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Database: UniProt
Entry: A0A061H552_9BASI
LinkDB: A0A061H552_9BASI
Original site: A0A061H552_9BASI 
ID   A0A061H552_9BASI        Unreviewed;       517 AA.
AC   A0A061H552;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Ribosomal RNA-processing protein 8 {ECO:0000256|RuleBase:RU365074};
DE            EC=2.1.1.- {ECO:0000256|RuleBase:RU365074};
GN   ORFNames=PFL1_06885 {ECO:0000313|EMBL:EPQ27564.1};
OS   Pseudozyma flocculosa PF-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX   NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ27564.1, ECO:0000313|Proteomes:UP000053664};
RN   [1] {ECO:0000313|EMBL:EPQ27564.1, ECO:0000313|Proteomes:UP000053664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PF-1 {ECO:0000313|EMBL:EPQ27564.1,
RC   ECO:0000313|Proteomes:UP000053664};
RX   PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA   Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA   Bakkeren G., Belanger R.R.;
RT   "The transition from a phytopathogenic smut ancestor to an anamorphic
RT   biocontrol agent deciphered by comparative whole-genome analysis.";
RL   Plant Cell 25:1946-1959(2013).
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; KE361638; EPQ27564.1; -; Genomic_DNA.
DR   RefSeq; XP_007880619.1; XM_007882428.1.
DR   AlphaFoldDB; A0A061H552; -.
DR   GeneID; 19320952; -.
DR   KEGG; pfp:PFL1_06885; -.
DR   eggNOG; KOG3045; Eukaryota.
DR   HOGENOM; CLU_027694_1_1_1; -.
DR   OrthoDB; 1694at2759; -.
DR   Proteomes; UP000053664; 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-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; 2.
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:UP000053664};
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          30..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          196..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..102
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..158
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..225
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   517 AA;  54920 MW;  4F6CF65B01F42D33 CRC64;
     MPDLDLGALQ AQLELNRSVL ADSIMSKFSS LGASSSSSSS PSKNGASATA QPPRSATLGV
     GATPKGKQAT LAANGKPSSI EDVKLKGRLL AKRKRHDEPA QGDEESEGDE EEGRAALVGS
     SSKRKSGKAA AAATGSNSAA DGSNAPSSSK SSNKKNSKDP FAVKGAAFQK QQQQQQAASK
     IIVDGKEVDL SSLSKAQRKK LNKRRRLEEE AAKRAAQHED GEETKAAAAS STLTPLQSQM
     LNRLTGSRFR TINEQLYTTD SASALSSFTA DPSIFDDYHK GFRSQVKSWP KNPLDILCSS
     LLAAKKPKAG TKPAKSQHTG QVKARYGACP LVIDLGAGEG MLARKLVKDG HFKVLSFDLV
     NTADGWVRKA DTATIGALPL PGFYDASDPL SLRGAAPPGS AQGQADIAIF CLSLMGTNWL
     SMILEASRCL RVGAELLVAE VSSRFVSVEG FVSLVEKVGF KLEGRDDTNT HFVVFEFVKL
     DPASSARRRE AGDDHLTESR LVELGSSLLK PCLYKRR
//
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