ID A0A2T0S6V6_9PSEU Unreviewed; 367 AA.
AC A0A2T0S6V6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Peptide chain release factor 2 {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=CLV43_12636 {ECO:0000313|EMBL:PRY29161.1};
OS Umezawaea tangerina.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Umezawaea.
OX NCBI_TaxID=84725 {ECO:0000313|EMBL:PRY29161.1, ECO:0000313|Proteomes:UP000239494};
RN [1] {ECO:0000313|EMBL:PRY29161.1, ECO:0000313|Proteomes:UP000239494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44720 {ECO:0000313|EMBL:PRY29161.1,
RC ECO:0000313|Proteomes:UP000239494};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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|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}.
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:PRY29161.1}.
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DR EMBL; PVTF01000026; PRY29161.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0S6V6; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000239494; 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00094};
KW Methylation {ECO:0000256|ARBA:ARBA00022481, ECO:0000256|HAMAP-
KW Rule:MF_00094}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00094};
KW Reference proteome {ECO:0000313|Proteomes:UP000239494}.
FT DOMAIN 243..259
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT MOD_RES 250
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 367 AA; 40885 MW; AEE06E8D41A197FC CRC64;
MNPDVEADIK DLSATLGSIE AVMDLDTLRA QVADLEEQAA LPDLWNDQEK AQKLTSELSH
KQGELRRITN LRGRLEDLGI MYELAEAEDD ADSIADADGE RAKLREEIAS LEVRTLLSGE
YDERNALITV RAEAGGIDAA DFAEMLLRMY SRWAERHGYG VDVFDTSYAE EAGIKSATFR
ITAPYAYGTL SVEQGTHRLV RISPFDNQGR RQTSFAGVEV VPVVEQTDHV EIDEKDLRVD
VYRSSGPGGQ GVNTTDSAVR LTHIPTGIVV SCQNERSQLQ NKATAMAVLQ AKLLERQRQE
DKDKMDALKD SGSSWGNQMR SYVLHPYQMV KDLRTEHEVG NPGAVLDGEI DDFLEAGIRW
RKQQQTS
//
