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RF1_ENDTX
ID   RF1_ENDTX               Reviewed;         356 AA.
AC   B1GZI5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Peptide chain release factor 1 {ECO:0000255|HAMAP-Rule:MF_00093};
DE            Short=RF-1 {ECO:0000255|HAMAP-Rule:MF_00093};
GN   Name=prfA {ECO:0000255|HAMAP-Rule:MF_00093}; OrderedLocusNames=TGRD_184;
OS   Endomicrobium trichonymphae.
OC   Bacteria; Elusimicrobia; Endomicrobia; Endomicrobiales; Endomicrobiaceae;
OC   Endomicrobium.
OX   NCBI_TaxID=1408204;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18391199; DOI=10.1073/pnas.0801389105;
RA   Hongoh Y., Sharma V.K., Prakash T., Noda S., Taylor T.D., Kudo T.,
RA   Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT   "Complete genome of the uncultured termite group 1 bacteria in a single
RT   host protist cell.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:5555-5560(2008).
CC   -!- FUNCTION: Peptide chain release factor 1 directs the termination of
CC       translation in response to the peptide chain termination codons UAG and
CC       UAA. {ECO:0000255|HAMAP-Rule:MF_00093}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00093}.
CC   -!- PTM: Methylated by PrmC. Methylation increases the termination
CC       efficiency of RF1. {ECO:0000255|HAMAP-Rule:MF_00093}.
CC   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000255|HAMAP-Rule:MF_00093}.
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DR   EMBL; AP009510; BAG13667.1; -; Genomic_DNA.
DR   RefSeq; WP_015423195.1; NC_020419.1.
DR   RefSeq; YP_001956128.1; NC_020419.1.
DR   AlphaFoldDB; B1GZI5; -.
DR   SMR; B1GZI5; -.
DR   STRING; 471821.TGRD_184; -.
DR   PRIDE; B1GZI5; -.
DR   EnsemblBacteria; BAG13667; BAG13667; TGRD_184.
DR   KEGG; rsd:TGRD_184; -.
DR   PATRIC; fig|471821.5.peg.272; -.
DR   HOGENOM; CLU_036856_0_1_0; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000001691; 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_00093; Rel_fac_1; 1.
DR   InterPro; IPR005139; PCRF.
DR   InterPro; IPR000352; Pep_chain_release_fac_I.
DR   InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR   InterPro; IPR004373; RF-1.
DR   Pfam; PF03462; PCRF; 1.
DR   Pfam; PF00472; RF-1; 1.
DR   SMART; SM00937; PCRF; 1.
DR   SUPFAM; SSF75620; SSF75620; 1.
DR   TIGRFAMs; TIGR00019; prfA; 1.
DR   PROSITE; PS00745; RF_PROK_I; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methylation; Protein biosynthesis.
FT   CHAIN           1..356
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000093520"
FT   MOD_RES         233
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   356 AA;  40866 MW;  AE2593933844457F CRC64;
     MFLEKLKLLN SIFEEVESKL SDLSVISNQE EYRELTKQHF YLRPLAEKYI RYSKLLNEIK
     DAEELQKSKD AEMKEIAFAE YNNLIEKRNQ MENEIKVLLI PTDPNEDKNI IVEIRAGTGG
     NEAALFVGDL YGMYTRFAER NGWKYEVLGS NPTGLGGYKE VVFEINGGKV WRCFKFERGA
     HRVQRVPETE ASGRVHTSAA TVAVLPEAEE VDVEIKMEDL RIDTYRASGA GGQHINKTDS
     AIRITHLPTG LVVACQDERS QIKNRAKAFK VLRAKIYEQR ILEHEMRLSS ERKQQIGSGD
     RSEKIRTYNF PQNRITDHRI GYSVYNITEV MDGNLSELVN KLIKADIESK LKENNI
 
 
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