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Database: UniProt
Entry: A0A550CAR8_9AGAR
LinkDB: A0A550CAR8_9AGAR
Original site: A0A550CAR8_9AGAR 
ID   A0A550CAR8_9AGAR        Unreviewed;       695 AA.
AC   A0A550CAR8;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=NOL1/NOP2/sun family-domain-containing protein {ECO:0000313|EMBL:TRM61895.1};
GN   ORFNames=BD626DRAFT_500837 {ECO:0000313|EMBL:TRM61895.1};
OS   Auriculariopsis ampla.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Schizophyllaceae; Auriculariopsis.
OX   NCBI_TaxID=97359 {ECO:0000313|EMBL:TRM61895.1, ECO:0000313|Proteomes:UP000320762};
RN   [1] {ECO:0000313|EMBL:TRM61895.1, ECO:0000313|Proteomes:UP000320762}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NL-1724 {ECO:0000313|EMBL:TRM61895.1,
RC   ECO:0000313|Proteomes:UP000320762};
RX   PubMed=31257601;
RA   Almasi E., Sahu N., Krizsan K., Balint B., Kovacs G.M., Kiss B.,
RA   Cseklye J., Drula E., Henrissat B., Nagy I., Chovatia M., Adam C.,
RA   LaButti K., Lipzen A., Riley R., Grigoriev I.V., Nagy L.G.;
RT   "Comparative genomics reveals unique wood-decay strategies and fruiting
RT   body development in the Schizophyllaceae.";
RL   New Phytol. 0:0-0(2019).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000256|ARBA:ARBA00004604}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|ARBA:ARBA00007494,
CC       ECO:0000256|PROSITE-ProRule:PRU01023}.
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:TRM61895.1}.
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DR   EMBL; VDMD01000015; TRM61895.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A550CAR8; -.
DR   STRING; 97359.A0A550CAR8; -.
DR   Proteomes; UP000320762; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR   InterPro; IPR031341; Methyltr_RsmF_N.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR011023; Nop2p.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR023273; RCMT_NOP2.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00446; nop2p; 1.
DR   PANTHER; PTHR22807:SF30; 28S RRNA (CYTOSINE(4447)-C(5))-METHYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF17125; Methyltr_RsmF_N; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   PRINTS; PR02012; RCMTNOP2.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000320762};
KW   Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU01023};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01023};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}.
FT   DOMAIN          330..618
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          222..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          622..695
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..80
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..105
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..123
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..244
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..263
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..640
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        653..672
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        547
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         422..428
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         446
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         473
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         490
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   695 AA;  76522 MW;  6322D800D261DE17 CRC64;
     MGRRAKNKQG PVAPLHSASS PRKLGKRKAP ADGDIESPKS AKKVKNADGK GKAKPAQADK
     ENTAKKGKKP QVKQAESDDD AGSGWEDIEE DDLKGATKSL FQESDDDEDA YIGDLDEFDV
     EGMDDDALRG HVEELDLGSD EEEEEEEPAQ VPVRGKKSKQ FERPTKIIPT ASDASSSDEE
     TDDEDGPITM ANMEARSRAL DAKALADADL DAEDLRNAGM LVDGDDEDVD MDDDEVDEEG
     DDDEEKFRLP TAAEREEEKK QGGIDVHSVQ RRMRECVRVL GKFNKLAEKG RSRTEYTEQL
     LADICSYYGY NEFLAEKLFL LFSVPEAIEF FEANEVPRPV TIRTNTLRTR RRDLAQTLIN
     RGVNLEPIGK WTNVGLQVFE STVPIGATPE YLAGHYMLQA ASSFLPVIAL DPKPHERVLD
     MASAPGGKTT HIAALLQNTG VVFANDANKA RTKSLTANVH RLGCKNVVVC SYDGREFPKV
     IGGFDRVLLD APCSGTGVIS KDASVKVNKS DRDFTLLAHL QKQLILCALD SVTPNSKTGG
     YVVYSTCSVT VDENEAVIDY ALRKRPNVKL VDTGLEFGRP AYASYRGKSF HPSVSLARRF
     YPHVHNMDGF FVAKFKVERR RGGEKEKAKD DGKSLVGIEG EDGDEQQPEA ETKFDDAEDA
     AILEDSRRRQ MKAKGLKPPP RNRPPKATKT VEAAA
//
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