ID   SYH_AZOPC               Reviewed;         458 AA.
AC   B6YS23;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   25-MAY-2022, entry version 67.
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=CFPG_732;
OS   Azobacteroides pseudotrichonymphae genomovar. CFP2.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC   Candidatus Azobacteroides.
OX   NCBI_TaxID=511995;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19008447; DOI=10.1126/science.1165578;
RA   Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., Kudo T.,
RA   Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT   "Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT
RT   protist cells in termite gut.";
RL   Science 322:1108-1109(2008).
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; AP010656; BAG83995.1; -; Genomic_DNA.
DR   RefSeq; WP_012573751.1; NC_011565.1.
DR   AlphaFoldDB; B6YS23; -.
DR   SMR; B6YS23; -.
DR   STRING; 511995.CFPG_732; -.
DR   EnsemblBacteria; BAG83995; BAG83995; CFPG_732.
DR   KEGG; aps:CFPG_732; -.
DR   eggNOG; COG0124; Bacteria.
DR   HOGENOM; CLU_025113_3_0_10; -.
DR   OMA; YQIQKVW; -.
DR   OrthoDB; 277998at2; -.
DR   Proteomes; UP000000723; 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   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; 2.
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..458
FT                   /note="Histidine--tRNA ligase"
FT                   /id="PRO_1000095528"
SQ   SEQUENCE   458 AA;  52096 MW;  9347498D4104EA8A CRC64;
     MQKLSIPKGT RDFTPCEMDK RNYIFDTIRS VFYLYGFKQI ETPALENLST LLGKYGEEND
     KLLFKILNSG DFISKVNPID WNNHQLSKLT KQISKKGLRY DLTLPLARFV VMHRNEITFP
     FKRFQIQPVW RSDRPQKGRY REFVQCDADI VGSDSLLNEV ELIQIIDEVF HRLSISISIK
     INNRKILNGI AEIISEEKKI TDITTAMDKL DKVGLTKVNE ELLQKGISIQ AIDQLQPFFL
     LKGSNQNKIS TLKNILSTSP IGIKGLQEIE TIFNKLNLIP TRNTIKFDLT LARGLNYYTG
     TIFEVKCLNV PIGSVLGGGR YDNLTNIFGL SNLSGVGISF GADRIFDILN QLNLYPNTNA
     SHTQILFVNL GEKGVDFILP VLFSLRKVGI NAELYPHNTK IKKQLSYAHN NQIPFVAIVG
     STEIAENKIT IKDMRSCSQF SIALDKLINF FQYERQSV