(data stored in SCRATCH zone)

SWISSPROT: A0A0E1P2F7_YERPA

ID   A0A0E1P2F7_YERPA        Unreviewed;       310 AA.
AC   A0A0E1P2F7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   08-MAY-2019, entry version 21.
DE   RecName: Full=Peptide chain release factor 2 {ECO:0000256|HAMAP-Rule:MF_00094, ECO:0000256|SAAS:SAAS00090452};
DE            Short=RF-2 {ECO:0000256|HAMAP-Rule:MF_00094};
GN   Name=prfB {ECO:0000256|HAMAP-Rule:MF_00094};
GN   OrderedLocusNames=YPA_0380 {ECO:0000313|EMBL:ABG12348.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12348.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12348.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12348.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- FUNCTION: Peptide chain release factor 2 directs the termination
CC       of translation in response to the peptide chain termination codons
CC       UGA and UAA. {ECO:0000256|HAMAP-Rule:MF_00094,
CC       ECO:0000256|SAAS:SAAS00090456}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00094,
CC       ECO:0000256|SAAS:SAAS00090449}.
CC   -!- PTM: Methylated by PrmC. Methylation increases the termination
CC       efficiency of RF2. {ECO:0000256|HAMAP-Rule:MF_00094}.
CC   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release
CC       factor family. {ECO:0000256|HAMAP-Rule:MF_00094,
CC       ECO:0000256|SAAS:SAAS00571647}.
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DR   EMBL; CP000308; ABG12348.1; -; Genomic_DNA.
DR   EnsemblBacteria; ABG12348; ABG12348; YPA_0380.
DR   EnsemblBacteria; AJJ81698; AJJ81698; CH58_3226.
DR   KEGG; ypa:YPA_0380; -.
DR   PATRIC; fig|360102.15.peg.3388; -.
DR   KO; K02836; -.
DR   OMA; YVFHPYQ; -.
DR   Proteomes; UP000001971; 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_II.
DR   InterPro; IPR004374; PrfB.
DR   Pfam; PF03462; PCRF; 1.
DR   Pfam; PF00472; RF-1; 1.
DR   SMART; SM00937; PCRF; 1.
DR   TIGRFAMs; TIGR00020; prfB; 1.
DR   PROSITE; PS00745; RF_PROK_I; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0E1P2F7.
DR   SWISS-2DPAGE; A0A0E1P2F7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00094,
KW   ECO:0000256|SAAS:SAAS00462595};
KW   Methylation {ECO:0000256|HAMAP-Rule:MF_00094};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00094,
KW   ECO:0000256|SAAS:SAAS00090461}.
FT   MOD_RES     197    197       N5-methylglutamine. {ECO:0000256|HAMAP-
FT                                Rule:MF_00094}.
SQ   SEQUENCE   310 AA;  34825 MW;  A7BC641C7C9A0D68 CRC64;
     MGKERSTLEE IVTTIDQLEQ GLEDVSGLLE LAVEADDEET FNETIAELEV LDGKLGQLEF
     RRMFSGEYDR ANCYLDLQAG SGGTEAQDWA SMLLRMYLRW AESRGFKTEI IEESDGDVAG
     LKSATVKIIG EYAFGWLRTE TGVHRLVRKS PFDSGGRRHT SFSSAFVYPE VDDDIDIEIN
     PADLRIDVYR ASGAGGQHVN KTESAVRITH IPTNIVTQCQ NDRSQHKNKD QAMKQLKAKL
     YEFEMQKKNA DKQVLEDNKS DIGWGSQIRS YVLDDSRIKD LRTGVETRNT QAVLDGDLDK
     FIEASLKAGL
//

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