ID   SYH_PSEPF               Reviewed;         429 AA.
AC   Q3K7B7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 113.
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=Pfl01_4600;
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1;
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000094; ABA76337.1; -; Genomic_DNA.
DR   RefSeq; WP_011335808.1; NC_007492.2.
DR   AlphaFoldDB; Q3K7B7; -.
DR   SMR; Q3K7B7; -.
DR   STRING; 205922.Pfl01_4600; -.
DR   PRIDE; Q3K7B7; -.
DR   EnsemblBacteria; ABA76337; ABA76337; Pfl01_4600.
DR   KEGG; pfo:Pfl01_4600; -.
DR   eggNOG; COG0124; Bacteria.
DR   HOGENOM; CLU_025113_1_1_6; -.
DR   OMA; CDFDFIG; -.
DR   Proteomes; UP000002704; 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   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.
FT   CHAIN           1..429
FT                   /note="Histidine--tRNA ligase"
FT                   /id="PRO_1000016423"
SQ   SEQUENCE   429 AA;  47997 MW;  BBF933D0B3F80736 CRC64;
     MSKSLQAIRG MNDILPEQTP VWRYFEGTVS RLLDNYGYKQ IRMPIVEFTE LFKRSIGEVT
     DIVEKEMYTF EDRNGDSLTL RPEGTAACVR AVLEHGITGG GQVQKLWYIG PMFRHERPQK
     GRYRQFHQIG LEVFNLDGPD IDAELIIMTW RLWGELGIRD AVKLELNSLG TSESRGRYRE
     ALVEYLSAHH DKLDEDSQRR LKTNPLRVLD TKNADTQAVL VDAPKMADYL DDESRAHFKG
     LKARLDAVGI PYVLNPKLVR GLDYYSKTVF EWVTDKLGAQ GTVCAGGRYD GLVEQMGGKP
     TPGVGFAMGI ERLVLLLETL EQIPEEISRQ VDVYLCAFGE EAELAGLALA ERVRDQLPNL
     RLQVNAGAGS FKSQFKKADK SGALYALILG DDEMAQQVVG FKPLRGQGEQ QSIAWDALAA
     HLATCVVQG