ID A0A0E0B6G7_9ORYZ Unreviewed; 1889 AA.
AC A0A0E0B6G7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Histone-lysine N-methyltransferase {ECO:0000313|EnsemblPlants:OGLUM09G19990.1};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM09G19990.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM09G19990.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM09G19990.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 40148.A0A0E0B6G7; -.
DR EnsemblPlants; OGLUM09G19990.1; OGLUM09G19990.1; OGLUM09G19990.
DR Gramene; OGLUM09G19990.1; OGLUM09G19990.1; OGLUM09G19990.
DR eggNOG; KOG0954; Eukaryota.
DR eggNOG; KOG4443; Eukaryota.
DR HOGENOM; CLU_238882_0_0_1; -.
DR Proteomes; UP000026961; Unassembled WGS sequence.
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; IPR034732; EPHD.
DR InterPro; IPR003616; Post-SET_dom.
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; PS51805; EPHD; 1.
DR PROSITE; PS50868; POST_SET; 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 Reference proteome {ECO:0000313|Proteomes:UP000026961};
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 1401..1451
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1533..1659
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 1744..1865
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1873..1889
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1076..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1178..1205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1287..1335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1098
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1157
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1287..1301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1889 AA; 208791 MW; C7635DD8AB025F82 CRC64;
MDDAWPARWP PPPPPPAPAP ATATATATPL PSQIDSASLR HILRPFAAQG AAAPEQLAAS
HPSSQYGQPA RAAPSTSLLA QVAGNHPHAT HVSDRKALFG MLNAGNAANV IDLTRASPLR
GAEPLPKHPR HGLEASSSVE QPSCLGALFQ NTSANVQGSF PGECSVNNGI SQGAIQFQDS
SACAVQKLPS QSTPRHHPAL LGDQIRVSCL NVGGEFFVGE AGIFGVRCFC HRLRMSVAKF
CEHSGGPAEK AGEIVIMDNG MTIVQWLKYC MGVGASISDT KWDWPEWAYM RYSSEEYWTK
SLLTTNNNME KTGLFSGHGK STGHINNPVY SSDIHNEVGR FTSVEKLVNK PDETFYRKSV
GLHEAFSKNP AIQQSSKINL ANHMIHDMNM NSISRPSERT YSTANMGITY SRNHLAHDYA
NFLEKNLNNL SRSPVPSSTR VLSNDSRACM PDVPHKIIQD GSGRASNTEL KLGQSSYHQS
MATLFPSVQS TIIEFQKPQH HLQFTTSNAY PKQTTKANKT IENIEPSFGN RKRSLDVSNG
TSHSELNEIT DDAAKNSFIS LFLSHLERNS TSESIDDVLN SNEHYLLKAP DVAYSSDRLK
TASPQVETRA NDNQLKLAPA IIHTKRISDS RSLPVPVASK GYVHQDVLHA NSQEPSINGD
CLPHLLPSQP NAGISKICAE VSSPVNCRCC NHVDDKSHLA HSETGAPCFY DRTARRYISF
ECADDLCTHK SLRATNYQCG RAFCSTANEF LPSFGQNDQS PIGKSMHRCC CKAQEDSSKL
GFRAGNFCRS HFCNDGTPVP AHRSIVEGLD EVRTRSTFIP RSSLCSRELM LQSCCHACPI
DGYYRSSMGH TANSLTKNTL LDAPNNTECS PYRDGKCCCS LAPKCFAGYG FTKHCVARID
QTDHTVQKSK DDGMQAAARC CTLGESEKLI CQCSSEIIAR KSDSKASFRN EVSTEVLNRP
CVPTLQQLKN VTEASAVGGH WPYETVKEKA SACRDSGIFK ELKSGFSSGF SSDVVTKFSA
SPELNKYGLE HKNLVFDEGS RIEKCSSSSY LPISTGCEEA QNSFSRFHLE PSLVKHKNNQ
ISEGSTRKEH ENEGQCSEMS KKTRTLRCCA NKSESDDCTR KIDLSSREGD SQPQHKAGPF
SRRVSKTKRK HPPTHLNKHV KRLHSNCKVL NVDNERSDDE GIYVGESNSS DRKKQEDNMT
TLDRTKCQQQ GSRLLVRKLP KYVSLNCIVN ETNSEDACSG SASIDSSLIA TGITNDNRKS
PKIVPLNLIL KKAKRCHAIK PLSKTENIHF SEEKSSDGSA DKSSSGDRSF SPQDELWSPK
KNRYSSNVSR PHVKTDCQSP CCVLEEDEPL SLADMGTSQL SASRSRGWRG VKNLQMNQQA
VLAAINTLRF KPVYIQRPSL DASCCVCGIS NLEPSNQLIE CSKCFIKVHQ ACYGVLKVPR
GQWFCKPCKI NTQDTVCVLC GYGGGAMTRA LKAQNILKSL LRGIATAKRS DKYVYSSGNV
NSECTSKLHG EYVRHDSFNG HRSRSFNAIS SFGIKEASIG SARGDIISKS WTSNRNSSLL
GPRTRQWVHV VCGLWTPGTK CPNTITMSAF DISGASLAKR NTECSMCNRT GGSFMGCRDV
NCSVLFHPWC AHQRGLLQSE PEGEHNENVG FYGRCLDHAM LDPNHVNPKK ECLRSNDWTC
ARTEGFRGRK GDSFGANRSR KPEEKFGECS VSQEQINAWI RINGSKSCMR GQEYVHYKQL
KGWKHLVVYK SSIHGLGLYT SEFIPRGSMV VQYVGEIVGQ CVADKREIEY QSGKRQQYKS
ACYFFKIGKE HIIDATRKGG IARFINHSCQ PNCVAKIISV RNEKKVVFFA ERHINPGEEI
TYDYHFNRED EGQRIPCFCR SRGCRRYLN
//
