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Database: UniProt
Entry: A0A0R0DJG3_9GAMM
LinkDB: A0A0R0DJG3_9GAMM
Original site: A0A0R0DJG3_9GAMM 
ID   A0A0R0DJG3_9GAMM        Unreviewed;       465 AA.
AC   A0A0R0DJG3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 40.
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=ABB28_00520 {ECO:0000313|EMBL:KRG77672.1};
OS   Stenotrophomonas chelatiphaga.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=517011 {ECO:0000313|EMBL:KRG77672.1, ECO:0000313|Proteomes:UP000051386};
RN   [1] {ECO:0000313|EMBL:KRG77672.1, ECO:0000313|Proteomes:UP000051386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21508 {ECO:0000313|EMBL:KRG77672.1,
RC   ECO:0000313|Proteomes:UP000051386};
RA   Patil P.P., Midha S., Patil P.B.;
RT   "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KRG77672.1}.
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DR   EMBL; LDJK01000002; KRG77672.1; -; Genomic_DNA.
DR   RefSeq; WP_057506745.1; NZ_LDJK01000002.1.
DR   AlphaFoldDB; A0A0R0DJG3; -.
DR   PATRIC; fig|517011.3.peg.849; -.
DR   Proteomes; UP000051386; 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; PTHR11476:SF7; HISTIDINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR11476; 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|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00127};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00127};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00127};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00127}.
FT   DOMAIN          22..379
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   465 AA;  51875 MW;  6F2D37DDC37B57A7 CRC64;
     MIKPRTPPGI MELLPREQIA FQRMLDVIRR NYERFGFLPV ETPVFELSDV LLTKSGGETE
     RQVYFVQSTG ALANAAQAGD TSLPELALRF DLTVPLARYV AEHEHELTFP FRRYQMQRVY
     RGERAQRGRF REFYQCDIDV IGKDALSIRY DAEVLAVIHA VFSELRIGAF AVQLNNRKLL
     RGFFETLGVA EGERQLAVLR EVDKLDKRGA DYVRDTLVGA DFNIPAAQVE RILAFVAVRS
     QGHDDALAQL ALLEADAAAS ETLRTGVAEL REVLQLVKAL GVPEQAYCLN FSIARGLDYY
     TGTVYETLLT DHPQIGSICS GGRYEDLASH YSKSKLPGVG ISIGLTRLFW QLREAGLIEG
     IEASSVHALV ALMDEQGMPH SLDIARRLRV GGINTEVQME AKKIGKQFQY AAKAGIRFVV
     LAGEDELARG VVAVKDLLRE QQFEVSREEL ASTLQVELEQ ARAMA
//
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