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RF1_RHILW
ID   RF1_RHILW               Reviewed;         359 AA.
AC   B5ZRR4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Rleg2_3524;
OS   Rhizobium leguminosarum bv. trifolii (strain WSM2304).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395492;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM2304;
RX   PubMed=21304679; DOI=10.4056/sigs.44642;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA   Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA   Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA   Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv trifolii strain
RT   WSM2304, an effective microsymbiont of the South American clover Trifolium
RT   polymorphum.";
RL   Stand. Genomic Sci. 2:66-76(2010).
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; CP001191; ACI56791.1; -; Genomic_DNA.
DR   RefSeq; WP_012559093.1; NC_011369.1.
DR   AlphaFoldDB; B5ZRR4; -.
DR   SMR; B5ZRR4; -.
DR   STRING; 395492.Rleg2_3524; -.
DR   EnsemblBacteria; ACI56791; ACI56791; Rleg2_3524.
DR   KEGG; rlt:Rleg2_3524; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_5; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000008330; 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..359
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000093494"
FT   REGION          280..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..301
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         235
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   359 AA;  40007 MW;  78662E1EFC6BF79D CRC64;
     MAKLPVEKMR ELERRFGEIE ARMSAGPAAD VYVKLASEYS ELQPVVTKIR AYEKAIAELA
     DLETLLEDKS VDREMRDLAE LELPEVKEQI EALEQEMQIL LLPKDAADEK SAILEIRAGT
     GGSEAALFAG DLFRMYERFS AEKGWKVEVL SASEGEAGGY KEIIATITGR GVFAKLKFES
     GVHRVQRVPE TEAGGRIHTS AATVAVLPEA EEIDIEIRPE DIRIDTMRSS GAGGQHVNTT
     DSAVRITHLP SGIVVTSSEK SQHQNRAKAM QVLRSRLYDA ERQRADSERS ADRKSQVGSG
     DRSERIRTYN FPQGRITDHR INLTLYKLDR MMEGEIEEVV DALMADYQAS QLAQLGEQQ
 
 
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