SYH_RICPU
ID SYH_RICPU Reviewed; 414 AA.
AC C4K1W2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 67.
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=RPR_04390;
OS Rickettsia peacockii (strain Rustic).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=562019;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rustic;
RX PubMed=20027221; DOI=10.1371/journal.pone.0008361;
RA Felsheim R.F., Kurtti T.J., Munderloh U.G.;
RT "Genome sequence of the endosymbiont Rickettsia peacockii and comparison
RT with virulent Rickettsia rickettsii: identification of virulence factors.";
RL PLoS ONE 4:E8361-E8361(2009).
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; CP001227; ACR47561.1; -; Genomic_DNA.
DR AlphaFoldDB; C4K1W2; -.
DR SMR; C4K1W2; -.
DR EnsemblBacteria; ACR47561; ACR47561; RPR_04390.
DR KEGG; rpk:RPR_04390; -.
DR HOGENOM; CLU_025113_1_0_5; -.
DR OMA; CDFDFIG; -.
DR Proteomes; UP000005015; 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 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.
FT CHAIN 1..414
FT /note="Histidine--tRNA ligase"
FT /id="PRO_1000203146"
SQ SEQUENCE 414 AA; 47428 MW; 3AAB1364082D299D CRC64;
MTEKLQPLRG MKDLLPDDYK VHDYIINTAR DVGVLYGYKQ MSTPIVEYTK VFNRSMGESS
DIISKEIYSF LDKSNDFVAL RPEFTACIIR SLISNRLQHK LPLKFFSTGP VFRYDRPQAG
RQRQFHQLNY EYIGAKGAIT DADTLKLAVD ILKALEIEQD TTLELNSLGC NESRSVYQQK
LVEYLNDFKD QLSKESKIRL SKNPMRILDS KSETDQKIIA NAPVLSEYYT DESKEYFEEL
IQYLDILGVK YSINPCLVRG LDYYCHTAFE FTTKKLGSQS TILAGGRYDG LAKIMGNNDD
VPAIGFAAGI ERIALIREYN ISEVKPVFVL PIGKNNICYA LEIVDKLRTE NIAIIIESLG
KIAKRMQRIF NENAQFIIFI GDEEQANNNL KIKDLKKEEE YIVDFAKALE LLKK