RF1_SHEB5
ID RF1_SHEB5 Reviewed; 363 AA.
AC A3D0G1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=Sbal_0696;
OS Shewanella baltica (strain OS155 / ATCC BAA-1091).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=325240;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS155 / ATCC BAA-1091;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brettar I.,
RA Klappenbach J., Konstantinidis K., Rodrigues J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS155.";
RL Submitted (FEB-2007) 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; CP000563; ABN60224.1; -; Genomic_DNA.
DR RefSeq; WP_011845827.1; NC_009052.1.
DR AlphaFoldDB; A3D0G1; -.
DR SMR; A3D0G1; -.
DR STRING; 325240.Sbal_0696; -.
DR EnsemblBacteria; ABN60224; ABN60224; Sbal_0696.
DR KEGG; sbl:Sbal_0696; -.
DR HOGENOM; CLU_036856_0_1_6; -.
DR OMA; ISDHRVG; -.
DR Proteomes; UP000001557; 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.
FT CHAIN 1..363
FT /note="Peptide chain release factor 1"
FT /id="PRO_1000004947"
FT REGION 286..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..304
FT /note="Basic and acidic residues"
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 363 AA; 40505 MW; 6ECCCBAB3BAF8FD9 CRC64;
MKESVIRKLE GLLERNEEVM ALLGDASVIS DQDRFRALSK EYAQLEDVVA GFKAYQQAQV
DLDSAKEMLE EDDAEMREMA QEEMKAAKAK LEHLEDELQI LLLPKDPDDD KNAFVEIRAG
AGGDEAAIFA GDLFRMYSRY AEANRWQIEI MSCNEGEHGG FKEVIMKVSG DGVYGKLKFE
SGGHRVQRVP ETESQGRVHT SAVTVVVLHE VPEAEAISIN PADLKVDTFR SSGAGGQHVN
KTDSAIRITH IPTGIVVECQ DQRSQHKNRA QAMSVLAARI QALEDEKRRS AEESTRRSLV
ASGDRSERVR TYNFPQGRVS EHRINLTLYR LNEVMEGDLD AILLPLMQEH QADQLAALAD
EQG
