ID   RRP8_CHATD              Reviewed;         586 AA.
AC   G0S8E7;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   16-MAR-2016, sequence version 2.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=25S rRNA (adenine-N(1))-methyltransferase;
DE            EC=2.1.1.-;
DE   AltName: Full=Ribosomal RNA-processing protein 8;
GN   Name=RPR8; ORFNames=CTHT_0029620;
OS   Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=759272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1495 / CBS 144.50 / IMI 039719;
RX   PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA   Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA   Arumugam M., Bork P., Hurt E.;
RT   "Insight into structure and assembly of the nuclear pore complex by
RT   utilizing the genome of a eukaryotic thermophile.";
RL   Cell 146:277-289(2011).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC       specifically methylates the N(1) position of a conserved adenine in
CC       helix 25.1 in 25S rRNA. Required both for ribosomal 40S and 60S
CC       subunits biogenesis. Required for efficient pre-rRNA cleavage at site
CC       A2. {ECO:0000250|UniProtKB:P38961}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:P38961}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RRP8 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EGS21121.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; GL988041; EGS21121.1; ALT_FRAME; Genomic_DNA.
DR   RefSeq; XP_006693417.1; XM_006693354.1.
DR   AlphaFoldDB; G0S8E7; -.
DR   SMR; G0S8E7; -.
DR   STRING; 759272.G0S8E7; -.
DR   PRIDE; G0S8E7; -.
DR   EnsemblFungi; EGS21121; EGS21121; CTHT_0029620.
DR   GeneID; 18257000; -.
DR   KEGG; cthr:CTHT_0029620; -.
DR   eggNOG; KOG3045; Eukaryota.
DR   HOGENOM; CLU_027694_3_1_1; -.
DR   OrthoDB; 962356at2759; -.
DR   Proteomes; UP000008066; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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   Methyltransferase; Nucleus; Reference proteome; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..586
FT                   /note="25S rRNA (adenine-N(1))-methyltransferase"
FT                   /id="PRO_0000435815"
FT   REGION          23..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          536..573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..99
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..161
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..183
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..226
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        539..573
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   586 AA;  65664 MW;  F110A0EE149439A7 CRC64;
     MFPVKGLSVS ADKLKVEPGA IVGTAPAAPA PASAPAVSSS KPSKKRKRHG GDKDVNVDAS
     NLVDLWEKVI EQKKEGVADG VKKHENKRLK KEHEGQGEKL SNSNNDGNQG ERKNNKKKNK
     NKNKNQGEHG IQVAQKKGPK KVEGEEDEDD NNDDADEWEG IDEDEKHASS EKPTPKKDDK
     KQQQLQQQQQ QKKQQKNQEK DNRNGTTSNW QQDKPQPKTA TPAPKLTPLQ ASMREKLISA
     RFRHLNETLY TRPSTEAFKL FEESPEMFTE YHEGFRRQVD VWPENPVDVY IKEIKERAKV
     RFAPKISGGA EGGKSLPPAR FPLPRDQKTK VCTIADLGCG DAKLAKTLVP LKQKLRLEIH
     SFDLQTGGCE LVTRADIANL PLPDNSVDLA IFCLALMGTN WLDFVEEAYR ILRWRGELWV
     AEIKSRFAGS QARVKQPPQK KVVAHSVGKR KKGSALAVAE EEEGDPEQNN LDLAVHVDGD
     TSKLKKPHET DITAFVEALK RRGFLLNRDF GDNSVDMGNK MFVRMHFVKA AVPTRGKCVP
     KDGQEDTTKN KKGGQKPKPK FIEEKDEQEE VKDEAAVLKP CVYKIR