RF1_RICCN
ID RF1_RICCN Reviewed; 355 AA.
AC Q92HK9;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 105.
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=RC0762;
OS Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=272944;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-613 / Malish 7;
RX PubMed=11557893; DOI=10.1126/science.1061471;
RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL Science 293:2093-2098(2001).
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; AE006914; AAL03300.1; -; Genomic_DNA.
DR PIR; B97795; B97795.
DR RefSeq; WP_010977378.1; NC_003103.1.
DR AlphaFoldDB; Q92HK9; -.
DR SMR; Q92HK9; -.
DR EnsemblBacteria; AAL03300; AAL03300; RC0762.
DR KEGG; rco:RC0762; -.
DR PATRIC; fig|272944.4.peg.866; -.
DR HOGENOM; CLU_036856_0_1_5; -.
DR OMA; ISDHRVG; -.
DR Proteomes; UP000000816; 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..355
FT /note="Peptide chain release factor 1"
FT /id="PRO_0000177730"
FT REGION 280..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 233
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 355 AA; 39746 MW; 8FF7C4DA2ACBEB8E CRC64;
MRFSDNLAKI LDKYENLGNK LSSGIMGDEF VKASKEYAEL EDVVAKIKEY NKAKSELEEA
NNFKLEVGLD NATLEMIEDE IYTLENSLPK LERAVKIALL PKDDADSKSA IIEVRAGSGG
EEAALFAAVL FNMYQRYAEL KGWHFEILAI SDTGIGGYKE ASASIKGKDV FSKLKFESGV
HRVQRVPETE SQGRIHTSAA TVAVLPEAEE VDIKIEDKDL RIDTYRASGA GGQHVNTTDS
AVRITHIPTG ITVALQDEKS QHKNKAKALK ILRARIYEEE RRKKEQERAD SRRGQVGSGD
RSERIRTYNF PQGRVSDHRI NLTLYKIDEV VKNGQLDEFV EALIADDEAK KLLEI