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Database: UniProt
Entry: A0A1F6DFG5_9BACT
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ID   A0A1F6DFG5_9BACT        Unreviewed;       418 AA.
AC   A0A1F6DFG5;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=A2765_01180 {ECO:0000313|EMBL:OGG60164.1};
OS   Candidatus Kaiserbacteria bacterium RIFCSPHIGHO2_01_FULL_56_24.
OC   Bacteria; Candidatus Kaiserbacteria.
OX   NCBI_TaxID=1798487 {ECO:0000313|EMBL:OGG60164.1, ECO:0000313|Proteomes:UP000176377};
RN   [1] {ECO:0000313|EMBL:OGG60164.1, ECO:0000313|Proteomes:UP000176377}
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:OGG60164.1}.
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DR   EMBL; MFLA01000013; OGG60164.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F6DFG5; -.
DR   Proteomes; UP000176377; 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   CDD; cd00859; HisRS_anticodon; 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   InterPro; IPR033656; HisRS_anticodon.
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          25..319
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   418 AA;  47309 MW;  4437E081F77099DE CRC64;
     MSDKNKLSAE PYKGVRDFYP EDQFIQDYIF EHMSQTCELF GYEEYGASIL EPTELYRSKT
     SDEIINQQSY TFTDRGDREV TLRPEMTPTL ARMVAAKSRE IPMPARWYSI PNCFRYERTQ
     KGRLREFWQL NADIIGSGGI EADAEVIALA HAVMRSFGAD ERNFEIRVSD RRLLDAAYDE
     IGIEPAERAE VTRLLDRRDK LDDFPAQLEK VLGDNATILI DHLDRTASTA YLEELRTRLV
     SMSIGNMIVD TKITRGFDYY TGMVFEVFDT SGDNKRSIAG GGRYDNLTQL FGAESIPAVG
     FAMGDAIIRD YLETHNLMPD YVPTTELMLC VVEDSAMSHA QKLAQDLRRE DVSVAINISG
     KKLGDQIRQA DKMKIAYIIA VGEKERDSGQ YTVKNLATGH ELTVSADRIA EHLFSSLG
//
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