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RF1_CHLPM
ID   RF1_CHLPM               Reviewed;         357 AA.
AC   A4SCF1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=Cvib_0136;
OS   Chlorobium phaeovibrioides (strain DSM 265 / 1930) (Prosthecochloris
OS   vibrioformis (strain DSM 265)).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=290318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 265 / 1930;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J.,
RA   Schuster S.C., Bryant D.A., Richardson P.;
RT   "Complete sequence of Prosthecochloris vibrioformis DSM 265.";
RL   Submitted (MAR-2007) 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; CP000607; ABP36160.1; -; Genomic_DNA.
DR   RefSeq; WP_011889389.1; NC_009337.1.
DR   AlphaFoldDB; A4SCF1; -.
DR   SMR; A4SCF1; -.
DR   STRING; 290318.Cvib_0136; -.
DR   PRIDE; A4SCF1; -.
DR   EnsemblBacteria; ABP36160; ABP36160; Cvib_0136.
DR   KEGG; pvi:Cvib_0136; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_10; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
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..357
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000075508"
FT   MOD_RES         234
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   357 AA;  41041 MW;  628CBB86D46BEA74 CRC64;
     MFDNLQSIKE RHLDLERLLA DPDAAGDQTR FRKLNKEYSD LREIVETYDR YSHIKKQLED
     SRQLLKNEQD QEMKALVEEE IEELQRQIPA LEQEIKVLLL PKDEADSRNV ILEIRAGTGG
     EEAALFTTDL FRMYQRYAEK QGWNFQMLDY NESSVPGGFR EATISITGHD VFGTMKYESG
     VHRVQRVPDT ETQGRIHTSA ASVAVLPEAE EVDVEIRKED LRLDTYRSGG KGGQNVNKVE
     TAVRITHMPT GMVAACQEER SQLQNKERAM KMLRAKLFDI QLAEQQQARA DLRRTMVATG
     DRSAKIRTYN YPQSRVTDHR IGFTTHALPQ FMQGEIGELI DALKMHDQTE RLQAAQQ
 
 
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