ID A0A1I4XVP4_9CLOT Unreviewed; 331 AA.
AC A0A1I4XVP4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Peptide chain release factor 2 {ECO:0000256|ARBA:ARBA00019192, ECO:0000256|HAMAP-Rule:MF_00094};
DE Short=RF-2 {ECO:0000256|HAMAP-Rule:MF_00094};
GN Name=prfB {ECO:0000256|HAMAP-Rule:MF_00094};
GN ORFNames=SAMN04488695_101184 {ECO:0000313|EMBL:SFN29319.1};
OS Proteiniclasticum ruminis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Proteiniclasticum.
OX NCBI_TaxID=398199 {ECO:0000313|EMBL:SFN29319.1, ECO:0000313|Proteomes:UP000181899};
RN [1] {ECO:0000313|EMBL:SFN29319.1, ECO:0000313|Proteomes:UP000181899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ML2 {ECO:0000313|EMBL:SFN29319.1,
RC ECO:0000313|Proteomes:UP000181899};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Peptide chain release factor 2 directs the termination of
CC translation in response to the peptide chain termination codons UGA and
CC UAA. {ECO:0000256|ARBA:ARBA00002613, ECO:0000256|HAMAP-Rule:MF_00094}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00094}.
CC -!- PTM: Methylated by PrmC. Methylation increases the termination
CC efficiency of RF2. {ECO:0000256|HAMAP-Rule:MF_00094}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000256|ARBA:ARBA00010835, ECO:0000256|HAMAP-
CC Rule:MF_00094}.
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DR EMBL; FOVK01000001; SFN29319.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4XVP4; -.
DR STRING; 398199.SAMN05421804_104238; -.
DR eggNOG; COG1186; Bacteria.
DR Proteomes; UP000181899; 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; 1.20.58.410; Release factor; 1.
DR HAMAP; MF_00094; Rel_fac_2; 1.
DR InterPro; IPR005139; PCRF.
DR InterPro; IPR000352; Pep_chain_release_fac_I.
DR InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR InterPro; IPR004374; PrfB.
DR NCBIfam; TIGR00020; prfB; 1.
DR PANTHER; PTHR43116; PEPTIDE CHAIN RELEASE FACTOR 2; 1.
DR PANTHER; PTHR43116:SF3; RF_PROK_I DOMAIN-CONTAINING PROTEIN; 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_00094};
KW Methylation {ECO:0000256|ARBA:ARBA00022481, ECO:0000256|HAMAP-
KW Rule:MF_00094};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00094}; Reference proteome {ECO:0000313|Proteomes:UP000181899}.
FT DOMAIN 203..219
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT COILED 16..43
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 232..266
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 210
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 331 AA; 37270 MW; BC5B48613A9858CD CRC64;
MQEGSFWNNL EEAKQVTQEE KAIESTIKEY SELRARVEDA LDMVELTDDD EEMQTLLLGE
VKDLKKGVEA MHLKVLLSGE YDNNDVILTL KSGVGGTDAQ DWTSMLLRMY TRWAEKKGFS
VELLSLQDGD EAGIRDASLK ITGPYAYGYL KAEKGIHRLV RISPFNASGK RQTSFASVEA
VPLLKDDSEV VIKDDELRID TYRSTGAGGQ HVNTTDSAVR ITHLPTGIVV TCQNERSQIQ
NKETAMKMLK AKLVELKERF HKEKIEDITG EMKDMGWGSQ IRSYVFNPYN LVKDHRTLEE
DANVDAVMDG DLDRFISAYL KSMSNGSLRA E
//
