MT810_ARATH
ID MT810_ARATH Reviewed; 359 AA.
AC Q9LS10; Q0WQ18;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Probable S-adenosylmethionine-dependent methyltransferase At5g38100;
DE EC=2.1.1.-;
GN OrderedLocusNames=At5g38100; ORFNames=F16F17.100;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LS10-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LS10-2; Sequence=VSP_033443;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; AB028606; BAA97544.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94267.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94268.1; -; Genomic_DNA.
DR EMBL; BX831638; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK228891; BAF00781.1; -; mRNA.
DR RefSeq; NP_001190433.1; NM_001203504.1. [Q9LS10-2]
DR RefSeq; NP_198626.2; NM_123170.3. [Q9LS10-1]
DR AlphaFoldDB; Q9LS10; -.
DR SMR; Q9LS10; -.
DR BioGRID; 19041; 1.
DR PaxDb; Q9LS10; -.
DR PRIDE; Q9LS10; -.
DR ProteomicsDB; 250804; -. [Q9LS10-1]
DR EnsemblPlants; AT5G38100.1; AT5G38100.1; AT5G38100. [Q9LS10-1]
DR EnsemblPlants; AT5G38100.2; AT5G38100.2; AT5G38100. [Q9LS10-2]
DR GeneID; 833790; -.
DR Gramene; AT5G38100.1; AT5G38100.1; AT5G38100. [Q9LS10-1]
DR Gramene; AT5G38100.2; AT5G38100.2; AT5G38100. [Q9LS10-2]
DR KEGG; ath:AT5G38100; -.
DR Araport; AT5G38100; -.
DR TAIR; locus:2144461; AT5G38100.
DR eggNOG; ENOG502QUIN; Eukaryota.
DR HOGENOM; CLU_019628_1_1_1; -.
DR InParanoid; Q9LS10; -.
DR OMA; NETSLMP; -.
DR OrthoDB; 742152at2759; -.
DR PhylomeDB; Q9LS10; -.
DR BioCyc; ARA:AT5G38100-MON; -.
DR PRO; PR:Q9LS10; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LS10; baseline and differential.
DR Genevisible; Q9LS10; 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 2: Evidence at transcript level;
KW Alternative splicing; Magnesium; Metal-binding; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..359
FT /note="Probable S-adenosylmethionine-dependent
FT methyltransferase At5g38100"
FT /id="PRO_0000333028"
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 62..63
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 62
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 68
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 102..105
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 133..135
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 150..152
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 151..155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 258
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT VAR_SEQ 250..359
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_033443"
SQ SEQUENCE 359 AA; 40945 MW; FF96527A80F95D34 CRC64;
MSTSSHMYPM SSGHDQHSYI HNSSYQKAAI SSAVEKTRRC IFEKLDLQLS SDFGTFRIAD
FGCSIGPNTF HVAQSIIDTV KSKRLEESTE NSLVPLEFQV FFNDQPTNDF NTLFRTQPLS
PEREYFSVGV PGSFYGRVLP RNSIHIGHTS YTTHWLSKVP DNVCDKKSMA WNKNYIQCNN
LLEEVTKAYK VQFIKDMEIF LDARAEELVP GGLMIVIGEC LPDGVSLYET WQGYVMDTIG
DCLMDMAKSG ITSEEKIDLF SLPVYFPQFS ELKGEIEKNG SFTIELMETT SHPLEGKPLT
NDFITSTFRA FLTTIIEKHF GDGVVDELFY RLAKKLSNHP IDFEMRKKQV VYCIVLKRK
