ID   RF1_BORT9               Reviewed;         357 AA.
AC   A1QYZ0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, 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=BT0196;
OS   Borrelia turicatae (strain 91E135).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX   NCBI_TaxID=314724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91E135;
RA   Porcella S.F., Raffel S.J., Schrumpf M.E., Montgomery B., Smith T.,
RA   Schwan T.G.;
RT   "The genome sequence of Borrelia hermsii and Borrelia turicatae:
RT   comparative analysis of two agents of endemic N. America relapsing fever.";
RL   Submitted (DEC-2004) 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; CP000049; AAX17532.1; -; Genomic_DNA.
DR   RefSeq; WP_011772151.1; NC_008710.1.
DR   AlphaFoldDB; A1QYZ0; -.
DR   SMR; A1QYZ0; -.
DR   STRING; 314724.BT0196; -.
DR   KEGG; btu:BT0196; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_12; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000001205; 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..357
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000193472"
FT   REGION          284..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..301
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         234
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   357 AA;  41671 MW;  51E81F2ADD74EFEA CRC64;
     MFLERLSPIE SKIKILEEKL QDTNLIKNQK EYAKVIKEYN YLEKIKEKKD EYENIISQID
     ENQKILSEEE NLEMKELIKQ ELTHLNLKKD EIEHTIKILL LHQDENDNKN IIIEIRAGTG
     GEEAALFAHN LYEMYTKYSE KKKWKTELIN FNETELGGFK EVSFEIKGKE VFKKLKHESG
     VHRVQRVPIT ESNGRLQTSA ATVAVLPEVE ETDIEINEKD LRIDVYRSSG AGGQHVNTTD
     SAVRITHLPT GIVVQCQNER SQHKNKDQAM KILRARLYKF EDLKKQEQRS NDRKQQVGSG
     DRSERIRTYN FPQNRVTEHR ANISLYKLEE IMQGELDLLL DTLALKLQEQ ALKDNPI