ID   RRP8_CAEEL              Reviewed;         343 AA.
AC   O44410;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Ribosomal RNA-processing protein 8;
DE            EC=2.1.1.-;
GN   ORFNames=T07A9.8;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Probable methyltransferase required to silence rDNA.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RRP8 family.
CC       {ECO:0000305}.
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DR   EMBL; FO081716; CCD73979.1; -; Genomic_DNA.
DR   PIR; T32579; T32579.
DR   RefSeq; NP_499920.1; NM_067519.4.
DR   AlphaFoldDB; O44410; -.
DR   SMR; O44410; -.
DR   BioGRID; 42025; 2.
DR   STRING; 6239.T07A9.8; -.
DR   EPD; O44410; -.
DR   PaxDb; O44410; -.
DR   PeptideAtlas; O44410; -.
DR   PRIDE; O44410; -.
DR   EnsemblMetazoa; T07A9.8.1; T07A9.8.1; WBGene00020296.
DR   GeneID; 176864; -.
DR   KEGG; cel:CELE_T07A9.8; -.
DR   UCSC; T07A9.8; c. elegans.
DR   CTD; 176864; -.
DR   WormBase; T07A9.8; CE17217; WBGene00020296; -.
DR   eggNOG; KOG3045; Eukaryota.
DR   GeneTree; ENSGT00390000006189; -.
DR   HOGENOM; CLU_027694_2_1_1; -.
DR   InParanoid; O44410; -.
DR   OMA; KWPTNPL; -.
DR   OrthoDB; 962356at2759; -.
DR   PhylomeDB; O44410; -.
DR   Reactome; R-CEL-427359; SIRT1 negatively regulates rRNA expression.
DR   PRO; PR:O44410; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00020296; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005677; C:chromatin silencing complex; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0033553; C:rDNA heterochromatin; ISS:UniProtKB.
DR   GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042149; P:cellular response to glucose starvation; IBA:GO_Central.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0000183; P:rDNA heterochromatin assembly; ISS:UniProtKB.
DR   GO; GO:0046015; P:regulation of transcription by glucose; IBA:GO_Central.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.2150; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR007823; RRP8.
DR   InterPro; IPR042036; RRP8_N.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR12787; PTHR12787; 1.
DR   Pfam; PF05148; Methyltransf_8; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator; Methyltransferase; Nucleus; Reference proteome;
KW   Repressor; rRNA processing; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN           1..343
FT                   /note="Ribosomal RNA-processing protein 8"
FT                   /id="PRO_0000390456"
FT   REGION          1..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..74
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         169
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O43159"
FT   BINDING         204
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O43159"
FT   BINDING         224
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O43159"
FT   BINDING         236
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O43159"
FT   BINDING         237
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O43159"
FT   BINDING         253
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O43159"
SQ   SEQUENCE   343 AA;  39448 MW;  FA12BDFF6756537B CRC64;
     MGKKRKITDE KDAQHVPAEK REKVENWLKK STEKPTSSQS DAEKKKKRPW RNKVRKLAAK
     KAAADKKSEN PEEPPLILEP KSSSDENTKK KRKRGPKKKK FKPEVAGKAA ETENDDVAAA
     PEEADPIAEA KKRLDAGRFR FLNEKLYTCT GSEAFDFFKE DPTAFDLYHK GFADQVKKWP
     NHPLREIIRW LQSKPDQQSV FDLGCGEAKI AEAVGEKHKI RSFDLVAVND RVESCDMSKL
     PAEDSSADIV IYCLSLMGTN LYDFIREARR VLKIGGILKI AEVTSRFVSI KQFCEAITKM
     GFEQSHRREL TDYFMMMEFK KVEKVEQKRP YGLKLKPCLY KKR