SYH_RICPR
ID SYH_RICPR Reviewed; 413 AA.
AC Q9ZDL9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 25-MAY-2022, entry version 123.
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=RP308;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA14769.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ235271; CAA14769.1; ALT_INIT; Genomic_DNA.
DR PIR; G71686; G71686.
DR RefSeq; NP_220692.1; NC_000963.1.
DR RefSeq; WP_004597402.1; NC_000963.1.
DR AlphaFoldDB; Q9ZDL9; -.
DR SMR; Q9ZDL9; -.
DR STRING; 272947.RP308; -.
DR EnsemblBacteria; CAA14769; CAA14769; CAA14769.
DR GeneID; 57569435; -.
DR KEGG; rpr:RP308; -.
DR PATRIC; fig|272947.5.peg.317; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_1_0_5; -.
DR Proteomes; UP000002480; 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; Reference proteome.
FT CHAIN 1..413
FT /note="Histidine--tRNA ligase"
FT /id="PRO_0000136240"
SQ SEQUENCE 413 AA; 47622 MW; 79797BED8648FFF4 CRC64;
MIENLQPLRG MKDLLPNDYQ IHNYIINKAR DVGALYGYKQ MSTPILEYTK VFNRSMGESS
DVMSKEIYSF VDKSNNAVAL RPEFTSGIIR SFISNGLQHK LPLKFFSTGP VFRYDRPQAG
RQRQFHQLNY EYLGAKGAIT DAETVKLAVD ILKALEIEED TTLELNSLGC HESRIVYQQK
LVEYLNDFKD QLSGESRLRL NKNPMRILDS KSEIDQKIIA HAPILSEYHT NESKKYFDEL
QKYLDILGIK YSVNPRLVRG LDYYCHTVFE FTTKKLGSQS TILAGGRYDM LSRIMGNYDV
HAIGFAAGIE RIALMREYKI SVIKPVFVLP IGKNNICYAL DIVDKLRLQN IVSIIDPIGK
IAKRIQRVLN EDAKFIIFIG DEEKMNNNLK FKDLKNQKEY IIDFEKVLEL LKQ