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Database: UniProt
Entry: A0A0R0EQU9_SOYBN
LinkDB: A0A0R0EQU9_SOYBN
Original site: A0A0R0EQU9_SOYBN 
ID   A0A0R0EQU9_SOYBN        Unreviewed;       985 AA.
AC   A0A0R0EQU9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Histone-lysine N-methyltransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=GLYMA_19G212100 {ECO:0000313|EMBL:KRG96461.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EMBL:KRG96461.1};
RN   [1] {ECO:0000313|EMBL:KRG96461.1, ECO:0000313|EnsemblPlants:KRG96461}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRG96461};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRG96461.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRG96461}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRG96461};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRG96461.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRG96461.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; CM000852; KRG96461.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R0EQU9; -.
DR   EnsemblPlants; KRG96461; KRG96461; GLYMA_19G212100.
DR   Gramene; KRG96461; KRG96461; GLYMA_19G212100.
DR   Proteomes; UP000008827; Chromosome 19.
DR   ExpressionAtlas; A0A0R0EQU9; baseline.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR   GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR   CDD; cd15495; PHD_ATX3_4_5_like; 1.
DR   CDD; cd15517; PHD_TCF19_like; 1.
DR   CDD; cd20143; PWWP_AtATX3-like; 1.
DR   CDD; cd10518; SET_SETD1-like; 1.
DR   Gene3D; 2.30.30.140; -; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR   InterPro; IPR042011; ATX3/4/5_PHD.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR025780; Hist-Lys_N-MeTrfase_ATX.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR000313; PWWP_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR13793:SF165; HISTONE-LYSINE N-METHYLTRANSFERASE ATX3; 1.
DR   PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF13831; PHD_2; 1.
DR   Pfam; PF00855; PWWP; 1.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF13832; zf-HC5HC2H_2; 1.
DR   SMART; SM00249; PHD; 3.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00293; PWWP; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR   PROSITE; PS51805; EPHD; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50812; PWWP; 1.
DR   PROSITE; PS51566; SAM_MT43_TRX_MLL; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
PE   4: Predicted;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          199..268
FT                   /note="PWWP"
FT                   /evidence="ECO:0000259|PROSITE:PS50812"
FT   DOMAIN          372..428
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          556..607
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          610..725
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   DOMAIN          844..961
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          969..985
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   REGION          22..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..82
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   985 AA;  110371 MW;  CBB5BAFD86C5A48B CRC64;
     MIIKRSLKTG LQKRKQYKPE NCDNLAIQKE PKPENCDNSA VQKKQRVNEV SSAEGGASGS
     CEVQSNSNSV DSNGTIQGLV PQSEEVQPPR PSRGRAKKLP RRFSDSVFYE RFGLVDENKN
     TLQYIADKRN QRDSPCSPNS IESGDFEFSV KTVKKTVNGG RKLLVKEKSN DAAGHSSNSE
     GVDGNGKKKD IFKLDDFVLG DIVWAKCGKK HPAWPAVVID PLLQAPKSVL SCCVPGALCV
     MFFGYSKIGK QRDYAWVKQG MIFPFLEFMD RCVSAAVVST QLYRGKASDF HAAMDEAYLV
     ENGIFEVQLG AEQNMDGVDS CVNQECADQD QDTISCAGCG LMSPCKTMKK IKDSSCATQH
     FCKPCAKLIK SRQYCGICKK IWHHSDGGNW VCCDGCNVWV HAECDKISSK LFKDLENADY
     YCPDCKGKFN YESSTSQTYK SKNISMETGK KPAIPENLVV LCNGLKGIYV PKDHMIICKC
     CLCGSRTHTL TEWERHAGSK ARKWRYSVKV ESTMQPLKEW IDEHNSGAGT SLQLDQQQIL
     SFLQEKYEPV YANWITERCA ICRWVEDWED NKIIICNRCQ IAVHQECYGA KNVQDFTSWV
     CRVCENPDVE RECCLCPVKG GALKPTDVEM LWVHVTCAWF RPEVIFQNDK AMEPASGILK
     IPPNSFSKTC VICKQSHGSC TSCCKCATYF HVMCASRKGY SMELHSTEKN GTLITNKLIY
     CAMHRVPNPE SGLVVHTPNE VFSSTTSLQN HPGSIRRSRL VSSEIVVLPE SANSEINEIE
     PLSAARCRVF IRPSRKDGVP IIHLLGGPNL HSLSAITQLN SNKDAQVFSS LKERLHHLQK
     TENQKVCLGK SGIHGWGLFA RRDLEEGEMV VEYRGEQLRR SITDLREAQY RSEGKDCYFF
     KINEEVVIDA TDKGNIARLI NHSCMPNCFA RIVPSGDQKN RIVLIAKTNV SAGEELTYNY
     SFDDERDEEK VPCRCKAPNC SGFMN
//
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