RF1_ALTMD
ID RF1_ALTMD Reviewed; 361 AA.
AC B4RSV6; F2G7L2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 85.
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};
GN OrderedLocusNames=MADE_1007645;
OS Alteromonas mediterranea (strain DSM 17117 / CIP 110805 / LMG 28347 / Deep
OS ecotype).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=1774373;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17117 / CIP 110805 / LMG 28347 / Deep ecotype;
RX PubMed=18670397; DOI=10.1038/ismej.2008.74;
RA Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S.,
RA Johnson J., Friedman R., Rodriguez-Valera F.;
RT "Comparative genomics of two ecotypes of the marine planktonic copiotroph
RT Alteromonas macleodii suggests alternative lifestyles associated with
RT different kinds of particulate organic matter.";
RL ISME J. 2:1194-1212(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; CP001103; AEA97669.1; -; Genomic_DNA.
DR RefSeq; WP_012518002.1; NC_011138.3.
DR AlphaFoldDB; B4RSV6; -.
DR SMR; B4RSV6; -.
DR EnsemblBacteria; AEA97669; AEA97669; MADE_1007645.
DR GeneID; 56341949; -.
DR KEGG; amc:MADE_1007645; -.
DR HOGENOM; CLU_036856_0_1_6; -.
DR OMA; ISDHRVG; -.
DR Proteomes; UP000001870; 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..361
FT /note="Peptide chain release factor 1"
FT /id="PRO_1000093419"
FT REGION 287..306
FT /note="Disordered"
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; 40417 MW; B79748B3C0C9D62C CRC64;
MKESVVRKLE HLVERFEEVQ ALLGDPEVIG DQDKFRNLSK EFSQLEDVVA GFNAYQQAQE
NLASAQEMLN EDDAEMREMA QEEMKEAKGE IERLETELQV LLLPKDPNDD NNCFLEIRAG
AGGDEAAIFA GDLFRMYSRY AESRGWRVEL VNANESEHGG YKEVVANVSG DGVYGVLKFE
SGGHRVQRVP ETESQGRIHT SACTVAVLPE IPESEAIEIN PAELRIDTFR ASGAGGQHVN
KTDSAIRITH LPTGLVVECQ DERSQHKNRA KAMSVLQARL NQIEEEKRAA EEASTRKSLV
GSGDRSERIR TYNFPQGRVT DHRINLTIYR LDEVVEGDLK QLVDPILQEH QADLLASLSD
E