RRP8_YEAST
ID RRP8_YEAST Reviewed; 392 AA.
AC P38961; Q7LHG2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=25S rRNA (adenine(645)-N(1))-methyltransferase;
DE EC=2.1.1.287;
DE AltName: Full=Ribosomal RNA-processing protein 8;
GN Name=RRP8; OrderedLocusNames=YDR083W; ORFNames=D4461;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF LYS-390.
RC STRAIN=JG535-2D;
RX PubMed=10864042; DOI=10.1017/s1355838200992288;
RA Bousquet-Antonelli C., Vanrobays E., Gelugne J.P., Caizergues-Ferrer M.,
RA Henry Y.;
RT "Rrp8p is a yeast nucleolar protein functionally linked to Gar1p and
RT involved in pre-rRNA cleavage at site A2.";
RL RNA 6:826-843(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=7483840; DOI=10.1002/yea.320110708;
RA Coster F., Jonniaux J.-L., Goffeau A.;
RT "Analysis of a 32.8 kb segment of yeast chromosome IV reveals 21 open
RT reading frames, including TPS2, PPH3, RAD55, SED1, PDC2, AFR1, SSS1, SLU7
RT and a tRNA for arginine.";
RL Yeast 11:673-679(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP FUNCTION.
RX PubMed=15161972; DOI=10.1073/pnas.0401263101;
RA Askree S.H., Yehuda T., Smolikov S., Gurevich R., Hawk J., Coker C.,
RA Krauskopf A., Kupiec M., McEachern M.J.;
RT "A genome-wide screen for Saccharomyces cerevisiae deletion mutants that
RT affect telomere length.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8658-8663(2004).
RN [8]
RP FUNCTION.
RX PubMed=16552446; DOI=10.1371/journal.pgen.0020035;
RA Gatbonton T., Imbesi M., Nelson M., Akey J.M., Ruderfer D.M., Kruglyak L.,
RA Simon J.A., Bedalov A.;
RT "Telomere length as a quantitative trait: genome-wide survey and genetic
RT mapping of telomere length-control genes in yeast.";
RL PLoS Genet. 2:304-315(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP GLY-209.
RX PubMed=23180764; DOI=10.1093/nar/gks1102;
RA Peifer C., Sharma S., Watzinger P., Lamberth S., Kotter P., Entian K.D.;
RT "Yeast Rrp8p, a novel methyltransferase responsible for m1A 645 base
RT modification of 25S rRNA.";
RL Nucleic Acids Res. 41:1151-1163(2013).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC specifically methylates the N(1) position of adenine 645 in 25S rRNA.
CC Required both for ribosomal 40S and 60S subunits biogenesis. Required
CC for efficient pre-rRNA cleavage at site A2. Also involved in telomere
CC length regulation and maintenance. {ECO:0000269|PubMed:10864042,
CC ECO:0000269|PubMed:15161972, ECO:0000269|PubMed:16552446,
CC ECO:0000269|PubMed:23180764}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(645) in 25S rRNA + S-adenosyl-L-methionine = H(+) +
CC N(1)-methyladenosine(645) in 25S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43792, Rhea:RHEA-COMP:10695, Rhea:RHEA-COMP:10696,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.287;
CC Evidence={ECO:0000269|PubMed:23180764};
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10864042,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:23180764}. Chromosome,
CC telomere {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 2780 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RRP8 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA57610.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA86805.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA98903.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X82086; CAA57610.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z46796; CAA86805.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z74379; CAA98903.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006938; DAA11930.1; -; Genomic_DNA.
DR PIR; S48770; S48770.
DR RefSeq; NP_010368.5; NM_001180391.3.
DR AlphaFoldDB; P38961; -.
DR SMR; P38961; -.
DR BioGRID; 32139; 349.
DR IntAct; P38961; 4.
DR STRING; 4932.YDR083W; -.
DR iPTMnet; P38961; -.
DR MaxQB; P38961; -.
DR PaxDb; P38961; -.
DR PRIDE; P38961; -.
DR EnsemblFungi; YDR083W_mRNA; YDR083W; YDR083W.
DR GeneID; 851656; -.
DR KEGG; sce:YDR083W; -.
DR SGD; S000002490; RRP8.
DR VEuPathDB; FungiDB:YDR083W; -.
DR eggNOG; KOG3045; Eukaryota.
DR GeneTree; ENSGT00390000006189; -.
DR HOGENOM; CLU_027694_1_0_1; -.
DR InParanoid; P38961; -.
DR OMA; FFHKNTD; -.
DR BioCyc; YEAST:G3O-29688-MON; -.
DR BRENDA; 2.1.1.287; 984.
DR Reactome; R-SCE-427359; SIRT1 negatively regulates rRNA expression.
DR PRO; PR:P38961; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P38961; protein.
DR GO; GO:0030686; C:90S preribosome; IDA:GO_Central.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0016433; F:rRNA (adenine) methyltransferase activity; IMP:SGD.
DR GO; GO:0106142; F:rRNA (adenine-N1-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IGI:SGD.
DR GO; GO:0031167; P:rRNA methylation; IMP:SGD.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
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 1: Evidence at protein level;
KW Chromosome; Coiled coil; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; rRNA processing; S-adenosyl-L-methionine; Telomere;
KW Transferase.
FT CHAIN 1..392
FT /note="25S rRNA (adenine(645)-N(1))-methyltransferase"
FT /id="PRO_0000202594"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 32..61
FT /evidence="ECO:0000255"
FT COILED 344..382
FT /evidence="ECO:0000255"
FT COMPBIAS 38..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 156
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43159"
FT BINDING 207
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"
FT BINDING 254
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43159"
FT BINDING 271
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43159"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 209
FT /note="G->A,R: Impaired methyltransferase activity and
FT ribosomal 60S subunit biogenesis. Does not affect pre-rRNA
FT cleavage at site A2 activity."
FT /evidence="ECO:0000269|PubMed:23180764"
FT MUTAGEN 390
FT /note="K->E: In RRP8-1; no effect. Synthetic lethal with
FT GAR1 mutant allele lacking its N- and C-terminal
FT glycine/arginine-rich (GAR) domains."
FT /evidence="ECO:0000269|PubMed:10864042"
SQ SEQUENCE 392 AA; 45985 MW; 58675E3493D9B57B CRC64;
MALFNVEGWS IKTKTVAFDN KTNKSSKDKK KNNRKNGKLT REQKLKEETE AELKEQVEDI
PSEGSVAKDI PKKNQEKSDQ NETSKKRKHD EEAPLMQVKE NIEKPTKKQL TPLQQKMMAK
LTGSRFRWIN EQLYTISSDE ALKLIKEQPQ LFDEYHDGFR SQVQAWPENP VDVFVDQIRY
RCMKPVNAPG GLPGLKDSKE IVIADMGCGE AQLALEINNF FKNYNKKAKK YLKRRHKVHS
FDLKKANERI TVADIRNVPL PDESCTIVVF CLALMGTNFL DFIKEAYRIL APRGELWIAE
IKSRFSDGKG NEFVDALKLM GFFHKKTFDE NKMFTRFEFF KPPAEIIEER RQKLERRQKF
IEVETEKEEL EKKRRKIAEG KWLLKPCIYK RR
