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RF2_RALPJ
ID   RF2_RALPJ               Reviewed;         367 AA.
AC   B2U8V1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Peptide chain release factor 2 {ECO:0000255|HAMAP-Rule:MF_00094};
DE            Short=RF-2 {ECO:0000255|HAMAP-Rule:MF_00094};
GN   Name=prfB {ECO:0000255|HAMAP-Rule:MF_00094}; OrderedLocusNames=Rpic_0895;
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12J;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome 1 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-2008) 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:0000255|HAMAP-Rule:MF_00094}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00094}.
CC   -!- PTM: Methylated by PrmC. Methylation increases the termination
CC       efficiency of RF2. {ECO:0000255|HAMAP-Rule:MF_00094}.
CC   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000255|HAMAP-Rule:MF_00094}.
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DR   EMBL; CP001068; ACD26045.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2U8V1; -.
DR   SMR; B2U8V1; -.
DR   STRING; 402626.Rpic_0895; -.
DR   EnsemblBacteria; ACD26045; ACD26045; Rpic_0895.
DR   KEGG; rpi:Rpic_0895; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_220733_0_0_4; -.
DR   OMA; YVFHPYQ; -.
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_00094; Rel_fac_2; 1.
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.
FT   CHAIN           1..367
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_1000093552"
FT   MOD_RES         254
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   367 AA;  41167 MW;  769765D2E8B46C5D CRC64;
     MEAERLNAIQ NTLADLKSRA DDLRRYLDYD VKSERLVEVD KELENPEVWN DPKRAQELGR
     EKKSLETVVL ALTKLDEDLT GAAELFELAR EEGDDETIEA IEADTAGMRA IVEDMEFRRM
     FSGPMDAANC FIDIQAGAGG TEACDWASML LRQYLKYCER KGFKTEVLEE SEGDVAGIKS
     ASIKVEGEYA FGFLRTETGV HRLVRKSPFD SAGGRHTSFS SIFVYPEVDD SIEIEVNPAD
     LRVDTYRASG AGGQHINKTD SAVRITHIPT GIVVQCQNDR SQHRNRAEAM TMLKSRLYEH
     ELRKRQAAAD AQEAAKTDVG WGHQIRSYVL DQSRIKDLRT NVEISNTQKV LDGDLDPFIQ
     ASLKQGV
 
 
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