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Database: UniProt
Entry: M1BBS2_SOLTU
LinkDB: M1BBS2_SOLTU
Original site: M1BBS2_SOLTU 
ID   M1BBS2_SOLTU            Unreviewed;       506 AA.
AC   M1BBS2;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=NOL1/NOP2/sun family protein {ECO:0000313|EnsemblPlants:PGSC0003DMT400041674};
GN   Name=102590670 {ECO:0000313|EnsemblPlants:PGSC0003DMT400041674};
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400041674, ECO:0000313|Proteomes:UP000011115};
RN   [1] {ECO:0000313|Proteomes:UP000011115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX   PubMed=21743474; DOI=10.1038/nature10158;
RG   The Potato Genome Sequencing Consortium;
RT   "Genome sequence and analysis of the tuber crop potato.";
RL   Nature 475:189-195(2011).
RN   [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400041674}
RP   IDENTIFICATION.
RC   STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400041674};
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR   AlphaFoldDB; M1BBS2; -.
DR   EnsemblPlants; PGSC0003DMT400041674; PGSC0003DMT400041674; PGSC0003DMG400016157.
DR   Gramene; PGSC0003DMT400041674; PGSC0003DMT400041674; PGSC0003DMG400016157.
DR   Gramene; RHC11H1G0366.2.1; RHC11H1G0366.2.1; RHC11H1G0366.2.
DR   HOGENOM; CLU_005316_4_4_1; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; M1BBS2; baseline.
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:UP000011115};
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          1..251
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          262..281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          320..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..281
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..390
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        103
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         50
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   506 AA;  56422 MW;  73F97C6C18EBE015 CRC64;
     MSTANLIVTN HEAQHFPSCR LDRNFANGSE TQTVRELDIN QLQFDRVLCD VPCSGDGTLR
     KAPDIWRKWN AGNGNGLHGL QIQIAMRGLS LLKVGGRMVY STCSMNPIEN EAVVAEILRR
     CGESVELVDV SSEVPQLVRR PGLKKWKVRD KGAWWTSYKD VPEGRRNAIV PGMFPSGKTY
     LDASEKNDDA TRDQLSDNGN NANVIEVLED PATAATISDE EVSTLPLERC MRIVPHDQNS
     GAFFVSVFQK LSPLPAAAFQ QKKPVSSRGK PNSSDVIQAE SLTTKVKEDV NVEDVKPVDS
     VGTQEVTMDD ADIQAESVTT KVKEDENTED VKPVNSVGSE DVTMDEAGNG TDETALDTEP
     SEILEKTEKE ETQPSTDTRA EPETVRGKRK LQMQGKWRGV DPVIFYKEEA VVSKIKDFYG
     IKESFLFEGH LITRNSDMNH VKRIYHVSKS VKEVLHLNFL AGQQLKIASV GLKMFVSLSE
     FDTSFLFVRL FSNLTRNFSS WGFYHI
//
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