RF1_SHEON
ID RF1_SHEON Reviewed; 363 AA.
AC Q8EAR3;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=SO_3833;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN56810.1; -; Genomic_DNA.
DR RefSeq; NP_719366.1; NC_004347.2.
DR RefSeq; WP_011073597.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EAR3; -.
DR SMR; Q8EAR3; -.
DR STRING; 211586.SO_3833; -.
DR PaxDb; Q8EAR3; -.
DR PRIDE; Q8EAR3; -.
DR KEGG; son:SO_3833; -.
DR PATRIC; fig|211586.12.peg.3721; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_6; -.
DR OMA; ISDHRVG; -.
DR OrthoDB; 928964at2; -.
DR PhylomeDB; Q8EAR3; -.
DR BioCyc; SONE211586:G1GMP-3558-MON; -.
DR Proteomes; UP000008186; 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..363
FT /note="Peptide chain release factor 1"
FT /id="PRO_0000177735"
FT REGION 284..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 237
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 363 AA; 40344 MW; CFB19752DD6D3545 CRC64;
MKESVIRKLE GLLERNEEVL ALLGDASVIA DQDRFRALSK EYSQLEEVVA GFKAYQQAQA
DLESAKEMLE EDDAEMREMA QEEIKAAKVE LERLEAELQI LLLPKDPNDD TNAFIEIRAG
AGGDEAAIFA GDLFRMYSRY AEANRWQLEI MSSNEGEHGG FKEIIVKVSG EGAYGKLKFE
SGGHRVQRVP ETESQGRVHT SAVTVVVMHE VPEAEAISIN PADLKVDTFR SSGAGGQHVN
KTDSAIRITH IPTGIVVECQ DQRSQHKNRA QAMSVLAARI QAVEDEKRRS AEESTRRSLV
ASGDRSERVR TYNFPQGRVS EHRINLTLYR LNEVMEGDLD AILGPLMQEH QADLLAALAD
EQG