RF1_ACIC5
ID RF1_ACIC5 Reviewed; 358 AA.
AC C1F2J1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 67.
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=ACP_2651;
OS Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / BCRC 80197 / JCM
OS 7670 / NBRC 15755 / NCIMB 13165 / 161).
OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae;
OC Acidobacterium.
OX NCBI_TaxID=240015;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51196 / DSM 11244 / BCRC 80197 / JCM 7670 / NBRC 15755 / NCIMB
RC 13165 / 161;
RX PubMed=19201974; DOI=10.1128/aem.02294-08;
RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT "Three genomes from the phylum Acidobacteria provide insight into the
RT lifestyles of these microorganisms in soils.";
RL Appl. Environ. Microbiol. 75:2046-2056(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; CP001472; ACO31733.1; -; Genomic_DNA.
DR RefSeq; WP_015897716.1; NC_012483.1.
DR AlphaFoldDB; C1F2J1; -.
DR SMR; C1F2J1; -.
DR STRING; 240015.ACP_2651; -.
DR EnsemblBacteria; ACO31733; ACO31733; ACP_2651.
DR KEGG; aca:ACP_2651; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_0; -.
DR OMA; ISDHRVG; -.
DR OrthoDB; 928964at2; -.
DR Proteomes; UP000002207; 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.
PE 3: Inferred from homology;
KW Cytoplasm; Methylation; Protein biosynthesis; Reference proteome.
FT CHAIN 1..358
FT /note="Peptide chain release factor 1"
FT /id="PRO_1000193462"
FT MOD_RES 232
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 358 AA; 40629 MW; AFECF9D6534B47BF CRC64;
MFERLEQIET RYEELGREMA DPALIADQQK YQKTAKQHRE LEDVVEKFRE YREVQNGIAD
ARGMMNEADA EIRAMAEEEL ASLEERLPQI EADLKLLLLP KDPNDEKNVV VEIRAGTGGD
EASLFAAEVF RMYARYAEQR RWKVEVLSMS ESSVGGAKEV IAIIEGDHVY SQMKYESGVH
RVQRVPATET QGRVHTSAIT VAVLPEAEEV DVKIEAKDLR IDTFCSSGPG GQSVNTTYSA
VRITHLPTNT VVSCQDEKSQ IKNREKAMRV LRSRLYEVEM ERQQQALAKE RKQQVGSGDR
SEKIRTYNFP QNRLTDHRIG LTIHQLAEVM EGRLQPVIDA LTAHFNAERL KAESEAVA
