ID A0A371P0M2_9BACL Unreviewed; 356 AA.
AC A0A371P0M2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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 ECO:0000313|EMBL:REK69489.1};
GN ORFNames=DX130_23555 {ECO:0000313|EMBL:REK69489.1};
OS Paenibacillus paeoniae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=2292705 {ECO:0000313|EMBL:REK69489.1, ECO:0000313|Proteomes:UP000261905};
RN [1] {ECO:0000313|EMBL:REK69489.1, ECO:0000313|Proteomes:UP000261905}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M4BSY-1 {ECO:0000313|EMBL:REK69489.1,
RC ECO:0000313|Proteomes:UP000261905};
RA Tuo L.;
RT "Paenibacillus sp. M4BSY-1, whole genome shotgun sequence.";
RL Submitted (AUG-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:REK69489.1}.
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DR EMBL; QUBQ01000007; REK69489.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371P0M2; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000261905; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00093};
KW Methylation {ECO:0000256|ARBA:ARBA00022481, ECO:0000256|HAMAP-
KW Rule:MF_00093};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00093}; Reference proteome {ECO:0000313|Proteomes:UP000261905}.
FT DOMAIN 62..177
FT /note="Peptide chain release factor"
FT /evidence="ECO:0000259|SMART:SM00937"
FT COILED 41..94
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 233
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 356 AA; 40339 MW; 22B4C911606F4DCA CRC64;
MFDRLQALAD RYEKLSELLC DPDVSSDPKR LRDLSKEQSD LQEAHDAYTE YKQVTEQLED
AKLMQGEKMD DEMREMVKME IDELSARKAE LEEIMRILLL PKDPNDDKNV IVEIRGAAGG
DEAALFAYEL YRMYTKFADS QGWRVELMEF TENDLGGFKE VIFSINGKGA YSKLKYESGA
HRVQRIPVTE SGGRIHTSTS TVAVMPEVEE VEIEISDKDI RIDTFCSSGA GGQSVNTTKS
AVRVLHVPTG IMATCQDGKS QNDNKAKALQ VLRARIYDIR RQEEEAKYAG ERKSKVGTGD
RSERIRTYNF PQSRVTDHRI NLTLHRLDSV MNGDIADIIS SLTIAEQADM MERESM
//
