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RF1_SHEPA
ID   RF1_SHEPA               Reviewed;         361 AA.
AC   A8H7A5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-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=Spea_3126;
OS   Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=398579;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700345 / ANG-SQ1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S.Z., Manno D., Hawari J., Richardson P.;
RT   "Complete sequence of Shewanella pealeana ATCC 700345.";
RL   Submitted (OCT-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; CP000851; ABV88442.1; -; Genomic_DNA.
DR   RefSeq; WP_012156344.1; NC_009901.1.
DR   AlphaFoldDB; A8H7A5; -.
DR   SMR; A8H7A5; -.
DR   STRING; 398579.Spea_3126; -.
DR   EnsemblBacteria; ABV88442; ABV88442; Spea_3126.
DR   KEGG; spl:Spea_3126; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_6; -.
DR   OMA; ISDHRVG; -.
DR   Proteomes; UP000002608; 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; Reference proteome.
FT   CHAIN           1..361
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000075516"
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;  40319 MW;  F027404F3DFADA98 CRC64;
     MKDSVIRKLE GLLERNEEVL ALLSDAGVIA DQERFRALSK EYSQLEDVVS TFKSFQQAEE
     DLESAKEMME EDDPELKEMA QEEYKVAKSA IAALEDELQI LLLPKDPNDD NNCFIEIRAG
     AGGDEAAIFA GDLFRMYSRY AESKRWQIEV MNTNEGEHGG FKEVIAKISG EGVYGKLKFE
     SGGHRVQRVP ETESQGRVHT SACTVIVLPE VPEAEAIEIN KADLKVDTFR ASGAGGQHVN
     KTDSAIRITH IPTGIVVECQ DQRSQHKNRA QAMSVLAARI QAVEDEKRRS AEESTRRNLV
     SSGDRSERIR TYNFPQGRVS EHRINLTLYR LGEFMEGDID CVVEPLIQEN QADMLAALGE
     G
 
 
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