ID   SYH_MYCGA               Reviewed;         419 AA.
AC   Q7NBS9;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Histidine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00127};
DE            EC=6.1.1.21 {ECO:0000255|HAMAP-Rule:MF_00127};
DE   AltName: Full=Histidyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00127};
DE            Short=HisRS {ECO:0000255|HAMAP-Rule:MF_00127};
GN   Name=hisS {ECO:0000255|HAMAP-Rule:MF_00127}; OrderedLocusNames=MYCGA1840;
GN   ORFNames=MGA_0947;
OS   Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS   (Mycoplasmoides gallisepticum).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=710127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R(low / passage 15 / clone 2);
RX   PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA   Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA   Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT   "The complete genome sequence of the avian pathogen Mycoplasma
RT   gallisepticum strain R(low).";
RL   Microbiology 149:2307-2316(2003).
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:0000255|HAMAP-Rule:MF_00127};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00127}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00127}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00127}.
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DR   EMBL; AE015450; AAP56534.2; -; Genomic_DNA.
DR   RefSeq; WP_011113416.1; NC_004829.2.
DR   AlphaFoldDB; Q7NBS9; -.
DR   SMR; Q7NBS9; -.
DR   PRIDE; Q7NBS9; -.
DR   KEGG; mga:MGA_0947; -.
DR   PATRIC; fig|233150.7.peg.201; -.
DR   HOGENOM; CLU_025113_1_1_14; -.
DR   OrthoDB; 277998at2; -.
DR   Proteomes; UP000001418; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00773; HisRS-like_core; 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   PANTHER; PTHR43707; PTHR43707; 1.
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..419
FT                   /note="Histidine--tRNA ligase"
FT                   /id="PRO_0000136197"
SQ   SEQUENCE   419 AA;  49313 MW;  56D14DD0D00F7A02 CRC64;
     MSNKQITAVR GTTDWFDQAM ILFNAISHKI IALSDLYTFQ RIKTPVFEHA ELFSRNLEHS
     DIVKKELYQL IDRSERKLAL RPEGTASIIR AVNEHKLLDQ NPWPLKLYYL EPMFRYERPQ
     KGRMREFYQY GIELVGELDQ LDYLQTILFA KKILDTFNFD CVLNINWLGN FASRKCWVEQ
     LNQYFKQYQD QLSELSVSRL DSYGVLRILD DKNESKKDFV RSAPTIDQFI SLEEQTQFKQ
     LLEQLDQLGI KYKYNSSLVR GLDYYSELVF EFILANNDQA QSTLIGGGCY QNLIAELTNK
     PLKAIGFALS IERFISYLDD KTKDSLINQD QKPRYLLINL VPNKELATLN LSQELINHNY
     QVYYQHKLNK VDKAIKYALR AKFTHLIIMG NDEWSKQTMT IKDLSSQTQQ TIKYKEFIK