ID M7SIV3_EUTLA Unreviewed; 863 AA.
AC M7SIV3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Putative nol1 nop2 sun family protein {ECO:0000313|EMBL:EMR64223.1};
GN ORFNames=UCREL1_8820 {ECO:0000313|EMBL:EMR64223.1};
OS Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS armeniacae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR64223.1, ECO:0000313|Proteomes:UP000012174};
RN [1] {ECO:0000313|Proteomes:UP000012174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT EL1.";
RL Genome Announc. 1:E0022813-E0022813(2013).
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR EMBL; KB707112; EMR64223.1; -; Genomic_DNA.
DR RefSeq; XP_007796693.1; XM_007798502.1.
DR AlphaFoldDB; M7SIV3; -.
DR STRING; 1287681.M7SIV3; -.
DR KEGG; ela:UCREL1_8820; -.
DR eggNOG; KOG2198; Eukaryota.
DR HOGENOM; CLU_005316_4_2_1; -.
DR OMA; QLFTEYV; -.
DR OrthoDB; 197651at2759; -.
DR Proteomes; UP000012174; 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; 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; 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:UP000012174};
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 61..470
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..831
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 351
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 180..186
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 241
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 268
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 298
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 863 AA; 96070 MW; 79480CA34610D30A CRC64;
MGRGKKNFRG GRKGGGGDNR RPRDGSGLPY RSYSELVKEN EKLERYYNTI VPLEDAEREQ
FWAALKRELP NSFRFCGSKG HALAVRRLLE SRYAPEIVKI ERYDGEPVEA PQPVPWYPDH
LAYSMSTPKH VIRKFPPFAA FQKFLVSETS VGNISRQEVV SMIPPLLLDV EPGMKVLDLC
AAPGSKAAQL LEMIHVGEEA RVRKVMQSFG ETKTDQVASD VDLSIDSGDD GRATGLLVAN
DADYKRSHML THQLKRLSSP NLIVTNHDAT LYPAFRLPRD PNDPEKGQYL KFDRILADVP
CAGDGTLRKN MNLWKDWQPG SALGLHTTQV RILVRALQML KPGGRVVYST CSMNPVENEA
VIASAIERCG GPSKIDIIDC SDRLPELKRS PGMHQWQIMD KSGRIWNSWE EVQQYVLTES
DGIVPSKLNE GMFPKPDTNE CSSLPLDRCM RIYAHQQDTG GFFITALEKK AEFKAKPEQP
AKSEVSNGTK ADPKEAAEKK VVEEVKAVLE EPTDEIPSTG AKRSLDDNGV EPAPEVKKIK
VEAVVESAPV VPESSTEPAE KEVKAEATPK ENTTPKDTTR PDRQVKRPDG SFEEPFKYMS
PDHEIIKGIQ DFYQISPRFP TDRYMVRNAT GEPAKAIYYT SALLRDILTE NEGRGVKFVH
GGVKMFMKQD APSAEVCRWR IQSEGMPIIS GYVGPGRIVR LTSKETFHKL LKEMFPKFVN
DDWKKLGEIG ERARDIGMGC CLLSVEPDGT DPDFAERMVL PLWKSFHSLN LMLPKEDRSA
TLLRVFNDTS PVVNQSLKEA AAKKAAAVKE ETKDEDEVKI EEEDKQPAVP TDGAEDEVMA
DLADANGESV TAAAPANGET SAE
//
