ID A0A1G9ECM9_9BACT Unreviewed; 356 AA.
AC A0A1G9ECM9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=SAMN05421823_103423 {ECO:0000313|EMBL:SDK73843.1};
OS Catalinimonas alkaloidigena.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Catalimonadaceae;
OC Catalinimonas.
OX NCBI_TaxID=1075417 {ECO:0000313|EMBL:SDK73843.1, ECO:0000313|Proteomes:UP000198510};
RN [1] {ECO:0000313|EMBL:SDK73843.1, ECO:0000313|Proteomes:UP000198510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25186 {ECO:0000313|EMBL:SDK73843.1,
RC ECO:0000313|Proteomes:UP000198510};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNFO01000003; SDK73843.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9ECM9; -.
DR STRING; 1075417.SAMN05421823_103423; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000198510; Unassembled WGS sequence.
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:UP000198510}.
FT DOMAIN 63..177
FT /note="Peptide chain release factor"
FT /evidence="ECO:0000259|SMART:SM00937"
FT MOD_RES 233
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 356 AA; 40571 MW; EEAC3A9E141E5206 CRC64;
MIDKLEAIRQ RFEEVGHLIV QPDVVSDMKR YSKLSKEYKD LEKIVEKYRP YRLTLDNIEN
AKQLLTTEKD PEFREMAKEE LETLQETREA QEEELKTMLI PKDPNDSRNV IMEIRGGAGG
DEAAIFAGDL FRMYQRFAEE RNWRMEILDY TEGTSGGYKE IIANVSGDDV YGMLKWESGV
HRVQRVPATE TQGRVHTSAA SVAVLPEVEE VDVELNMNDI RKDTFCSSGP GGQSVNTTYS
AIRLTHIPTG IVVQCQDEKS QIKNFEKALK VLRSRLYDIE LAKQNEELGA QRKAMVGSGD
RSDKIRTYNY PQSRVTDHRI GHTVYNLPAV MDGDIGDFIE QLRLADNAEK LKEGQA
//
