RF1_SALRD
ID RF1_SALRD Reviewed; 357 AA.
AC Q2S2U3;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=SRU_1364;
OS Salinibacter ruber (strain DSM 13855 / M31).
OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC Rhodothermaceae; Salinibacter.
OX NCBI_TaxID=309807;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13855 / CECT 5946 / M31;
RX PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H.,
RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA Legault B., Rodriguez-Valera F.;
RT "The genome of Salinibacter ruber: convergence and gene exchange among
RT hyperhalophilic bacteria and archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
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; CP000159; ABC45712.1; -; Genomic_DNA.
DR RefSeq; WP_011404116.1; NC_007677.1.
DR RefSeq; YP_445488.1; NC_007677.1.
DR AlphaFoldDB; Q2S2U3; -.
DR SMR; Q2S2U3; -.
DR STRING; 309807.SRU_1364; -.
DR PRIDE; Q2S2U3; -.
DR EnsemblBacteria; ABC45712; ABC45712; SRU_1364.
DR GeneID; 61495974; -.
DR KEGG; sru:SRU_1364; -.
DR PATRIC; fig|309807.25.peg.1418; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_10; -.
DR OMA; ISDHRVG; -.
DR Proteomes; UP000008674; 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.
PE 3: Inferred from homology;
KW Cytoplasm; Methylation; Protein biosynthesis; Reference proteome.
FT CHAIN 1..357
FT /note="Peptide chain release factor 1"
FT /id="PRO_0000263344"
FT REGION 249..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 234
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 357 AA; 40293 MW; 5B29190AFE883D2E CRC64;
MIEREKLDKV KHRFQEVESL MADPEVANDP DRMRELGQEH SRLEEVVEAI DRYERLLDER
DELEGMIRDE SGEMEALAKE ELEQLETKLP AVEEDLKQKL IPKDPEEEKN AIVEIRAGAG
GDEASLFAGD LFRLYTQYAK QQGWTYELID ASPGTQGGFR EVIFAVKGED VYGTLKYEAG
VHRVQRVPET ESSGRIHTSA ATVAVLPEAE EVDVDINPSD LTIETFKATG PGGQSVNTTD
SAVRIKHAPS GVEVSCQDEK SQHKNRSKAM RVLRSRVYEK KREEQQAERE EARRSMVGSG
DRSAKIRTYN FPQDRVTDHR LEGGQKNHSL QPIMDGEIDP IIDALRAEEH AEKLANL
