ID A0A1Y0H3G8_9BACT Unreviewed; 354 AA.
AC A0A1Y0H3G8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Peptide chain release factor 1 {ECO:0000256|HAMAP-Rule:MF_00093};
DE Short=RF-1 {ECO:0000256|HAMAP-Rule:MF_00093};
GN Name=prfA {ECO:0000256|HAMAP-Rule:MF_00093};
GN ORFNames=CCB80_13325 {ECO:0000313|EMBL:ARU42608.1};
OS Armatimonadetes bacterium Uphvl-Ar1.
OC Bacteria; Armatimonadota.
OX NCBI_TaxID=2004467 {ECO:0000313|EMBL:ARU42608.1, ECO:0000313|Proteomes:UP000196284};
RN [1] {ECO:0000313|EMBL:ARU42608.1, ECO:0000313|Proteomes:UP000196284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Uphvl-Ar1 {ECO:0000313|EMBL:ARU42608.1,
RC ECO:0000313|Proteomes:UP000196284};
RA Woodhouse J.N., Makower A.K., Ionescu D., Grossart H.-P., Neilan B.A.,
RA Dittmann E.;
RT "Draft genome sequences of three Uncultured Armatimonadetes, binned from a
RT Microcystis sp. enrichment culture and from Microcystis bloom
RT metagenomes.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00002986, ECO:0000256|HAMAP-Rule:MF_00093}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00093}.
CC -!- PTM: Methylated by PrmC. Methylation increases the termination
CC efficiency of RF1. {ECO:0000256|HAMAP-Rule:MF_00093}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000256|ARBA:ARBA00010835, ECO:0000256|HAMAP-
CC Rule:MF_00093}.
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DR EMBL; CP021423; ARU42608.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0H3G8; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000196284; 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 Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 3.30.70.1660; -; 1.
DR Gene3D; 6.10.140.1950; -; 1.
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 NCBIfam; TIGR00019; prfA; 1.
DR PANTHER; PTHR43804; LD18447P; 1.
DR PANTHER; PTHR43804:SF7; LD18447P; 1.
DR Pfam; PF03462; PCRF; 1.
DR Pfam; PF00472; RF-1; 1.
DR SMART; SM00937; PCRF; 1.
DR SUPFAM; SSF75620; Release factor; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00093};
KW Methylation {ECO:0000256|ARBA:ARBA00022481, ECO:0000256|HAMAP-
KW Rule:MF_00093}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00093};
KW Reference proteome {ECO:0000313|Proteomes:UP000196284}.
FT DOMAIN 59..174
FT /note="Peptide chain release factor"
FT /evidence="ECO:0000259|SMART:SM00937"
FT MOD_RES 230
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 354 AA; 39813 MW; 931ACC61E8376CA9 CRC64;
MIDKLTDIER KFEGVQERLM DPAVASNPAE MKSLGKTRAE LEPVVVVIRE YKSVVQQIAE
AEELLNDSEM REFANEELDK LRPLVPGLEA QLKVLLLPKD VNDDKSVIIE IRPAAGGDEA
GLFAAELFRM YTRYAERMSW KYDVIEFEET GIGGASRVVF SIDKEGAYSQ LKHESGVHRV
QRVPATETGG RIHTSTATVA VMPEAEEAEI EIKAEDIEVS TFRSSSAGGQ HMQKNETAIR
IVHKPSGVVV TCQDERSQQQ NKLRAMSVLR TKLYEMEQER IASERGELRR GQIGSGDRSE
KIRTYNFPQD RLTDHRIGLT LHSLPMIMDG DIQRVLDALV QEHQARLLAE DDGN
//
