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RF2_RICBR
ID   RF2_RICBR               Reviewed;         368 AA.
AC   Q1RIY5;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=RBE_0598;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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; CP000087; ABE04679.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1RIY5; -.
DR   SMR; Q1RIY5; -.
DR   STRING; 336407.RBE_0598; -.
DR   EnsemblBacteria; ABE04679; ABE04679; RBE_0598.
DR   KEGG; rbe:RBE_0598; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_221951_1_0_5; -.
DR   OMA; YVFHPYQ; -.
DR   Proteomes; UP000001951; 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_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..368
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_0000277909"
FT   MOD_RES         250
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   368 AA;  41379 MW;  274C719612025AE8 CRC64;
     MRAEIENYVK KIEQSLELLR RSLDVETSAA RLAELEELAA SPDLWNDQAN AQKLLREKSN
     LEEQLGAYNK IRSNLKDALE LEEMAEAEND LEIMQQVEKD LQSLSTIAAK FETECLFSGE
     ADSNNCFLEI NAGAGGTESH DWASIMMRMY LRFAERLGFK TEIINMINGE EAGIKSCTIR
     IIGRRAYGWL KTEAGVHRLV RISPFNAAGK RMTSFASSWV YPEIDDNIAI TIEDKDLRID
     TFRASGAGGQ HVNTTDSAVR ITHIPTGTVT QCQSDRSQHK NKAQAMKMLQ AKLYELEMQK
     RTDSVNEQNA AKTDNSWGHQ IRSYVLQPYQ MVKDLRTDYE TSDTKGVLDG DLEEFVSASL
     AMNAGSKK
 
 
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