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Salicylate/benzoate carboxyl methyltransferase (Benzoate O-methyltransferase) (EC 2.1.1.273) (S-adenosyl-L-methionine:benzoic acid carboxyl methyltransferase) (S-adenosyl-L-methionine:salicylate acid carboxyl methyltransferase) (SABATH methyltransferase) (Salicylate carboxymethyltransferase) (EC 2.1.1.274)

 BSMT1_ARATH             Reviewed;         379 AA.
Q6XMI3; Q9CAX9;
29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
13-FEB-2019, entry version 94.
RecName: Full=Salicylate/benzoate carboxyl methyltransferase;
AltName: Full=Benzoate O-methyltransferase;
EC=2.1.1.273;
AltName: Full=S-adenosyl-L-methionine:benzoic acid carboxyl methyltransferase;
AltName: Full=S-adenosyl-L-methionine:salicylate acid carboxyl methyltransferase;
AltName: Full=SABATH methyltransferase;
AltName: Full=Salicylate carboxymethyltransferase;
EC=2.1.1.274;
Name=BSMT1; OrderedLocusNames=At3g11480; ORFNames=F24K9.15;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, INDUCTION BY BIOTIC
AND ABIOTIC STRESSES, AND SUBUNIT.
STRAIN=cv. Columbia;
PubMed=14617060; DOI=10.1046/j.1365-313X.2003.01902.x;
Chen F., D'Auria J.C., Tholl D., Ross J.R., Gershenzon J., Noel J.P.,
Pichersky E.;
"An Arabidopsis thaliana gene for methylsalicylate biosynthesis,
identified by a biochemical genomics approach, has a role in
defense.";
Plant J. 36:577-588(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
INDUCTION BY JASMONIC ACID.
PubMed=17364223; DOI=10.1007/s11103-006-9123-x;
Koo Y.J., Kim M.A., Kim E.H., Song J.T., Jung C., Moon J.K., Kim J.H.,
Seo H.S., Song S.I., Kim J.K., Lee J.S., Cheong J.J., Choi Y.D.;
"Overexpression of salicylic acid carboxyl methyltransferase reduces
salicylic acid-mediated pathogen resistance in Arabidopsis thaliana.";
Plant Mol. Biol. 64:1-15(2007).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19669626; DOI=10.1007/s10059-009-0108-x;
Song J.T., Koo Y.J., Park J.B., Seo Y.J., Cho Y.J., Seo H.S.,
Choi Y.D.;
"The expression patterns of AtBSMT1 and AtSAGT1 encoding a salicylic
acid (SA) methyltransferase and a SA glucosyltransferase,
respectively, in Arabidopsis plants with altered defense responses.";
Mol. Cells 28:105-109(2009).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=20407809; DOI=10.1007/s10886-010-9787-1;
Snoeren T.A., Mumm R., Poelman E.H., Yang Y., Pichersky E., Dicke M.;
"The herbivore-induced plant volatile methyl salicylate negatively
affects attraction of the parasitoid Diadegma semiclausum.";
J. Chem. Ecol. 36:479-489(2010).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19958141; DOI=10.1094/MPMI-23-1-0082;
Liu P.P., Yang Y., Pichersky E., Klessig D.F.;
"Altering expression of benzoic acid/salicylic acid carboxyl
methyltransferase 1 compromises systemic acquired resistance and PAMP-
triggered immunity in arabidopsis.";
Mol. Plant Microbe Interact. 23:82-90(2010).
-!- FUNCTION: Methyltransferase involved in the biosynthesis of
methylsalicylate in response to stresses. Utilizes salicylic acid
(SA) more efficiently than benzoic acid (BA). Can also use
anthranilic acid and m-hydroxybenzoic acid as substrate.
{ECO:0000269|PubMed:14617060, ECO:0000269|PubMed:19669626,
ECO:0000269|PubMed:19958141, ECO:0000269|PubMed:20407809}.
-!- CATALYTIC ACTIVITY:
Reaction=benzoate + S-adenosyl-L-methionine = methyl benzoate + S-
adenosyl-L-homocysteine; Xref=Rhea:RHEA:36099,
ChEBI:CHEBI:16150, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
ChEBI:CHEBI:72775; EC=2.1.1.273;
Evidence={ECO:0000269|PubMed:14617060};
-!- CATALYTIC ACTIVITY:
Reaction=S-adenosyl-L-methionine + salicylate = methyl salicylate
+ S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:36095,
ChEBI:CHEBI:30762, ChEBI:CHEBI:31832, ChEBI:CHEBI:57856,
ChEBI:CHEBI:59789; EC=2.1.1.274;
Evidence={ECO:0000269|PubMed:14617060};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q9FLN8};
Note=Binds 1 Mg(2+) ion per subunit.
{ECO:0000250|UniProtKB:Q9FLN8};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=67 uM for S-adenosyl-L-methionine
{ECO:0000269|PubMed:14617060};
KM=65 uM for benzoic acid {ECO:0000269|PubMed:14617060};
KM=16 uM for salicylic acid {ECO:0000269|PubMed:14617060};
Note=kcat is 0.19 sec(-1) for benzoic acid. kcat is 0.07 sec(-1)
for salicylic acid.;
pH dependence:
Optimum pH is 7.0-8.0. {ECO:0000269|PubMed:14617060};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14617060}.
-!- TISSUE SPECIFICITY: Expressed in flowers and at lower levels in
leaves and stems. Hardly detected in roots and siliques. Expressed
in the sepals and the leaf trichomes and hydathodes.
{ECO:0000269|PubMed:14617060}.
-!- INDUCTION: Up-regulated by alamethicin, herbivory, uprooting,
woundingd, jasmonic acid and methyl jasmonate, but not by
salicylic acid. Induced specifically around the lesions.
{ECO:0000269|PubMed:14617060, ECO:0000269|PubMed:17364223}.
-!- DISRUPTION PHENOTYPE: Loss of accumulation of methyl salicylate
upon pathogen infection, no accumulation of salicylic acid or its
glucoside in uninoculated leaves and no development of systemic
acquired resistance. Increased attractivity to parasitoids.
{ECO:0000269|PubMed:19669626, ECO:0000269|PubMed:19958141,
ECO:0000269|PubMed:20407809}.
-!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
methyltransferase family. SABATH subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG51446.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; AY224595; AAP57210.1; -; mRNA.
EMBL; AC008153; AAG51446.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002686; AEE75053.1; -; Genomic_DNA.
EMBL; BT022049; AAY25461.1; -; mRNA.
EMBL; AK221911; BAD94303.1; -; mRNA.
RefSeq; NP_187755.2; NM_111981.5.
UniGene; At.39742; -.
ProteinModelPortal; Q6XMI3; -.
STRING; 3702.AT3G11480.1; -.
PaxDb; Q6XMI3; -.
PRIDE; Q6XMI3; -.
EnsemblPlants; AT3G11480.1; AT3G11480.1; AT3G11480.
GeneID; 820321; -.
Gramene; AT3G11480.1; AT3G11480.1; AT3G11480.
KEGG; ath:AT3G11480; -.
Araport; AT3G11480; -.
TAIR; locus:2080747; AT3G11480.
eggNOG; ENOG410IKGQ; Eukaryota.
eggNOG; ENOG4112BHH; LUCA.
HOGENOM; HOG000238197; -.
InParanoid; Q6XMI3; -.
KO; K21484; -.
OMA; INMIAHH; -.
OrthoDB; 689338at2759; -.
PhylomeDB; Q6XMI3; -.
BioCyc; MetaCyc:AT3G11480-MONOMER; -.
BRENDA; 2.1.1.273; 399.
BRENDA; 2.1.1.274; 399.
PRO; PR:Q6XMI3; -.
Proteomes; UP000006548; Chromosome 3.
Genevisible; Q6XMI3; AT.
GO; GO:0052624; F:2-phytyl-1,4-naphthoquinone methyltransferase activity; IDA:TAIR.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0080150; F:S-adenosyl-L-methionine:benzoic acid carboxyl methyl transferase activity; IDA:TAIR.
GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:TAIR.
GO; GO:0006952; P:defense response; IEP:TAIR.
GO; GO:0051707; P:response to other organism; IEP:TAIR.
GO; GO:0009611; P:response to wounding; IEP:TAIR.
InterPro; IPR005299; MeTrfase_7.
InterPro; IPR029063; SAM-dependent_MTases.
PANTHER; PTHR31009; PTHR31009; 1.
Pfam; PF03492; Methyltransf_7; 1.
SUPFAM; SSF53335; SSF53335; 1.
1: Evidence at protein level;
Complete proteome; Magnesium; Metal-binding; Methyltransferase;
Plant defense; Reference proteome; S-adenosyl-L-methionine;
Transferase.
CHAIN 1 379 Salicylate/benzoate carboxyl
methyltransferase.
/FTId=PRO_0000422309.
REGION 43 47 Substrate binding.
{ECO:0000250|UniProtKB:A4GE69}.
REGION 81 82 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:Q9FLN8}.
REGION 117 120 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:A4GE70}.
REGION 155 157 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:Q9FLN8}.
REGION 172 174 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:Q9FLN8}.
REGION 173 177 Substrate binding.
{ECO:0000250|UniProtKB:A4GE70}.
METAL 188 188 Magnesium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q9FLN8}.
METAL 275 275 Magnesium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q9FLN8}.
METAL 277 277 Magnesium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q9FLN8}.
METAL 278 278 Magnesium.
{ECO:0000250|UniProtKB:Q9FLN8}.
BINDING 40 40 S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:A4GE70}.
BINDING 40 40 Substrate.
{ECO:0000250|UniProtKB:A4GE70}.
BINDING 81 81 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250|UniProtKB:A4GE69}.
BINDING 87 87 S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:A4GE70}.
SEQUENCE 379 AA; 43365 MW; 09C96CCB184D25F9 CRC64;
MDPRFINTIP SLRYDDDKCD DEYAFVKALC MSGGDGANSY SANSRLQKKV LSMAKPVLVR
NTEEMMMNLD FPTYIKVAEL GCSSGQNSFL AIFEIINTIN VLCQHVNKNS PEIDCCLNDL
PENDFNTTFK FVPFFNKELM ITNKSSCFVY GAPGSFYSRL FSRNSLHLIH SSYALHWLSK
VPEKLENNKG NLYITSSSPQ SAYKAYLNQF QKDFTMFLRL RSEEIVSNGR MVLTFIGRNT
LNDPLYRDCC HFWTLLSNSL RDLVFEGLVS ESKLDAFNMP FYDPNVQELK EVIQKEGSFE
INELESHGFD LGHYYEEDDF EAGRNEANGI RAVSEPMLIA HFGEEIIDTL FDKYAYHVTQ
HANCRNKTTV SLVVSLTKK


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Pathways :
WP1700: Selenoamino acid metabolism
WP1006: metapathway biotransformation
WP1124: metapathway biotransformation
WP1212: metapathway biotransformation
WP1251: metapathway biotransformation
WP1286: metapathway biotransformation
WP1581: Histidine metabolism
WP1673: Naphthalene and anthracene degradation
WP1714: Tyrosine metabolism
WP702: metapathway biotransformation
WP889: metapathway biotransformation
WP1008: amino acid conjugation of benzoic acid
WP1127: amino acid conjugation of benzoic acid
WP1252: amino acid conjugation of benzoic acid
WP1287: amino acid conjugation of benzoic acid
WP1577: amino acid conjugation of benzoic acid
WP521: amino acid conjugation of benzoic acid
WP891: amino acid conjugation of benzoic acid
WP1020: Fatty Acid Biosynthesis
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Related Genes :
[BSMT1 At3g11480 F24K9.15] Salicylate/benzoate carboxyl methyltransferase (Benzoate O-methyltransferase) (EC 2.1.1.273) (S-adenosyl-L-methionine:benzoic acid carboxyl methyltransferase) (S-adenosyl-L-methionine:salicylate acid carboxyl methyltransferase) (SABATH methyltransferase) (Salicylate carboxymethyltransferase) (EC 2.1.1.274)
[ICMTB STE14B At5g08335 F8L15.70] Protein-S-isoprenylcysteine O-methyltransferase B (AtICMTB) (EC 2.1.1.100) (Isoprenylcysteine carboxylmethyltransferase B) (Prenylated protein carboxyl methyltransferase B) (Prenylcysteine carboxyl methyltransferase B)
[PCMT1] Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PIMT) (EC 2.1.1.77) (L-isoaspartyl protein carboxyl methyltransferase) (Protein L-isoaspartyl/D-aspartyl methyltransferase) (Protein-beta-aspartate methyltransferase)
[ICMTA PCM STE14 STE14A At5g23320 MKD15.18] Protein-S-isoprenylcysteine O-methyltransferase A (AtICMTA) (EC 2.1.1.100) (Isoprenylcysteine carboxylmethyltransferase A) (Prenylated protein carboxyl methyltransferase A) (Prenylcysteine carboxyl methyltransferase A) (AtPCM)
[COQ3 YOL096C HRF316] Ubiquinone biosynthesis O-methyltransferase, mitochondrial (3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase) (DHHB methyltransferase) (DHHB-MT) (DHHB-MTase) (3-demethylubiquinol 3-O-methyltransferase) (EC 2.1.1.64) (3-demethylubiquinone-6 3-O-methyltransferase) (Hexaprenyldihydroxybenzoate methyltransferase) (Polyprenyldihydroxybenzoate methyltransferase) (EC 2.1.1.114)
[Pcmt1] Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PIMT) (EC 2.1.1.77) (L-isoaspartyl protein carboxyl methyltransferase) (Protein L-isoaspartyl/D-aspartyl methyltransferase) (Protein-beta-aspartate methyltransferase)
[Pcmt1] Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PIMT) (EC 2.1.1.77) (L-isoaspartyl protein carboxyl methyltransferase) (Protein L-isoaspartyl/D-aspartyl methyltransferase) (Protein-beta-aspartate methyltransferase)
[L] Large structural protein (Protein L) (Replicase) (Transcriptase) [Includes: RNA-directed RNA polymerase (EC 2.7.7.48); mRNA (guanine-N(7)-)-methyltransferase (EC 2.1.1.56); GDP polyribonucleotidyltransferase (EC 2.7.7.88); Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2 (EC 2.1.1.296)]
[L] RNA-directed RNA polymerase L (Protein L) (Large structural protein) (Replicase) (Transcriptase) [Includes: RNA-directed RNA polymerase (EC 2.7.7.48); mRNA (guanine-N(7)-)-methyltransferase (EC 2.1.1.56); GDP polyribonucleotidyltransferase (EC 2.7.7.88); Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2 (EC 2.1.1.296)]
[IEMT1] (Iso)eugenol O-methyltransferase (EC 2.1.1.146) (S-adenosysl-L-methionine:(Iso)eugenol O-methyltransferase) (IEMT)
[pcm-1 C10F3.5] Protein-L-isoaspartate O-methyltransferase (PIMT) (EC 2.1.1.77) (L-isoaspartyl protein carboxyl methyltransferase) (Protein L-isoaspartyl methyltransferase) (Protein-beta-aspartate methyltransferase)
[PIMT1 PCM At3g48330 T29H11.150] Protein-L-isoaspartate O-methyltransferase 1 (AtPIMT1) (EC 2.1.1.77) (L-isoaspartyl protein carboxyl methyltransferase) (Protein L-isoaspartyl methyltransferase) (Protein-beta-aspartate methyltransferase)
[DLO1 SAG108 At4g10500 F3H7.16 F7L13.80] Protein DMR6-LIKE OXYGENASE 1 (EC 1.14.11.-) (2-oxoglutarate (2OG)-Fe(II) oxygenase-like protein DLO1) (Protein SENESCENCE-ASSOCIATED GENE 108) (Salicylate 3-hydroxylase DLO1) (S3H DLO1) (SA 3-hydroxylase DLO1) (Salicylic acid 3-hydroxylase DLO1) (EC 1.14.13.-)
[4'OMT2] 3'-hydroxy-N-methyl-(S)-coclaurine 4'-O-methyltransferase 2 (4'-OMT2) (Ps4'OMT2) (EC 2.1.1.116) (S-adenosyl-L-methionine:3'-hydroxy-N-methylcoclaurine 4'-O-methyltransferase)
[OMT1 COMT1 At5g54160 K18G13.3] Flavone 3'-O-methyltransferase 1 (AtOMT1) (EC 2.1.1.42) (Acetylserotonin O-methyltransferase OMT1) (EC 2.1.1.4) (Caffeate O-methyltransferase 1) (EC 2.1.1.68) (Quercetin 3'-O-methyltransferase 1)
[TRMT10C MRPP1 RG9MTD1] tRNA methyltransferase 10 homolog C (HBV pre-S2 trans-regulated protein 2) (Mitochondrial ribonuclease P protein 1) (Mitochondrial RNase P protein 1) (RNA (guanine-9-)-methyltransferase domain-containing protein 1) (Renal carcinoma antigen NY-REN-49) (mRNA methyladenosine-N(1)-methyltransferase) (EC 2.1.1.-) (tRNA (adenine(9)-N(1))-methyltransferase) (EC 2.1.1.218) (tRNA (guanine(9)-N(1))-methyltransferase) (EC 2.1.1.221)
[tlyA Rv1694] 16S/23S rRNA (cytidine-2'-O)-methyltransferase TlyA (EC 2.1.1.226) (EC 2.1.1.227) (16S rRNA (cytidine1409-2'-O)-methyltransferase) (23S rRNA (cytidine1920-2'-O)-methyltransferase) (Hemolysin TlyA)
[PRMT5 HRMT1L5 IBP72 JBP1 SKB1] Protein arginine N-methyltransferase 5 (EC 2.1.1.320) (72 kDa ICln-binding protein) (Histone-arginine N-methyltransferase PRMT5) (Jak-binding protein 1) (Shk1 kinase-binding protein 1 homolog) (SKB1 homolog) (SKB1Hs) [Cleaved into: Protein arginine N-methyltransferase 5, N-terminally processed]
[L] RNA-directed RNA polymerase L (Protein L) (Large structural protein) (Replicase) (Transcriptase) [Includes: RNA-directed RNA polymerase (EC 2.7.7.48); mRNA (guanine-N(7)-)-methyltransferase (EC 2.1.1.56); GDP polyribonucleotidyltransferase (EC 2.7.7.88); Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2 (EC 2.1.1.296)]
[dim-5 29E8.110 NCU04402] Histone-lysine N-methyltransferase, H3 lysine-9 specific dim-5 (EC 2.1.1.43) (Histone H3-K9 methyltransferase dim-5) (H3-K9-HMTase dim-5) (HKMT)
[L] RNA-directed RNA polymerase L (Protein L) (Large structural protein) (Replicase) (Transcriptase) [Includes: RNA-directed RNA polymerase (EC 2.7.7.48); mRNA (guanine-N(7)-)-methyltransferase (EC 2.1.1.56); GDP polyribonucleotidyltransferase (EC 2.7.7.88); Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2 (EC 2.1.1.296)]
[DMR6 At5g24530 K18P6.6] Protein DOWNY MILDEW RESISTANCE 6 (AtDMR6) (EC 1.14.11.-) (2-oxoglutarate (2OG)-Fe(II) oxygenase-like protein DMR6) (Salicylate 3-hydroxylase DMR6) (S3H DMR6) (SA 3-hydroxylase DMR6) (Salicylic acid 3-hydroxylase DMR6) (EC 1.14.13.-)
[OMT2] Tricetin 3',4',5'-O-trimethyltransferase (TaOMT2) (EC 2.1.1.169) (Caffeic acid 3-O-methyltransferase) (TaCM) (Flavone O-methyltransferase 2)
[] Isoliquiritigenin 2'-O-methyltransferase (MsCHMT) (EC 2.1.1.154) (Chalcone O-methyltransferase) (ChOMT) (Licodione 2'-O-methyltransferase) (MsLMT) (EC 2.1.1.65)
[L] Large structural protein (Protein L) (Replicase) (Transcriptase) [Includes: RNA-directed RNA polymerase (EC 2.7.7.48); mRNA (guanine-N(7)-)-methyltransferase (EC 2.1.1.56); GDP polyribonucleotidyltransferase (EC 2.7.7.88); Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2 (EC 2.1.1.296)]
[L] Large structural protein (Protein L) (Replicase) (Transcriptase) [Includes: RNA-directed RNA polymerase (EC 2.7.7.48); mRNA (guanine-N(7)-)-methyltransferase (EC 2.1.1.56); GDP polyribonucleotidyltransferase (EC 2.7.7.88); Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2 (EC 2.1.1.296)]
[TRM8 YDL201W D1075] tRNA (guanine-N(7)-)-methyltransferase (EC 2.1.1.33) (Transfer RNA methyltransferase 8) (tRNA (guanine(46)-N(7))-methyltransferase) (tRNA(m7G46)-methyltransferase)
[PRMT1 HMT2 HRMT1L2 IR1B4] Protein arginine N-methyltransferase 1 (EC 2.1.1.319) (Histone-arginine N-methyltransferase PRMT1) (Interferon receptor 1-bound protein 4)
[KMT2A ALL1 CXXC7 HRX HTRX MLL MLL1 TRX1] Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.43) (ALL-1) (CXXC-type zinc finger protein 7) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]

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