ID A0A246JL76_9BURK Unreviewed; 436 AA.
AC A0A246JL76;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Histidine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00127};
DE EC=6.1.1.21 {ECO:0000256|HAMAP-Rule:MF_00127};
DE AltName: Full=Histidyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00127};
DE Short=HisRS {ECO:0000256|HAMAP-Rule:MF_00127};
GN Name=hisS {ECO:0000256|HAMAP-Rule:MF_00127};
GN ORFNames=CDN99_02095 {ECO:0000313|EMBL:OWQ93300.1};
OS Roseateles aquatilis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=431061 {ECO:0000313|EMBL:OWQ93300.1, ECO:0000313|Proteomes:UP000197468};
RN [1] {ECO:0000313|EMBL:OWQ93300.1, ECO:0000313|Proteomes:UP000197468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 48205 {ECO:0000313|EMBL:OWQ93300.1,
RC ECO:0000313|Proteomes:UP000197468};
RX PubMed=18175673; DOI=10.1099/ijs.0.65169-0;
RA Gomila M., Bowien B., Falsen E., Moore E.R., Lalucat J.;
RT "Description of Roseateles aquatilis sp. nov. and Roseateles terrae sp.
RT nov., in the class Betaproteobacteria, and emended description of the genus
RT Roseateles.";
RL Int. J. Syst. Evol. Microbiol. 58:6-11(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:0000256|ARBA:ARBA00001137, ECO:0000256|HAMAP-
CC Rule:MF_00127};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_00127}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00127}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00127}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWQ93300.1}.
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DR EMBL; NIOF01000001; OWQ93300.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A246JL76; -.
DR OrthoDB; 9800814at2; -.
DR Proteomes; UP000197468; Unassembled WGS sequence.
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; 3.40.50.800; Anticodon-binding domain; 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 NCBIfam; TIGR00442; hisS; 1.
DR PANTHER; PTHR43707:SF1; HISTIDINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43707; HISTIDYL-TRNA SYNTHETASE; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00127};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00127};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00127};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00127};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00127};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00127}; Reference proteome {ECO:0000313|Proteomes:UP000197468}.
FT DOMAIN 30..347
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 436 AA; 48415 MW; 5DFA0920FE212CF8 CRC64;
MTDTKKLQAL QAVKGMNDIL PPESARWEWL EAMMRSVLQR YGYQNVRTPI VEPTALFVRG
IGEVTDIVEK EMYAFEDRAD KHGQAEHLAL RPEMTAGVVR AMTEHSFLRD SGRRLYYFGP
MFRREKPQKG RYRQFHQMGV EAMGFAGPDV DAEVILMGSR LLRELGLKDG EHFRLELNCL
GEPAERRAHR EALIAYLEQH QALLDEDSRR RMHSNPLRVL DTKNPALQDM ANGAPKLLDF
LGEASLAHFN GVRAILDAAG IAYQINPRLV RGLDYYNLTV FEWVTERLGS QGTVCGGGRY
DYLIEQLGGK PAPAVGFGMG IERLLLLLEE VGTLPAPDVP DAYAVIPSAQ GLPQVMVALE
ALRAAGVRVV MHPGQGSMKS QFKKADGSGA RFALIFGEDE LARGEVAVKP LRDEGAAQTT
RSLYDVAGWA AELRNA
//
