ID A0A1G1ZQ23_9BACT Unreviewed; 306 AA.
AC A0A1G1ZQ23;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=histidine--tRNA ligase {ECO:0000256|ARBA:ARBA00012815};
DE EC=6.1.1.21 {ECO:0000256|ARBA:ARBA00012815};
DE AltName: Full=Histidyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030619};
DE Flags: Fragment;
GN ORFNames=A3A04_02455 {ECO:0000313|EMBL:OGY65917.1};
OS Candidatus Harrisonbacteria bacterium RIFCSPLOWO2_01_FULL_40_28.
OC Bacteria; Candidatus Harrisonbacteria.
OX NCBI_TaxID=1798406 {ECO:0000313|EMBL:OGY65917.1, ECO:0000313|Proteomes:UP000178517};
RN [1] {ECO:0000313|EMBL:OGY65917.1, ECO:0000313|Proteomes:UP000178517}
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};
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
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:OGY65917.1}.
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DR EMBL; MHJI01000011; OGY65917.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1ZQ23; -.
DR STRING; 1798406.A3A04_02455; -.
DR Proteomes; UP000178517; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR041715; HisRS-like_core.
DR InterPro; IPR004516; HisRS/HisZ.
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.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 6..193
FT /note="Class II Histidinyl-tRNA synthetase (HisRS)-like
FT catalytic core"
FT /evidence="ECO:0000259|Pfam:PF13393"
FT DOMAIN 216..300
FT /note="Anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF03129"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OGY65917.1"
SQ SEQUENCE 306 AA; 34897 MW; 46BB3FFDB9137473 CRC64;
SDPIYDAQII VLINRLLRGL GIKNIVTEIN SLGCKACRLN YKRKLIAYYK EKKGKMCEDC
ERRLALNPLR LLDCKEEKCL ALRNEAPSIL DHLCKSCNIH FKQVLEFIEE MKIPYRLNHF
LVRGLDYYNR TVFEIFADGA LEQKEAEKHE EEVVSHVSSK LALASGGRYD FLGEILGSRS
ISAVGVAMGI ERVIELLKKY EIIPKPLRKK RIFFVYIGET AKKKSLPIID ALIDAGFNVM
EALGKESLKA QLRLADKERI EWALIFGQKE AFEDSVILRD MKTGAQEAIA LKSLTERLHK
KLGARV
//
