ID   SYDC_YEAST              Reviewed;         557 AA.
AC   P04802; D6VXY6;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 228.
DE   RecName: Full=Aspartate--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.12;
DE   AltName: Full=Aspartyl-tRNA synthetase;
DE            Short=AspRS;
GN   Name=DPS1; Synonyms=APS, APS1; OrderedLocusNames=YLL018C;
GN   ORFNames=L1295;
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].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=3278298; DOI=10.1093/nar/16.3.1212;
RA   Reid G.A.;
RT   "Sequence polymorphisms in the yeast gene encoding aspartyl tRNA
RT   synthase.";
RL   Nucleic Acids Res. 16:1212-1212(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3513127; DOI=10.1093/nar/14.4.1657;
RA   Sellami M., Fasiolo F., Dirheimer G., Ebel J.-P., Gangloff J.;
RT   "Nucleotide sequence of the gene coding for yeast cytoplasmic aspartyl-tRNA
RT   synthetase (APS); mapping of the 5' and 3' termini of AspRS mRNA.";
RL   Nucleic Acids Res. 14:1657-1666(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9046100;
RX   DOI=10.1002/(sici)1097-0061(199702)13:2<183::aid-yea65>3.0.co;2-v;
RA   Purnelle B., Goffeau A.;
RT   "The sequence of 32kb on the left arm of yeast chromosome XII reveals six
RT   known genes, a new member of the seripauperins family and a new ABC
RT   transporter homologous to the human multidrug resistance protein.";
RL   Yeast 13:183-188(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [5]
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   [6]
RP   PROTEIN SEQUENCE OF 2-557.
RX   PubMed=3902099; DOI=10.1016/s0300-9084(85)80200-5;
RA   Amiri I., Mejdoub H., Hounwanou N., Boulanger Y., Reinbolt J.;
RT   "The complete amino acid sequence of cytoplasmic aspartyl-tRNA synthetase
RT   from Saccharomyces cerevisiae.";
RL   Biochimie 67:607-613(1985).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81.
RC   STRAIN=ATCC 90840 / EAY235 / FY23;
RX   PubMed=8810043;
RX   DOI=10.1002/(sici)1097-0061(19960615)12:7<693::aid-yea956>3.0.co;2-g;
RA   Miosga T., Zimmermann F.K.;
RT   "Sequence analysis of the CEN12 region of Saccharomyces cerevisiae on a
RT   43.7 kb fragment of chromosome XII including an open reading frame
RT   homologous to the human cystic fibrosis transmembrane conductance regulator
RT   protein CFTR.";
RL   Yeast 12:693-708(1996).
RN   [8]
RP   PARTIAL PROTEIN SEQUENCE, AND MUTAGENESIS.
RX   PubMed=2021621; DOI=10.1021/bi00231a026;
RA   Gasparini S., Vincendon P., Eriani G., Gangloff J., Boulanger Y.,
RA   Reinbolt J., Kern D.;
RT   "Identification of structurally and functionally important histidine
RT   residues in cytoplasmic aspartyl-tRNA synthetase from Saccharomyces
RT   cerevisiae.";
RL   Biochemistry 30:4284-4289(1991).
RN   [9]
RP   MUTAGENESIS OF PRO-273.
RX   PubMed=8248175; DOI=10.1073/pnas.90.22.10816;
RA   Eriani G., Cavarelli J., Martin F., Dirheimer G., Moras D., Gangloff J.;
RT   "Role of dimerization in yeast aspartyl-tRNA synthetase and importance of
RT   the class II invariant proline.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:10816-10820(1993).
RN   [10]
RP   ACETYLATION AT SER-2.
RX   PubMed=9298649; DOI=10.1002/elps.1150180810;
RA   Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,
RA   Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R.,
RA   Payne W.E.;
RT   "Proteome studies of Saccharomyces cerevisiae: identification and
RT   characterization of abundant proteins.";
RL   Electrophoresis 18:1347-1360(1997).
RN   [11]
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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, AND IDENTIFICATION BY
RP   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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-301 AND SER-502, AND
RP   IDENTIFICATION BY 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   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301 AND SER-502, 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   [16]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX   PubMed=2047877; DOI=10.1126/science.2047877;
RA   Ruff M., Krishnaswamy S., Boeglin M., Poterszman A., Mitschler A.,
RA   Podjarny A., Rees B., Thierry J.-C., Moras D.;
RT   "Class II aminoacyl transfer RNA synthetases: crystal structure of yeast
RT   aspartyl-tRNA synthetase complexed with tRNA(Asp).";
RL   Science 252:1682-1689(1991).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), AND MUTAGENESIS.
RX   PubMed=8313877; DOI=10.1002/j.1460-2075.1994.tb06265.x;
RA   Cavarelli J., Eriani G., Rees B., Ruff M., Boeglin M., Mitschler A.,
RA   Martin F., Gangloff J., Thierry J.-C., Moras D.;
RT   "The active site of yeast aspartyl-tRNA synthetase: structural and
RT   functional aspects of the aminoacylation reaction.";
RL   EMBO J. 13:327-337(1994).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-
CC         aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660,
CC         Rhea:RHEA-COMP:9678, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516,
CC         ChEBI:CHEBI:456215; EC=6.1.1.12;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: Present with 5750 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Type 2 subfamily. {ECO:0000305}.
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DR   EMBL; X03606; CAA27269.1; -; Genomic_DNA.
DR   EMBL; X06665; CAA29865.1; -; Genomic_DNA.
DR   EMBL; X97560; CAA66172.1; -; Genomic_DNA.
DR   EMBL; Z73123; CAA97464.1; -; Genomic_DNA.
DR   EMBL; Z73122; CAA97463.1; -; Genomic_DNA.
DR   EMBL; X91488; CAA62772.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09302.1; -; Genomic_DNA.
DR   PIR; A23508; SYBYDC.
DR   RefSeq; NP_013083.1; NM_001181838.1.
DR   PDB; 1ASY; X-ray; 2.90 A; A/B=68-557.
DR   PDB; 1ASZ; X-ray; 3.00 A; A/B=68-557.
DR   PDB; 1EOV; X-ray; 2.30 A; A=71-557.
DR   PDBsum; 1ASY; -.
DR   PDBsum; 1ASZ; -.
DR   PDBsum; 1EOV; -.
DR   AlphaFoldDB; P04802; -.
DR   SMR; P04802; -.
DR   BioGRID; 31235; 152.
DR   DIP; DIP-4093N; -.
DR   IntAct; P04802; 17.
DR   MINT; P04802; -.
DR   STRING; 4932.YLL018C; -.
DR   CarbonylDB; P04802; -.
DR   GlyGen; P04802; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P04802; -.
DR   MaxQB; P04802; -.
DR   PaxDb; 4932-YLL018C; -.
DR   PeptideAtlas; P04802; -.
DR   EnsemblFungi; YLL018C_mRNA; YLL018C; YLL018C.
DR   GeneID; 850643; -.
DR   KEGG; sce:YLL018C; -.
DR   AGR; SGD:S000003941; -.
DR   SGD; S000003941; DPS1.
DR   VEuPathDB; FungiDB:YLL018C; -.
DR   eggNOG; KOG0556; Eukaryota.
DR   GeneTree; ENSGT01030000234618; -.
DR   HOGENOM; CLU_004553_2_1_1; -.
DR   InParanoid; P04802; -.
DR   OMA; WVHEIRD; -.
DR   OrthoDB; 382728at2759; -.
DR   BioCyc; YEAST:G3O-32123-MONOMER; -.
DR   BRENDA; 6.1.1.12; 984.
DR   SABIO-RK; P04802; -.
DR   BioGRID-ORCS; 850643; 1 hit in 10 CRISPR screens.
DR   EvolutionaryTrace; P04802; -.
DR   PRO; PR:P04802; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P04802; Protein.
DR   GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0004815; F:aspartate-tRNA ligase activity; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IDA:SGD.
DR   GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IDA:SGD.
DR   CDD; cd04320; AspRS_cyto_N; 1.
DR   CDD; cd00776; AsxRS_core; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   HAMAP; MF_02075; Asp_tRNA_synth_type2; 1.
DR   InterPro; IPR004364; Aa-tRNA-synt_II.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004523; Asp-tRNA_synthase_2.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   NCBIfam; TIGR00458; aspS_nondisc; 1.
DR   PANTHER; PTHR43450:SF1; ASPARTATE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR43450; ASPARTYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding;
KW   Cytoplasm; Direct protein sequencing; Ligase; Nucleotide-binding;
KW   Phosphoprotein; Protein biosynthesis; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:3902099,
FT                   ECO:0000269|PubMed:9298649"
FT   CHAIN           2..557
FT                   /note="Aspartate--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000111014"
FT   REGION          1..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          303..306
FT                   /note="Aspartate"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        28..71
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         281
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         325..327
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         325
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         333..335
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         478
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         481
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         485
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         528..531
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:9298649"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         301
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         502
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         546
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MUTAGEN         273
FT                   /note="P->G: Loss of activity; important for dimerization."
FT                   /evidence="ECO:0000269|PubMed:8248175"
FT   STRAND          73..77
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   HELIX           85..87
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   HELIX           96..98
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   TURN            101..106
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   STRAND          108..120
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   STRAND          122..132
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   STRAND          135..142
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   STRAND          145..149
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   HELIX           151..157
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   STRAND          165..174
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   STRAND          182..198
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   HELIX           208..211
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   HELIX           215..220
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   HELIX           228..233
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   HELIX           235..238
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   HELIX           242..264
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   STRAND          274..278
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   STRAND          280..284
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   STRAND          288..291
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   STRAND          294..298
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   HELIX           303..311
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   STRAND          316..324
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   STRAND          331..333
FT                   /evidence="ECO:0007829|PDB:1ASZ"
FT   STRAND          336..346
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   HELIX           352..372
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   HELIX           374..383
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   STRAND          393..395
FT                   /evidence="ECO:0007829|PDB:1ASY"
FT   STRAND          398..401
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   HELIX           402..411
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   STRAND          418..420
FT                   /evidence="ECO:0007829|PDB:1ASY"
FT   HELIX           424..437
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   STRAND          441..446
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   HELIX           450..452
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   STRAND          461..463
FT                   /evidence="ECO:0007829|PDB:1ASZ"
FT   STRAND          466..474
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   STRAND          477..485
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   HELIX           489..498
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   TURN            506..508
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   HELIX           509..515
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   STRAND          522..528
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   HELIX           529..536
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   HELIX           542..545
FT                   /evidence="ECO:0007829|PDB:1EOV"
FT   STRAND          546..548
FT                   /evidence="ECO:0007829|PDB:1ASY"
SQ   SEQUENCE   557 AA;  63516 MW;  6656279B3E9011A5 CRC64;
     MSQDENIVKA VEESAEPAQV ILGEDGKPLS KKALKKLQKE QEKQRKKEER ALQLEAEREA
     REKKAAAEDT AKDNYGKLPL IQSRDSDRTG QKRVKFVDLD EAKDSDKEVL FRARVHNTRQ
     QGATLAFLTL RQQASLIQGL VKANKEGTIS KNMVKWAGSL NLESIVLVRG IVKKVDEPIK
     SATVQNLEIH ITKIYTISET PEALPILLED ASRSEAEAEA AGLPVVNLDT RLDYRVIDLR
     TVTNQAIFRI QAGVCELFRE YLATKKFTEV HTPKLLGAPS EGGSSVFEVT YFKGKAYLAQ
     SPQFNKQQLI VADFERVYEI GPVFRAENSN THRHMTEFTG LDMEMAFEEH YHEVLDTLSE
     LFVFIFSELP KRFAHEIELV RKQYPVEEFK LPKDGKMVRL TYKEGIEMLR AAGKEIGDFE
     DLSTENEKFL GKLVRDKYDT DFYILDKFPL EIRPFYTMPD PANPKYSNSY DFFMRGEEIL
     SGAQRIHDHA LLQERMKAHG LSPEDPGLKD YCDGFSYGCP PHAGGGIGLE RVVMFYLDLK
     NIRRASLFPR DPKRLRP
//