HARS1_BOVIN
ID HARS1_BOVIN Reviewed; 509 AA.
AC Q2KI84;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
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;
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=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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; BC112731; AAI12732.1; -; mRNA.
DR RefSeq; NP_001039531.1; NM_001046066.2.
DR AlphaFoldDB; Q2KI84; -.
DR SMR; Q2KI84; -.
DR STRING; 9913.ENSBTAP00000025094; -.
DR PaxDb; Q2KI84; -.
DR PeptideAtlas; Q2KI84; -.
DR PRIDE; Q2KI84; -.
DR Ensembl; ENSBTAT00000025094; ENSBTAP00000025094; ENSBTAG00000018847.
DR GeneID; 510937; -.
DR KEGG; bta:510937; -.
DR CTD; 3035; -.
DR VEuPathDB; HostDB:ENSBTAG00000018847; -.
DR VGNC; VGNC:29753; HARS1.
DR eggNOG; KOG1936; Eukaryota.
DR GeneTree; ENSGT00390000005922; -.
DR HOGENOM; CLU_025113_4_2_1; -.
DR InParanoid; Q2KI84; -.
DR OMA; CDFDFIG; -.
DR OrthoDB; 1065556at2759; -.
DR TreeFam; TF300652; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000018847; Expressed in Ammon's horn and 102 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0004821; F:histidine-tRNA ligase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; ISS:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; 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 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 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 TIGRFAMs; TIGR00442; hisS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS00762; WHEP_TRS_1; 1.
DR PROSITE; PS51185; WHEP_TRS_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT CHAIN 2..509
FT /note="Histidine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000245021"
FT DOMAIN 3..59
FT /note="WHEP-TRS"
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 173
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 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99KK9"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12081"
SQ SEQUENCE 509 AA; 57285 MW; 54A2CAFD638D4358 CRC64;
MADRAALEDL VRVQGERVRG LKQQKASAEQ IEEEVAKLLK LKAQLGPDEG KPKFVLKTPK
GTRDYSPRQM AVREKVFDVI ISCFKRHGAE VIDTPVFELK ETLTGKYGED SKLIYDLKDQ
GGELLSLRYD LTVPFARYLA MNKLTNIKRY HIAKVYRRDN PAMTRGRYRE FYQCDFDIAG
QFDPMLPDAE CLKIMCEILS SLQIGDFLVK VNDRRILDGM FAICGVPDSK FRTICSSVDK
LDKVSWEEVK NEMVGEKGLA PEVADRIGDY VQQHGGVSLV EQLLQDPKLS QNKQALEGLG
DLKLLFEYLT LFGIADKISF DLSLARGLDY YTGVIYEAVL LQPPARAGEE PLGVGSVAAG
GRYDGLVGMF DPKGRKVPCV GLSIGVERIF SIVEQRLEAL EEKVRTTETQ VLVASAQKKL
LEERLKLISE LWDAGIKAEL LYKKNPKLLN QLQYCEETGI PLVAIIGEQE LKDGVIKLRS
VASREEVDVR REDLVEEIKR RTSQPLCIC
