RF1_CHLAA
ID RF1_CHLAA Reviewed; 360 AA.
AC A9WE79;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=Caur_0491;
OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=324602;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
RX PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT "Complete genome sequence of the filamentous anoxygenic phototrophic
RT bacterium Chloroflexus aurantiacus.";
RL BMC Genomics 12:334-334(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000909; ABY33739.1; -; Genomic_DNA.
DR RefSeq; WP_012256395.1; NC_010175.1.
DR RefSeq; YP_001634128.1; NC_010175.1.
DR AlphaFoldDB; A9WE79; -.
DR SMR; A9WE79; -.
DR STRING; 324602.Caur_0491; -.
DR EnsemblBacteria; ABY33739; ABY33739; Caur_0491.
DR KEGG; cau:Caur_0491; -.
DR PATRIC; fig|324602.8.peg.558; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_0; -.
DR InParanoid; A9WE79; -.
DR OMA; ISDHRVG; -.
DR Proteomes; UP000002008; 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; Reference proteome.
FT CHAIN 1..360
FT /note="Peptide chain release factor 1"
FT /id="PRO_1000075486"
FT MOD_RES 232
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 360 AA; 40586 MW; D906A637AF8957B2 CRC64;
MFDKLAAVAA RYDELTELMA QPEVATNVTL LQQYAREQRE IEDIVNAYRE YQATQRAIEE
AEAMLEDSDP ELRALAQEEL ETQRKRLASL EEQLKLLLLP RDPNDSKDVI MEIRQGEGGD
EAALFAADLF RMYTRFAESR GWKVEVDSLT ENGIGGIKEV IFQIHGEGAY SQLKYEGGVH
RVQRVPATEA RGRIHTSTAT VAVLPEVEET EIEIKPEDLR IDVFRSAGHG GQGVNTTDSA
VRIVYKPGTP EEIVVTCQDG RSQIQNRERA MTVLRARLYA REQEKRQREI GASRLAQVGS
GERAEKIRTY NFPQDRITDH RIGQNFSNLP AVLDGELDKI IEALIIYDNA ERLRASGVST