RF1_SOLM1
ID RF1_SOLM1 Reviewed; 357 AA.
AC C4XIQ1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=DMR_31280;
OS Solidesulfovibrio magneticus (strain ATCC 700980 / DSM 13731 / RS-1)
OS (Desulfovibrio magneticus).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Solidesulfovibrio.
OX NCBI_TaxID=573370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700980 / DSM 13731 / RS-1;
RX PubMed=19675025; DOI=10.1101/gr.088906.108;
RA Nakazawa H., Arakaki A., Narita-Yamada S., Yashiro I., Jinno K., Aoki N.,
RA Tsuruyama A., Okamura Y., Tanikawa S., Fujita N., Takeyama H.,
RA Matsunaga T.;
RT "Whole genome sequence of Desulfovibrio magneticus strain RS-1 revealed
RT common gene clusters in magnetotactic bacteria.";
RL Genome Res. 19:1801-1808(2009).
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; AP010904; BAH76619.1; -; Genomic_DNA.
DR RefSeq; WP_015861773.1; NC_012796.1.
DR AlphaFoldDB; C4XIQ1; -.
DR SMR; C4XIQ1; -.
DR STRING; 573370.DMR_31280; -.
DR PRIDE; C4XIQ1; -.
DR EnsemblBacteria; BAH76619; BAH76619; DMR_31280.
DR KEGG; dma:DMR_31280; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_7; -.
DR OMA; ISDHRVG; -.
DR Proteomes; UP000009071; 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..357
FT /note="Peptide chain release factor 1"
FT /id="PRO_1000202690"
FT REGION 282..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 232
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 357 AA; 39967 MW; 0EF0C9EBA17752E7 CRC64;
MFAKLESLER KYEDLERQLS APDVVSDQER FRKLSKTHSD LSDVVAAFRE YKKIAQDLED
NQEMAQDPDP EIRELAQAET KALKEAQVEL EARLKVLLLP KDPMDEKNIL LEIRAGTGGD
EAALFAGDLF RMYTRYAETK RWKVEIMSQS ETGSGGFKEV IASISGDKVY SRLKYESGAH
RVQRVPATES QGRIHTSAVT VAIMPEAEEV DVAIDPNELR IDVYRSSGPG GQSVNTTDSA
VRVTHIPSGL VVICQDEKSQ HKNKAKALKV LRSRLLQVEQ DKQRAEQEAA RRSQVGTGDR
SERIRTYNFP QGRVTDHRIN LTLYRLDAVL EGDLDELCGA LIGHYQAEAL KAQADAA
