ID A0A4Y8DE71_9HELO Unreviewed; 937 AA.
AC A0A4Y8DE71;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN ORFNames=BOTCAL_0024g00150 {ECO:0000313|EMBL:TEY83807.1};
OS Botryotinia calthae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botryotinia.
OX NCBI_TaxID=38488 {ECO:0000313|EMBL:TEY83807.1, ECO:0000313|Proteomes:UP000297299};
RN [1] {ECO:0000313|EMBL:TEY83807.1, ECO:0000313|Proteomes:UP000297299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUCL2830 {ECO:0000313|EMBL:TEY83807.1,
RC ECO:0000313|Proteomes:UP000297299};
RA Valero-Jimenez C.A., Tapia P., Veloso J., Silva-Moreno E., Staats M.,
RA Valdes J.H., Van Kan J.A.L.;
RT "Comparative genomics of Botrytis spp.";
RL Submitted (NOV-2017) 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:TEY83807.1}.
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DR EMBL; PHWZ01000024; TEY83807.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Y8DE71; -.
DR STRING; 38488.A0A4Y8DE71; -.
DR Proteomes; UP000297299; 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:UP000297299};
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 62..463
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 345
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 181..187
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 235
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 262
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 292
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 937 AA; 103364 MW; C3461C7EE1EE7719 CRC64;
MGQRGKGGRG GRGGRGGRNG GRSRDNQVDN RCSFEKVPKS NEKFERYYNE LLNLEEAEKE
EFWGALKREL PNSFRFAGSK GHAIAVQKQL KERYIPEISE IKQFDGSPVE PPMPVPWYPD
ELAWSMKTSK TVIRKSPPFA KFQKFLVSET SVGNISRQEI VSMIPPLVMD LKPGMTVLDM
CAAPGSKAAQ LLEMVHHGEE NRVQAVLKGD GSADAELELD PSDDGRATGL LIANDADYKR
SHMLIHQLKR LSSPNLIVTN HDAIMFPSIK LPPTPENPAT NRYLKFDRIL ADVPCSGDGT
TRKNVNLWKD WNPGNALGLY VTQVRILVRA LQMLKVGGRV VYSTCSMNPI ENEAVVASAI
ERCGGPEKVK LVSSDDQLPL LKRRPGLKTW TVMDKKGRVW KSWAELQKFI AENGQDDWTG
RLVEGMFPPT DESMSSVPLD QCMRVYAHLQ DTGGFFITIL EKQAEFKAKP ESENKKIAPK
PPITAIVDEI ESAPAPKDGE TVAPKIEAAD ELTHPTSSTL DEVTPVARQN QEQSGSDATH
TVGSKRPASE IEDTEMDAAV ENKKLKTEDT EIHASAPTEG RTEHFPPPPG AELDLTTRPG
DQQADAPPKK LLNKYGQNQA FEEAFKYIPG DHSQVQDIES FYKLSEKFPR DRFLVRNATG
EPAKTIYYTT ALIRDILSEN EGKGIKFVHA GVKMFMKQDV QGEGVCRWRI QSEGMPILQG
YVGDGRVVNL SKKETLRTLL IEMFPKVSGD GWKDLGEIGE RVRDIGMGCC VLRIEPGEGE
DVFTERMVLP LWRSMHSLNL MLAKEDRSAM LLRIFNDTTP LVNNSVGAQR EAELKKEGES
KTEVAAGFKV ENGEIKVDVD GGLEGAAATE AKKGDQRDGD VQIREGPYDT LVAGVEQVAN
RGVDVKAEKI EKGEETGGSE VQMGGMGGIE GQEGGVA
//
