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Database: UniProt
Entry: R6DFN5_9CLOT
LinkDB: R6DFN5_9CLOT
Original site: R6DFN5_9CLOT 
ID   R6DFN5_9CLOT            Unreviewed;       358 AA.
AC   R6DFN5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=BN547_01740 {ECO:0000313|EMBL:CDA87328.1};
OS   Clostridium sp. CAG:230.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262782 {ECO:0000313|EMBL:CDA87328.1, ECO:0000313|Proteomes:UP000017961};
RN   [1] {ECO:0000313|EMBL:CDA87328.1, ECO:0000313|Proteomes:UP000017961}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:230 {ECO:0000313|Proteomes:UP000017961};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDA87328.1}.
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DR   EMBL; CBCQ010000143; CDA87328.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6DFN5; -.
DR   STRING; 1262782.BN547_01740; -.
DR   Proteomes; UP000017961; 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; -; 2.
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:UP000017961}.
FT   DOMAIN          226..242
FT                   /note="Prokaryotic-type class I peptide chain release
FT                   factors"
FT                   /evidence="ECO:0000259|PROSITE:PS00745"
FT   REGION          280..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          48..94
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        280..300
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         233
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   358 AA;  40828 MW;  90951383D421CD54 CRC64;
     MFERLEDLVR RLEELNIELT DPDTINNQEK YRQLMKEQNE LTPIVEKYLE YKKAKEGVED
     SLALLEEEND EEMRELAKEE LNECKQTVEQ CEQELKILML PKDPNDDKNV IVEIRGGAGG
     DEAALFAADL FRMYSKFAER NHWKVEVMSA NENGIGGFKE IVFMVIGQGA YSKLKYESGV
     HRVQRIPSTE SGGRIHTSTA TVAIMPEVED VEVYVDPNDC KIDVYRASGN GGQCVNTTDS
     AVRITHIPTG IVVTCQDEKS QLKNKDKAMK VLRSRIYDME QEKANSEQAA ERRSQVGTGD
     RSEKIRTYNF PQGRVTDHRI KFTSHRLNEI LEGDINELLQ NIIMADQTAK LEKMNESA
//
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