RF1_CHLTR
ID RF1_CHLTR Reviewed; 359 AA.
AC O84026;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Peptide chain release factor 1;
DE Short=RF-1;
GN Name=prfA; OrderedLocusNames=CT_023;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Methylated by PrmC. Methylation increases the termination
CC efficiency of RF1 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000305}.
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DR EMBL; AE001273; AAC67613.1; -; Genomic_DNA.
DR PIR; B71566; B71566.
DR RefSeq; NP_219525.1; NC_000117.1.
DR RefSeq; WP_009871370.1; NC_000117.1.
DR AlphaFoldDB; O84026; -.
DR SMR; O84026; -.
DR STRING; 813.O172_00125; -.
DR EnsemblBacteria; AAC67613; AAC67613; CT_023.
DR GeneID; 884175; -.
DR KEGG; ctr:CT_023; -.
DR PATRIC; fig|272561.5.peg.28; -.
DR HOGENOM; CLU_036856_0_1_0; -.
DR InParanoid; O84026; -.
DR OMA; ISDHRVG; -.
DR Proteomes; UP000000431; 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..359
FT /note="Peptide chain release factor 1"
FT /id="PRO_0000177658"
FT REGION 287..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 235
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 359 AA; 40052 MW; 0ED087BCC230CE7A CRC64;
MEIKVLECLK RLEEVEKQIS DPNIFSNPKE YSSLSKEHAR LSEIKNAHES LVATKKILQD
DKLALSTEKD PEIVAMLEEG VLVGEEAVER LSKQLENLLI PPDPDDDLSV IMELRAGTGG
DEAALFVGDC VRMYHLYAAS KGWQCEVLST SESDLGGYKE YVMGISGASV KRFLQYEAGT
HRVQRVPETE TQGRVHTSAV TVAVLPEPAE DDEEVFIDEK DLRIDTFRSS GAGGQHVNVT
DSAVRITHIP SGVVVTCQDE RSQHKNKAKA MRVLKARIRD AEVQKRAQEA SAMRSAQVGS
GDRSERIRTY NFPQNRVTDH RIGLTLYNLD RVMEGELDMI TTALVTHVHR QLFGHEETA