SYH_RHOPB
ID SYH_RHOPB Reviewed; 519 AA.
AC Q21AX3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=RPC_0893;
OS Rhodopseudomonas palustris (strain BisB18).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316056;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB18;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000301; ABD86463.1; -; Genomic_DNA.
DR RefSeq; WP_011471371.1; NC_007925.1.
DR AlphaFoldDB; Q21AX3; -.
DR SMR; Q21AX3; -.
DR STRING; 316056.RPC_0893; -.
DR EnsemblBacteria; ABD86463; ABD86463; RPC_0893.
DR KEGG; rpc:RPC_0893; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_3_2_5; -.
DR OMA; CDFDFIG; -.
DR OrthoDB; 277998at2; -.
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 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.
FT CHAIN 1..519
FT /note="Histidine--tRNA ligase"
FT /id="PRO_1000016431"
SQ SEQUENCE 519 AA; 57397 MW; 0D6532480ED1EB1A CRC64;
MAEKPKKSQK LRARLPRGLA DRGPAELAAT RAMVETIRAV YERYGFEPVE TPAFEFTDAL
GKFLPDQDRP NEGVFSFQDD DEQWISLRYD LTAPLARYVA ENFDSLPKPY RSYRNGYVYR
NEKPGPGRFR QFMQFDADTV GSASPAADAE MCMMAADAME ALGIPRGSYV VKVNNRKVLD
GVMESIGLGG EENAGRRLTV LRAIDKLDRL GIEGVKLLLG EGRWDGGEQG KGDFTIGAQL
SPETSTPILN YLDLGIRVAR DRVESPNREL GIVGYLEQIV SGSETGAQGT TELAQIVRLV
EAAGYDDGRI RIDPSVVRGL EYYTGPVYEV ELLLDTKDEK GRPVRFGSVG GGGRYDGLVS
RFRGEPVPAT GFSIGVSRLQ AALTLLGKLD TRPQAGPVVV TVFDRDRVAD YQKMVARLRA
ENIRAELYLG NPKNMGNQLK YADKRNSPCV IIQGSDEKND PDGAQIIVKD LVLGAELASL
EKDREEYLQK QAEAQRKVPE ADLVDEVRRI LAKHSVRWS