ID A0A0M8SC34_9ACTN Unreviewed; 407 AA.
AC A0A0M8SC34;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=ADK51_08965 {ECO:0000313|EMBL:KOU30525.1};
OS Streptomyces sp. WM6368.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415554 {ECO:0000313|EMBL:KOU30525.1, ECO:0000313|Proteomes:UP000037718};
RN [1] {ECO:0000313|EMBL:KOU30525.1, ECO:0000313|Proteomes:UP000037718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM6368 {ECO:0000313|EMBL:KOU30525.1,
RC ECO:0000313|Proteomes:UP000037718};
RA Noorani M.;
RL Submitted (JUL-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:KOU30525.1}.
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DR EMBL; LGDA01000082; KOU30525.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8SC34; -.
DR PATRIC; fig|1415554.3.peg.1866; -.
DR Proteomes; UP000037718; 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|HAMAP-Rule:MF_00127};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00127};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00127};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00127};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00127}.
FT DOMAIN 20..312
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 407 AA; 44039 MW; 54FE15BB7985FB6C CRC64;
MIPPYSAKYL AVRDAISAPL RKAGYGYIET PGFEDVNLFA RGVGESTDIV TKEMFTLTTK
GGTNLALRPE GTASVLRAAL EASLHKQGNL PAKLWYSGSY YRYERPQKGR YRHFSQVGAE
AIGAEDPALD AELIILADQA YRTLGLSNFR ILLNSLGDKE CRPVYREALQ TFLRGLDLDE
ETVRRAEINP LRVLDDKRAE VQKQLVGAPV LRDYLCDACK AYHEEVRELI TAAGVVFEDD
EKLVRGLDYY TRTTFEFVHD GLGAQSAVGG GGRYDGLSEM IGGPALPSVG WALGVDRTVL
ALEAEGIELD IPAATTVFAV ALGEAKPTVF GLVTQLRKAG VAADMSYGGK GLKGAMKDAN
RSGARFAVVV GERDLAEGVV QLKDMESGEQ ASVPVAELVD TVRARLA
//