RF1_SYNS3
ID RF1_SYNS3 Reviewed; 364 AA.
AC Q0ID34;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=sync_0408;
OS Synechococcus sp. (strain CC9311).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=64471;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9311;
RX PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA Paulsen I.T.;
RT "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT coastal environment.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(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}.
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DR EMBL; CP000435; ABI46749.1; -; Genomic_DNA.
DR RefSeq; WP_011618376.1; NC_008319.1.
DR AlphaFoldDB; Q0ID34; -.
DR SMR; Q0ID34; -.
DR STRING; 64471.sync_0408; -.
DR EnsemblBacteria; ABI46749; ABI46749; sync_0408.
DR KEGG; syg:sync_0408; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_3; -.
DR OMA; ISDHRVG; -.
DR OrthoDB; 928964at2; -.
DR Proteomes; UP000001961; 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..364
FT /note="Peptide chain release factor 1"
FT /id="PRO_0000263373"
FT REGION 289..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 239
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 364 AA; 40518 MW; CBCEAB97E2DAD419 CRC64;
MDTTTLISRL EAASSSFHNL ERQLADPDVA ADPQRLETIA RERSRLEPLV LDYTSLQKVE
AEQVQAKSLL KESRGDAAME ELAQQELQEL DRHHADLIQR ITLALLPKDP RDERSVMLEI
RAGAGGDEAC LWAGDLARMY ERFSSRRGWS VTPVSANEAD LGGYKELILS VKGDAVFSEL
KFEAGVHRVQ RVPSTESQGR VHTSTATVAV MPEADPVEVQ IDPRDLDIST ARSGGAGGQN
VNKVETAVDL MHKPTGIRVF CTQERSQMQN RERALEILRA KLYERQLAEA NASERSARRS
QVGTGDRSEK IRTYNAKDNR MTDHRLGRNF SLDPVLEGQM DDVIDACIAE EQRGKLADLS
EQAD
