ID M1D492_SOLTU Unreviewed; 802 AA.
AC M1D492;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=Putative rRNA methyltransferase {ECO:0000256|HAMAP-Rule:MF_03163};
DE EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_03163};
DE AltName: Full=2'-O-ribose RNA methyltransferase SPB1 homolog {ECO:0000256|HAMAP-Rule:MF_03163};
GN Name=102589886 {ECO:0000313|EnsemblPlants:PGSC0003DMT400080984};
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:PGSC0003DMT400080984, 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:PGSC0003DMT400080984}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400080984};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- FUNCTION: Probable methyltransferase involved in the maturation of rRNA
CC and in the biogenesis of ribosomal subunits. {ECO:0000256|HAMAP-
CC Rule:MF_03163}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleotide in rRNA + S-adenosyl-L-methionine = a 2'-O-
CC methylribonucleotide in rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:48628, Rhea:RHEA-COMP:12164, Rhea:RHEA-COMP:12165,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:90675, ChEBI:CHEBI:90676; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03163};
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000256|HAMAP-
CC Rule:MF_03163}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase RlmE family. SPB1 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03163}.
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DR RefSeq; XP_006367704.1; XM_006367642.2.
DR AlphaFoldDB; M1D492; -.
DR STRING; 4113.M1D492; -.
DR PaxDb; 4113-PGSC0003DMT400080984; -.
DR EnsemblPlants; PGSC0003DMT400080984; PGSC0003DMT400080984; PGSC0003DMG400031553.
DR GeneID; 102589886; -.
DR Gramene; PGSC0003DMT400080984; PGSC0003DMT400080984; PGSC0003DMG400031553.
DR KEGG; sot:102589886; -.
DR eggNOG; KOG1098; Eukaryota.
DR HOGENOM; CLU_009422_8_1_1; -.
DR InParanoid; M1D492; -.
DR OMA; MQNSLVI; -.
DR OrthoDB; 119516at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:0016435; F:rRNA (guanine) methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008650; F:rRNA (uridine-2'-O-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_01547; RNA_methyltr_E; 1.
DR HAMAP; MF_03163; RNA_methyltr_E_SPB1; 1.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR015507; rRNA-MeTfrase_E.
DR InterPro; IPR012920; rRNA_MeTfrase_SPB1-like_C.
DR InterPro; IPR024576; rRNA_MeTfrase_Spb1_DUF3381.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR028589; SPB1-like.
DR PANTHER; PTHR10920; RIBOSOMAL RNA METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10920:SF21; RRNA METHYLTRANSFERASE-RELATED; 1.
DR Pfam; PF11861; DUF3381; 1.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF07780; Spb1_C; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_03163};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03163};
KW Reference proteome {ECO:0000313|Proteomes:UP000011115};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517, ECO:0000256|HAMAP-
KW Rule:MF_03163}; rRNA processing {ECO:0000256|HAMAP-Rule:MF_03163};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_03163};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03163}.
FT DOMAIN 22..201
FT /note="Ribosomal RNA methyltransferase FtsJ"
FT /evidence="ECO:0000259|Pfam:PF01728"
FT DOMAIN 234..379
FT /note="DUF3381"
FT /evidence="ECO:0000259|Pfam:PF11861"
FT DOMAIN 596..788
FT /note="Ribosomal RNA methyltransferase SPB1-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07780"
FT REGION 419..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..717
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..736
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..802
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT BINDING 54
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT BINDING 56
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT BINDING 74
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT BINDING 90
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT BINDING 118
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
SQ SEQUENCE 802 AA; 90923 MW; CA3DE0CC9BAF8C9D CRC64;
MGKLKGRDRR DKYYHLARES RYRSRAAFKL MQLNSKFSFL TSSQSVLDLC AAPGGWMQVV
VKKAPVGSLV IGVDIDPIRP IAGAISLQED ITTAKCKSTI KRIIAQKGCS GFDLILHDGS
PNMGGAWAME ATMQNSLVID SVKLAAQFLL PNGTFVTKVF RSQDYTAVLY CLRQLFEKVE
VEKPLASRSE SAEIYVIGFK YKAPAKIDPR LLDIKHLFQG GQEPLKAVDV LRVTKQKRHR
DGYEDGETVL RKVCSAADFV WSDIKSLGSV TSIMFDDPAS LPMRDHPLTT EEVRTLCEDL
RVLGEQDLKH LSKWRKLMRK ALAPSETISN PKVVIECERE EDEDTRLVKE MEELKETELR
KTKREKRVLA KRQAKDKARE LLGMQSDAAE DGFADPELFS LTLIKCKRDV VVVDDDECDD
GTAEVNSEAD GNDLEAPENA STDMDSEEER LRRDDEIEGL LEDHDKRYMA RGERKTKRSR
ISYLDDCKLL ERGDEDGMTH SAQDSDSDKG EDQVNPLIIP LETAPSQEEV VKTWFTQDVF
VEPEEQEMLD KYNSEDEMLV VGEITPISKT QTTGELLAPI LSKKRMNGLL QVPSHETPND
FEIVPVPPTD SSDSSSDESG DDIDRKAEIL SVAKKLILKK QREAMMDDGY NKYMFDDEGL
PKWFVDEEKR HRQLIMPVTK EEIAAMRAQF KEINARPAKK VAEAKARKKR AAQRKLEKIR
KKANSISDQA DVSDRSKSRM IEQLYRKATP KRAEREYVVA KKGVQVKVGR GKVLVDRRMK
KDARRRGMSK QGLKKGGRDR KP
//
