ID   SYH_CERSK               Reviewed;         494 AA.
AC   B9KU51;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 71.
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};
GN   OrderedLocusNames=RSKD131_3719;
OS   Cereibacter sphaeroides (strain KD131 / KCTC 12085) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=557760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KD131 / KCTC 12085;
RX   PubMed=19028901; DOI=10.1128/jb.01565-08;
RA   Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K.;
RT   "Complete genome sequence of Rhodobacter sphaeroides KD131.";
RL   J. Bacteriol. 191:1118-1119(2009).
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; CP001151; ACM03579.1; -; Genomic_DNA.
DR   RefSeq; WP_012641234.1; NC_011958.1.
DR   AlphaFoldDB; B9KU51; -.
DR   SMR; B9KU51; -.
DR   EnsemblBacteria; ACM03579; ACM03579; RSKD131_3719.
DR   GeneID; 67449030; -.
DR   KEGG; rsk:RSKD131_3719; -.
DR   HOGENOM; CLU_025113_3_2_5; -.
DR   OMA; CDFDFIG; -.
DR   Proteomes; UP000001597; Chromosome 2.
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; 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.
FT   CHAIN           1..494
FT                   /note="Histidine--tRNA ligase"
FT                   /id="PRO_1000199147"
SQ   SEQUENCE   494 AA;  53454 MW;  85AB6EAB5FD4C3B6 CRC64;
     MAKDKASRRP RAETPKGFRD YFGADVTERK AMLDAVAEVY HRYGFDPLET SAVETVEALG
     KFLPDVDRPN EGVFGWQDED GDWLALRYDL TAPLARVAAQ FRNDLPSPYR RYAMGPVWRN
     EKPGPGRFRQ FYQCDADTVG SASVAADAEI CAMLSDALEV VGIPRGDYIV RVNNRKVLNG
     VMEVAGVLDP SDPAKFEAER GIVLRAIDKI DRLGKTGVRA LLGAGRKDES GDFTKGAGLS
     DEQAEVVMGF MAAKRDTGAA TAARLRELVG ASTLGCEGVQ ELETIAELLD AQGYGPDRIV
     VDPSVVRGLG YYTGPVFEAE LTFEILDEKG RKRQFGSVAG GGRYDDLVKR FTGQSVPATG
     VSIGVDRLLA ALRAKGRAGA EAQGPVVVTV MDRDRMGDYM AMVGELRRAG LRAELYLGNP
     KNFGNQLKYA DARKSPVAVI QGSDEATRGV VVLKDLVLGA QIAAGASLEE WKSRPAQVEV
     PRADLVRAVQ DMLS