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Database: UniProt
Entry: W9YFL8_9EURO
LinkDB: W9YFL8_9EURO
Original site: W9YFL8_9EURO 
ID   W9YFL8_9EURO            Unreviewed;       870 AA.
AC   W9YFL8;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN   ORFNames=A1O1_04973 {ECO:0000313|EMBL:EXJ88046.1};
OS   Capronia coronata CBS 617.96.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX   NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ88046.1, ECO:0000313|Proteomes:UP000019484};
RN   [1] {ECO:0000313|EMBL:EXJ88046.1, ECO:0000313|Proteomes:UP000019484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ88046.1,
RC   ECO:0000313|Proteomes:UP000019484};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capronia coronata CBS 617.96.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:EXJ88046.1}.
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DR   EMBL; AMWN01000004; EXJ88046.1; -; Genomic_DNA.
DR   RefSeq; XP_007724052.1; XM_007725862.1.
DR   AlphaFoldDB; W9YFL8; -.
DR   STRING; 1182541.W9YFL8; -.
DR   GeneID; 19159851; -.
DR   eggNOG; KOG2198; Eukaryota.
DR   HOGENOM; CLU_005316_4_2_1; -.
DR   OrthoDB; 197651at2759; -.
DR   Proteomes; UP000019484; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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:UniProt.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
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; 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; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019484};
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          58..457
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          498..576
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          789..870
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..539
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..560
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        793..808
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        344
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         176..182
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         231
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         258
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         291
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   870 AA;  96951 MW;  4AE9B454B414C17D CRC64;
     MGKRGGKRNG RGRGGGGGGP RPRQDNRTNK EEISRYNDKF EEYYNQLGII PDAEKSQFWE
     AMRRDLPNSF RFTGSRAHAL AVQQRLRDYY IPEITGITYE GQYVEAPRPV EWYPDQLAWY
     MTTPKNVIRR FKPFANFQKF LVAETEVGNI TRQEVVSMIP PLLMDLKPGM TVLDLCAAPG
     SKSAQLIEMI HSGEEDRCRQ VASNIANGLD RPEGEDFEDD GRATGLLVAN DVDYRRAHML
     VHQMKRLSSP NIIVTNHDAT VFPSIKVSSP PTAQGKPVQN RYLKFDRILA DVPCSGDGTV
     RKNMEIWKKW SPSNGLGLHA TQVRILIRAL QMLKVGGRVV YSTCSMNPVE DEAVLAEAIN
     RCGGPDLVRL LETKNYLPGL KRCPGLKEWT VMDKAGRIWK DYDSVLKQKE SAGEEGLGRL
     SESMFPPKND LPLDRAMRVY PHQQDTGAFF IAILEKQSEI RAKPEEKPAV MSQTTKVLAA
     DSNGLKVELE TAPDGVVEKV NGSTAADSET PFKRKRSVDE EEVAPVKRVK SEDHLAPEAD
     TGSEQIPTTN DSAAEPLTTA PSNAQPPPPK KKNRDQPFEE AFKYLSPSIP ELAQIKEFYN
     LSPRFPSDRY MVRNAQGTAT KNIYYTNALA KEILQENEGK GLKFVHAGVK MYVKQDAPAP
     DVCPWRIQTD GLRLLEAWVG PERIVKLHKK ETLRKLLIEM FPKFHGEEYK NLGEVGEQIL
     PLEMGCCVLI VDPSEAEDGL SERMVFPLWK SVQSLNLMLP KEERRAMLLR LFNDDTPLVN
     PSKGWIAAGK KGDAAAAKEK DAQKPGESDA MDVDATSVQE TPREPAIPVR NSSSPEPVAD
     DTVNDEGEDA TAVPETGISE DEEDGGVQIS
//
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