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Database: UniProt
Entry: A0A0G0R4W5_9BACT
LinkDB: A0A0G0R4W5_9BACT
Original site: A0A0G0R4W5_9BACT 
ID   A0A0G0R4W5_9BACT        Unreviewed;       449 AA.
AC   A0A0G0R4W5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=UT79_C0001G0433 {ECO:0000313|EMBL:KKR44821.1};
OS   Candidatus Moranbacteria bacterium GW2011_GWC2_40_12.
OC   Bacteria; Candidatus Moranbacteria.
OX   NCBI_TaxID=1618699 {ECO:0000313|EMBL:KKR44821.1, ECO:0000313|Proteomes:UP000034716};
RN   [1] {ECO:0000313|EMBL:KKR44821.1, ECO:0000313|Proteomes:UP000034716}
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, 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:KKR44821.1}.
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DR   EMBL; LBYD01000001; KKR44821.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0R4W5; -.
DR   PATRIC; fig|1618699.3.peg.469; -.
DR   Proteomes; UP000034716; 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|HAMAP-Rule:MF_00127};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00127};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00127, ECO:0000313|EMBL:KKR44821.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00127};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00127}.
FT   DOMAIN          47..353
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   449 AA;  51201 MW;  AD2717EBBE98C2AE CRC64;
     MPRQKKISKK SIRKIKAAKP EKEELLLQSP RGMRDILPAD QIYWQQVRRV SEKAAADFGY
     RRIDVPLVEF TNIFSRSIGE GTDIIDKEMY SFSTKGGEKV SLRPEFTAGI ARAYIQHGMH
     VSPKPVKLYY TGPCYRYDRP QEGRFREFFQ FGCEALGEQD PVIDAQMIQM GWRVIYQLGI
     KNVRVNVNSI GCPSCRKSYR NLLIHYFESK KQKLCIDCKR RLETNPLRIL DCKEDKCVQV
     RASAPQSIDH LCEECRTHFK ELLEYLEELE IPFELDSNLV RGLDYYTKTV FEFMSVSESG
     EEKRKNALGG GGRYDGLVKM LGGENTPAVG FSLGLDRLAA EMKKLGARIY KEPKPRVFLA
     QLGVFAKKKS LKMFEGLERS GIRVAESFGR GSLKSQLKVA DRLGVEITLI LGQKEAIDQT
     VIVKDMASGN QEIIDAGKVI DEIKRRLKK
//
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