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ASHH3_ARATH
ID   ASHH3_ARATH             Reviewed;         363 AA.
AC   Q945S8; O80584; Q94AQ1;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Histone-lysine N-methyltransferase ASHH3;
DE            EC=2.1.1.-;
DE   AltName: Full=ASH1 homolog 3;
DE   AltName: Full=Protein SET DOMAIN GROUP 7;
GN   Name=ASHH3; Synonyms=SDG7, SET7; OrderedLocusNames=At2g44150;
GN   ORFNames=F6E13.28;
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;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 11-135, AND 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; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00911};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere
CC       {ECO:0000250}. Note=Associates with centromeric constitutive
CC       heterochromatin. {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:PRU00911}.
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DR   EMBL; AC004005; AAC23419.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10383.1; -; Genomic_DNA.
DR   EMBL; AY045886; AAK76560.1; -; mRNA.
DR   EMBL; AY091447; AAM14386.1; -; mRNA.
DR   EMBL; AF408060; AAL01111.1; -; mRNA.
DR   PIR; T00695; T00695.
DR   RefSeq; NP_566010.1; NM_129978.4.
DR   AlphaFoldDB; Q945S8; -.
DR   SMR; Q945S8; -.
DR   BioGRID; 4357; 10.
DR   IntAct; Q945S8; 10.
DR   STRING; 3702.AT2G44150.1; -.
DR   PaxDb; Q945S8; -.
DR   PRIDE; Q945S8; -.
DR   ProteomicsDB; 246851; -.
DR   EnsemblPlants; AT2G44150.1; AT2G44150.1; AT2G44150.
DR   GeneID; 819021; -.
DR   Gramene; AT2G44150.1; AT2G44150.1; AT2G44150.
DR   KEGG; ath:AT2G44150; -.
DR   Araport; AT2G44150; -.
DR   TAIR; locus:2051769; AT2G44150.
DR   eggNOG; KOG1081; Eukaryota.
DR   HOGENOM; CLU_020840_1_0_1; -.
DR   InParanoid; Q945S8; -.
DR   OMA; WLNKGKP; -.
DR   OrthoDB; 1316920at2759; -.
DR   PhylomeDB; Q945S8; -.
DR   PRO; PR:Q945S8; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q945S8; baseline and differential.
DR   Genevisible; Q945S8; AT.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IBA:GO_Central.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:TAIR.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   Gene3D; 2.170.270.10; -; 1.
DR   InterPro; IPR006560; AWS_dom.
DR   InterPro; IPR025787; Hist-Lys_N-MeTrfase_SET2_plant.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00570; AWS; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF82199; SSF82199; 1.
DR   PROSITE; PS51215; AWS; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS51578; SAM_MT43_SET2_2; 1.
DR   PROSITE; PS50280; SET; 1.
PE   2: Evidence at transcript level;
KW   Centromere; Chromatin regulator; Chromosome; Methyltransferase; Nucleus;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..363
FT                   /note="Histone-lysine N-methyltransferase ASHH3"
FT                   /id="PRO_0000233372"
FT   DOMAIN          63..114
FT                   /note="AWS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00562"
FT   DOMAIN          116..233
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   DOMAIN          239..255
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT   CONFLICT        55
FT                   /note="K -> E (in Ref. 4; AAL01111)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   363 AA;  41286 MW;  BA4CB48ACF54DFBF CRC64;
     MPASKKISDR NHLGQVFDKL LNQIGESEEF ELPEWLNKGK PTPYIFIRRN IYLTKKVKRR
     VEDDGIFCSC SSSSPGSSST VCGSNCHCGM LFSSCSSSCK CGSECNNKPF QQRHVKKMKL
     IQTEKCGSGI VAEEEIEAGE FIIEYVGEVI DDKTCEERLW KMKHRGETNF YLCEITRDMV
     IDATHKGNKS RYINHSCNPN TQMQKWIIDG ETRIGIFATR GIKKGEHLTY DYQFVQFGAD
     QDCHCGAVGC RRKLGVKPSK PKIASDEAFN LVAHELAQTL PKVHQNGLVN RHIDAGKSWN
     NLSQRDTCSR NCIGVVIRLS RPTSDRCFGL VRHFDEYSRK HSVMFEDGVT EFVDMSREDW
     EIV
 
 
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