ID A0A1F4ZDB5_9BACT Unreviewed; 406 AA.
AC A0A1F4ZDB5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=A2989_03485 {ECO:0000313|EMBL:OGD03717.1};
OS Candidatus Amesbacteria bacterium RIFCSPLOWO2_01_FULL_48_25.
OC Bacteria; Candidatus Amesbacteria.
OX NCBI_TaxID=1797259 {ECO:0000313|EMBL:OGD03717.1, ECO:0000313|Proteomes:UP000177080};
RN [1] {ECO:0000313|EMBL:OGD03717.1, ECO:0000313|Proteomes:UP000177080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGD03717.1}.
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DR EMBL; MEXN01000005; OGD03717.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4ZDB5; -.
DR STRING; 1797259.A2989_03485; -.
DR Proteomes; UP000177080; 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; PTHR11476:SF7; HISTIDINE--TRNA LIGASE; 1.
DR PANTHER; PTHR11476; 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|HAMAP-Rule:MF_00127};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00127};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00127, ECO:0000313|EMBL:OGD03717.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00127};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00127}.
FT DOMAIN 29..319
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 406 AA; 45779 MW; 1892B9666140229E CRC64;
MTTQTLKGFR DFLPPQAAAR QWLKGQMIKV FEKWGYEPLE TPTLESYELF KGEIGEDEKL
FYKFKDLGDR EIMLRYDQTV PTCRVIGQYF NQLTFPFRRY QIQSNFRAEK PQAGRYREFV
QADVDIFGVA SPLADAETIA ISLDLYKSLG FKQVVAVVNN RDLMKDIPYA AISAIDKLDK
IGSDGVISSM ISKGITPDLA QKYFDQVRNI QPDETINTIF DYLKNAGFPP DWYRFQPTLA
RAFSYSQGPI WEIVIPEYSS GSVGGGERYD ALVERITGQK IPGTGIAFGF DRTLEAAEKL
GLVPQFKTPT QVLVTVFSPE LLNNSLSLSQ SLRSQNINTE LYPDPNIKLD KQLKYASAKG
IPYVAILGPE EIEKGTVTLK NMATGEQKTL SQNYLVIELA QLSQSQ
//