RRP8_DICDI
ID RRP8_DICDI Reviewed; 390 AA.
AC Q54CP1;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Ribosomal RNA-processing protein 8;
DE EC=2.1.1.-;
GN Name=rrp8; ORFNames=DDB_G0292960;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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; AAFI02000197; EAL61029.1; -; Genomic_DNA.
DR RefSeq; XP_629375.1; XM_629373.1.
DR AlphaFoldDB; Q54CP1; -.
DR SMR; Q54CP1; -.
DR STRING; 44689.DDB0219795; -.
DR PaxDb; Q54CP1; -.
DR PRIDE; Q54CP1; -.
DR EnsemblProtists; EAL61029; EAL61029; DDB_G0292960.
DR GeneID; 8628893; -.
DR KEGG; ddi:DDB_G0292960; -.
DR dictyBase; DDB_G0292960; -.
DR eggNOG; KOG3045; Eukaryota.
DR HOGENOM; CLU_027694_2_1_1; -.
DR InParanoid; Q54CP1; -.
DR OMA; DICMERR; -.
DR PhylomeDB; Q54CP1; -.
DR Reactome; R-DDI-427359; SIRT1 negatively regulates rRNA expression.
DR PRO; PR:Q54CP1; -.
DR Proteomes; UP000002195; Chromosome 6.
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:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; ISS:UniProtKB.
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..390
FT /note="Ribosomal RNA-processing protein 8"
FT /id="PRO_0000390458"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 201
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 256
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43159"
FT BINDING 268
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43159"
FT BINDING 285
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43159"
SQ SEQUENCE 390 AA; 45193 MW; 234BD07E9E3C0BB0 CRC64;
MTNTKKSKQK NTVGNKVKKT NTNKNNNNNN NNNNKNKQNK INNKNNKNNK NNDSNNKNNN
TNNKNNINIK NKNLKKVENN KSLKVISSNK NKNILNNLKK EEKVNSNDIL IQQQQNREKE
DITNEDDDEK YNLWNPKPTS SVSVSSSKSS KSLKTTDLQN EMSEKLKGSR FRWLNETLYT
THSKEAFKEF SEDRSLFDQY HSGFKSQVES WPINPLDLII DDLSSIKQRK RIADLGCGEA
KLAERLQHKH TIQSFDLVAV NERVTACDIS NLPLKNESID IAVFCLSLMG TNFIDFIIEA
ERVLVKGGLL KIAEIESRIT DINAFTNEIQ QHGFNLIKKN EQNQYFTLFE FSKLQKKDQQ
FMRSLKQYQK LKKQQATNEP VLKPCLYKKR
