ID A0A096PYN4_MAIZE Unreviewed; 982 AA.
AC A0A096PYN4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Histone-lysine N-methyltransferase ATX2 {ECO:0000313|EMBL:ONM53893.1};
GN ORFNames=ZEAMMB73_Zm00001d019907 {ECO:0000313|EMBL:ONM53893.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM53893.1};
RN [1] {ECO:0000313|EMBL:ONM53893.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Seedling {ECO:0000313|EMBL:ONM53893.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CM007650; ONM53877.1; -; Genomic_DNA.
DR EMBL; CM007650; ONM53893.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A096PYN4; -.
DR ExpressionAtlas; A0A096PYN4; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042054; F:histone methyltransferase activity; IEA:EnsemblPlants.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0048578; P:positive regulation of long-day photoperiodism, flowering; IEA:EnsemblPlants.
DR CDD; cd15662; ePHD_ATX1_2_like; 1.
DR CDD; cd15494; PHD_ATX1_2_like; 1.
DR CDD; cd20142; PWWP_AtATX1-like; 1.
DR CDD; cd10518; SET_SETD1-like; 1.
DR CDD; cd20404; Tudor_Agenet_AtEML-like; 1.
DR Gene3D; 2.30.30.140; -; 2.
DR Gene3D; 3.30.160.360; -; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR041956; ATX1/2_ePHD.
DR InterPro; IPR042010; ATX1/2_PHD.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003889; FYrich_C.
DR InterPro; IPR003888; FYrich_N.
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:SF140; HISTONE-LYSINE N-METHYLTRANSFERASE ATX2; 1.
DR PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR Pfam; PF05965; FYRC; 1.
DR Pfam; PF05964; FYRN; 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; SM00542; FYRC; 1.
DR SMART; SM00541; FYRN; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00293; PWWP; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51543; FYRC; 1.
DR PROSITE; PS51542; FYRN; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:ONM53893.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Transferase {ECO:0000313|EMBL:ONM53893.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 267..330
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 564..615
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 620..744
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 861..979
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 1..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 982 AA; 111093 MW; DA64554D549C76FA CRC64;
MVIAVEGNGF VHDDEEDDGD RPIRYLPLGH IYSSSTPAPA PRPPAQKKPR FDDGRPPMKV
YYRRRRKKLR VDESLSPPSP TTAPLAPPER DEKAGPSRRK DSLKHELLSL GPASPALDGE
EPERRLGRTR RCGGAEKTVC FSEPERRRQP ARPKGSVGRR WVELDIQTAD PNAFVGLVCK
VFWPLDDDWY KGSIAWYNEA TKKHSVKYDD GEAEDLSLAD ERIKFFISSE EMKSLNLKLG
ISNQDKKGHD ELLALAVSFH DYQGLDPGDL VWAKITGHAM WPAVVVDESN VPATRALKSI
RLDQSILVQF FGTHDFARIK LKQAVPFLNG LVSSLHLKCK QASFSRSLEE AKEFLHTQQL
PEIMLQLRKS VQHDVSDVNS YEGKVDSCSN LSEALALQNG EDAEMTQIEL GNLRVSNLGR
IVSDSDHFHN KKDIWPEGYT AFRKYMSIED PHAVTLYKME VLRNSDTKAR PLFRVISEDG
VQIDGSTPNA CWKEIYRRIK EKQCTELERN VCQSSGSYMF GFSNPQIRQL IQELPNARSC
LKYFENGGDT ILGYRAVQVN WKDLDYCNVC DMDEEYEDNL FLQCDKCRMM VHARCYGELK
QLDGGLWLCN LCRPGAPRVS PKCCLCPVTG GAMKPTTDGR WAHLACAIWI PETCLKDVKR
MEPIDGLSRI NKDRWKLVCS ICGVSYGVCI QCSHPTCRVA YHPLCARAAD LCIELENDDK
IHHMYLDEDE DPCIRLLSYC KKHRQPSAAE RPSLESDPPE PIQVVQTDMA SSSGCARTEP
YNLHRRRGQK QPQVVATASL KRLYVENRPH IVSGYCQNRV GNTCGESIQP FGLSDAVQQE
AIGNVSSMVE KYTIVKATFR KRLTFGKSKI HGYGVFAKVA HKAGDMMVEY IGEIVRPPIS
DTRERRIYNS LVGAGTYMFR IDDERVIDAT RVGSIARLIN HSCEPNCYSR AITILGDEHI
IIFAKRDIDP WEELTYDYRS EG
//
