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Database: UniProt
Entry: A0A1A9GM67_9ACTN
LinkDB: A0A1A9GM67_9ACTN
Original site: A0A1A9GM67_9ACTN 
ID   A0A1A9GM67_9ACTN        Unreviewed;       450 AA.
AC   A0A1A9GM67;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Histidine--tRNA ligase {ECO:0000256|ARBA:ARBA00017399};
DE            EC=6.1.1.21 {ECO:0000256|ARBA:ARBA00012815};
DE   AltName: Full=Histidyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030619};
GN   Name=hisS {ECO:0000313|EMBL:ANH39389.1};
GN   ORFNames=I601_2978 {ECO:0000313|EMBL:ANH39389.1};
OS   Nocardioides dokdonensis FR1436.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1300347 {ECO:0000313|EMBL:ANH39389.1, ECO:0000313|Proteomes:UP000077868};
RN   [1] {ECO:0000313|EMBL:ANH39389.1, ECO:0000313|Proteomes:UP000077868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FR1436 {ECO:0000313|EMBL:ANH39389.1,
RC   ECO:0000313|Proteomes:UP000077868};
RA   Kwon S.-K., Kim K., Kim J.F.;
RT   "Complete genome sequence of a soil Actinobacterium, Nocardioides
RT   dokdonensis FR1436.";
RL   Submitted (MAR-2016) 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};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226}.
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DR   EMBL; CP015079; ANH39389.1; -; Genomic_DNA.
DR   RefSeq; WP_068111238.1; NZ_CP015079.1.
DR   AlphaFoldDB; A0A1A9GM67; -.
DR   STRING; 1300347.I601_2978; -.
DR   KEGG; ndk:I601_2978; -.
DR   PATRIC; fig|1300347.3.peg.2976; -.
DR   OrthoDB; 9800814at2; -.
DR   Proteomes; UP000077868; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00773; HisRS-like_core; 1.
DR   Gene3D; 3.40.50.800; Anticodon-binding domain; 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; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ANH39389.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077868}.
FT   DOMAIN          21..349
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          414..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   450 AA;  49355 MW;  A9F65C0AFB38C139 CRC64;
     MSAKIRPLSG FPELLPAARA VEREVIASLS RTFELHGFTN IETRVVEPLD RLAKGGEIDK
     EIYVLQRLQQ GGETSEAELG MHFDLTVPFA RYVLEHAGHL EFPFRRFQIQ PVWRGERPQE
     GRYRQFTQAD VDIVGRDVLD FHHDVEVMRV MVEALDALPV PALSFQFNNR KLIQGFYRGL
     GVPDVTAAIR TIDKLDKLPG EKVAELLVSD AGATPEQAER CLALATIRVP DTSFVEQVRA
     LGVTDDLLDE GLAELAAVIE GCSAAERRHV SVEANLRIAR GLDYYTGTVV EIFMDGYERL
     KSVGGGGRYD ALASDGRTTY PGVGVSFGVS RSLIPLLADG VLAGSRPVPS AVLIAVTSED
     SRPESDAIAA ALRAHGVPCE VAPTAAKFGK QIRTAERRGI PYVWFTGETG HQVKDIRTGE
     QVDADPATWA PPHDDLRPKV VSRTDQEQNQ
//
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