MT799_ARATH
ID MT799_ARATH Reviewed; 362 AA.
AC Q9FKC8; F4K8P6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Probable S-adenosylmethionine-dependent methyltransferase At5g37990;
DE EC=2.1.1.-;
GN OrderedLocusNames=At5g37990; ORFNames=K18L3.150;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09044.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB012241; BAB09044.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED94255.2; -; Genomic_DNA.
DR RefSeq; NP_198615.3; NM_123158.4.
DR AlphaFoldDB; Q9FKC8; -.
DR SMR; Q9FKC8; -.
DR STRING; 3702.AT5G37990.1; -.
DR PaxDb; Q9FKC8; -.
DR PRIDE; Q9FKC8; -.
DR ProteomicsDB; 250803; -.
DR EnsemblPlants; AT5G37990.1; AT5G37990.1; AT5G37990.
DR GeneID; 833778; -.
DR Gramene; AT5G37990.1; AT5G37990.1; AT5G37990.
DR KEGG; ath:AT5G37990; -.
DR Araport; AT5G37990; -.
DR eggNOG; ENOG502QUIN; Eukaryota.
DR HOGENOM; CLU_019628_1_1_1; -.
DR InParanoid; Q9FKC8; -.
DR OMA; HFAHSSM; -.
DR OrthoDB; 742152at2759; -.
DR PhylomeDB; Q9FKC8; -.
DR BioCyc; ARA:AT5G37990-MON; -.
DR PRO; PR:Q9FKC8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKC8; baseline and differential.
DR Genevisible; Q9FKC8; 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 At5g37990"
FT /id="PRO_0000333027"
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; 41025 MW; CBB39C5FD6EADB02 CRC64;
MPTFPQSFPM NGGDGPHSYI HNSSYQKVAI DGAKEKTSEA ILKNLDLELL NRNSDENILR
IADFGCSIGP NTFEVVQNII DTVKQKNLKE NNAYIGAPLE FQVCFNDQPN NDFNTLFRTQ
PISSKQAYLS VGVPGSFHGR VLPKNSLHIG HITYALHWLS TVPQHVCDKK SPALNKSYIQ
CNNLVEEVTE AYRVQFKKDM GDFLGARAEE LVSGGLMILS GQCLPDGVPK ALTWQGVVID
MIGDCLMDMA KQGITTKEKI ELFSLPIYIP HISEFKAEIE RNENFSIETM EKISHPMDYK
PLTNDFITSM FRAILNTIIE EHFGDGVVNE LFDRFAKKLN KYPIDFKRCK KYVNYFIVLK
RK
