ID A0A3L6ZSA0_9MICO Unreviewed; 369 AA.
AC A0A3L6ZSA0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
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 ECO:0000313|EMBL:RLP70744.1};
GN ORFNames=D9V29_09610 {ECO:0000313|EMBL:RLP70744.1};
OS Mycetocola manganoxydans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Mycetocola.
OX NCBI_TaxID=699879 {ECO:0000313|EMBL:RLP70744.1, ECO:0000313|Proteomes:UP000270299};
RN [1] {ECO:0000313|EMBL:RLP70744.1, ECO:0000313|Proteomes:UP000270299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC AB209002 {ECO:0000313|EMBL:RLP70744.1,
RC ECO:0000313|Proteomes:UP000270299};
RA Li J.;
RL Submitted (OCT-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:RLP70744.1}.
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DR EMBL; RCUV01000009; RLP70744.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L6ZSA0; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000270299; 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}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00094};
KW Reference proteome {ECO:0000313|Proteomes:UP000270299}.
FT DOMAIN 244..260
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT COILED 62..115
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 251
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 369 AA; 40735 MW; CFC2196384C2BC67 CRC64;
MLDLDLNDQI AAIRTTFADI REVVGIDRLR AEIADLSEQA GVPDLWDDTD KAQKITSDLS
HRQSELARIT AIENQLDDLE VLVGLAIAEG DEESAAEARS ELIDLQKQIG DLEVQTLLNG
EYDPMAAVVT IRAGAGGVDA ADFADMLFRM YLRWAEQHKY KAKVLDTSYA EEAGIKSATF
EIDAPYAFGT LSVEAGTHRL VRMSPFNSAG KRQTSFAAVE VVPLMPETEE VDIPDNDIRV
DVFRSSGPGG QSVNTTDSAV RITHLPTGIV VSCQNEKSQI QNRAAAMRVL KSRLLLVQRE
QENAKKKELA GNITASWGDQ MRSYVLAPYQ MVKDLRTEHE VNNPQNVFDG DIDGFIAAGI
RWRKQPTDD
//
