SYH_YEAST
ID SYH_YEAST Reviewed; 546 AA.
AC P07263; D6W443; Q12095;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Histidine--tRNA ligase, mitochondrial;
DE EC=6.1.1.21;
DE AltName: Full=Histidyl-tRNA synthetase;
DE Short=HisRS;
DE Flags: Precursor;
GN Name=HTS1; OrderedLocusNames=YPR033C; ORFNames=YP9367.13C;
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], FUNCTION, AND ALTERNATIVE INITIATION.
RX PubMed=3521891; DOI=10.1016/0092-8674(86)90740-3;
RA Natsoulis G., Hilger F., Fink G.R.;
RT "The HTS1 gene encodes both the cytoplasmic and mitochondrial histidine
RT tRNA synthetases of S. cerevisiae.";
RL Cell 46:235-243(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
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 [4]
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 [5]
RP FUNCTION, ALTERNATIVE INITIATION, AND SUBCELLULAR LOCATION.
RX PubMed=1459448; DOI=10.1093/genetics/132.4.987;
RA Chiu M.I., Mason T.L., Fink G.R.;
RT "HTS1 encodes both the cytoplasmic and mitochondrial histidyl-tRNA
RT synthetase of Saccharomyces cerevisiae: mutations alter the specificity of
RT compartmentation.";
RL Genetics 132:987-1001(1992).
RN [6]
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 [7]
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 [8]
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 198-LEU--LYS-207; LEU-198 AND
RP VAL-381.
RX PubMed=21464306; DOI=10.1073/pnas.1103471108;
RA Pierce S.B., Chisholm K.M., Lynch E.D., Lee M.K., Walsh T., Opitz J.M.,
RA Li W., Klevit R.E., King M.C.;
RT "Mutations in mitochondrial histidyl tRNA synthetase HARS2 cause ovarian
RT dysgenesis and sensorineural hearing loss of Perrault syndrome.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:6543-6548(2011).
CC -!- FUNCTION: Catalyzes the aminoacylation of histidyl-tRNA in both the
CC cytoplasm and the mitochondrion. {ECO:0000269|PubMed:1459448,
CC ECO:0000269|PubMed:3521891}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-
CC histidyl-tRNA(His); Xref=Rhea:RHEA:17313, Rhea:RHEA-COMP:9665,
CC Rhea:RHEA-COMP:9689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57595, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78527, ChEBI:CHEBI:456215; EC=6.1.1.21;
CC -!- SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Mitochondrial;
CC IsoId=P07263-1; Sequence=Displayed;
CC Name=Cytoplasmic;
CC IsoId=P07263-2; Sequence=VSP_018907;
CC -!- DISRUPTION PHENOTYPE: Lethal. {ECO:0000269|PubMed:21464306}.
CC -!- MISCELLANEOUS: Present with 26800 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: [Isoform Cytoplasmic]: Produced by alternative
CC initiation at Met-21 of isoform Mitochondrial. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; M14048; AAA34695.1; -; Genomic_DNA.
DR EMBL; M14048; AAA34696.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA94983.1; -; Genomic_DNA.
DR EMBL; Z49274; CAA89287.1; -; Genomic_DNA.
DR EMBL; AY692751; AAT92770.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11459.1; -; Genomic_DNA.
DR PIR; S54507; SYBYHM.
DR RefSeq; NP_015358.1; NM_001184130.1. [P07263-1]
DR AlphaFoldDB; P07263; -.
DR SMR; P07263; -.
DR BioGRID; 36211; 161.
DR DIP; DIP-3909N; -.
DR IntAct; P07263; 6.
DR MINT; P07263; -.
DR STRING; 4932.YPR033C; -.
DR iPTMnet; P07263; -.
DR MaxQB; P07263; -.
DR PaxDb; P07263; -.
DR PeptideAtlas; P07263; -.
DR PRIDE; P07263; -.
DR EnsemblFungi; YPR033C_mRNA; YPR033C; YPR033C. [P07263-1]
DR GeneID; 856145; -.
DR KEGG; sce:YPR033C; -.
DR SGD; S000006237; HTS1.
DR VEuPathDB; FungiDB:YPR033C; -.
DR eggNOG; KOG1936; Eukaryota.
DR GeneTree; ENSGT00390000005922; -.
DR HOGENOM; CLU_025113_4_0_1; -.
DR InParanoid; P07263; -.
DR OMA; CDFDFIG; -.
DR BioCyc; YEAST:G3O-34192-MON; -.
DR BRENDA; 6.1.1.21; 984.
DR PRO; PR:P07263; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P07263; protein.
DR GO; GO:0005737; C:cytoplasm; IMP:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IMP:SGD.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004821; F:histidine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; IDA:SGD.
DR GO; GO:0032543; P:mitochondrial translation; IGI:SGD.
DR CDD; cd00773; HisRS-like_core; 1.
DR CDD; cd00859; HisRS_anticodon; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR015807; His-tRNA-ligase.
DR InterPro; IPR041715; HisRS-like_core.
DR InterPro; IPR004516; HisRS/HisZ.
DR InterPro; IPR033656; HisRS_anticodon.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00442; hisS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW Ligase; Mitochondrion; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..20
FT /note="Mitochondrion"
FT CHAIN 21..546
FT /note="Histidine--tRNA ligase, mitochondrial"
FT /id="PRO_0000035804"
FT BINDING 129..131
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT BINDING 156
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT BINDING 172
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT BINDING 176
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT BINDING 326
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT BINDING 330..331
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT VAR_SEQ 1..20
FT /note="Missing (in isoform Cytoplasmic)"
FT /evidence="ECO:0000305"
FT /id="VSP_018907"
FT MUTAGEN 198..207
FT /note="Missing: Does not rescue the lethal phenotype of the
FT deletion mutant."
FT /evidence="ECO:0000269|PubMed:21464306"
FT MUTAGEN 198
FT /note="L->V: Rescues the lethal phenotype of the deletion
FT mutant."
FT /evidence="ECO:0000269|PubMed:21464306"
FT MUTAGEN 381
FT /note="V->L: Partially rescues the lethal phenotype of the
FT deletion mutant."
FT /evidence="ECO:0000269|PubMed:21464306"
FT CONFLICT 476..478
FT /note="AAE -> TTK (in Ref. 1; AAA34695/AAA34696)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 546 AA; 59953 MW; 8BDCCEAB4DD73973 CRC64;
MLSRSLNKVV TSIKSSSIIR MSSATAAATS APTANAANAL KASKAPKKGK LQVSLKTPKG
TKDWADSDMV IREAIFSTLS GLFKKHGGVT IDTPVFELRE ILAGKYGEDS KLIYNLEDQG
GELCSLRYDL TVPFARYVAM NNIQSIKRYH IAKVYRRDQP AMTKGRMREF YQCDFDVAGT
FESMVPDSEC LSILVEGLTS LGIKDFKIKL NHRKILDGIF QIAGVKDEDV RKISSAVDKL
DKSPWEAVKK EMTEEKGQSE ETADKIGEYV KLNGSLKEIH AVLSADANIT SNEKAKQGLD
DIATLMKYTE AFDIDSFISF DLSLARGLDY YTGLIYEVVT SASAPPENAS ELKKKAKSAE
DASEFVGVGS IAAGGRYDNL VNMFSEASGK KSTQIPCVGI SFGVERIFSL IKQRINSSTT
IKPTATQVFV MAFGGGKDWT GYLPERMKVT KQLWDAGIEA EYVYKAKANP RKQFDAAEKA
GCHIAVILGK EEYLEGKLRV KRLGQEFADD DGELVSAADI VPIVQEKLSQ IHEDGLNEVT
RLIKGL
