RF1_DESDA
ID RF1_DESDA Reviewed; 356 AA.
AC B8J4R4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=Ddes_2299;
OS Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=525146;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27774 / DSM 6949 / MB;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Hazen T.C.;
RT "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str.
RT ATCC 27774.";
RL Submitted (JAN-2009) 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; CP001358; ACL50194.1; -; Genomic_DNA.
DR RefSeq; WP_015939299.1; NC_011883.1.
DR AlphaFoldDB; B8J4R4; -.
DR SMR; B8J4R4; -.
DR STRING; 525146.Ddes_2299; -.
DR EnsemblBacteria; ACL50194; ACL50194; Ddes_2299.
DR KEGG; dds:Ddes_2299; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_7; -.
DR OMA; ISDHRVG; -.
DR OrthoDB; 928964at2; -.
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..356
FT /note="Peptide chain release factor 1"
FT /id="PRO_1000193486"
FT REGION 281..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 232
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 356 AA; 40054 MW; A8F77E16263A6BA4 CRC64;
MFAKLEGLEK KYLELEEALA QPDVFNDQDQ YRKLTKAHAD LSDVVELFRR HRAVSEELAE
NRLLLHDEDP EIRAMAQEEV HRGEAELPNL EHELKVMLLP SDPLDEKNTI LEIRAGTGGE
EAALFAADLF RMYTRYAELK NWKVEIMSES PSENGGYKEI ICLIAGDRVY SHLKFEAGTH
RVQRVPATEA QGRIHTSAAT VAVMPEAEEV DVEIRPEDLR IDIYRASGAG GQHVNKTESA
VRITHLPTNT VVTCQDERSQ HKNKARAMKV LASRILAAER ERQSSELSAD RKAQVGSGDR
SERIRTYNFP QGRCTDHRIN LTLYSLDRIM EGELESLVEA LGTAAQAEAL KAQASE
