ID A0A2N5MNG8_9BACI Unreviewed; 356 AA.
AC A0A2N5MNG8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-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 ECO:0000313|EMBL:PLT35882.1};
GN ORFNames=CUU64_00995 {ECO:0000313|EMBL:PLT35882.1};
OS Bacillus sp. V5-8f.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2053044 {ECO:0000313|EMBL:PLT35882.1, ECO:0000313|Proteomes:UP000235260};
RN [1] {ECO:0000313|EMBL:PLT35882.1, ECO:0000313|Proteomes:UP000235260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V5-8f {ECO:0000313|EMBL:PLT35882.1,
RC ECO:0000313|Proteomes:UP000235260};
RA Seuylemezian A., Cooper K., Vaishampayan P.;
RT "Comparitive Functional Genomics of Dry Heat Resistant Strains Isolated
RT from the Viking Spacecraft.";
RL Submitted (NOV-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}.
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:PLT35882.1}.
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DR EMBL; PGUW01000001; PLT35882.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5MNG8; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000235260; 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.
DR PROSITE; PS00745; RF_PROK_I; 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:UP000235260}.
FT DOMAIN 226..242
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT COILED 48..101
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; 40732 MW; C63244777CBE87B1 CRC64;
MLDRLQAVED RYEKLNELLS DPETLNDSKK LREYSKEQSD IQETVQAYRE YKEVREQFQD
AKAMLEEKLD AEMREMVKEE LNELEERMES LEERLKILLI PKDPNDDKNV IMEIRGAAGG
DEAALFAGSL YRMYTRYAET KGWKIDVMDS NPTGLGGFKE IIFMINGNGA YSRLKYENGA
HRVQRVPETE SGGRIHTSTA TVAVLPEAEE VEVEIHEKDI RVDTFASSGP GGQSVNTTMS
AVRLTHMPTG IVVSMQDEKS QIKNKEKAMK ILRARVYDKF QQEAQAEYDQ NRKLAVGTGD
RSERIRTYNF PQNRVTDHRI GLTIQKLDQI IEGKLDEVID TLILEDQSSK LQNADE
//
