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}.
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; 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
//