C1TC_YEAST
ID C1TC_YEAST Reviewed; 946 AA.
AC P07245; D6VUY6;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=C-1-tetrahydrofolate synthase, cytoplasmic;
DE Short=C1-THF synthase;
DE Includes:
DE RecName: Full=Methylenetetrahydrofolate dehydrogenase;
DE EC=1.5.1.5 {ECO:0000269|PubMed:3514599, ECO:0000269|PubMed:8464869};
DE Includes:
DE RecName: Full=Methenyltetrahydrofolate cyclohydrolase;
DE EC=3.5.4.9 {ECO:0000269|PubMed:3514599, ECO:0000305|PubMed:8464869};
DE Includes:
DE RecName: Full=Formyltetrahydrofolate synthetase;
DE EC=6.3.4.3 {ECO:0000269|PubMed:3514599, ECO:0000269|PubMed:8464869};
GN Name=ADE3; OrderedLocusNames=YGR204W; ORFNames=G7733;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-10, FUNCTION,
RP CATALYTIC ACTIVITY, AND DOMAIN.
RX PubMed=3514599; DOI=10.1016/s0021-9258(17)38548-4;
RA Staben C., Rabinowitz J.C.;
RT "Nucleotide sequence of the Saccharomyces cerevisiae ADE3 gene encoding C1-
RT tetrahydrofolate synthase.";
RL J. Biol. Chem. 261:4629-4637(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8904340;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<273::aid-yea898>3.0.co;2-1;
RA Guerreiro P., Barreiros T., Soares H., Cyrne L., Maia e Silva A.,
RA Rodrigues-Pousada C.;
RT "Sequencing of a 17.6 kb segment on the right arm of yeast chromosome VII
RT reveals 12 ORFs, including CCT, ADE3 and TR-I genes, homologues of the
RT yeast PMT and EF1G genes, of the human and bacterial electron-transferring
RT flavoproteins (beta-chain) and of the Escherichia coli phosphoserine
RT phosphohydrolase, and five new ORFs.";
RL Yeast 12:273-280(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP PROTEIN SEQUENCE OF 2-4, FUNCTION, AND SUBUNIT.
RX PubMed=329838; DOI=10.1016/s0006-291x(77)80176-9;
RA Paukert J.L., Williams G.R., Rabinowitz J.C.;
RT "Formyl-methenyl-methylenetetrahydrofolate synthetase (combined);
RT correlation of enzymic activities with limited proteolytic degradation of
RT the protein from yeast.";
RL Biochem. Biophys. Res. Commun. 77:147-154(1977).
RN [7]
RP MUTAGENESIS.
RX PubMed=2541774; DOI=10.1021/bi00431a020;
RA Barlowe C.K., Williams M.E., Rabinowitz J.C., Appling D.R.;
RT "Site-directed mutagenesis of yeast C1-tetrahydrofolate synthase: analysis
RT of an overlapping active site in a multifunctional enzyme.";
RL Biochemistry 28:2099-2106(1989).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8464869; DOI=10.1073/pnas.90.7.2636;
RA Song J.M., Rabinowitz J.C.;
RT "Function of yeast cytoplasmic C1-tetrahydrofolate synthase.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:2636-2640(1993).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [10]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176; THR-318 AND SER-322, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Cytoplasmic isozyme of C-1-tetrahydrofolate synthase. The
CC trifunctional enzyme catalyzes the interconversion of the one-carbon
CC derivatives of tetrahydrofolate (THF) between different oxidation
CC states by the enzymatic activities 10-formyltetrahydrofolate
CC synthetase, 5,lO-methenyltetrahydrofolate cyclohydrolase, and 5,lO-
CC methylenetetrahydrofolate dehydrogenase. Involved in the generation of
CC one-carbon intermediates in the biosynthesis of the purine bases.
CC {ECO:0000269|PubMed:329838, ECO:0000269|PubMed:3514599,
CC ECO:0000269|PubMed:8464869}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-
CC methenyltetrahydrofolate + NADPH; Xref=Rhea:RHEA:22812,
CC ChEBI:CHEBI:15636, ChEBI:CHEBI:57455, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.5.1.5; Evidence={ECO:0000269|PubMed:3514599,
CC ECO:0000269|PubMed:8464869};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22813;
CC Evidence={ECO:0000305|PubMed:3514599, ECO:0000305|PubMed:8464869};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22814;
CC Evidence={ECO:0000305|PubMed:3514599, ECO:0000305|PubMed:8464869};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,10-methenyltetrahydrofolate + H2O = (6S)-10-
CC formyltetrahydrofolate + H(+); Xref=Rhea:RHEA:23700,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57454,
CC ChEBI:CHEBI:57455; EC=3.5.4.9; Evidence={ECO:0000269|PubMed:3514599,
CC ECO:0000305|PubMed:8464869};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23701;
CC Evidence={ECO:0000305|PubMed:3514599, ECO:0000305|PubMed:8464869};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23702;
CC Evidence={ECO:0000305|PubMed:3514599, ECO:0000305|PubMed:8464869};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-
CC formyltetrahydrofolate + ADP + phosphate; Xref=Rhea:RHEA:20221,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57453, ChEBI:CHEBI:57454, ChEBI:CHEBI:456216; EC=6.3.4.3;
CC Evidence={ECO:0000269|PubMed:3514599, ECO:0000269|PubMed:8464869};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20222;
CC Evidence={ECO:0000305|PubMed:3514599, ECO:0000305|PubMed:8464869};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20223;
CC Evidence={ECO:0000305|PubMed:3514599, ECO:0000305|PubMed:8464869};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:329838}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: This trifunctional enzyme consists of two major domains: an N-
CC terminal part containing the methylene-THF dehydrogenase and
CC cyclohydrolase activities and a larger C-terminal part containing
CC formyl-THF synthetase activity. {ECO:0000305|PubMed:3514599}.
CC -!- MISCELLANEOUS: Present with 35600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the tetrahydrofolate
CC dehydrogenase/cyclohydrolase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the formate--
CC tetrahydrofolate ligase family. {ECO:0000305}.
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DR EMBL; M12878; AAA66316.1; -; Genomic_DNA.
DR EMBL; Z49133; CAA88997.1; -; Genomic_DNA.
DR EMBL; Z72989; CAA97231.1; -; Genomic_DNA.
DR EMBL; AY692966; AAT92985.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08297.1; -; Genomic_DNA.
DR PIR; A29550; A29550.
DR RefSeq; NP_011720.3; NM_001181333.3.
DR AlphaFoldDB; P07245; -.
DR SMR; P07245; -.
DR BioGRID; 33457; 67.
DR DIP; DIP-3867N; -.
DR IntAct; P07245; 14.
DR MINT; P07245; -.
DR STRING; 4932.YGR204W; -.
DR iPTMnet; P07245; -.
DR MaxQB; P07245; -.
DR PaxDb; P07245; -.
DR PRIDE; P07245; -.
DR EnsemblFungi; YGR204W_mRNA; YGR204W; YGR204W.
DR GeneID; 853118; -.
DR KEGG; sce:YGR204W; -.
DR SGD; S000003436; ADE3.
DR VEuPathDB; FungiDB:YGR204W; -.
DR eggNOG; KOG4230; Eukaryota.
DR HOGENOM; CLU_003601_2_0_1; -.
DR InParanoid; P07245; -.
DR OMA; TATESEX; -.
DR BioCyc; YEAST:YGR204W-MON; -.
DR BRENDA; 3.5.4.9; 984.
DR BRENDA; 6.3.4.3; 984.
DR Reactome; R-SCE-196757; Metabolism of folate and pterines.
DR UniPathway; UPA00193; -.
DR PRO; PR:P07245; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P07245; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004329; F:formate-tetrahydrofolate ligase activity; IMP:SGD.
DR GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; IMP:SGD.
DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IMP:SGD.
DR GO; GO:0006760; P:folic acid-containing compound metabolic process; IMP:SGD.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IMP:SGD.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IBA:GO_Central.
DR CDD; cd00477; FTHFS; 1.
DR CDD; cd01080; NAD_bind_m-THF_DH_Cyclohyd; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_01543; FTHFS; 1.
DR HAMAP; MF_01576; THF_DHG_CYH; 1.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR000559; Formate_THF_ligase.
DR InterPro; IPR020628; Formate_THF_ligase_CS.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000672; THF_DH/CycHdrlase.
DR InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom.
DR InterPro; IPR020867; THF_DH/CycHdrlase_CS.
DR InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom.
DR Pfam; PF01268; FTHFS; 1.
DR Pfam; PF00763; THF_DHG_CYH; 1.
DR Pfam; PF02882; THF_DHG_CYH_C; 1.
DR PRINTS; PR00085; THFDHDRGNASE.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR PROSITE; PS00721; FTHFS_1; 1.
DR PROSITE; PS00722; FTHFS_2; 1.
DR PROSITE; PS00766; THF_DHG_CYH_1; 1.
DR PROSITE; PS00767; THF_DHG_CYH_2; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; ATP-binding; Cytoplasm; Direct protein sequencing;
KW Histidine biosynthesis; Hydrolase; Ligase; Methionine biosynthesis;
KW Multifunctional enzyme; NADP; Nucleotide-binding; Nucleus;
KW One-carbon metabolism; Oxidoreductase; Phosphoprotein; Purine biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:329838,
FT ECO:0000269|PubMed:3514599"
FT CHAIN 2..946
FT /note="C-1-tetrahydrofolate synthase, cytoplasmic"
FT /id="PRO_0000199326"
FT REGION 2..319
FT /note="Methylenetetrahydrofolate dehydrogenase and
FT cyclohydrolase"
FT /evidence="ECO:0000305|PubMed:3514599"
FT REGION 320..946
FT /note="Formyltetrahydrofolate synthetase"
FT /evidence="ECO:0000305|PubMed:3514599"
FT BINDING 51..55
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 98..100
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 169..171
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 277..281
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 384..391
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 318
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 11
FT /note="C->S: Almost no effect on activity."
FT /evidence="ECO:0000269|PubMed:2541774"
FT MUTAGEN 144
FT /note="C->S: Cyclohydrolase activity is reduced 20-fold.
FT Dehydrogenase Km is increased 7-fold."
FT /evidence="ECO:0000269|PubMed:2541774"
FT MUTAGEN 257
FT /note="C->S: Cyclohydrolase activity is increased 2-fold.
FT Dehydrogenase Km is increased 2-fold."
FT /evidence="ECO:0000269|PubMed:2541774"
FT CONFLICT 4
FT /note="Q -> P (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 946 AA; 102205 MW; BC2897EC380CBA6F CRC64;
MAGQVLDGKA CAQQFRSNIA NEIKSIQGHV PGFAPNLAII QVGNRPDSAT YVRMKRKAAE
EAGIVANFIH LDESATEFEV LRYVDQLNED PHTHGIIVQL PLPAHLDEDR ITSRVLAEKD
VDGFGPTNIG ELNKKNGHPF FLPCTPKGII ELLHKANVTI EGSRSVVIGR SDIVGSPVAE
LLKSLNSTVT ITHSKTRDIA SYLHDADIVV VAIGQPEFVK GEWFKPRDGT SSDKKTVVID
VGTNYVADPS KKSGFKCVGD VEFNEAIKYV HLITPVPGGV GPMTVAMLMQ NTLIAAKRQM
EESSKPLQIP PLPLKLLTPV PSDIDISRAQ QPKLINQLAQ ELGIYSHELE LYGHYKAKIS
PKVIERLQTR QNGKYILVSG ITPTPLGEGK STTTMGLVQA LTAHLGKPAI ANVRQPSLGP
TLGVKGGAAG GGYSQVIPMD EFNLHLTGDI HAIGAANNLL AAAIDTRMFH ETTQKNDATF
YNRLVPRKNG KRKFTPSMQR RLNRLGIQKT NPDDLTPEEI NKFARLNIDP DTITIKRVVD
INDRMLRQIT IGQAPTEKNH TRVTGFDITV ASELMAILAL SKDLRDMKER IGRVVVAADV
NRSPVTVEDV GCTGALTALL RDAIKPNLMQ TLEGTPVLVH AGPFANISIG ASSVIADRVA
LKLVGTEPEA KTEAGYVVTE AGFDFTMGGE RFFNIKCRSS GLTPNAVVLV ATVRALKSHG
GAPDVKPGQP LPSAYTEENI EFVEKGAANM CKQIANIKQF GVPVVVAINK FETDTEGEIA
AIRKAALEAG AFEAVTSNHW AEGGKGAIDL AKAVIEASNQ PVDFHFLYDV NSSVEDKLTT
IVQKMYGGAA IDILPEAQRK IDMYKEQGFG NLPICIAKTQ YSLSHDATLK GVPTGFTFPI
RDVRLSNGAG YLYALAAEIQ TIPGLATYAG YMAVEVDDDG EIDGLF
