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RF1_THEYD
ID   RF1_THEYD               Reviewed;         353 AA.
AC   B5YIQ7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=THEYE_A0369;
OS   Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC   Bacteria; Nitrospirae; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC   Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX   NCBI_TaxID=289376;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51303 / DSM 11347 / YP87;
RA   Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT   "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT   ATCC 51303 / DSM 11347 / YP87.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001147; ACI21157.1; -; Genomic_DNA.
DR   RefSeq; WP_012545879.1; NC_011296.1.
DR   RefSeq; YP_002248216.1; NC_011296.1.
DR   AlphaFoldDB; B5YIQ7; -.
DR   SMR; B5YIQ7; -.
DR   STRING; 289376.THEYE_A0369; -.
DR   EnsemblBacteria; ACI21157; ACI21157; THEYE_A0369.
DR   KEGG; tye:THEYE_A0369; -.
DR   PATRIC; fig|289376.4.peg.362; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_0; -.
DR   InParanoid; B5YIQ7; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000000718; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; Methylation; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..353
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000093518"
FT   MOD_RES         232
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   353 AA;  40283 MW;  B5590A3362C339F7 CRC64;
     MLEKLMEVEN KYEKITQTLS DPKVFSNKDE YMKYSREQAE LEPIVTKFRE YKRILKQIEE
     AEEMIKSGDP DLKELAEEEL QQLKKIKPQI EQELKVLLLP KDPRDEKNVI LEIRAGTGGE
     EAALFAANLF RMYAKYAESK GWKVEIIDSH PTGLGGFKEI IATISGKGAF SKLKYESGVH
     RVQRIPVTEA SGRIHTSTAT VAVLPEAEEV DIKIDEKDLR IDTFCSSGPG GQSVNTAYSA
     VRIVHIPTGI IVQCQDERSQ IKNREKAMKV LRARLLEIER QKKEAERAAE RKGQVGTGER
     SERIRTYNFP QNRVTDHRIG LTLYKLEQVL NGNIDEIIDA LISYYQAEKL KEM
 
 
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