RRP8_SCHPO
ID RRP8_SCHPO Reviewed; 318 AA.
AC Q10257;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
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; ORFNames=SPAC56F8.09;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC specifically methylates the N(1) position of adenine in helix 25.1 in
CC 25S rRNA. Required both for ribosomal 40S and 60S subunits biogenesis.
CC Required for efficient pre-rRNA cleavage at site A2 (By similarity).
CC {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RRP8 family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAA93580.1; -; Genomic_DNA.
DR PIR; T38919; T38919.
DR RefSeq; NP_593223.1; NM_001018620.2.
DR AlphaFoldDB; Q10257; -.
DR SMR; Q10257; -.
DR BioGRID; 279647; 11.
DR STRING; 4896.SPAC56F8.09.1; -.
DR MaxQB; Q10257; -.
DR PaxDb; Q10257; -.
DR EnsemblFungi; SPAC56F8.09.1; SPAC56F8.09.1:pep; SPAC56F8.09.
DR GeneID; 2543219; -.
DR KEGG; spo:SPAC56F8.09; -.
DR PomBase; SPAC56F8.09; rrp8.
DR VEuPathDB; FungiDB:SPAC56F8.09; -.
DR eggNOG; KOG3045; Eukaryota.
DR HOGENOM; CLU_027694_1_0_1; -.
DR InParanoid; Q10257; -.
DR OMA; FFHKNTD; -.
DR PhylomeDB; Q10257; -.
DR BRENDA; 2.1.1.287; 5613.
DR Reactome; R-SPO-427359; SIRT1 negatively regulates rRNA expression.
DR PRO; PR:Q10257; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0016433; F:rRNA (adenine) methyltransferase activity; IBA:GO_Central.
DR GO; GO:0106142; F:rRNA (adenine-N1-)-methyltransferase activity; IGI:PomBase.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IBA:GO_Central.
DR GO; GO:0031167; P:rRNA methylation; IGI:PomBase.
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 Methyltransferase; Nucleus; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..318
FT /note="25S rRNA (adenine(645)-N(1))-methyltransferase"
FT /id="PRO_0000116569"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 132
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43159"
FT BINDING 175
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43159"
FT BINDING 197
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43159"
FT BINDING 209
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"
SQ SEQUENCE 318 AA; 36329 MW; 623181910971F721 CRC64;
MFKVDWDLGP VSKSASDQTK ESRKEKKRKK GERKNVGDKG EKLNEKVLKK AKSVTTNNSL
KSEIKKEKSV PSIKEKNKGD AKHTKLTSLQ QKMKDKLDGA NFRWINEQLY TTESDKAVQM
FKENPDLFDI YHAGFRYQVE GWPENPVDIF IQHLKIRFEH SNAKKKNNIV IADLGCGEAK
IASTFRKSRS LQVHSFDLVA PNEHVVACDI ANVPMADETV DIAVFCLSLM GTNWQSFLKE
AYRILKVGGL LWVAEIKSRF SDKSGEVFAK ELPKLGFETK SIQLQNKMFT LFEFKKVPVH
GKCEELPPIL SACIYKRR
