ID R1GTL3_BOTPV Unreviewed; 874 AA.
AC R1GTL3;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Putative methyltransferase protein {ECO:0000313|EMBL:EOD51606.1};
GN ORFNames=UCRNP2_1607 {ECO:0000313|EMBL:EOD51606.1};
OS Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS (Neofusicoccum parvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Neofusicoccum.
OX NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD51606.1, ECO:0000313|Proteomes:UP000013521};
RN [1] {ECO:0000313|Proteomes:UP000013521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA Blanco-Ulate B., Rolshausen P., Cantu D.;
RT "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT vascular pathogen associated with grapevine cankers.";
RL Genome Announc. 1:E0033913-E0033913(2013).
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}.
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DR EMBL; KB915836; EOD51606.1; -; Genomic_DNA.
DR RefSeq; XP_007580910.1; XM_007580848.1.
DR AlphaFoldDB; R1GTL3; -.
DR STRING; 1287680.R1GTL3; -.
DR KEGG; npa:UCRNP2_1607; -.
DR eggNOG; KOG2198; Eukaryota.
DR HOGENOM; CLU_005316_4_2_1; -.
DR OMA; KSLWPQG; -.
DR OrthoDB; 197651at2759; -.
DR Proteomes; UP000013521; 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:UP000013521};
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 57..473
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 212..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..862
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 354
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 175..181
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 246
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 273
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 301
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 874 AA; 97429 MW; 96F78F30A48E3643 CRC64;
MGKRGGRGGG RGRGRGNRGG HGGSSRGDWK EVEKHNVNFE KYYNELAIVP EEEREQFWTA
LKKELPNSFR FTGSKGHALA VQQRLVEHYI PEISKVTFDG QLVEPPTQLE WFPEKLAWQM
TTAKNVIRKF PPFASFQKFL VSETTVGNIS RQEVVSMIPP LLIDIKPWHT VLDLCAAPGS
KSAQLCEAIH NGEEARLRKN LRKIAPELGR EISPDGAEVE AEKDQAGEQE DYSDDGRATG
LLICNDVDNR RAHMLVHQVK RLNSPNLVVT NHDATLFPSI RIPSEKGQPN KYLKFDRILA
DVPCSGDGTA RKNPGVWKDW TAGNGLGLYI TQQRILVRAL QMLKVGGRVV YSTCSLNPIE
NEAVVASAID RCGGMSKVKI IDCSQELPGL KRVPGLNTWK VMDKAGRMWN SWEDVVAKKS
EPGEEGLNKI LEGMFPPKAT ENEDEKVPLE RCIRVYPHHQ NTGGFFITVI EKKEEIRARP
EYQANASGSK AVPPAPITNL INEIEQKTEN GEKLEGLKSL DEVTNTDSKA EVDPVQGNDP
AAVRSNLPPP SPTKRSLEDT EAEDPVAKRT KIEVIQHDEV PPAVSEREHR GPPEKKRRDQ
PHEEPFKYLD PKHEVLEDIF GFYEIASRFP RDRFMVRNAS GEPAKAVYYT STLAREILTM
NEGKGMKFVH CGVKMFMKQD AQGQDICRWR IQSEGLPIIE PWVGENRIVR LYKRSTLHKL
LIEMFPKVAG NSWKDLGEIG ERVRDIGMGC CVLRVETSDD EDGFKAMLLR LYNDNSELID
HSKTYNKSNG ANGESAPKDA PEDSALNNGD GGVALDAGMD IDAKDTTTGA DPEVEAIVAE
DRLDSAKQDE KDNTRETAEG DVVAPEDDVV NTTV
//
