ID   SYHM_BOVIN              Reviewed;         506 AA.
AC   A5D7V9;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Histidine--tRNA ligase, mitochondrial;
DE            EC=6.1.1.21 {ECO:0000250|UniProtKB:P49590};
DE   AltName: Full=Histidyl-tRNA synthetase;
DE            Short=HisRS;
DE   Flags: Precursor;
GN   Name=HARS2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mitochondrial aminoacyl-tRNA synthetase that catalyzes the
CC       ATP-dependent ligation of histidine to the 3'-end of its cognate tRNA,
CC       via the formation of an aminoacyl-adenylate intermediate (His-AMP).
CC       {ECO:0000250|UniProtKB:P49590}.
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         Evidence={ECO:0000250|UniProtKB:P49590};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P49590}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P49590}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; BC140699; AAI40700.1; -; mRNA.
DR   RefSeq; NP_001091602.1; NM_001098133.2.
DR   AlphaFoldDB; A5D7V9; -.
DR   SMR; A5D7V9; -.
DR   STRING; 9913.ENSBTAP00000035214; -.
DR   PaxDb; A5D7V9; -.
DR   PRIDE; A5D7V9; -.
DR   GeneID; 615182; -.
DR   KEGG; bta:615182; -.
DR   CTD; 23438; -.
DR   eggNOG; KOG1936; Eukaryota.
DR   InParanoid; A5D7V9; -.
DR   OrthoDB; 1065556at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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:0042802; F:identical protein binding; IBA:GO_Central.
DR   GO; GO:0006427; P:histidyl-tRNA aminoacylation; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW   Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..33
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..506
FT                   /note="Histidine--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000341688"
FT   BINDING         131..133
FT                   /ligand="L-histidine"
FT                   /ligand_id="ChEBI:CHEBI:57595"
FT                   /evidence="ECO:0000250|UniProtKB:P12081"
FT   BINDING         158
FT                   /ligand="L-histidine"
FT                   /ligand_id="ChEBI:CHEBI:57595"
FT                   /evidence="ECO:0000250|UniProtKB:P12081"
FT   BINDING         174
FT                   /ligand="L-histidine"
FT                   /ligand_id="ChEBI:CHEBI:57595"
FT                   /evidence="ECO:0000250|UniProtKB:P12081"
FT   BINDING         178
FT                   /ligand="L-histidine"
FT                   /ligand_id="ChEBI:CHEBI:57595"
FT                   /evidence="ECO:0000250|UniProtKB:P12081"
FT   BINDING         327
FT                   /ligand="L-histidine"
FT                   /ligand_id="ChEBI:CHEBI:57595"
FT                   /evidence="ECO:0000250|UniProtKB:P12081"
FT   BINDING         331..332
FT                   /ligand="L-histidine"
FT                   /ligand_id="ChEBI:CHEBI:57595"
FT                   /evidence="ECO:0000250|UniProtKB:P12081"
FT   MOD_RES         67
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P49590"
FT   MOD_RES         444
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P49590"
SQ   SEQUENCE   506 AA;  56914 MW;  3341230ACA738598 CRC64;
     MPQLGLLPGR AWTVLLGLLR PPPGALCIRA VRSHSQVAEA LFASQLKPHQ EKSNFTIKTP
     KGTRDLSPQQ MVVREKILDV VVSCFKRHGA KGLDTPAFEL KEILTEKYGE DSGLIYDLKD
     QGGELLSLRY DLTVPFARYL AMNKVKKMKR YHVGKVWRRE SPTIVQGRYR EFYQCDFDIA
     GQFDPMIPDA ECLKIMCEIL SGLHLGDFLI KVSDRRILDG IFAVCGVPES KFHAICSSVD
     KLDKISWKDV RHEMVVKKGL APEVADRIGD YVQCHGGISL VEQMFQDPRL SQNKQALEGL
     GDLKLLFEYL TLFGVAEKVS FDLSLARGLD YYTGVIYEAV LLQTPVHAEE EPLNMGSVAA
     GGRYDGLVGM FDPRGHKVPC VGLSIGVERI FSIVEQRIKT FGEKIRTTET QVFVATPQKN
     FLQERLKLIA ELWDAGIKAE LMYKNNPKLL PQLHYCENMG IPLVVIIGEQ ELKEGVIKLR
     SVASREEVAI KRENLVAEIQ KRLSES