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Database: UniProt
Entry: E6J4M7_9ACTN
LinkDB: E6J4M7_9ACTN
Original site: E6J4M7_9ACTN 
ID   E6J4M7_9ACTN            Unreviewed;       426 AA.
AC   E6J4M7;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
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   ECO:0000313|EMBL:EFV93460.1};
GN   ORFNames=ES5_00772 {ECO:0000313|EMBL:EFV93460.1};
OS   Dietzia cinnamea P4.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Dietziaceae;
OC   Dietzia.
OX   NCBI_TaxID=910954 {ECO:0000313|EMBL:EFV93460.1, ECO:0000313|Proteomes:UP000004165};
RN   [1] {ECO:0000313|EMBL:EFV93460.1, ECO:0000313|Proteomes:UP000004165}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P4 {ECO:0000313|EMBL:EFV93460.1,
RC   ECO:0000313|Proteomes:UP000004165};
RX   PubMed=21901521; DOI=10.1007/s10482-011-9633-7;
RA   Procopio L., Alvarez V.M., Jurelevicius D.A., Hansen L., Sorensen S.J.,
RA   Cardoso J.S., Padula M., Leitao A.C., Seldin L., van Elsas J.D.;
RT   "Insight from the draft genome of Dietzia cinnamea P4 reveals mechanisms of
RT   survival in complex tropical soil habitats and biotechnology potential.";
RL   Antonie Van Leeuwenhoek 101:289-302(2012).
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:EFV93460.1}.
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DR   EMBL; AEKG01000031; EFV93460.1; -; Genomic_DNA.
DR   RefSeq; WP_007626304.1; NZ_AEKG01000031.1.
DR   AlphaFoldDB; E6J4M7; -.
DR   Proteomes; UP000004165; 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          38..349
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   426 AA;  45663 MW;  491A5C9BE4BFAB56 CRC64;
     MTGTEKKTAL KAPKGVPDYV PPASAGFVAV RDAITTAARR AGYGHIELPI FEDTALFARG
     VGESTDVVSK EMYSFEDRGG RSVTLRPEGT AGVMRAVIEH GLDRGQLPVK LCYAGPFFRY
     ERPQAGRYRQ LQQVGIEAIG VDDPALDAEV IAVADEAFRS LGLTGFRLEL TSLGDETCRP
     QYRERLQSFL AGLDLDEATR ERARINPLRV LDDKRPEVRA QLEDAPLMID HLSDASAEHF
     ATVRAHLDAL GVPYTVNPRM VRGLDYYTKT TFEFVHDGLG AQSGIGGGGR YDGLMEQLGG
     QALSGIGFGI GVDRTVLALQ AEGLDPAAQG RVDVYGVALG AAAKAAMVPV LAEFRRNGLR
     ADMAYGDRGM KGAFKAADRS GAAVTVVIGE NELETGTAVV KTMSTGEQEP VPLEAILGHV
     TRAVER
//
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