RF1_ANADE
ID RF1_ANADE Reviewed; 370 AA.
AC Q2IMW2;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=Adeh_0366;
OS Anaeromyxobacter dehalogenans (strain 2CP-C).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=290397;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2CP-C;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R.,
RA Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N.,
RA Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R.,
RA Zhulin I.B., Loeffler F.E., Richardson P.;
RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL Submitted (JAN-2006) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000251; ABC80142.1; -; Genomic_DNA.
DR RefSeq; WP_011419425.1; NC_007760.1.
DR AlphaFoldDB; Q2IMW2; -.
DR SMR; Q2IMW2; -.
DR STRING; 290397.Adeh_0366; -.
DR EnsemblBacteria; ABC80142; ABC80142; Adeh_0366.
DR KEGG; ade:Adeh_0366; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_7; -.
DR OMA; ISDHRVG; -.
DR Proteomes; UP000001935; 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..370
FT /note="Peptide chain release factor 1"
FT /id="PRO_0000263230"
FT REGION 286..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 237
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 370 AA; 41072 MW; ED9ADDCB1716DC45 CRC64;
MLSPDVLKKL EAIEQRFEEL TQLLSDPAVA GNGDRFRKVA KERASIEQTV TALRAYRKLL
DDVAGNEALL GDKDPELREL AKEELAQLRP QVEPAEEQLK LYLVPKDPND EKDVIVEIRA
GAGGDEAGLF AAEVMRMYVR YAERRGWRVE LMDTSGGALG GVKEATLTVS GDAVYSSLKY
ESGVHRVQRV PATEAQGRIH TSTVTVAVMP EAEEIDVQVN PADVEMDVFR STGSGGQSVN
TTDSAVRLTH KPTGIVVKCQ QEKSQLKNRT MAMKMLRAKL FEIEQERQRS ARDATRKSQV
GTGDRSEKIR TYNFPQDRLT DHRVNYTRHN LPAVMDGDVQ DVIDACRTFY AAQALREASR
GDAGAAERRA