RF1_SHESA
ID RF1_SHESA Reviewed; 363 AA.
AC A0KT88;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 25-MAY-2022, entry version 84.
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=Shewana3_0769;
OS Shewanella sp. (strain ANA-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=94122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANA-3;
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 Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL Submitted (SEP-2006) 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; CP000469; ABK47007.1; -; Genomic_DNA.
DR RefSeq; WP_011715925.1; NC_008577.1.
DR AlphaFoldDB; A0KT88; -.
DR SMR; A0KT88; -.
DR STRING; 94122.Shewana3_0769; -.
DR EnsemblBacteria; ABK47007; ABK47007; Shewana3_0769.
DR KEGG; shn:Shewana3_0769; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_6; -.
DR OMA; ISDHRVG; -.
DR OrthoDB; 928964at2; -.
DR Proteomes; UP000002589; 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_1000004951"
FT REGION 284..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..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; 40330 MW; 76705AFA466C6E59 CRC64;
MKESVIRKLE GLLERNEEVL ALLGDASVIA DQERFRALSK EYSQLEEVVA GFKAYQQAQA
DLESAKEMLE EDDAEMREMA QEEIKAAKAE LERLEAELQI LLLPKDPNDD TNAFIEIRAG
AGGDEAAIFA GDLFRMYSRY AEANRWQLEI MSSNEGEHGG FKEIIVKVSG EGAYGKLKFE
SGGHRVQRVP ETESQGRVHT SAVTVVVMHE VPEAEAISIN PADLKVDTFR SSGAGGQHVN
KTDSAIRITH IPTGIVVECQ DQRSQHKNRA QAMSVLAARI QAVEDEKRRS AEESTRRSLV
ASGDRSERVR TYNFPQGRVS EHRINLTLYR LNEVMEGDLD AILGPLMQEH QADLLAALAD
EQG
