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Database: UniProt
Entry: A0A0D2FB60_9EURO
LinkDB: A0A0D2FB60_9EURO
Original site: A0A0D2FB60_9EURO 
ID   A0A0D2FB60_9EURO        Unreviewed;       512 AA.
AC   A0A0D2FB60;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   08-OCT-2025, entry version 34.
DE   RecName: Full=Ribosomal RNA-processing protein 8 {ECO:0000256|ARBA:ARBA00076672, ECO:0000256|RuleBase:RU365074};
DE            EC=2.1.1.- {ECO:0000256|RuleBase:RU365074};
GN   ORFNames=PV05_05868 {ECO:0000313|EMBL:KIW57299.1};
OS   Exophiala xenobiotica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW57299.1, ECO:0000313|Proteomes:UP000054342};
RN   [1] {ECO:0000313|EMBL:KIW57299.1, ECO:0000313|Proteomes:UP000054342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW57299.1,
RC   ECO:0000313|Proteomes:UP000054342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KN847319; KIW57299.1; -; Genomic_DNA.
DR   RefSeq; XP_013317883.1; XM_013462429.1.
DR   AlphaFoldDB; A0A0D2FB60; -.
DR   STRING; 348802.A0A0D2FB60; -.
DR   GeneID; 25327776; -.
DR   HOGENOM; CLU_027694_3_1_1; -.
DR   OrthoDB; 10258825at2759; -.
DR   Proteomes; UP000054342; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016433; F:rRNA (adenine) methyltransferase activity; IEA:UniProtKB-ARBA.
DR   GO; GO:0042273; P:ribosomal large subunit biogenesis; IEA:TreeGrafter.
DR   FunFam; 1.10.10.2150:FF:000001; Ribosomal RNA-processing protein 8; 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; RIBOSOMAL RNA-PROCESSING PROTEIN 8; 1.
DR   PANTHER; PTHR12787:SF0; RIBOSOMAL RNA-PROCESSING PROTEIN 8; 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:UP000054342};
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..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          382..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..82
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..150
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   512 AA;  56831 MW;  E3B9BBB186A15A3E CRC64;
     MFAVPGWNVS PTSLVKEKQT QKPDKGQSSG NGTPVTKKRK STTSHDGQTS KISGTDLERL
     WNQRHETKVH RQTDPSRSKP EPYSRSNNVS TKAGKEQKPT KQADSNAVAV GRKETSQKKN
     KNKNKPDVQD EQKPVADKQN VDQNSHKSEK NGNSGDIGKQ SSSTKALIEA LPPAPPATKL
     TALQAKMRNK LTSARFRHLN ETLYTTTSSQ ALDLFTSSPD LFAEYHAGFA QQVKESWPQN
     PVEQYVRTIK TRGNLNEKEK DTALPLPRRK TGSCTIADLG CGDAPLARGC QSQVKNLKLK
     FHNYDLHAAN NFVTKADITN LPLRDGEADI AVFCLSLMGT NWLSFVDEAW RILRGDGKGE
     VWVAEVKSRF GRVTRRPGHV VENSVGKRRK KQKPKGGDSD DEAVGNGIFV EESEGNQADE
     TDISAFVKVF SRRGFVLRED SVDKRNKMFV SMVFVKSGVP TAGKHKGLKW NGHEYQRVQD
     GKMRFVAGKG DDEDISPQDE AKALKPCVYK TR
//
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