RF1_BORA1
ID RF1_BORA1 Reviewed; 360 AA.
AC Q2KZZ3;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
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}; OrderedLocusNames=BAV0297;
OS Bordetella avium (strain 197N).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N;
RX PubMed=16885469; DOI=10.1128/jb.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAJ47902.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AM167904; CAJ47902.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_039051975.1; NC_010645.1.
DR AlphaFoldDB; Q2KZZ3; -.
DR SMR; Q2KZZ3; -.
DR STRING; 360910.BAV0297; -.
DR PRIDE; Q2KZZ3; -.
DR EnsemblBacteria; CAJ47902; CAJ47902; BAV0297.
DR GeneID; 41392226; -.
DR KEGG; bav:BAV0297; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_4; -.
DR OrthoDB; 928964at2; -.
DR Proteomes; UP000001977; 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..360
FT /note="Peptide chain release factor 1"
FT /id="PRO_0000263240"
FT REGION 284..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..302
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 360 AA; 40062 MW; 8192BC8D899AEE40 CRC64;
MKSSMLGRLE QLAHRLIEVD ALLADPDSAG DMDRFRRLSR ERAELEPVVL AFNAFQSTQA
DLATAQEMLA DPEMKAMAEE EIKAARERIE VLEGELQVLL LPRDPNDGRS LFLEIRAGTG
GDESALFSGD LLRMYSRYAE SQGWRVEIMS ESPSELGGYK EVIARIDGDG AYGRLKFESG
AHRVQRVPAT EAQGRIHTSA CTVAVMPEAD EMNDIVINPA DLRIDTFRAS GAGGQHINKT
DSAVRITHLP TGLVVECQDD RSQHRNKDRA MQVLAARLKD KELRERQSKE AAERKSLVGS
GDRSERIRTY NYPQGRVTDH RINLTLYKLQ QILEGDLNEL TGALLAEHQA EQLAALGEDI
