ID   RF1_PARD8               Reviewed;         369 AA.
AC   A6LDR9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=BDI_2102;
OS   Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS   5825 / NCTC 11152).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=435591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(2007).
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; CP000140; ABR43833.1; -; Genomic_DNA.
DR   RefSeq; WP_005854384.1; NC_009615.1.
DR   AlphaFoldDB; A6LDR9; -.
DR   SMR; A6LDR9; -.
DR   STRING; 435591.BDI_2102; -.
DR   EnsemblBacteria; ABR43833; ABR43833; BDI_2102.
DR   GeneID; 57235009; -.
DR   KEGG; pdi:BDI_2102; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_10; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   BioCyc; PDIS435591:G1G5A-2157-MON; -.
DR   Proteomes; UP000000566; 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..369
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000004926"
FT   MOD_RES         238
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   369 AA;  41607 MW;  E86AE0C5F543176D CRC64;
     MAENSLLGKL DGLVSRFEEV GTLITDPAVI ADMKRFVKLN KEYRDLEKIV GARSEYVKVL
     NGIEEAKALL ESEQDPEMRE MAREELDTCN ERIPALEEEI KLLLVPADPQ DDKNAIVEIR
     GGTGGDEAAL FAGDLYRMYV KYCELKGWKI SVSSFSEGSS GGFKEIIFTV SGEKVYGTLK
     YESGVHRVQR VPATETQGRV HTSAATVAVL PEADEFDVEI NEGEIKWDTF RSGGAGGQNV
     NKVESGVRLR YVWKNPITGV SEEILIECTE TRDQPKNKER ALTRLRSFIY DKEHQKYLDD
     IASKRKTMVS TGDRSAKIRT YNYPQGRITD HRINYTIYNL SAFMDGEIQD CLDHLIVAEN
     AERLKESEL