RF1_PSET1
ID RF1_PSET1 Reviewed; 361 AA.
AC Q3IK95;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=PSHAa1058;
OS Pseudoalteromonas translucida (strain TAC 125).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=326442;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAC 125;
RX PubMed=16169927; DOI=10.1101/gr.4126905;
RA Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C.,
RA Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z.,
RA Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT "Coping with cold: the genome of the versatile marine Antarctica bacterium
RT Pseudoalteromonas haloplanktis TAC125.";
RL Genome Res. 15:1325-1335(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; CR954246; CAI86133.1; -; Genomic_DNA.
DR RefSeq; WP_011327744.1; NC_007481.1.
DR AlphaFoldDB; Q3IK95; -.
DR SMR; Q3IK95; -.
DR STRING; 326442.PSHAa1058; -.
DR EnsemblBacteria; CAI86133; CAI86133; PSHAa1058.
DR KEGG; pha:PSHAa1058; -.
DR PATRIC; fig|326442.8.peg.1015; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_6; -.
DR OMA; ISDHRVG; -.
DR OrthoDB; 928964at2; -.
DR BioCyc; PHAL326442:PSHA_RS05210-MON; -.
DR Proteomes; UP000006843; Chromosome I.
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..361
FT /note="Peptide chain release factor 1"
FT /id="PRO_0000263320"
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 361 AA; 40545 MW; C1CDFEB77CA60912 CRC64;
MKESVYHKLE ILVERYEEVQ ALLSDPSVIR DQNRFRALSK EYSDLEEVVK TFLSYQQAQQ
DVISAEEMLK DSDPDIREMA QEEYKEAKAQ ILTIEDEIQV LMLPKDPKDN NNVYLEVRAG
TGGDEAAIFA GDLFRMYSRY AETKKWKVDV VTTNEGEHGG YKEIIANISG EGVFGQLKFE
SGVHRVQRVP ETESQGRVHT SACTVAVMAE VPEAEAIEIN SADLKVDTFR ASGAGGQHVN
KTDSAIRITH IPTGVVVECQ DQRSQHKNRA KAMSVLAARL QQAEDEKRDA AEASERRNLV
GSGDRSERIR TYNYPQGRIT DHRINLTLYR LNEVVAGDLS CIVEPLMQEH QADLLAAMGD
E
