ID   HARS1_MESAU             Reviewed;         508 AA.
AC   P07178;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Histidine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.21 {ECO:0000250|UniProtKB:P12081};
DE   AltName: Full=Histidyl-tRNA synthetase;
DE            Short=HisRS;
GN   Name=HARS1; Synonyms=HARS, HRS;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3554142; DOI=10.1093/nar/15.8.3349;
RA   Tsui F.W.L., Siminovitch L.;
RT   "Isolation, structure and expression of mammalian genes for histidyl-tRNA
RT   synthetase.";
RL   Nucleic Acids Res. 15:3349-3367(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-3.
RX   PubMed=3446579; DOI=10.1016/0378-1119(87)90198-3;
RA   Tsui F.W.L., Siminovitch L.;
RT   "Structural analysis of the 5' region of the chromosomal gene for hamster
RT   histidyl-tRNA synthetase.";
RL   Gene 61:349-361(1987).
CC   -!- FUNCTION: Catalyzes the ATP-dependent ligation of histidine to the 3'-
CC       end of its cognate tRNA, via the formation of an aminoacyl-adenylate
CC       intermediate (His-AMP). Plays a role in axon guidance.
CC       {ECO:0000250|UniProtKB:P12081}.
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:P12081};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P12081}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:F1Q5D5}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; X05346; CAA28957.1; -; mRNA.
DR   EMBL; M19147; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P07178; -.
DR   SMR; P07178; -.
DR   PRIDE; P07178; -.
DR   BRENDA; 6.1.1.21; 3239.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0004821; F:histidine-tRNA ligase activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0006427; P:histidyl-tRNA aminoacylation; ISS:UniProtKB.
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; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR036621; Anticodon-bd_dom_sf.
DR   InterPro; IPR041715; HisRS-like_core.
DR   InterPro; IPR004516; HisRS/HisZ.
DR   InterPro; IPR033656; HisRS_anticodon.
DR   InterPro; IPR009068; S15_NS1_RNA-bd.
DR   InterPro; IPR000738; WHEP-TRS_dom.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF13393; tRNA-synt_His; 1.
DR   Pfam; PF00458; WHEP-TRS; 1.
DR   PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR   SMART; SM00991; WHEP-TRS; 1.
DR   SUPFAM; SSF47060; SSF47060; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   PROSITE; PS00762; WHEP_TRS_1; 1.
DR   PROSITE; PS51185; WHEP_TRS_2; 1.
PE   2: Evidence at transcript level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..508
FT                   /note="Histidine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000136333"
FT   DOMAIN          3..59
FT                   /note="WHEP-TRS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00531"
FT   BINDING         130..132
FT                   /ligand="L-histidine"
FT                   /ligand_id="ChEBI:CHEBI:57595"
FT                   /evidence="ECO:0000250|UniProtKB:P12081"
FT   BINDING         157
FT                   /ligand="L-histidine"
FT                   /ligand_id="ChEBI:CHEBI:57595"
FT                   /evidence="ECO:0000250|UniProtKB:P12081"
FT   BINDING         177
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   MOD_RES         66
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99KK9"
SQ   SEQUENCE   508 AA;  57426 MW;  ABDF334CD5551ADC CRC64;
     MASPALEELV LNSRHRLVRG LKQQKASADQ IEEEVAKLLK LKAQLGHDES KQKFVLKTPK
     GTRDYSPRQM AVREKVFDVI ICCFKRHGAE VIDTPVFELK ETLMGKYGQD CKLIYDLKDQ
     GGELLSLRYD LTVPFGRYLA MNNLTNIKRY HIAKVYRRDN PAMTRGRYLN SITVDFDIAG
     QFDPMIPDAE CLKIMCEILS SLQIGKFLVK VNDRRILDGM FAVCGVPDSK FRTICSSVDK
     LDKVSWEEVK NEMVGEKGLA PEVADRIGDY VQQHGEVCLV EQLLQDPKLS QNKQAVEGLG
     DLKLLFEYLT LFGIDDKISF DLSLARGLDY YTGVIYVAVL LQMPTGAGEE PWCGQCGCWR
     RYDGLVGMFD PKGRKVPCVG LSIGVERIFS IVEQRLEALE EKVRTTETQV LVASAQKKLA
     GGETKACLQL WDAGIKAELL YKKNPKLLNQ LQYCEETGIP LVAIIGEQEL KDGVIKLRSV
     ASREEVDVRR EDLVEEIRRR TNQPLYVC