RF1_PROMP
ID RF1_PROMP Reviewed; 364 AA.
AC Q7UZX1;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 99.
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=PMM1529;
OS Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS MED4).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1986 / NIES-2087 / MED4;
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(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; BX548174; CAE19988.1; -; Genomic_DNA.
DR RefSeq; WP_011133157.1; NC_005072.1.
DR AlphaFoldDB; Q7UZX1; -.
DR SMR; Q7UZX1; -.
DR STRING; 59919.PMM1529; -.
DR EnsemblBacteria; CAE19988; CAE19988; PMM1529.
DR KEGG; pmm:PMM1529; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_3; -.
DR OMA; ISDHRVG; -.
DR OrthoDB; 928964at2; -.
DR Proteomes; UP000001026; 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..364
FT /note="Peptide chain release factor 1"
FT /id="PRO_0000263318"
FT MOD_RES 239
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 364 AA; 40966 MW; 93356F8BA780AE44 CRC64;
MEYTTLIARL KNASESFVNL EMQLADPDIA NNPKKLESIA RERAKLEPLV LDFNQLLDTD
KEIGDSKQLL KENRNDKDME SLINEELFSL EDLKNQLIEK LTIALLPKDP RDERSVMLEI
RAGAGGNEAC IWAGDLARMY ERYGQKIGWT VKPISASESD MGGFKELVIS VKGDSVYSQL
KFEAGVHRVQ RVPATESQGR VHTSTATVAV MPEADPVEVK IDPTEIEIGT ARSGGAGGQN
VNKVETAIDL IHKPTGIRVF CTQERSQLQN RERAMEILRA KLYEIQLKEA NAKERSQRLM
QVGSGDRSEK IRTYNFKDNR TTDHRLGSNF ALEPILAGQL DDVIYACLAQ EQKRMLEDFN
ENEN