ID A0A1Y1YJI6_9PLEO Unreviewed; 558 AA.
AC A0A1Y1YJI6;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Ribosomal RNA-processing protein 8 {ECO:0000256|RuleBase:RU365074};
DE EC=2.1.1.- {ECO:0000256|RuleBase:RU365074};
GN ORFNames=BCR34DRAFT_628458 {ECO:0000313|EMBL:ORX98118.1};
OS Clohesyomyces aquaticus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Lindgomycetaceae; Clohesyomyces.
OX NCBI_TaxID=1231657 {ECO:0000313|EMBL:ORX98118.1, ECO:0000313|Proteomes:UP000193144};
RN [1] {ECO:0000313|EMBL:ORX98118.1, ECO:0000313|Proteomes:UP000193144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115471 {ECO:0000313|EMBL:ORX98118.1,
RC ECO:0000313|Proteomes:UP000193144};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORX98118.1}.
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DR EMBL; MCFA01000221; ORX98118.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1YJI6; -.
DR STRING; 1231657.A0A1Y1YJI6; -.
DR OrthoDB; 1694at2759; -.
DR Proteomes; UP000193144; 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; 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:UP000193144};
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..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 558 AA; 60888 MW; 4D7C9DB66535D6E4 CRC64;
MFAVPGWNVS APLKTQTEVA KPTPEGKKSK KRKRKNQDFK ANEENISEVL SGNVHPKKAK
GTGANNIEVG ERAAGVANDG DSEKPSKKRK RKGDKSQKEA DQAGEEAEVN GIETPAKSQV
DDENVAADKP AGEDKATSKR EKKKRKRDQK NAEAGDSTTQ APTSTTAKSK TVEKNAIPAA
PPSLPAPSKT LTPLQQTMRA KLASARFRHL NEALYTKPSQ ASLSIFAENP DMFDDYHRGF
AQQVEVWPEN PVDGYVSRIR TRGKAKDKKK KDKRSRQQAY SAVNTDQPDT GIKPLPRDFK
GNCTIADLGC GTASLAQRLQ PNLQSLHMTI HSFDLSKPAG PNAPLVTIAD ISALPLPDSS
VDVTIFCLAL MGTNWLEFID EAYRILRWKG ELWIAEIKSR FGRVARSRKP PINSVGSLRK
PDKKEKSKKK KTDGAVEEGV QGSEDEAELA QQVDGVQGKD GTDVSAFVEV LQKRGFVLDG
EQSAAVDLSN KMFVKMQFVK GANPAKGKNV KKAESGDRAG GIRMGLKGKK FTTVAAEDED
EGDEKDGKVL KPCLYKIR
//
