RF1_STRMK
ID RF1_STRMK Reviewed; 360 AA.
AC B2FQ14;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 71.
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=Smlt0870;
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a;
RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA Parkhill J., Thomson N.R., Avison M.B.;
RT "The complete genome, comparative and functional analysis of
RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT resistance determinants.";
RL Genome Biol. 9:R74.1-R74.13(2008).
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; AM743169; CAQ44444.1; -; Genomic_DNA.
DR RefSeq; WP_005412330.1; NC_010943.1.
DR AlphaFoldDB; B2FQ14; -.
DR SMR; B2FQ14; -.
DR STRING; 522373.Smlt0870; -.
DR EnsemblBacteria; CAQ44444; CAQ44444; Smlt0870.
DR GeneID; 61464779; -.
DR KEGG; sml:Smlt0870; -.
DR PATRIC; fig|522373.3.peg.842; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_6; -.
DR OMA; ISDHRVG; -.
DR OrthoDB; 928964at2; -.
DR Proteomes; UP000008840; 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_1000093510"
FT REGION 281..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 235
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 360 AA; 39912 MW; BC6A30B89075B894 CRC64;
MTPTLRRKLE ALAERREELE RLLAEPDVVA DNTRFRDLSR EFAQLEPIAI ALADESRAKA
DLAAAEGMRA DPDLRELADE EIAAAQARLL ELEQELALLL VPRDPRDEGN LFLEVRAGTG
GDEAAIFAGD LFRMYARYAE RQGWKVEIES DNPGEHGGYK EVVARVVGRG AFSRLKFESG
THRVQRVPAT ESQGRIHTSA ATVAIIPEAD EVDDIVINPA DLKVDTFRSS GAGGQHVNKT
ESAIRITHVP TGVVVECQTE RSQHANRDKA MKRLKAQLLD AERQRQDAAQ AESRRLQVGS
GDRSQRIRTY NFPQGRITDH RVEGLTLYDL PNILAGDLDP LLQRLSHEHQ VDALAQLSAG
