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RF1_LACLA
ID   RF1_LACLA               Reviewed;         357 AA.
AC   Q9CHX3;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Peptide chain release factor 1;
DE            Short=RF-1;
GN   Name=prfA; OrderedLocusNames=LL0595; ORFNames=L0373;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
CC   -!- FUNCTION: Peptide chain release factor 1 directs the termination of
CC       translation in response to the peptide chain termination codons UAG and
CC       UAA. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: Methylated by PrmC. Methylation increases the termination
CC       efficiency of RF1 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000305}.
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DR   EMBL; AE005176; AAK04693.1; -; Genomic_DNA.
DR   PIR; C86699; C86699.
DR   RefSeq; NP_266751.1; NC_002662.1.
DR   RefSeq; WP_003129495.1; NC_002662.1.
DR   AlphaFoldDB; Q9CHX3; -.
DR   SMR; Q9CHX3; -.
DR   STRING; 272623.L0373; -.
DR   PaxDb; Q9CHX3; -.
DR   EnsemblBacteria; AAK04693; AAK04693; L0373.
DR   GeneID; 60355798; -.
DR   GeneID; 66441509; -.
DR   KEGG; lla:L0373; -.
DR   PATRIC; fig|272623.7.peg.635; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_9; -.
DR   OMA; ISDHRVG; -.
DR   Proteomes; UP000002196; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00093; Rel_fac_1; 1.
DR   InterPro; IPR005139; PCRF.
DR   InterPro; IPR000352; Pep_chain_release_fac_I.
DR   InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR   InterPro; IPR004373; RF-1.
DR   Pfam; PF03462; PCRF; 1.
DR   Pfam; PF00472; RF-1; 1.
DR   SMART; SM00937; PCRF; 1.
DR   SUPFAM; SSF75620; SSF75620; 1.
DR   TIGRFAMs; TIGR00019; prfA; 1.
DR   PROSITE; PS00745; RF_PROK_I; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methylation; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..357
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_0000177685"
FT   MOD_RES         234
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   357 AA;  40405 MW;  9E8DCB9171C88F79 CRC64;
     MFDQLESIVG RYEELGELLS DPEVVSDTKR FMELSREEAD LRDKVATYNE YKKVLETISD
     SEEMLGEGGL DDDMKEMLKE ELSSAKSQKE LLEEEIKILL LPKDPNDGKN IILEIRGAAG
     GDEAALFAGD LLNMYQHFSE SQGWKFEIME ANITGIGGYK EVSALISGPS VYSKLKYESG
     AHRVQRVPVT ETQGRVHTST ATVLVMPEVE EFEMTIDQKD LRVDIYHASG AGGQNVNKVA
     TAVRMVHLPT GIKVEMQEER TQQKNRDKAI KLLNTKVFDY YQQIELDKQN AERKSTVGTG
     DRSERIRTYN FPQNRVTDHR IGLTLQKLDS ILSGKMDEVI DALIVYDQTK KLEELNK
 
 
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