ANM6_ARATH
ID ANM6_ARATH Reviewed; 435 AA.
AC Q08A71; Q9LJZ9;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Probable protein arginine N-methyltransferase 6;
DE EC=2.1.1.-;
GN Name=PRMT6; OrderedLocusNames=At3g20020; ORFNames=MAL21.12;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
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;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17005254; DOI=10.1016/j.pharmthera.2006.06.007;
RA Krause C.D., Yang Z.-H., Kim Y.-S., Lee J.-H., Cook J.R., Pestka S.;
RT "Protein arginine methyltransferases: evolution and assessment of their
RT pharmacological and therapeutic potential.";
RL Pharmacol. Ther. 113:50-87(2007).
CC -!- FUNCTION: Arginine methyltransferase that can both catalyze the
CC formation of omega-N monomethylarginine (MMA) and asymmetrical
CC dimethylarginine (aDMA). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q08A71-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q08A71-2; Sequence=VSP_026574;
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family. PRMT6
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01015}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01859.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP000383; BAB01859.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76320.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76321.1; -; Genomic_DNA.
DR EMBL; BT029008; ABI93917.1; -; mRNA.
DR RefSeq; NP_001078191.1; NM_001084722.1. [Q08A71-2]
DR RefSeq; NP_188637.2; NM_112893.4. [Q08A71-1]
DR AlphaFoldDB; Q08A71; -.
DR SMR; Q08A71; -.
DR STRING; 3702.AT3G20020.1; -.
DR iPTMnet; Q08A71; -.
DR PaxDb; Q08A71; -.
DR PRIDE; Q08A71; -.
DR ProteomicsDB; 245003; -. [Q08A71-1]
DR EnsemblPlants; AT3G20020.1; AT3G20020.1; AT3G20020. [Q08A71-1]
DR EnsemblPlants; AT3G20020.2; AT3G20020.2; AT3G20020. [Q08A71-2]
DR GeneID; 821541; -.
DR Gramene; AT3G20020.1; AT3G20020.1; AT3G20020. [Q08A71-1]
DR Gramene; AT3G20020.2; AT3G20020.2; AT3G20020. [Q08A71-2]
DR KEGG; ath:AT3G20020; -.
DR Araport; AT3G20020; -.
DR TAIR; locus:2087540; AT3G20020.
DR eggNOG; KOG1499; Eukaryota.
DR HOGENOM; CLU_017375_1_2_1; -.
DR InParanoid; Q08A71; -.
DR OMA; SARHICI; -.
DR PhylomeDB; Q08A71; -.
DR PRO; PR:Q08A71; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q08A71; baseline and differential.
DR Genevisible; Q08A71; AT.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0018216; P:peptidyl-arginine methylation; IEA:InterPro.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11006; PTHR11006; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..435
FT /note="Probable protein arginine N-methyltransferase 6"
FT /id="PRO_0000293996"
FT DOMAIN 80..418
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 191
FT /evidence="ECO:0000250"
FT ACT_SITE 200
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT VAR_SEQ 156..177
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_026574"
SQ SEQUENCE 435 AA; 48271 MW; BBFEF1694183497C CRC64;
MQSGGDFSNG FHGDHHRELE LEDKQGPSLS SFGRAKKRSH AGARDPRGGL ANVLRVSDQL
GEHKSLETSE SSPPPCTDFD VAYFHSYAHV GIHEEMIKDR ARTETYREAI MQHQSLIEGK
VVVDVGCGTG ILSIFCAQAG AKRVYAVDAS DIAVQAKEVV KANGLSDKVI VLHGRVEDVE
IDEEVDVIIS EWMGYMLLYE SMLGSVITAR DRWLKPGGLI LPSHATLYMA PISHPDRYSH
SIDFWRNVYG IDMSAMMQLA KQCAFEEPSV ESISGENVLT WPEVVKHIDC KTIKIQELDS
VTARYKFNSM MRAPMHGFAF WFDVEFSGPA SSPAKNTSET SIASGSSSIS PSGEVNQKKR
TNPSDALVLS TSPESPPTHW QQTIVYFYDP IDVEQDQVIE GSVTLSQSKE NKRFMNIHLE
YSSAGRSFVK ESVMR
