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RF1_SYNE7
ID   RF1_SYNE7               Reviewed;         368 AA.
AC   Q31L36;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 84.
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};
GN   OrderedLocusNames=Synpcc7942_2203;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) 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; CP000100; ABB58233.1; -; Genomic_DNA.
DR   RefSeq; WP_011244204.1; NC_007604.1.
DR   AlphaFoldDB; Q31L36; -.
DR   SMR; Q31L36; -.
DR   STRING; 1140.Synpcc7942_2203; -.
DR   PRIDE; Q31L36; -.
DR   EnsemblBacteria; ABB58233; ABB58233; Synpcc7942_2203.
DR   KEGG; syf:Synpcc7942_2203; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_3; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_2203-MON; -.
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..368
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_0000263378"
FT   MOD_RES         239
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   368 AA;  41575 MW;  235D529BBBD71004 CRC64;
     MAEPYLIEKL QSVEQTFQDL TRRLADPEIA TDPREFQRVA RMRSSMEELV TTYEEWKQRD
     AELKGAREIL RESSGDPELR EMAALEVNEL EALLVSLEER LKILLLPRDP NDDKNIMLEI
     RAGTGGDEAS LWAGDLLRMY SRYAESQGWR VKLLSESTGE LGGYKEAILE IQGESVYSKL
     KFEAGVHRVQ RVPATEAGGR VHTSTATVAI MPEVDEVEVS IDPKDIELTT ARSGGAGGQN
     VNKVETAVDL FHKPTGIRIF CTEERSQLQN RERAMQILRA KLYEMKLQEQ QEAVSSMRRS
     QVGTGSRSEK IRTYNYKDNR ATDHRLGLNF SLNPVLEGEI EEVIQACISK DQTEQLAQMA
     QDQEAAKV
 
 
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