ID A0A7H2BLZ0_9MICC Unreviewed; 371 AA.
AC A0A7H2BLZ0;
DT 10-FEB-2021, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2021, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=Peptide chain release factor 2 {ECO:0000256|HAMAP-Rule:MF_00094, ECO:0000256|NCBIfam:TIGR00020};
DE Short=RF-2 {ECO:0000256|HAMAP-Rule:MF_00094};
GN Name=prfB {ECO:0000256|HAMAP-Rule:MF_00094,
GN ECO:0000313|EMBL:QNV40686.1};
GN ORFNames=IDM48_04590 {ECO:0000313|EMBL:QNV40686.1};
OS Rothia amarae.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC Micrococcaceae; Rothia.
OX NCBI_TaxID=169480 {ECO:0000313|EMBL:QNV40686.1, ECO:0000313|Proteomes:UP000516421};
RN [1] {ECO:0000313|EMBL:QNV40686.1, ECO:0000313|Proteomes:UP000516421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KJZ-9 {ECO:0000313|EMBL:QNV40686.1,
RC ECO:0000313|Proteomes:UP000516421};
RA Ou Y., Kang Q.;
RT "Investigation of environmental microbe.";
RL Submitted (SEP-2020) 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; CP061538; QNV40686.1; -; Genomic_DNA.
DR RefSeq; WP_068171615.1; NZ_BAAAHX010000004.1.
DR AlphaFoldDB; A0A7H2BLZ0; -.
DR KEGG; rama:IDM48_04590; -.
DR Proteomes; UP000516421; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-UniRule.
DR FunFam; 3.30.160.20:FF:000004; Peptide chain release factor 1; 1.
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:SF3; CLASS I PEPTIDE CHAIN RELEASE FACTOR; 1.
DR PANTHER; PTHR43116; PEPTIDE CHAIN RELEASE FACTOR 2; 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|ARBA:ARBA00022490, 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:UP000516421}.
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 371 AA; 41308 MW; 4E353AE2E6DC1767 CRC64;
MASIDFSSEI KNLRFTYASI AQVSDIDALK KSIAELSEEA GAPSLWDDPE KAQKITSQLS
HRQSELERLT QTEESINDLE AMVELAEEED EADLLAEAEE DLKVIAKKLA ELEVVTLLSG
EYDQREAVVT IRSGAGGVDA ADFAEMLQRM YLRWAESHGF TTQILDTSFA EEAGIKSTTF
EVQAPYAYGR LSIEAGTHRL VRISPFNSQG KRMTSFAAVE VIPLIEQTEF IDIPDTEIKV
DVFRSSGPGG QSVNTTDSAV RLTHIPTGIV VSMQNEKSQI QNRAAALRVL QSRLLLLKKE
QEDAKKKELA GDVKASWGDQ MRSYVLNPYQ MVKDLRTNHE EGNPSAVFDG KIDDFIDAGI
RWRASMRNEK E
//
