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Database: UniProt
Entry: A0A1D6EUU6_MAIZE
LinkDB: A0A1D6EUU6_MAIZE
Original site: A0A1D6EUU6_MAIZE 
ID   A0A1D6EUU6_MAIZE        Unreviewed;      1893 AA.
AC   A0A1D6EUU6;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Histone-lysine N-methyltransferase ATX4 {ECO:0000313|EMBL:ONM23421.1};
GN   ORFNames=ZEAMMB73_Zm00001d006323 {ECO:0000313|EMBL:ONM23421.1};
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:ONM23421.1};
RN   [1] {ECO:0000313|EMBL:ONM23421.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Seedling {ECO:0000313|EMBL:ONM23421.1};
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; CM007648; ONM23421.1; -; Genomic_DNA.
DR   ExpressionAtlas; A0A1D6EUU6; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd15571; ePHD; 1.
DR   CDD; cd15492; PHD_BRPF_JADE_like; 1.
DR   CDD; cd10518; SET_SETD1-like; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR032308; TDBD.
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; PTHR45838:SF4; HISTONE-LYSINE N-METHYLTRANSFERASE TRITHORAX; 1.
DR   PANTHER; PTHR45838; HISTONE-LYSINE-N-METHYLTRANSFERASE 2 KMT2 FAMILY MEMBER; 1.
DR   Pfam; PF13831; PHD_2; 1.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF16135; TDBD; 1.
DR   Pfam; PF13832; zf-HC5HC2H_2; 1.
DR   SMART; SM00249; PHD; 2.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF82199; SET domain; 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:0000313|EMBL:ONM23421.1};
KW   Transferase {ECO:0000313|EMBL:ONM23421.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
SQ   SEQUENCE   1893 AA;  208678 MW;  53468D5E38B9FFD1 CRC64;
     MDGASWPARW PPPVPPLPSQ MDGVTLRHLL RPFAAQEAAA AGRVAAAPEQ LFASHSTLQS
     GPPPRVGPSN ELLTQVPGNY CTFDLAPDLT RANASNAAGT IDFTRAGPSS SAATLPKYPR
     HGLPASSSNE QSSFGALFPN RSANGMGIFT CQSSANEGIA NVGVQFQDSS VHGLQKLPFK
     SMTHQHPTLP GDRIRVTCGE FFVGEAGLFG VICLCHRLRM SVAKFCEHAG GIPEKAGEIV
     CLENGMSIAQ WFKFCIGVGG SIANTRWDWP EWAHMKSSPE EHILKSLASR NSGTGKMGLL
     SRYGKITGHM NKPAYSNDLS VEGGGHTNVE KLVNRTDETY YRKSVDVHET FTKNSALLQN
     SAVVNLGPAK NHPVHAFDLN PLTTPSGSPH FEASMGRHYN GNHLAHSHGI HLEKNFDASF
     CNPMPRFTGV MNHDSRACRP NFSNKTFQDT LSNASNTELK LGQSSYHQSM TTLSPLGQST
     MIEFQKPQTH RPPINQNPSP KQATKISKSL SEHNEPSIST GNKKQPLEVV NGMKRSEGDE
     LTDDTSKNSF ISLFLSHLER NNTPEPIDDI LNSNEHYLPK ALDVACGSDH PESATRQIET
     RVPNDKHSKL ASAIVHTKRR SEGISLSVAS SGYNPQDASH ANSQEHLIHG DSLSHLLPSQ
     PNTGISKISA RVSCHANCMS CIHVGNKSHQ VAHGEIGVPC FYDKMARGHG TFERVDDCTH
     RSLRAFTKIS CDNGKSCCSS RELLPSFCQN DQPTLGKSIC GCCCKIQEDA SKLGFIPGHM
     CRTHFSSDVG PVLANKPTIE GLDEFCACSC STFTQRSSLC SREYVLQSSC DSCPINGLHC
     RSCMGHAADS LTKHSLFDPL NTKERGSCCN GRCCYSVVPK CLSSCDFTKH CDVIIDQIGH
     AAPKDNHQLQ MPTRCCTLGE NEKLICQCLS NKIAVRNLPQ TSHCKDVSEK VMNQPSIAIT
     ERLENVSEPS VADDSSSKAV AEKKDAYRDS AVSKGQPNFG FSSGSSSIIV TKFQKSPEFN
     NVSSTAKHSK HKNLCDEGSR IEKSSASSYV PTSTGCEEPL NSSAKSELGP SRVKRKCNQI
     SEGRRLEETD NEEHCSELLK KTRTLRCSVK GSESDDCTRA SSQSSQKGVY QPQNEVNSFS
     CRVLRTKRKH PIMHLNKHVK QLHRQTKFFE GDEQPDAKGN FLGGLDSYDR KRQVEDMSTL
     DKTRHHQEGS RAFVRKLPKY VSLNCIVNEP NTNSEGACSG SGGIDSSLIA TGITNDNRKS
     PKIVPLNLVL KKAKRCNAVK LRKTESTHLY EEKSSDCSVN SSDYSIEKYS VDDENCSPQA
     EYELQDSKRS RYSSNDLRSH VALHKRTSGV IGEDDSLGLT DVEINCLSIS SSSNGTKNRR
     TSVSLARIKK FGSKSVCYSG SDKDNAVLAH EVNARRYSGR LSSNSPCCVC GISDLEPCNR
     LIECSKCYIK VHQACYGVLK VPRGQWFCRP CKNNTMDTVC VLCGYGGGAM TRALKTKNIL
     KSLLQGLMNL ERSEYYVDSL GNASSECTSL QNPVDSAHGD NIMNAKNITS NSWTSGKYYS
     SLLGPQPMQW VHMVCGLWTP GTKCPNDTTM SAFDVSGASP AKRNTACSIC DRTGGSFVKC
     RAVNCLVFFH AWCAHQRGLL QSEPEGEHNE NIGFYGRCVS HAIVFSSHVN PKKEYFRNNN
     WTCARTEGFK GRKGEGFSDS SHKKYEEYSG EFGVSQEQIN AWLRINGSKP CGRGQKEYIH
     YKQLKGWKHL VVYKSGIHGL GLYTSVFIPR GSMVVEYVGE IVGQRVADRR EIEYQSGKRQ
     QYKSACYFFK IDREHIIDAT RKGGIARFVN HSCQPNCVAK IISVRNEKKV MFFAERHINP
     GEEITYDYHF NREDEGQRIL CFCRSRYCRR YLN
//
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