ANM3_ARATH
ID ANM3_ARATH Reviewed; 601 AA.
AC Q0WVD6; Q9C7D0; Q9LHH9;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Probable protein arginine N-methyltransferase 3;
DE EC=2.1.1.-;
GN Name=PRMT3; OrderedLocusNames=At3g12270; ORFNames=F28J15.7;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.
RN [5]
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: Methylates (mono and asymmetric dimethylation) the guanidino
CC nitrogens of arginyl residues in some proteins. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The zinc-finger is responsible for substrate specificity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01015}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51062.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB03136.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP002047; BAB03136.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC069472; AAG51062.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75178.1; -; Genomic_DNA.
DR EMBL; AK226816; BAE98912.1; -; mRNA.
DR RefSeq; NP_187835.2; NM_112063.4.
DR AlphaFoldDB; Q0WVD6; -.
DR SMR; Q0WVD6; -.
DR BioGRID; 5741; 2.
DR IntAct; Q0WVD6; 2.
DR STRING; 3702.AT3G12270.1; -.
DR iPTMnet; Q0WVD6; -.
DR PaxDb; Q0WVD6; -.
DR PRIDE; Q0WVD6; -.
DR ProteomicsDB; 240324; -.
DR EnsemblPlants; AT3G12270.1; AT3G12270.1; AT3G12270.
DR GeneID; 820407; -.
DR Gramene; AT3G12270.1; AT3G12270.1; AT3G12270.
DR KEGG; ath:AT3G12270; -.
DR Araport; AT3G12270; -.
DR TAIR; locus:2082244; AT3G12270.
DR eggNOG; KOG1499; Eukaryota.
DR HOGENOM; CLU_017375_6_1_1; -.
DR InParanoid; Q0WVD6; -.
DR OMA; ETHWQQG; -.
DR OrthoDB; 840669at2759; -.
DR PhylomeDB; Q0WVD6; -.
DR PRO; PR:Q0WVD6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q0WVD6; baseline and differential.
DR Genevisible; Q0WVD6; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0018216; P:peptidyl-arginine methylation; IEA:InterPro.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR11006; PTHR11006; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Metal-binding; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..601
FT /note="Probable protein arginine N-methyltransferase 3"
FT /id="PRO_0000293990"
FT DOMAIN 242..554
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT ZN_FING 57..78
FT /note="C2H2-type"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 365
FT /evidence="ECO:0000250"
FT ACT_SITE 374
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 310
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 601 AA; 67344 MW; 32155B0CBF6812A2 CRC64;
MAATMVKHEI LNYSEDEEEN YSDEGDWGDW KADDNGIEGG EEEEEDDGDD SESDFLCLFC
DSHFVSCDLL FEHCRLSHGF DFHGVRKELK LDFYSSFKLI NYIRSQVAEN MCFSWKIEAD
DYKDVKFPWD EEKYLKPFWQ EDSLLYSFAD DEEDEEVTFD REEVMEELQK LGDLSIDVEA
LGESSMSNSD KCNINGSKDV TSLSNCNGLK QSSADDLIVN GKDAEPKVCD GRLVNRNIRK
VNENYFGSYS SFGIHREMLS DKVRTEAYRD ALLKNPTLLN GSVVMDVGCG TGILSLFAAK
AGASRVVAVE ASEKMAKVAT KIAKDNKVFN DNEHNGVLEV AHSMVEELDK SIQIQPHSVD
VLVSEWMGYC LLYESMLSSV LYARDRWLKP GGAILPDTAT MFVAGFGKGA TSLPFWEDVY
GFDMSSIGKE IHDDTTRLPI VDVIAERDLV TQPTLLQTFD LATMKPDEVD FTATATLEPT
ESEAKTRLCH GVVLWFDTGF TSRFCKENPT VLSTSPYTPP THWAQTILTF QEPISVAPAS
VLSGNDRREA IGTEECPASS IHLRVSVARA HEHRSIDISL EATGLSSKGQ KRHWPVQIFN
L
