RF1_CHLMU
ID RF1_CHLMU Reviewed; 359 AA.
AC Q9PL16;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Peptide chain release factor 1;
DE Short=RF-1;
GN Name=prfA; OrderedLocusNames=TC_0292;
OS Chlamydia muridarum (strain MoPn / Nigg).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=243161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MoPn / Nigg;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
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; AE002160; AAF39160.1; -; Genomic_DNA.
DR PIR; B81718; B81718.
DR RefSeq; WP_010230060.1; NZ_CP027217.1.
DR AlphaFoldDB; Q9PL16; -.
DR SMR; Q9PL16; -.
DR STRING; 243161.TC_0292; -.
DR PRIDE; Q9PL16; -.
DR EnsemblBacteria; AAF39160; AAF39160; TC_0292.
DR GeneID; 1246462; -.
DR KEGG; cmu:TC_0292; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_0; -.
DR OMA; ISDHRVG; -.
DR OrthoDB; 928964at2; -.
DR Proteomes; UP000000800; 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_0000177655"
FT REGION 285..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..310
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; 40207 MW; 2F58985DA434038B CRC64;
MEVKVLECLR RLEEVEKLIS DPNIFSNPKE YSSLSKEHAR LSEIKNAHES ILAAKKILHD
DKLALSTEKD PEMIAMLEEG IQGGEESLER LSKQLENLLI PPDPDDDLSV IMELRAGTGG
DEAALFVGDC VRMYHLYASI KGWQCEVLSA SESDLGGYKE YIMGVSGTSV KRFLQYEAGT
HRVQRVPETE TQGRVHTSAV TIAVLPEPAE DDEEVFIDEK DLRIDTFRSS GAGGQHVNVT
DSAVRITHIP TGVVVSCQDE RSQHKNKAKA MRVLKARIRD AEVQKREQEA SAMRSAQVGS
GDRSERIRTY NFPQNRVTDH RIGLTLYNLD RVMQGELDMI TTALVSHAHR QLFGHEETN