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Database: UniProt
Entry: A0A8E0QVG9_9EURO
LinkDB: A0A8E0QVG9_9EURO
Original site: A0A8E0QVG9_9EURO 
ID   A0A8E0QVG9_9EURO        Unreviewed;       885 AA.
AC   A0A8E0QVG9;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   18-JUN-2025, entry version 15.
DE   SubName: Full=Multisite-specific tRNA:(Cytosine-C(5))-methyltransferase {ECO:0000313|EMBL:GFF23538.1};
GN   ORFNames=Aud_008147 {ECO:0000313|EMBL:GIC91698.1}, IFM46972_00713
GN   {ECO:0000313|EMBL:GFF23538.1};
OS   Aspergillus udagawae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=91492 {ECO:0000313|EMBL:GIC91698.1, ECO:0000313|Proteomes:UP000036893};
RN   [1] {ECO:0000313|Proteomes:UP000036893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 46973 {ECO:0000313|Proteomes:UP000036893};
RA   Kusuya Y., Takahashi-Nakaguchi A., Takahashi H., Yaguchi T.;
RT   "Draft Genome Sequence of the Pathogenic Filamentous Fungus Aspergillus
RT   udagawae Strain IFM 46973T.";
RL   Genome Announc. 3:e00834-15(2015).
RN   [2] {ECO:0000313|EMBL:GIC91698.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IFM 46973 {ECO:0000313|EMBL:GIC91698.1};
RX   PubMed=26251487; DOI=10.1128/genomeA.00834-15;
RA   Kusuya Y., Takahashi-Nakaguchi A., Takahashi H., Yaguchi T.;
RT   "Draft Genome Sequence of the Pathogenic Filamentous Fungus Aspergillus
RT   udagawae Strain IFM 46973T.";
RL   Genome Announc. 3:e00834-e00815(2015).
RN   [3] {ECO:0000313|EMBL:GFF23538.1, ECO:0000313|Proteomes:UP000465221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 46972 {ECO:0000313|EMBL:GFF23538.1,
RC   ECO:0000313|Proteomes:UP000465221};
RA   Takahashi H., Yaguchi T.;
RT   "Draft genome sequence of Aspergillus udagawae IFM 46972.";
RL   Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:GIC91698.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IFM 46973 {ECO:0000313|EMBL:GIC91698.1};
RA   Takahashi H., Umemura M., Ninomiya A., Kusuya Y., Urayama S., Shimizu M.,
RA   Watanabe A., Kamei K., Yaguchi T., Hagiwara D.;
RT   "Pan-genome distribution and transcriptional activeness of fungal secondary
RT   metabolism genes in Aspergillus section Fumigati.";
RL   Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:GIC91698.1}.
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DR   EMBL; BLKC01000003; GFF23538.1; -; Genomic_DNA.
DR   EMBL; BBXM02000006; GIC91698.1; -; Genomic_DNA.
DR   RefSeq; XP_043148964.1; XM_043293029.1.
DR   GeneID; 66995624; -.
DR   Proteomes; UP000036893; Unassembled WGS sequence.
DR   Proteomes; UP000465221; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016428; F:tRNA (cytidine-5-)-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030488; P:tRNA methylation; IEA:TreeGrafter.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR023270; RCMT_NCL1.
DR   InterPro; IPR018314; RsmB/NOL1/NOP2-like_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22808; NCL1 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR22808:SF1; RNA CYTOSINE-C(5)-METHYLTRANSFERASE NSUN2-RELATED; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF25376; Pre-PUA_NSUN2; 1.
DR   Pfam; PF25378; PUA_NSUN2; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   PRINTS; PR02011; RCMTNCL1.
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}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
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}; tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT   DOMAIN          50..455
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          530..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          816..885
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..10
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..557
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        581..593
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        816..826
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        865..875
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        339
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         168..174
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         226
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         253
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         286
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   885 AA;  99572 MW;  A3A023E0F39D58B2 CRC64;
     MAKRGGRKGG RGGGARGQRQ NYADIPKTNE KLERFYTEQG FIPEEEREAF WEALRRDLPN
     SFRFTGSKGH ALAVQEKLKN HYIPEITSIQ YEGNFVEPPR PVPWYPDQLA WWMTTPKNVV
     RRFKPFASFQ KFLVAETDVG NITRQEVVSM IPPLLIDVRP GMTVLDMCAA PGSKSAQLME
     LLHAGEEDAM RQVAQQVKEG TAGPEPIGPE GLNDDGRTTG LLIANDSDFK RAHMLVHQMK
     RLSSPNLIVT NHDATMYPSI RLPPLPESDG KPQKNRYLKF DRILADVPCT GDGTARKNIS
     VWKEWGPANA LGLHATQVRI LVRALQMLKV GGRVVYSTCS MNPVENEAVV ASAINRCGGS
     ANVEILDCSD ELPGLKRAAG VRTWKVMDRE GRMYNSWKEV EEQREREGIN GLGRIGEGMF
     PPTGENADLP LERCIRVYPH LQDTGGFFIT VLEKKSEIRA KPEDSSKVIP KASIAALTEE
     LDFKQKHGNA RPLEKLNALD DLVAPDQEAQ LEMDKNASVA EATHQVPYFA TNQISPAKRD
     AEDMEDEVPS KKTKVEDGTE VVLGDRPIHR PPPEAEDPDV SESTPTPLPT ETPQAESTET
     KPQPPQKRKP GQPIEEPFKY LDPDNEEIDP IFKFYEISER FPRDRFMVRN AQATPTRTIY
     YTSALARDIL TANEGHGMKF VHCGVKMFVK QDAQRPNVCR WRIQTDGLRI LEPWVGPGRA
     VVLTKKETLR KLLVEMFPKV ADDSWKDLGE IGERVRDIEM GCSILYVQPE ENFSEHMVLP
     LWRSLHSVNL MLPKEERRAM LLRIFNDEPQ LLNITQQGTP QTSTPVTPAV ETNEEDVSGM
     APTEAEENAL KQENLVLGED QQEQVDARET WTKAGDEEDR FNTTV
//
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