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RF2_CYTFI
ID   RF2_CYTFI               Reviewed;         294 AA.
AC   P96314;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-2002, sequence version 2.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Peptide chain release factor 2;
DE            Short=RF-2;
DE   Flags: Fragment;
GN   Name=prfB;
OS   Cytobacillus firmus (Bacillus firmus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Cytobacillus.
OX   NCBI_TaxID=1399;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Bauer M., Baeuerlein E.;
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Peptide chain release factor 2 directs the termination of
CC       translation in response to the peptide chain termination codons UGA and
CC       UAA. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: Methylated by PrmC. Methylation increases the termination
CC       efficiency of RF2 (By similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: The gene for this protein contains a UGA in-frame
CC       termination codon after Leu-24; a naturally occurring frameshift
CC       enables complete translation of RF-2. This provides a mechanism for the
CC       protein to regulate its own production.
CC   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA67778.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X99401; CAA67778.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; P96314; -.
DR   SMR; P96314; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016149; F:translation release factor activity, codon specific; IEA:InterPro.
DR   InterPro; IPR005139; PCRF.
DR   InterPro; IPR000352; Pep_chain_release_fac_I.
DR   InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR   InterPro; IPR004374; PrfB.
DR   Pfam; PF03462; PCRF; 1.
DR   Pfam; PF00472; RF-1; 1.
DR   SMART; SM00937; PCRF; 1.
DR   SUPFAM; SSF75620; SSF75620; 1.
DR   TIGRFAMs; TIGR00020; prfB; 1.
DR   PROSITE; PS00745; RF_PROK_I; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methylation; Protein biosynthesis; Ribosomal frameshifting.
FT   CHAIN           1..>294
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_0000166802"
FT   MOD_RES         251
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000250"
FT   NON_TER         294
SQ   SEQUENCE   294 AA;  33454 MW;  355349250C762DE6 CRC64;
     MELVEVKQEL AAMAKRLTDF RGSLDLEAKQ ERMAELDEFM TAPDFWDDQE AAQTVINESN
     GLKEQVNVFL ELEEKYENLE VSYELVKEEA DEELEKELEA GVKELISRLN DFELQLLLSE
     PYDKNNAILE LHPGAGGTES QDWASMLLRM YTRWSEQRGF KVETMDYLPG DEAGVKSVTL
     LIKGHNAYGY LKAEKGVHRL VRISPFDSSG RRHTSFVSCE VMPELDDNVE IDIRTEDLKV
     DTYRASGAGG QHINTTDSAI RITHLPTNTV VTCQSERSQI KNRDQAMKML KAKL
 
 
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