RF1_SYNY3
ID RF1_SYNY3 Reviewed; 365 AA.
AC P74707;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Peptide chain release factor 1;
DE Short=RF-1;
GN Name=prfA; OrderedLocusNames=sll1110;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Methylated by PrmC. Methylation increases the termination
CC efficiency of RF1 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000305}.
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DR EMBL; BA000022; BAA18826.1; -; Genomic_DNA.
DR PIR; S76914; S76914.
DR AlphaFoldDB; P74707; -.
DR SMR; P74707; -.
DR IntAct; P74707; 2.
DR STRING; 1148.1653916; -.
DR PaxDb; P74707; -.
DR EnsemblBacteria; BAA18826; BAA18826; BAA18826.
DR KEGG; syn:sll1110; -.
DR eggNOG; COG0216; Bacteria.
DR InParanoid; P74707; -.
DR OMA; ISDHRVG; -.
DR PhylomeDB; P74707; -.
DR Proteomes; UP000001425; 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 GO; GO:0009658; P:chloroplast organization; IBA:GO_Central.
DR GO; GO:0010027; P:thylakoid membrane organization; IBA:GO_Central.
DR GO; GO:0006415; P:translational termination; IBA:GO_Central.
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..365
FT /note="Peptide chain release factor 1"
FT /id="PRO_0000177760"
FT MOD_RES 239
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 365 AA; 41126 MW; D565402A35E27EAC CRC64;
MAETYLLDKL ASVEQTYQEL TRMLADPDIA TNPDELQRVA KARSSLEETV DTYETWKRSQ
EDLKGARQIV KESGNDPEMR EMAQLEVEEL ENAIGELEKR LTILLLPKDP NDEKNIMLEI
RAGTGGDEAS IWAGDLVRMY TRYAESQGWK VSLLSESLAD MGGFKEAILE VKGDRVYSQL
KFEAGVHRVQ RVPVTEAGGR VHTSTATVAI MPEVDDVEVK IDPKDIEMST ARSGGAGGQN
VNKVETAVDL FHKPTGIRIF CTEERSQLQN RERAMQILRA KLYDMMLQEQ NDAISSNRRS
QVGTGSRSEK IRTYNYKDNR VTDHRLGRNF DLNTALEGEI HTIIESCISQ DQQERLAELA
EATNN