT /evidence="ECO:0007829|PDB:6U5V"
FT TURN 701..703
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 705..712
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 715..728
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 734..739
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 745..755
FT /evidence="ECO:0007829|PDB:6U5V"
FT TURN 759..762
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 769..773
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 784..786
FT /evidence="ECO:0007829|PDB:6U5W"
FT HELIX 789..798
FT /evidence="ECO:0007829|PDB:6U5V"
FT TURN 799..802
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 803..812
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 820..826
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 830..834
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 839..843
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 844..849
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 852..855
FT /evidence="ECO:0007829|PDB:6U5V"
FT TURN 859..861
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 862..869
FT /evidence="ECO:0007829|PDB:6U5V"
FT TURN 877..881
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 882..884
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 885..889
FT /evidence="ECO:0007829|PDB:6U5V"
FT TURN 890..892
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 898..906
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 907..909
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 911..917
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 922..926
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 930..932
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 936..969
FT /evidence="ECO:0007829|PDB:6U5V"
FT TURN 971..973
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 974..976
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 998..1004
FT /evidence="ECO:0007829|PDB:6U5V"
FT TURN 1009..1011
FT /evidence="ECO:0007829|PDB:6U5W"
FT HELIX 1014..1016
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 1018..1027
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1032..1040
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1049..1055
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 1058..1066
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 1069..1079
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1087..1098
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 1100..1104
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1107..1110
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1115..1117
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 1118..1125
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 1133..1135
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1137..1147
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1148..1150
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 1151..1155
FT /evidence="ECO:0007829|PDB:6U5V"
FT TURN 1157..1159
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 1162..1166
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 1171..1178
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 1184..1188
FT /evidence="ECO:0007829|PDB:6U5V"
FT TURN 1195..1198
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1201..1206
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1209..1223
FT /evidence="ECO:0007829|PDB:6U5V"
FT TURN 1224..1226
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1230..1232
FT /evidence="ECO:0007829|PDB:6U5V"
FT TURN 1234..1236
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1239..1241
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 1242..1244
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1253..1260
FT /evidence="ECO:0007829|PDB:6U5V"
FT TURN 1261..1266
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1273..1275
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 1277..1279
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1282..1289
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 1303..1305
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1309..1319
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 1324..1332
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1336..1344
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1352..1356
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1361..1363
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 1380..1388
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1389..1395
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 1402..1409
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 1417..1419
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1423..1427
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1440..1442
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1444..1476
FT /evidence="ECO:0007829|PDB:6U5V"
FT TURN 1477..1480
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1486..1512
FT /evidence="ECO:0007829|PDB:6U5V"
FT TURN 1516..1519
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 1521..1523
FT /evidence="ECO:0007829|PDB:6U5W"
FT HELIX 1525..1530
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1531..1533
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1537..1539
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 1540..1544
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1553..1567
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 1576..1579
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1582..1585
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1589..1591
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1592..1606
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 1616..1618
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1620..1622
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 1642..1649
FT /evidence="ECO:0007829|PDB:6U5V"
FT TURN 1650..1652
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 1653..1660
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1662..1664
FT /evidence="ECO:0007829|PDB:6U5V"
FT TURN 1665..1667
FT /evidence="ECO:0007829|PDB:6U5V"
FT HELIX 1671..1698
FT /evidence="ECO:0007829|PDB:6U5V"
FT TURN 1712..1714
FT /evidence="ECO:0007829|PDB:6U5W"
FT HELIX 1716..1719
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 1727..1729
FT /evidence="ECO:0007829|PDB:6U5V"
FT STRAND 1732..1734
FT /evidence="ECO:0007829|PDB:6U5V"
FT TURN 1738..1741
FT /evidence="ECO:0007829|PDB:6U5W"
FT STRAND 1743..1745
FT /evidence="ECO:0007829|PDB:6U5V"
SQ SEQUENCE 1885 AA; 207589 MW; 4835D57F362372E0 CRC64;
MKPEIEQELS HTLLTELLAY QFASPVRWIE TQDVFLKQHN TERIIEIGPS PTLAGMANRT
IKAKYESYDA ALSLQRQVLC YSKDAKEIYY KPDPADLAPK ETPKQEESTP SAPAAATPTP
AAAAAPTPAP APASAGPVES IPDEPVKANL LIHVLVAQKL KKPLDAVPMT KAIKDLVNGK
STVQNEILGD LGKEFGSTPE KPEDTPLEEL AEQFQDSFSG QLGKTSTSLI GRLMSSKMPG
GFSITTARKY LESRFGLGAG RQDSVLLMAL TNEPANRLGS EADAKTFFDG IAQKYASSAG
ISLSSGAGSG AGAANSGGAV VDSAALDALT AENKKLAKQQ LEVLARYLQS RLKQGSLKSF
IKEKEASAVL QKELDLWEAE HGEFYAKGIQ PTFSALKSRT YDSYWNWARQ DVLSMYFDII
FGKLTSVDRE TINQCIQIMN RANPTLIKFM QYHIDHCPEY KGETYKLAKR LGQQLIDNCK
QVLTEDPVYK DVSRITGPKT KVSAKGNIEY EETQKDSVRK FEQYVYEMAQ GGAMTKVSQP
TIQEDLARVY KAISKQASKD SKLELQRVYE DLLKVVESSK EIETEQLTKD ILQAATVPTT
PTEEVDDPCT PSSDDEIASL PDKTSIIQPV SSTIPSQTIP FLHIQKKTKD GWEYNKKLSS
LYLDGLESAA INGLTFKDKY VLVTGAGAGS IGAEILQGLI SGGAKVIVTT SRFSKKVTEY
YQNMYARYGA AGSTLIVVPF NQGSKQDVDA LVQYIYDEPK KGGLGWDLDA IIPFAAIPEN
GNGLDNIDSK SEFAHRIMLT NLLRLLGAVK SKKPTDTRPA QCILPLSPNH GTFGFDGLYS
ESKISLETLF NRWYSEDWGS KLTVCGAVIG WTRGTGLMSA NNIIAEGIEK LGVRTFSQKE
MAFNILGLLT PEIVQLCQEE PVMADLNGGL QFIDNLKDFT SKLRTDLLET ADIRRAVSIE
SAIEQKVVNG DNVDANYSKV MVEPRANMKF DFPTLKSYDE IKQIAPELEG MLDLENVVVV
TGFAEVGPWG NSRTRWEMEA YGEFSLEGAI EMAWIMGFIK YHNGNLQGKP YSGWVDAKTQ
TPIDEKDIKS KYEEEILEHS GIRLIEPELF NGYDPKKKQM IQEIVVQHDL EPFECSKETA
EQYKHEHGEK CEIFEIEESG EYTVRILKGA TLYVPKALRF DRLVAGQIPT GWDARTYGIP
EDTISQVDPI TLYVLVATVE ALLSAGITDP YEFYKYVHVS EVGNCSGSGM GGVSALRGMF
KDRYADKPVQ NDILQESFIN TMSAWVNMLL LSSSGPIKTP VGACATAVES VDIGIETILS
GKAKVVLVGG YDDFQEEGSY EFANMNATSN SIEEFKHGRT PKEMSRPTTT TRNGFMEAQG
SGIQVIMTAD LALKMGVPIH AVLAMTATAT DKIGRSVPAP GKGILTTARE HHGNLKYPSP
LLNIKYRKRQ LNKRLEQIKS WEETELSYLQ EEAELAKEEF GDEFSMHEFL KERTEEVYRE
SKRQVSDAKK QWGNSFYKSD PRIAPLRGAL AAFNLTIDDI GVASFHGTST VANDKNESAT
INNMMKHLGR SEGNPVFGVF QKYLTGHPKG AAGAWMLNGA IQILESGLVP GNRNADNVDK
LLEQYEYVLY PSRSIQTDGI KAVSVTSFGF GQKGAQAVVV HPDYLFAVLD RSTYEEYATK
VSARNKKTYR YMHNAITRNT MFVAKDKAPY SDELEQPVYL DPLARVEENK KKLVFSDKTI
QSNQSYVGEV AQKTAKALST LNKSSKGVGV DVELLSAINI DNETFIERNF TGNEVEYCLN
TAHPQASFTG TWSAKEAVFK ALGVESKGAG ASLIDIEITR DVNGAPKVIL HGEAKKAAAK
AGVKNVNISI SHDDFQATAV ALSEF
