ID   RF1_MOOTA               Reviewed;         356 AA.
AC   Q2RFW0;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=Moth_2397;
OS   Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Moorella group; Moorella.
OX   NCBI_TaxID=264732;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39073 / JCM 9320;
RX   PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA   Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA   Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT   "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT   thermoaceticum).";
RL   Environ. Microbiol. 10:2550-2573(2008).
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; CP000232; ABC20679.1; -; Genomic_DNA.
DR   RefSeq; WP_011393874.1; NC_007644.1.
DR   RefSeq; YP_431222.1; NC_007644.1.
DR   AlphaFoldDB; Q2RFW0; -.
DR   SMR; Q2RFW0; -.
DR   STRING; 264732.Moth_2397; -.
DR   EnsemblBacteria; ABC20679; ABC20679; Moth_2397.
DR   GeneID; 61291120; -.
DR   KEGG; mta:Moth_2397; -.
DR   PATRIC; fig|264732.11.peg.2610; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_9; -.
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.
PE   3: Inferred from homology;
KW   Cytoplasm; Methylation; Protein biosynthesis.
FT   CHAIN           1..356
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_0000263297"
FT   REGION          284..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..300
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         233
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   356 AA;  40573 MW;  4A87082387C56571 CRC64;
     MLEKLEQIEA RYEELGRLMG DPEVIADPEQ LQKHARAHAA LEDIVTTFRR YRQVSNELAE
     DKAMLEEEKD REFQELLKAE IERLTGEQER LEQELKILLL PKDPNDEKDI IMEIRAGAGG
     EEAALFAGDL FRMYQRYAEK KRWRTEIISS HPTELGGFKE IIFQVEGQGV YSRLKFESGV
     HRVQRIPTTE SGGRIHTSTA TVAVLPEAEE VDVEIKPEDL RVDIFCSSGP GGQSVNTTYS
     AVRITHLPTG LVVSCQDEKS QLKNKEKAMR VLRARLLDMA RAEREGELAE ERRSQVGSGD
     RSERIRTYNF PQNRVTDHRI GLTLHHLDQV LAGELDEIID ALVTTDQAER LKNMEA