RF1_GLOVI
ID RF1_GLOVI Reviewed; 364 AA.
AC Q7ND15;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 102.
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=glr4421;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
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; BA000045; BAC92362.1; -; Genomic_DNA.
DR RefSeq; NP_927367.1; NC_005125.1.
DR RefSeq; WP_011144404.1; NC_005125.1.
DR AlphaFoldDB; Q7ND15; -.
DR SMR; Q7ND15; -.
DR STRING; 251221.35214996; -.
DR EnsemblBacteria; BAC92362; BAC92362; BAC92362.
DR KEGG; gvi:glr4421; -.
DR PATRIC; fig|251221.4.peg.4451; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_3; -.
DR InParanoid; Q7ND15; -.
DR OMA; ISDHRVG; -.
DR OrthoDB; 928964at2; -.
DR PhylomeDB; Q7ND15; -.
DR Proteomes; UP000000557; 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..364
FT /note="Peptide chain release factor 1"
FT /id="PRO_0000177677"
FT MOD_RES 239
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 364 AA; 41131 MW; 6B907C43AAED998B CRC64;
MASPDLMVQK LNDIERTYND LTTRLGDPSL ASNPQEMLRI VRMRAGLERT VEAYDHWQRL
CAERNAVRQM IRDEQDPELR ELAEEEHTGL EERIARLEDE ITLLLLPRDP NDDKNVMLEI
RAGTGGDEAA IFAGDLMRMY IRYAEGQGWS VKLASESPAE MGGFKEVILE IRGESVYSKL
KFEAGVHRVQ RVPVTETQGR VHTSTATVAI MPEVEEVDVE INPNDIEITT TRSGGAGGQN
VNKVETAVHL VHKPSGIHIH CQEERSQLQN KARAMQILRV KLYDIKQREQ HEQVSGLRRS
QVGTGDRSEK IRTYNYKDNR VTDHRLSQNF TLNTAIEGEI ETLIQSAIAA AQREQLAELA
RSSG
