ID A0A0G1M9Y6_9BACT Unreviewed; 455 AA.
AC A0A0G1M9Y6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
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};
GN ORFNames=UX07_C0024G0008 {ECO:0000313|EMBL:KKU04907.1};
OS Parcubacteria group bacterium GW2011_GWA2_45_30.
OC Bacteria.
OX NCBI_TaxID=1618834 {ECO:0000313|EMBL:KKU04907.1, ECO:0000313|Proteomes:UP000033829};
RN [1] {ECO:0000313|EMBL:KKU04907.1, ECO:0000313|Proteomes:UP000033829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKU04907.1}.
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DR EMBL; LCKU01000024; KKU04907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1M9Y6; -.
DR Proteomes; UP000033829; 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; 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; 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.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 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, ECO:0000313|EMBL:KKU04907.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 35..361
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 455 AA; 50983 MW; 567CA7583A3C8560 CRC64;
MSKQKSQEKD IIASLDRLPA REEIYAKLQK KFGSLAEYYG FEPIFTPPFE RYRQFLPLIK
AGFLDERIPV QCRCGLDNDY MLRVSGILSA LRAYISHKMS DRPQPVKLAF EGEVFFAESR
RDATLHGRYE CGLLMAGEEG PVAAAEIVQI IWKILDGIGV DVGDLELRVN AIGCVSCYPS
FRSALAAYFR SRAARLCRSC RKAAKSRPVR ALSCADEKCK IFAKHTPQVL DFLCDQCKKQ
LRGFLEFLDE LKIPYYLDPR FFRDGLWFNT LIFEFSGKAK EKPIPAAVVD DNGVKGDVAS
ESGILSGADH ETAIIIGEGG GCTRAAELIF GKRVEAVGFE LYVDRLIAFL SRRRLVGAQK
PIIYLTHLGD LAKRKSLALM ETLRNGEIEV KESLSRDSIK SQLKLAEKAE AKFALIMGQK
EALDDTIIVR EVGSGIQETI SQEKLIDFLK AKLKK
//
