ID A0A4Y7JD46_PAPSO Unreviewed; 606 AA.
AC A0A4Y7JD46;
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=tRNA (guanine(26)-N(2))-dimethyltransferase {ECO:0000256|ARBA:ARBA00039099, ECO:0000256|PROSITE-ProRule:PRU00958};
DE EC=2.1.1.216 {ECO:0000256|ARBA:ARBA00039099, ECO:0000256|PROSITE-ProRule:PRU00958};
GN ORFNames=C5167_005754 {ECO:0000313|EMBL:RZC58456.1};
OS Papaver somniferum (Opium poppy).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Papaver.
OX NCBI_TaxID=3469 {ECO:0000313|EMBL:RZC58456.1, ECO:0000313|Proteomes:UP000316621};
RN [1] {ECO:0000313|EMBL:RZC58456.1, ECO:0000313|Proteomes:UP000316621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HN1 {ECO:0000313|Proteomes:UP000316621};
RC TISSUE=Leaves {ECO:0000313|EMBL:RZC58456.1};
RX PubMed=30166436; DOI=.1126/science.aat4096;
RA Guo L., Winzer T., Yang X., Li Y., Ning Z., He Z., Teodor R., Lu Y.,
RA Bowser T.A., Graham I.A., Ye K.;
RT "The opium poppy genome and morphinan production.";
RL Science 362:343-347(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) +
CC N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43140, Rhea:RHEA-COMP:10359, Rhea:RHEA-COMP:10360,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74513; EC=2.1.1.216;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU00958};
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Trm1 family. {ECO:0000256|PROSITE-ProRule:PRU00958}.
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DR EMBL; CM010718; RZC58456.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Y7JD46; -.
DR STRING; 3469.A0A4Y7JD46; -.
DR EnsemblPlants; RZC58456; RZC58456; C5167_005754.
DR Gramene; RZC58456; RZC58456; C5167_005754.
DR OMA; CCYSRSP; -.
DR OrthoDB; 942596at2759; -.
DR Proteomes; UP000316621; Chromosome 4.
DR GO; GO:0160102; F:tRNA (guanine(10)-N2)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0160104; F:tRNA (guanine(26)-N2)-dimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006400; P:tRNA modification; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.30.56.70; N2,N2-dimethylguanosine tRNA methyltransferase, C-terminal domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002905; Trm1.
DR InterPro; IPR042296; tRNA_met_Trm1_C.
DR NCBIfam; TIGR00308; TRM1; 1.
DR PANTHER; PTHR10631; N 2 ,N 2 -DIMETHYLGUANOSINE TRNA METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10631:SF3; TRNA (GUANINE(26)-N(2))-DIMETHYLTRANSFERASE; 1.
DR Pfam; PF02005; TRM; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51626; SAM_MT_TRM1; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU00958}; Reference proteome {ECO:0000313|Proteomes:UP000316621};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00958};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU00958};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00958}; tRNA processing {ECO:0000256|PROSITE-ProRule:PRU00958};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|PROSITE-
KW ProRule:PRU00958}.
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 606 AA; 66646 MW; D08AD5E291F2A438 CRC64;
MGDEAGGGEE MKQNSNTTMS TDPNDYTIIK EGEAEILMHA NNEVFYNKTQ VNNRDLSIAV
LRTFISKRKE EHEAMLSKKK KRVPKVSSGE ASNGPIPQEI TTQNGEKSNG KCEEHVEPSK
EPGNVSEEPI RATDGKGREL KPPRVLEALA ASGLRSIRYA REVEEIGQVV ALDNDKASVE
ACRRNIKCNG SVTTAKVESH LTDARVFMLS HPKEFDVVDL DPYGSPSVFL DSAVQSVADG
GILMCTATDM AVLCGGNGEV CYSKYGSYPL RGKYCHEMAL RIVLACIESH ANRYKRYIVP
VLSVQMDFYV RVFVRIFTSA SEMKNTPLKL SHVYQCVGCD SFHLQSLART VSKNNSVRYL
PGFGPVVPQE CTDCGKKFNM GGPIWSAPIH DQEWVTSILE NVQSLKERYP AYDRISAVLT
TVSEELPDVP LFLSLHNLCG TLKCTSPSAV MFRSAVLNAG YRISGTHVNP LGLKSDAPMD
VIWDIMRCWV KSHPVKAQPA DQSGTVILAK EPTLQANFAR AVASLSKAQA KKVARFLPNP
ERHWGPKLRA GRTITSKHVS LLGPKALNGS NKDEEGSNGN QEGTGEEEPE LKRQKTEDPT
IPMSES
//
