RF1_DEIDV
ID RF1_DEIDV Reviewed; 366 AA.
AC C1CWJ1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 66.
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=Deide_15940;
OS Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=546414;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115;
RX PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT bacterium Deinococcus deserti.";
RL PLoS Genet. 5:E1000434-E1000434(2009).
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; CP001114; ACO46558.1; -; Genomic_DNA.
DR AlphaFoldDB; C1CWJ1; -.
DR SMR; C1CWJ1; -.
DR STRING; 546414.Deide_15940; -.
DR PaxDb; C1CWJ1; -.
DR PRIDE; C1CWJ1; -.
DR EnsemblBacteria; ACO46558; ACO46558; Deide_15940.
DR KEGG; ddr:Deide_15940; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_0; -.
DR OMA; CHQDTRM; -.
DR Proteomes; UP000002208; 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 PROSITE; PS00745; RF_PROK_I; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methylation; Protein biosynthesis; Reference proteome.
FT CHAIN 1..366
FT /note="Peptide chain release factor 1"
FT /id="PRO_1000202688"
FT REGION 283..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 230
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 366 AA; 40044 MW; 99ADD22FBA6FD43C CRC64;
MSGRLSELAA EFGMVERALG DPAALADPQA YTRLTRRHRE LLPLVTLLRE REALESDLRG
AQELLSDPDM RELAQNEITE ATARLEQLGA ELEVLLLPTD PDDLKNVILE LRAGAGGAEA
GLFVMDLLRM YTRYAEDRGL RLNVLEASES DLGGASKVVA EISGEFAFRA FKWERGVHRV
QRVPATESQG RIHTSTVTVA VLPEAEQGEV QLDLSEVRID VFRSQGAGGQ GVNTTDSAVR
AVYRAGTPDE IMVVCQDGRS QIKNREKALV VLASRLAERE RAARDAQEAR DRAAQVGSGE
RSEKIRTYNY PQNRVTDHRL EGDSKNHPLD SVMAGGLGPV VSALARDERE RQLLAASAEE
ARDGAA
