ID   RF1_UREP2               Reviewed;         359 AA.
AC   B1AHY9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=UPA3_0003;
OS   Ureaplasma parvum serovar 3 (strain ATCC 27815 / 27 / NCTC 11736).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX   NCBI_TaxID=505682;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27815 / 27 / NCTC 11736;
RA   Methe B.A., Glass J., Waites K., Shrivastava S.;
RT   "Genome sequence of Ureaplasma parvum serovar 3.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000942; ACA33038.1; -; Genomic_DNA.
DR   RefSeq; WP_006688457.1; NC_010503.1.
DR   AlphaFoldDB; B1AHY9; -.
DR   SMR; B1AHY9; -.
DR   EnsemblBacteria; ACA33038; ACA33038; UPA3_0003.
DR   GeneID; 29672265; -.
DR   KEGG; upa:UPA3_0003; -.
DR   HOGENOM; CLU_036856_0_1_14; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000002162; 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.
FT   CHAIN           1..359
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000075521"
FT   MOD_RES         236
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   359 AA;  40577 MW;  4ADABAA2E2164AA5 CRC64;
     MEYNKKLYEA IERVAIKNDA LKKELETVVT DFKKIKEINI QLKKTTKIAE AFAKYKQKLD
     TGIAAEKILN TEKDLELIEL AQMDLDEAKI NIPIIENDLK IMLLPTDPND DKNVIVEMRP
     AAGGDESSIF VGNLFDTYRA YAENNNWKMK IIEMTPNAVG FSFISFMISG EEVYSRMKFE
     SGVHRVQRVP ATESKGRVHT STITVAVLPE QDEVDVVINP TELRIDTYRA SGAGGQHVNR
     TESAVRITHI PTGVVAACQE GKSQIENRET AMKMLRAKLW EAAQEQQNAE FANLRKNQVG
     TGDRSEKIRT YNYPQNRVTD HRINLTLNKL DQIMMGELDE IIDALIADEQ TGLMANLDI