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RF2_MYCTO
ID   RF2_MYCTO               Reviewed;         371 AA.
AC   P9WHG0; L0TD65; O05782; P66026;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Peptide chain release factor 2;
DE            Short=RF-2;
GN   Name=prfB; OrderedLocusNames=MT3188;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK47527.1; -; Genomic_DNA.
DR   PIR; H70919; H70919.
DR   RefSeq; WP_003416129.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WHG0; -.
DR   SMR; P9WHG0; -.
DR   EnsemblBacteria; AAK47527; AAK47527; MT3188.
DR   GeneID; 45427104; -.
DR   KEGG; mtc:MT3188; -.
DR   HOGENOM; CLU_036856_6_0_11; -.
DR   Proteomes; UP000001020; 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..371
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_0000428193"
FT   MOD_RES         253
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   371 AA;  41473 MW;  59C30D8370242FF5 CRC64;
     MDPDRQADIA ALDCTLTTVE RVLDVEGLRS RIEKLEHEAS DPHLWDDQTR AQRVTSELSH
     TQGELRRVEE LRRRLDDLPV LYELAAEEAG AAAADAVAEA DAELKSLRAD IEATEVRTLL
     SGEYDEREAL VTIRSGAGGV DAADWAEMLM RMYIRWAEQH KYPVEVFDTS YAEEAGIKSA
     TFAVHAPFAY GTLSVEQGTH RLVRISPFDN QSRRQTSFAE VEVLPVVETT DHIDIPEGDV
     RVDVYRSSGP GGQSVNTTDS AVRLTHIPSG IVVTCQNEKS QLQNKIAAMR VLQAKLLERK
     RLEERAELDA LKADGGSSWG NQMRSYVLHP YQMVKDLRTE YEVGNPAAVL DGDLDGFLEA
     GIRWRNRRND D
 
 
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