MT797_ARATH
ID MT797_ARATH Reviewed; 362 AA.
AC Q9FKD0; F4K8P4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Probable S-adenosylmethionine-dependent methyltransferase At5g37970;
DE EC=2.1.1.-;
GN OrderedLocusNames=At5g37970; ORFNames=K18L3.130;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9FLN8};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9FLN8};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9FLN8}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; AB012241; BAB09042.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94253.2; -; Genomic_DNA.
DR RefSeq; NP_198613.2; NM_123156.2.
DR AlphaFoldDB; Q9FKD0; -.
DR SMR; Q9FKD0; -.
DR STRING; 3702.AT5G37970.1; -.
DR iPTMnet; Q9FKD0; -.
DR PaxDb; Q9FKD0; -.
DR PRIDE; Q9FKD0; -.
DR EnsemblPlants; AT5G37970.1; AT5G37970.1; AT5G37970.
DR GeneID; 833776; -.
DR Gramene; AT5G37970.1; AT5G37970.1; AT5G37970.
DR KEGG; ath:AT5G37970; -.
DR Araport; AT5G37970; -.
DR eggNOG; ENOG502QUIN; Eukaryota.
DR HOGENOM; CLU_019628_1_1_1; -.
DR InParanoid; Q9FKD0; -.
DR OMA; MEEISHP; -.
DR OrthoDB; 742152at2759; -.
DR PhylomeDB; Q9FKD0; -.
DR BioCyc; ARA:AT5G37970-MON; -.
DR PRO; PR:Q9FKD0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKD0; baseline and differential.
DR Genevisible; Q9FKD0; AT.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IBA:GO_Central.
DR Gene3D; 1.10.1200.270; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR005299; MeTrfase_7.
DR InterPro; IPR042086; MeTrfase_capping.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR31009; PTHR31009; 1.
DR Pfam; PF03492; Methyltransf_7; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 3: Inferred from homology;
KW Magnesium; Metal-binding; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..362
FT /note="Probable S-adenosylmethionine-dependent
FT methyltransferase At5g37970"
FT /id="PRO_0000333026"
FT BINDING 19
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 19
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 22..26
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 65..66
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 65
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 71
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 105..108
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 136..138
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 153..155
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 154..158
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 261
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 263
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
SQ SEQUENCE 362 AA; 41414 MW; 619791CA68CB8365 CRC64;
MPTFPQSFPM NGGDGPHSYI HNSSYQKVAI DGVKERTSEA ILEKLDLEFL NRNSEENILR
IVDFGCSIGP NTFDVVQNII DTVKQKRLKE NKTYIGAPLE FQVCFNDQPN NDFNTLFRTQ
PFFSRKEYFS VGVPGSFHGR VLPKNSLHIG HTSYTLHWLS NVPQHVCDKK SPALNKSYIQ
CNNLVDEVTK AYKIQFRKDF GGFLEARAEE LVSGGLMILS GQCLPDGIPK ALTWQGVVID
MIGDCLMDLA KLGITSKEKI ELFSLPTYIP HISEFKANIE QNENFNVETM EEISHPMDYM
PLTNDFITSM FRAILNTIIE EHFGEGVVNE LFSRLAKRLD KYPIDFKRCK KYVNYFIVLK
RK
