RF1_NEIM0
ID RF1_NEIM0 Reviewed; 358 AA.
AC A9M1Q8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=NMCC_1599;
OS Neisseria meningitidis serogroup C (strain 053442).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=374833;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=053442;
RX PubMed=18031983; DOI=10.1016/j.ygeno.2007.10.004;
RA Peng J., Yang L., Yang F., Yang J., Yan Y., Nie H., Zhang X., Xiong Z.,
RA Jiang Y., Cheng F., Xu X., Chen S., Sun L., Li W., Shen Y., Shao Z.,
RA Liang X., Xu J., Jin Q.;
RT "Characterization of ST-4821 complex, a unique Neisseria meningitidis
RT clone.";
RL Genomics 91:78-87(2008).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000381; ABX73747.1; -; Genomic_DNA.
DR RefSeq; WP_012221933.1; NC_010120.1.
DR AlphaFoldDB; A9M1Q8; -.
DR SMR; A9M1Q8; -.
DR EnsemblBacteria; ABX73747; ABX73747; NMCC_1599.
DR KEGG; nmn:NMCC_1599; -.
DR HOGENOM; CLU_036856_0_1_4; -.
DR OMA; ISDHRVG; -.
DR Proteomes; UP000001177; 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..358
FT /note="Peptide chain release factor 1"
FT /id="PRO_1000075505"
FT MOD_RES 235
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 358 AA; 39660 MW; FC3CCDBBF5EDD5EC CRC64;
MKPSILEKLQ QLGDRLEEVT HLLGQPEATA DMDNYRKLTR EHAELTPVVE VFQNYRLAQS
DLADAEEMLS DPEMKDFAAE EIEAAKAKIG ALDTELQKLL LPKDADDDKN IFIEVRAGTG
GDEAALFAGD LLRMYSRYAE RNRWQVEIVS ANESELGGYK EVIARIIGLG AYSRLKFESG
GHRVQRVPAT ESQGRIHTSA CTVAVMPEAD ELEDIELNPV DLRIDTFRAS GAGGQHINKT
DSAVRITHLP TGMVVECQDG RSQHANKAQA MKVLAARLND AQKREAQAKE AAERKSLIGS
GDRSERIRTY NYPQGRVTDH RINLTLHKLD FVMDGDLAEI TDALIAEHQA ELLAAMGD