SYH_GRAFK
ID SYH_GRAFK Reviewed; 456 AA.
AC A0M0E2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Histidine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00127};
DE EC=6.1.1.21 {ECO:0000255|HAMAP-Rule:MF_00127};
DE AltName: Full=Histidyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00127};
DE Short=HisRS {ECO:0000255|HAMAP-Rule:MF_00127};
GN Name=hisS {ECO:0000255|HAMAP-Rule:MF_00127}; OrderedLocusNames=GFO_1113;
OS Gramella forsetii (strain KT0803).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Gramella.
OX NCBI_TaxID=411154;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT0803;
RX PubMed=17107561; DOI=10.1111/j.1462-2920.2006.01152.x;
RA Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E.,
RA Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K.,
RA Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I.,
RA Gloeckner F.O.;
RT "Whole genome analysis of the marine Bacteroidetes'Gramella forsetii'
RT reveals adaptations to degradation of polymeric organic matter.";
RL Environ. Microbiol. 8:2201-2213(2006).
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:0000255|HAMAP-Rule:MF_00127};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00127}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00127}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00127}.
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DR EMBL; CU207366; CAL66087.1; -; Genomic_DNA.
DR RefSeq; WP_011709006.1; NC_008571.1.
DR AlphaFoldDB; A0M0E2; -.
DR SMR; A0M0E2; -.
DR STRING; 411154.GFO_1113; -.
DR PRIDE; A0M0E2; -.
DR EnsemblBacteria; CAL66087; CAL66087; GFO_1113.
DR KEGG; gfo:GFO_1113; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_3_0_10; -.
DR OMA; YQIQKVW; -.
DR OrthoDB; 277998at2; -.
DR Proteomes; UP000000755; Chromosome.
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; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 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 Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF13393; tRNA-synt_His; 2.
DR PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00442; hisS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..456
FT /note="Histidine--tRNA ligase"
FT /id="PRO_1000057829"
SQ SEQUENCE 456 AA; 51177 MW; 6DB12A8869A55BD0 CRC64;
MAQKPSIPKG TRDFSPEEVA KRNYIFNTIQ TEFKGFGFQP IETPSFENSS TLMGKYGDEG
DRLIFKILNS GDFLKKADKD ALANSDSLKL TSSISEKALR YDLTVPFARY VVQHQNEIEF
PFKRYQIQPV WRADRPQKGR FREFFQCDAD VVGSNSLWQE VEFVQLYDAV FNKLGLEGVT
IKINNRKVLS GFAEVIGEQD KLIDFTVALD KLDKIGEEGV KKEMREKGIS EEALNKIQPI
FNLNGNFAEK IEGLKTILEG SETGQKGIEE LQFIQNAIEE MPLSVAKLDL DVTLARGLNY
YTGAIFEVAA PENVKMGSIG GGGRYDDLTG IFGLKDMSGI GISFGLDRIY LVLEELGLFP
ATVTENTKVL FINFGEKEAL YAMKAVKRLR EENIIAELYP DSAKMGKQMK YADKRSIPYV
VLAGEEEIND KKFTLKHMKS GEQSNLDFNG LSGALK