RF1_FRATT
ID RF1_FRATT Reviewed; 361 AA.
AC Q5NIA8;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=FTT_0168;
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4;
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(2005).
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; AJ749949; CAG44801.1; -; Genomic_DNA.
DR RefSeq; WP_003019960.1; NZ_CP010290.1.
DR RefSeq; YP_169234.1; NC_006570.2.
DR AlphaFoldDB; Q5NIA8; -.
DR SMR; Q5NIA8; -.
DR IntAct; Q5NIA8; 9.
DR STRING; 177416.FTT_0168; -.
DR DNASU; 3191241; -.
DR EnsemblBacteria; CAG44801; CAG44801; FTT_0168.
DR KEGG; ftu:FTT_0168; -.
DR eggNOG; COG0216; Bacteria.
DR OMA; ISDHRVG; -.
DR Proteomes; UP000001174; 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..361
FT /note="Peptide chain release factor 1"
FT /id="PRO_0000177673"
FT REGION 287..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..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 361 AA; 40401 MW; 2E434C61C8045104 CRC64;
MKDSIKAKLQ SLIERHEEVS ALLSEAGIIS DQNKFRDLSK EYSHLEPIVK AFKKYTQALE
DKQAAYEMLN EKDAELVEMA KEELKLANEA IEKLESELQI FLLPRDPNDD ANVFLEIRAG
TGGDEASIFS GDLFKMYSKY AEQRGWKIEV ISASEGEHGG YKEIISRIYG DGVYSQLKFE
SGAHRVQRVP ATESQGRIHT SACTVAVMPE ADEVEGIDIN PADIKVDTFR ASGAGGQHVN
KTDSAIRITH IPTGVVVECQ DQRSQHKNRA AAMSMLKSKL LQAEIDKQQK EQSDTRKSLV
GSGDRSERIR TYNYPQGRVT DHRINLTLYK LDEVMEGSLD SIIQPLVLEH QADLLATMSD
E