ASHR1_ARATH
ID ASHR1_ARATH Reviewed; 480 AA.
AC Q7XJS0; A4VCM6;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Histone-lysine N-methyltransferase ASHR1;
DE EC=2.1.1.-;
DE AltName: Full=ASH1-related protein 1;
DE AltName: Full=Protein SET DOMAIN GROUP 37;
GN Name=ASHR1; Synonyms=SDG37, SET37; OrderedLocusNames=At2g17900;
GN ORFNames=T13L16.8;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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].
RC STRAIN=cv. Columbia;
RA Bautista-Mercan V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C.,
RA Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NOMENCLATURE.
RX PubMed=11691919; DOI=10.1093/nar/29.21.4319;
RA Baumbusch L.O., Thorstensen T., Krauss V., Fischer A., Naumann K.,
RA Assalkhou R., Schulz I., Reuter G., Aalen R.B.;
RT "The Arabidopsis thaliana genome contains at least 29 active genes encoding
RT SET domain proteins that can be assigned to four evolutionarily conserved
RT classes.";
RL Nucleic Acids Res. 29:4319-4333(2001).
CC -!- FUNCTION: Histone methyltransferase. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)-
CC methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC -!- INTERACTION:
CC Q7XJS0; P42777: GBF4; NbExp=3; IntAct=EBI-15192553, EBI-15192551;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. SET2 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; CP002685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BT030467; ABP88121.1; -; mRNA.
DR PIR; T00834; T00834.
DR AlphaFoldDB; Q7XJS0; -.
DR SMR; Q7XJS0; -.
DR BioGRID; 1657; 3.
DR IntAct; Q7XJS0; 3.
DR STRING; 3702.AT2G17900.1; -.
DR iPTMnet; Q7XJS0; -.
DR PaxDb; Q7XJS0; -.
DR PeptideAtlas; Q7XJS0; -.
DR PRIDE; Q7XJS0; -.
DR EnsemblPlants; AT2G17900.1; AT2G17900.1; AT2G17900.
DR Gramene; AT2G17900.1; AT2G17900.1; AT2G17900.
DR Araport; AT2G17900; -.
DR TAIR; locus:2827831; AT2G17900.
DR eggNOG; KOG2084; Eukaryota.
DR HOGENOM; CLU_018406_2_0_1; -.
DR InParanoid; Q7XJS0; -.
DR PhylomeDB; Q7XJS0; -.
DR PRO; PR:Q7XJS0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q7XJS0; baseline and differential.
DR Genevisible; Q7XJS0; AT.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0034968; P:histone lysine methylation; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR002893; Znf_MYND.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Chromosome; Metal-binding; Methyltransferase; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..480
FT /note="Histone-lysine N-methyltransferase ASHR1"
FT /id="PRO_0000233374"
FT DOMAIN 11..248
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 56..93
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
SQ SEQUENCE 480 AA; 54828 MW; 6A90425589785D1E CRC64;
MADLQRFLQD RCLGVSNLPQ KGRSLFTARD FRPGEVILSQ KPYICVPNNT SSESRCDGCF
KTNNLKKCSA CQVVWYCGSS CQKSEWKLHR DECKALTRLE KEKRKFVTPT IRLMVRLYIK
RNLQNEKVLP ITTTDNYSLV EALVSHMSEI DEKQMLLYAQ MANLVNLILQ FPSVDLREIA
ENFSKFSCNA HSICDSELRP QGIGLFPLVS IINHSCSPNA VLVFEEQMAV VRAMDNISKD
SEITISYIET AGSTLTRQKS LKEQYLFHCQ CARCSNFGKP HDIEESAILE GYRCANEKCT
GFLLRDPEEK GFVCQKCLLL RSKEEVKKLA SDLKTVSEKA PTSPSAEDKQ AAIELYKTIE
KLQVKLYHSF SIPLMRTREK LLKMLMDVEI WREALNYCRL IVPVYQRVYP ATHPLIGLQF
YTQGKLEWLL GETKEAVSSL IKAFDILRIS HGISTPFMKE LSAKLEEARA EASYKQLALH
