ID   HARS1_TAKRU             Reviewed;         519 AA.
AC   P70076;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 122.
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, hiss;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Testis;
RX   PubMed=8710896; DOI=10.1073/pnas.93.16.8485;
RA   Brenner S., Corrochano L.M.;
RT   "Translocation events in the evolution of aminoacyl-tRNA synthetases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:8485-8489(1996).
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; Z54243; CAA91012.1; -; Genomic_DNA.
DR   RefSeq; XP_011616429.1; XM_011618127.1.
DR   AlphaFoldDB; P70076; -.
DR   SMR; P70076; -.
DR   STRING; 31033.ENSTRUP00000023001; -.
DR   PRIDE; P70076; -.
DR   Ensembl; ENSTRUT00000023098; ENSTRUP00000023002; ENSTRUG00000009144.
DR   eggNOG; KOG1936; Eukaryota.
DR   GeneTree; ENSGT00390000005922; -.
DR   InParanoid; P70076; -.
DR   OMA; CDFDFIG; -.
DR   OrthoDB; 1065556at2759; -.
DR   BRENDA; 6.1.1.21; 6209.
DR   Proteomes; UP000005226; Chromosome 14.
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   HAMAP; MF_00127; His_tRNA_synth; 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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..519
FT                   /note="Histidine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000136337"
FT   BINDING         135..137
FT                   /ligand="L-histidine"
FT                   /ligand_id="ChEBI:CHEBI:57595"
FT                   /evidence="ECO:0000250|UniProtKB:P12081"
FT   BINDING         162
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         182
FT                   /ligand="L-histidine"
FT                   /ligand_id="ChEBI:CHEBI:57595"
FT                   /evidence="ECO:0000250|UniProtKB:P12081"
FT   BINDING         331
FT                   /ligand="L-histidine"
FT                   /ligand_id="ChEBI:CHEBI:57595"
FT                   /evidence="ECO:0000250|UniProtKB:P12081"
FT   BINDING         335..336
FT                   /ligand="L-histidine"
FT                   /ligand_id="ChEBI:CHEBI:57595"
FT                   /evidence="ECO:0000250|UniProtKB:P12081"
SQ   SEQUENCE   519 AA;  57913 MW;  A1CBF5752070759E CRC64;
     MLAMHCARVC SVLMGCRTTT RALSIRSFPG VTLAQIDEEV AKLLELKAHL GGDDGKHQFV
     LKTAKGTRDY NPKQMAIREK VFNTIVSCFK RHGAETIDTP VFELKETLTG KYGEDSKLIY
     DLKDQGGELL SLRYDLTVPF ARYLAMNKIT NIKRYHIAKV YRRDNPAMTR GRYREFYQCD
     FDIAGQYDAM IPDAECLKIV HEILSELDLG DFRIKVNDRR ILDGMFAVCG VPDNMFRTIC
     STVDKLDKLP WEAVKNEMVN EKGLSEEAAD QIGVYVGMQG GMDLAERLLQ DQKMCQSTQA
     CAGLTDIKLL FSYLQLFQVT DKVVFDLSLA RGLDYYTGII YEAILTQAGV APVAPETSNE
     APTEECVTVG SVAGGGRYDG LVGMFDPKGR KVPCVGVSIG IERIFSIMEQ KAEASTEKIR
     TTEVQVMVAA AQKNLLEERL RLITELWNAG IKAELMYKKS PKLLSQLQHC EESGIPLVAI
     LGEQELKNGV VKLRNVATRD EVDISRADLI AEIKKRTSA