ID A0A2K5LB29_CERAT Unreviewed; 140 AA.
AC A0A2K5LB29;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Ribosomal RNA-processing protein 8 {ECO:0000256|ARBA:ARBA00020203, ECO:0000256|RuleBase:RU365074};
DE EC=2.1.1.- {ECO:0000256|RuleBase:RU365074};
GN Name=RRP8 {ECO:0000313|Ensembl:ENSCATP00000010159.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000010159.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000010159.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Essential component of the eNoSC (energy-dependent nucleolar
CC silencing) complex, a complex that mediates silencing of rDNA in
CC response to intracellular energy status and acts by recruiting histone-
CC modifying enzymes. The eNoSC complex is able to sense the energy status
CC of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio
CC activates SIRT1, leading to histone H3 deacetylation followed by
CC dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation
CC of silent chromatin in the rDNA locus. In the complex, RRP8 binds to
CC H3K9me2 and probably acts as a methyltransferase.
CC {ECO:0000256|RuleBase:RU365074}.
CC -!- SUBUNIT: Component of the eNoSC complex.
CC {ECO:0000256|RuleBase:RU365074}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|RuleBase:RU365074}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RRP8 family.
CC {ECO:0000256|RuleBase:RU365074}.
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DR AlphaFoldDB; A0A2K5LB29; -.
DR Ensembl; ENSCATT00000034266.1; ENSCATP00000010159.1; ENSCATG00000029344.1.
DR GeneTree; ENSGT00390000006189; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000029344; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR007823; RRP8.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR023576; UbiE/COQ5_MeTrFase_CS.
DR PANTHER; PTHR12787:SF0; RIBOSOMAL RNA-PROCESSING PROTEIN 8; 1.
DR PANTHER; PTHR12787; UNCHARACTERIZED; 1.
DR Pfam; PF05148; Methyltransf_8; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS01184; UBIE_2; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|RuleBase:RU365074};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365074};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552,
KW ECO:0000256|RuleBase:RU365074};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU365074};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365074}.
SQ SEQUENCE 140 AA; 15379 MW; 960EF31A23AD793A CRC64;
MFEEPEWASA APVAAGLGPV ISRPPPAAAL QNKVPLEDES VDVAVFCLSL MGTNIRDFLE
EANRVLKPGG LLKVAEVSSR FEDVRTFLRA VTKLGFKIVS KDLTNSHFFL FDFQKTGPPQ
VGPKAQLSGL KLHPCLYKRR
//
