ID   RF1_UREU1               Reviewed;         359 AA.
AC   B5ZAH6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-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=UUR10_0003;
OS   Ureaplasma urealyticum serovar 10 (strain ATCC 33699 / Western).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX   NCBI_TaxID=565575;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33699 / Western;
RA   Shrivastava S., Methe B.A., Glass J., White K., Duffy L.B.;
RT   "Genome sequence of Ureaplasma urealyticum serovar 10 ATCC-33699.";
RL   Submitted (OCT-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; CP001184; ACI60091.1; -; Genomic_DNA.
DR   RefSeq; WP_012560280.1; NC_011374.1.
DR   AlphaFoldDB; B5ZAH6; -.
DR   SMR; B5ZAH6; -.
DR   STRING; 565575.UUR10_0003; -.
DR   EnsemblBacteria; ACI60091; ACI60091; UUR10_0003.
DR   GeneID; 45015559; -.
DR   KEGG; uue:UUR10_0003; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_14; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000002018; 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_1000093521"
FT   MOD_RES         236
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   359 AA;  40487 MW;  3469B203EEDE4D76 CRC64;
     MEYNKKLYEA IERVAVKNKT LKQELETITS DFKKIKEINI QLKKTTKIAE AFAKYKQKID
     AGIVAEELLN TEKDLELVEL AQMDLDDAKA SIPVIENELK IMLLPTDPND DKNVIVEMRP
     AAGGDESSIF VGNLFDTYRA YTESNNWKMK IIEMTPNAVG FSFISFMISG EEVYSRMKFE
     SGVHRVQRVP ATESKGRVHT STITVAVLPE QDEVDVVINP SDLRIDTYRA SGAGGQHVNR
     TESAVRITHI PTGVVAACQE GKSQIENRET AMKMLRAKLW EAAQEQQNAE FANLRKNQVG
     TGDRSEKIRT YNYPQNRVTD HRISLTLNKL DQIMMGELDE IIDALITDEQ TNLMANLGI