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RF1_SYNSC
ID   RF1_SYNSC               Reviewed;         365 AA.
AC   Q3AMQ9;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=Syncc9605_0347;
OS   Synechococcus sp. (strain CC9605).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=110662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9605;
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., Martinez M., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9605.";
RL   Submitted (JUL-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; CP000110; ABB34123.1; -; Genomic_DNA.
DR   RefSeq; WP_011363371.1; NC_007516.1.
DR   AlphaFoldDB; Q3AMQ9; -.
DR   SMR; Q3AMQ9; -.
DR   STRING; 110662.Syncc9605_0347; -.
DR   EnsemblBacteria; ABB34123; ABB34123; Syncc9605_0347.
DR   KEGG; syd:Syncc9605_0347; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_3; -.
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..365
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_0000263374"
FT   REGION          289..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         239
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   365 AA;  40699 MW;  641DAE025BEB968A CRC64;
     MDASTLFTRL ETATASFRNL ERQLADPDVA ADPKRLESIA RERSRLEPLV LDFEELQRLE
     SERDSARQLL KDSRGDAAME ELAQDELASL QEQHATLTER LTLALLPRDP RDERSVMLEI
     RAGAGGDEAC LWAGDLARMY ERYSQKVGWA VQSISCTEAD LGGFRELILS VRGDSVYSQL
     KFEAGVHRVQ RVPATESQGR VHTSTATVAV MPEADAVEVQ LDPKDLDIST ARSGGAGGQN
     VNKVETAVDL LHKPTGIRVF CTQERSQLQN RERALEILRA KLLEREQAAA AERESSDRRA
     QVGSGDRSEK IRTYNYKDNR TTDHRLGRNF TLEPVLEGQL EDLIGACIAE EQRQKLEALS
     DQAEA
 
 
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