ID   RRP8_CAEBR              Reviewed;         332 AA.
AC   A8XI07;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Ribosomal RNA-processing protein 8;
DE            EC=2.1.1.-;
GN   ORFNames=CBG13492;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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; HE600980; CAP32280.1; -; Genomic_DNA.
DR   RefSeq; XP_002634957.1; XM_002634911.1.
DR   AlphaFoldDB; A8XI07; -.
DR   SMR; A8XI07; -.
DR   STRING; 6238.CBG13492; -.
DR   EnsemblMetazoa; CBG13492.1; CBG13492.1; WBGene00034250.
DR   GeneID; 8576951; -.
DR   KEGG; cbr:CBG_13492; -.
DR   CTD; 8576951; -.
DR   WormBase; CBG13492; CBP03301; WBGene00034250; -.
DR   eggNOG; KOG3045; Eukaryota.
DR   HOGENOM; CLU_027694_2_1_1; -.
DR   InParanoid; A8XI07; -.
DR   OMA; KWPTNPL; -.
DR   OrthoDB; 962356at2759; -.
DR   Proteomes; UP000008549; Chromosome IV.
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..332
FT                   /note="Ribosomal RNA-processing protein 8"
FT                   /id="PRO_0000390455"
FT   REGION          1..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..67
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..109
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         158
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O43159"
FT   BINDING         193
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O43159"
FT   BINDING         213
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O43159"
FT   BINDING         225
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O43159"
FT   BINDING         226
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O43159"
FT   BINDING         242
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O43159"
SQ   SEQUENCE   332 AA;  38143 MW;  119658C7A6D41364 CRC64;
     MGKKRINEVS TTEGAPAEKK KKVEKWLNTS SEDGEGTKKK KRPWRNKVRK LAAKKAAAER
     RVENSEESTI LEPVATAEEA TKKKKKRGPK KKKYKPEAAE VEKKNEEGDT VKENPIAEAK
     KRLDAGRFRM LNEKLYTCTG SEAFDFFKED RTAFDLYHRG FADQVKKWPN HPLREIIRWL
     QAKPDKQAVF DLGCGEAKIA EAVGEKHTIR SFDLVAVNDR VESCDMSKLP AEDGSADVVI
     FCLSLMGTNL YDFIKEARRV LRTGGVLKIG EVTSRFVSIK QFCEAINKMG FETTNRRQLT
     DYFMMFDFRK IDKVEQKRPY GLKLKPCLYK KR