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Database: UniProt
Entry: A0A0G0D6T7_9BACT
LinkDB: A0A0G0D6T7_9BACT
Original site: A0A0G0D6T7_9BACT 
ID   A0A0G0D6T7_9BACT        Unreviewed;       433 AA.
AC   A0A0G0D6T7;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
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=UR91_C0009G0012 {ECO:0000313|EMBL:KKP88998.1};
OS   Candidatus Nomurabacteria bacterium GW2011_GWC2_35_8.
OC   Bacteria; Candidatus Nomurabacteria.
OX   NCBI_TaxID=1618752 {ECO:0000313|EMBL:KKP88998.1, ECO:0000313|Proteomes:UP000034798};
RN   [1] {ECO:0000313|EMBL:KKP88998.1, ECO:0000313|Proteomes:UP000034798}
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:KKP88998.1}.
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DR   EMBL; LBQZ01000009; KKP88998.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0D6T7; -.
DR   PATRIC; fig|1618752.3.peg.195; -.
DR   Proteomes; UP000034798; 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}; Cytoplasm {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}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00127}.
FT   DOMAIN          29..325
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   433 AA;  49108 MW;  96977B38ACBCF5ED CRC64;
     MKKTTNKNKG AEISSPKGMR DLMNEQYYAF QGFFEKAQEV AVYYGFKPIE TPILENEEIF
     TSGIGEGTDI VDKEMYNLKT KGGDHLALRP EHTAPTVRAY IEHGMQTFPQ PVMLYQYGPV
     FRHDKPQRGR YRQFWQFDLD SLGNEKSIMD ALVIKTGMTI LEEAGAENLS IDINSIGDKE
     CRNGYLKELT SYYRKHMSDL APIDRERLKT NPLRILDSKE EKTKIINENA PDSVSFLCPS
     CKKHFKEVLE YLEEMNIPYN INKNLVRGLS YYTRTVFEIL EQGGAEDGSP LALAGGGRYD
     YLARQIGGKK DVPAVGISIG VDRIVASPWY KKLSPRILKK PKMYFIQLGS EAKLKSLNII
     EILRKAHVPI AQALSKDSLG SQLAIAERLA IPYALIFGVK EAIDNSVIVR DMSNRSQNTV
     KLNKLLEYLK ELK
//
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