RF1_FRATM
ID RF1_FRATM Reviewed; 361 AA.
AC B2SFF6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=FTM_0232;
OS Francisella tularensis subsp. mediasiatica (strain FSC147).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=441952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSC147;
RX PubMed=19521508; DOI=10.1371/journal.ppat.1000472;
RA Larsson P., Elfsmark D., Svensson K., Wikstroem P., Forsman M., Brettin T.,
RA Keim P., Johansson A.;
RT "Molecular evolutionary consequences of niche restriction in Francisella
RT tularensis, a facultative intracellular pathogen.";
RL PLoS Pathog. 5:E1000472-E1000472(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}.
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DR EMBL; CP000915; ACD30309.1; -; Genomic_DNA.
DR RefSeq; WP_012429139.1; NC_010677.1.
DR AlphaFoldDB; B2SFF6; -.
DR SMR; B2SFF6; -.
DR KEGG; ftm:FTM_0232; -.
DR HOGENOM; CLU_036856_0_1_6; -.
DR OMA; ISDHRVG; -.
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..361
FT /note="Peptide chain release factor 1"
FT /id="PRO_1000093458"
FT REGION 286..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..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; 40416 MW; FE634A4560244B2B CRC64;
MKDSIKAKLQ SLIERHEEVS ALLSEAGIIS DQNKFRDLSK EYSHLEPIVK AFKEYTQALE
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 SIIQPLILEH QADLLATMSD
E