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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
 
 
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