ID   RF1_WOLPP               Reviewed;         363 AA.
AC   B3CL87;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=WP0043;
OS   Wolbachia pipientis subsp. Culex pipiens (strain wPip).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX   NCBI_TaxID=570417;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=wPip;
RX   PubMed=18550617; DOI=10.1093/molbev/msn133;
RA   Klasson L., Walker T., Sebaihia M., Sanders M.J., Quail M.A., Lord A.,
RA   Sanders S., Earl J., O'Neill S.L., Thomson N., Sinkins S.P., Parkhill J.;
RT   "Genome evolution of Wolbachia strain wPip from the Culex pipiens group.";
RL   Mol. Biol. Evol. 25:1877-1887(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; AM999887; CAQ54152.1; -; Genomic_DNA.
DR   RefSeq; WP_007302826.1; NC_010981.1.
DR   AlphaFoldDB; B3CL87; -.
DR   SMR; B3CL87; -.
DR   STRING; 570417.WP0043; -.
DR   EnsemblBacteria; CAQ54152; CAQ54152; WP0043.
DR   KEGG; wpi:WP0043; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_5; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000008814; 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..363
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000093523"
FT   REGION          286..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         236
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   363 AA;  41454 MW;  D14C1D02F25AA994 CRC64;
     MDIENNLQDL KKKFSDVERN LENPTNLSQK EFVSFSKEYS ELRPIIEIID EYNILKEEIS
     DLEEIMKDEN SDGDIKELAK EELLEKQKIV LPKVKAKLKL ALLPKDEDDS RNAILEIRAG
     TGGEEAALFA AMLFRMYQKY AERRNWKFEP ISISNTGIGG YKEASALING TEVFARLKFE
     SGVHRVQRVP ETESSGRLHT SAATVAILPE VEEVDFEIEE KDLRIDVYRS SGPGGQSVNT
     TDSAVRVTHL PTGIVVIQQD EKSQHKNKAK ALKVLRARLY EIERQKKEME RSTMRKSQIG
     SGDRSERIRT YNFPQSRITD HRINLTSHRL EQIIKEGELD EFIEALISRN EAERLTGGGN
     VTF