SYH_THEMA
ID SYH_THEMA Reviewed; 420 AA.
AC Q9X0H5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Histidine--tRNA ligase;
DE EC=6.1.1.21;
DE AltName: Full=Histidyl-tRNA synthetase;
DE Short=HisRS;
GN Name=hisS; OrderedLocusNames=TM_1090;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AE000512; AAD36166.1; -; Genomic_DNA.
DR PIR; A72298; A72298.
DR RefSeq; NP_228896.1; NC_000853.1.
DR RefSeq; WP_004080372.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9X0H5; -.
DR SMR; Q9X0H5; -.
DR STRING; 243274.THEMA_08900; -.
DR DNASU; 898676; -.
DR EnsemblBacteria; AAD36166; AAD36166; TM_1090.
DR KEGG; tma:TM1090; -.
DR eggNOG; COG0124; Bacteria.
DR InParanoid; Q9X0H5; -.
DR OMA; CDFDFIG; -.
DR OrthoDB; 277998at2; -.
DR Proteomes; UP000008183; 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; IBA:GO_Central.
DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; IBA:GO_Central.
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 PANTHER; PTHR43707; PTHR43707; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
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; Reference proteome.
FT CHAIN 1..420
FT /note="Histidine--tRNA ligase"
FT /id="PRO_0000136282"
SQ SEQUENCE 420 AA; 48275 MW; 98C42EADC3F00362 CRC64;
MKYRRIKGTN DIFGEEIWYW RYVEETFRNV CESAGIEEIR TPIFEQTELF VRSVGEESDI
VQKEMYTFQD KAGRSITLRP EGTAPVVRAF LENSLIDRGF QQRYYYIGPM FRYEKPQSGR
LRQFHQVGFE IIGPESPKAD FEVIMLVDTF LRRLGLTKYK IHLNSIGCPV CRKNYREALK
EYYGRILDNL CDDCKRRYET NILRLLDCKV DHEYSLNAPK SVDYLCDSCR AHYKKLKEYL
NTFEIEYVED HTLVRGLDYY TRTVFEVRHE GLGAQSAIAG GGRYDGLFAE LGGSSVPALG
FAGGIERIIL ALKAEGIEIP MKNVHLVYIA TLGEKAFMDG VRLAGELRKK GLSVDVDIMD
RKLSGQLKHA SRMGSRYAVI IGDEELEKGI VILRDLETGD QVEIDRDFAA DYIAERVSKD