ID   SYH_MYCPU               Reviewed;         420 AA.
AC   Q98QM8;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Histidine--tRNA ligase;
DE            EC=6.1.1.21;
DE   AltName: Full=Histidyl-tRNA synthetase;
DE            Short=HisRS;
GN   Name=hisS; OrderedLocusNames=MYPU_3330;
OS   Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=272635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAB CTIP;
RX   PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA   Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA   Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT   "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT   pulmonis.";
RL   Nucleic Acids Res. 29:2145-2153(2001).
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AL445564; CAC13506.1; -; Genomic_DNA.
DR   PIR; E90553; E90553.
DR   RefSeq; WP_010925137.1; NC_002771.1.
DR   AlphaFoldDB; Q98QM8; -.
DR   SMR; Q98QM8; -.
DR   STRING; 272635.MYPU_3330; -.
DR   EnsemblBacteria; CAC13506; CAC13506; CAC13506.
DR   KEGG; mpu:MYPU_3330; -.
DR   eggNOG; COG0124; Bacteria.
DR   HOGENOM; CLU_025113_1_2_14; -.
DR   OMA; CDFDFIG; -.
DR   OrthoDB; 277998at2; -.
DR   BioCyc; MPUL272635:G1GT6-333-MON; -.
DR   Proteomes; UP000000528; 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   HAMAP; MF_00127; His_tRNA_synth; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR015807; His-tRNA-ligase.
DR   InterPro; IPR041715; HisRS-like_core.
DR   InterPro; IPR004516; HisRS/HisZ.
DR   PANTHER; PTHR43707; PTHR43707; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..420
FT                   /note="Histidine--tRNA ligase"
FT                   /id="PRO_0000136206"
SQ   SEQUENCE   420 AA;  49308 MW;  951B094769B34915 CRC64;
     MKFQKLKGTR DYYFQDSNKL EIIRNAFFTS AKKFNFSFLE TPIIENVELF KRTSGDFSDL
     VKKELYSFED KSKRQIALRP EGTAPALRAI VENNLLQKHN KFFYFGPMFR YENPQKGRQR
     QFFSGGIEWL EKQSPFTNIE IIFFAKNFLD TLKIDDYEIV INWIGHPEQR KNYLDHLKNY
     LNQFENQLEE ISKERLKNNA LRILDDKIES QKAFVKNAPK IHDFLPKESL ENFYQLQDLF
     KKFDIKFKVD PFLVRGLDYY SDFVFEFVST NQNLGAQKTL LGGGVYSSLL KELGGENIEG
     IGFGFGLERI MEVIDLNNFK DDAKKITAFA SNEDDLIALL KLRNNFGDLI KIDCINKVVN
     FKKIFKSKQI KESDFLIFKE LNNAQNEVSL KNKFNDQKLV VDLINPNIEN IKKYIKENSD