ID G2Y0J8_BOTF4 Unreviewed; 498 AA.
AC G2Y0J8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Ribosomal RNA-processing protein 8 {ECO:0000256|RuleBase:RU365074};
DE EC=2.1.1.- {ECO:0000256|RuleBase:RU365074};
GN ORFNames=BofuT4_P117130.1 {ECO:0000313|EMBL:CCD46163.1};
OS Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD46163.1, ECO:0000313|Proteomes:UP000008177};
RN [1] {ECO:0000313|Proteomes:UP000008177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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.
CC {ECO:0000256|RuleBase:RU365074}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604, ECO:0000256|RuleBase:RU365074}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RRP8 family.
CC {ECO:0000256|ARBA:ARBA00006301, ECO:0000256|RuleBase:RU365074}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQ790281; CCD46163.1; -; Genomic_DNA.
DR AlphaFoldDB; G2Y0J8; -.
DR STRING; 999810.G2Y0J8; -.
DR eggNOG; KOG3045; Eukaryota.
DR HOGENOM; CLU_027694_3_1_1; -.
DR InParanoid; G2Y0J8; -.
DR Proteomes; UP000008177; Unplaced contigs.
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-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.10.10.2150; Ribosomal RNA-processing protein 8, N-terminal domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR007823; RRP8.
DR InterPro; IPR042036; RRP8_N.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12787:SF0; RIBOSOMAL RNA-PROCESSING PROTEIN 8; 1.
DR PANTHER; PTHR12787; UNCHARACTERIZED; 1.
DR Pfam; PF05148; Methyltransf_8; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|RuleBase:RU365074};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365074};
KW Reference proteome {ECO:0000313|Proteomes:UP000008177};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552,
KW ECO:0000256|RuleBase:RU365074};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU365074};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365074}.
FT REGION 1..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 498 AA; 55537 MW; D94391BABFF1A0D9 CRC64;
MFAVPGWSVS SSLLKTQKAE PVAAASKADE EGAPAETKSS KKRKRAKNPD VNAANLSELW
DSVIEGKPKA KKVKNAEKDG ETKEKKEKVA KEVTTDEVES KPANLSNEST EVSESKKEKK
QKKNKKDKKD KDSKPSDNDQ STKDDTSTKA PPPPKPAAKL TPLQASMRQK LISARFRHLN
QSLYTTPSAE SLATFQQNPE MFTEYHEGFR RQVEVWPENP VDGYSLQIRQ RGKLRRDMRG
QPAQEKTDLT PLPRTDGTCR IADLGCGDAA LSTGLQKDLK KLNLKIHSFD LQSPSPLVTR
ADIANLPLED GSIDIAIFCL ALMGTNWIDF IEEAFRILRW KGELWIAEIK SRFGRVGGNN
KKVVEHSVGH RKKNQPVNKK AIKAADDEEN EADLMVHVDG NEDNKQETDV SAFVEVLKKR
GFVLQTEKSV DLSNKMFVKM HFVKGATPIK GKCVPVPKGM PEGETWKKKP KAKFLDEPED
VPVSSEASVL KPCVYKLR
//
