RF1_LEPCP
ID RF1_LEPCP Reviewed; 360 AA.
AC B1XYX1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=Lcho_0580;
OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS discophora (strain SP-6)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Leptothrix.
OX NCBI_TaxID=395495;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51168 / LMG 8142 / SP-6;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT "Complete sequence of Leptothrix cholodnii SP-6.";
RL Submitted (MAR-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; CP001013; ACB32855.1; -; Genomic_DNA.
DR RefSeq; WP_012345617.1; NC_010524.1.
DR AlphaFoldDB; B1XYX1; -.
DR SMR; B1XYX1; -.
DR STRING; 395495.Lcho_0580; -.
DR PRIDE; B1XYX1; -.
DR EnsemblBacteria; ACB32855; ACB32855; Lcho_0580.
DR KEGG; lch:Lcho_0580; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_4; -.
DR OMA; ISDHRVG; -.
DR OrthoDB; 928964at2; -.
DR Proteomes; UP000001693; 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..360
FT /note="Peptide chain release factor 1"
FT /id="PRO_1000093472"
FT MOD_RES 235
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 360 AA; 39585 MW; 74C400A9E23C00A5 CRC64;
MTPFLRQQLS RQALRLAEID AALADPKVCS QIGTLRSLNR EHARVSALVD RWQRYEQREQ
DLAGAQELLD EPEMAELARA EIGAAQADLD RLDSELLTAL MPRDADDDRN AFVEIRAGTG
GEESALFAAD LARMYLRHAE RRGWKTELMS ESVSDLGGYK DVVLHIIGDA VFEALKYESG
GHRVQRVPAT EAQGRIHTSA CTVAVLAEAD EAEEVSLNPA ELRIDTYRAS GAGGQHINKT
DSAVRVTHLP TGLVAECQDD RSQHRNKARA LAVLAARLRD RVRQEQAAKD AAARKSLIGS
GDRSDRIRTY NFPQGRLTDH RINLTLYKLG AVLEGDLDEV IGALQAAHAA EQLAELETQA