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RF2_RHOOB
ID   RF2_RHOOB               Reviewed;         368 AA.
AC   C1B1L3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-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=ROP_64610;
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=632772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) 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; AP011115; BAH54708.1; -; Genomic_DNA.
DR   RefSeq; WP_015890161.1; NC_012522.1.
DR   AlphaFoldDB; C1B1L3; -.
DR   SMR; C1B1L3; -.
DR   STRING; 632772.ROP_64610; -.
DR   EnsemblBacteria; BAH54708; BAH54708; ROP_64610.
DR   KEGG; rop:ROP_64610; -.
DR   PATRIC; fig|632772.20.peg.6744; -.
DR   HOGENOM; CLU_036856_6_0_11; -.
DR   OMA; YVFHPYQ; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000002212; 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_1000193557"
FT   MOD_RES         249
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   368 AA;  41435 MW;  374051AACE04A84C CRC64;
     MHPDVSADLS ELDTTLRTVE SVLDVEELRR RIDELEHQAA DPELWNDQEH AQQVTSQLSH
     SQAELRRVEE LRTRLDDMPV LYELAEDEGA EAIADADAER HSLREDIAAM EVKTMLSGEY
     DERDALVNIR SGAGGVDAAD WAEMLMRMYI RWAEKHGYGV EVYDTSYAEE AGIKSATFAV
     KAPYSYGTLS VEMGTHRLVR ISPFDNQGRR QTSFAEVEVL PVVETTDHID VNENDVRVDV
     YRSSGPGGQS VNTTDSAVRL THIPTGIVVT CQNEKSQLQN KVSAMRVLQA KLLEVKRKEE
     RAEMDALKGD GGSSWGNQMR SYVLHPYQMV KDLRTEYEVN NPSSVLDGDI DGFLESGIRW
     RMRENQAS
 
 
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