ID A0A0N4URA6_DRAME Unreviewed; 2249 AA.
AC A0A0N4URA6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Histone-lysine N-methyltransferase {ECO:0000313|WBParaSite:DME_0001058101-mRNA-1};
GN ORFNames=DME_LOCUS4009 {ECO:0000313|EMBL:VDN54036.1};
OS Dracunculus medinensis (Guinea worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Dracunculoidea; Dracunculidae; Dracunculus.
OX NCBI_TaxID=318479 {ECO:0000313|Proteomes:UP000038040, ECO:0000313|WBParaSite:DME_0001058101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:DME_0001058101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN54036.1, ECO:0000313|Proteomes:UP000274756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; UYYG01000245; VDN54036.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4URA6; -.
DR STRING; 318479.A0A0N4URA6; -.
DR WBParaSite; DME_0001058101-mRNA-1; DME_0001058101-mRNA-1; DME_0001058101.
DR Proteomes; UP000038040; Unplaced.
DR Proteomes; UP000274756; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR CDD; cd15489; PHD_SF; 1.
DR CDD; cd19171; SET_KMT2C_2D; 1.
DR Gene3D; 3.30.160.360; -; 1.
DR Gene3D; 1.10.30.10; High mobility group box domain; 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; IPR034732; EPHD.
DR InterPro; IPR003889; FYrich_C.
DR InterPro; IPR003888; FYrich_N.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
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; PTHR45888; HL01030P-RELATED; 1.
DR PANTHER; PTHR45888:SF6; HL01030P-RELATED; 1.
DR Pfam; PF05965; FYRC; 1.
DR Pfam; PF05964; FYRN; 1.
DR Pfam; PF00628; PHD; 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; 4.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF47095; HMG-box; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51543; FYRC; 1.
DR PROSITE; PS51542; FYRN; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000274756};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 61..113
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 353..408
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1706..1814
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 2106..2225
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 2233..2249
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 227..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1097..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1136..1182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1417..1450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 991..1025
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 612..627
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2249 AA; 253442 MW; 0A447632BD77A313 CRC64;
MDSAQLSLSF DKASLSDNGN ARTRKSESSE VCADNPQCIV KEVQKSLQSL SKTDFQTNSS
TSFCTSCSHS LSPGAAIRTC SICHRWIHLE CDHDSNSVGS VEVEYICPPC RNSPLVADAM
MTSASGGSLA PSPASISTHD DSSRNAIFDN VYSHASSNRN SPFTELNLDS SFNDIFSITH
QSNQEEGPSS VVVSNNAENC SSEASPVYYS DANAAAEIDE FHISNRREKS EGVSHSHRGG
RNGVSKPLST LLRSNSMRTR SFAGFHDVSD YSISNRGKRG ARGAMKNGRG RRSRGGKTSS
MLALVSAATA AIASRETDQE SSEPEELKNR LEENEYIRTV VITDAEDTFF LQMPVCLICG
SIGKDVEGTM VSCATCAQSY HTFCVGLHNT LNQTIVKRGW RCLNCMICET CGEARDESHL
ILCDECDISY HTCSACRRCE KQIEKCTDLH RMESLCETCF SLRKCLRWFH GKCEEVFGEE
ILEAASEHGF RCSLCRPHGK LQINDSLNIL VCDNVAMNRS AWEVLQMRYG GLLTKSSLTF
HNETIYGAQY YGYGARTHSY DDIMDDEEVE ITPPMPSGRG RGMRGGPGRR VLKLGVGGFF
VRIPRHRLLA AEEDTNGDDD SALGKPKIKR PRKPRRSQLE DNYPPVIQES FFGMRPIEGR
VLIEMVVEEP TLQEIQKTVF NVEKHHLPCE LSETSVDALR DGESVLDIME NEIMNNIESI
DFDNLDIGIF GVYDEEDDDV IMDVAESEEN GGTEEGMSSM QTSNYEQQHI VPFGYSSSMA
QNRQFDARRS DEIVQNQNRA SISQQNLSYP LQSNIQSQSN SRCSSQMAES FIERVNQATE
RWEEDEPLGE RATKAAVLYA NVNHPEWKKD YPEWNERVKQ IHRMWRSLDA NSRQEYVNRA
RENRANRAKI PKVKRVHAGC VRAIASSSQC SSPLQIGMSG TTYYSQGIER TGGAVLTDTR
NQASSLAHLS KDILDNYSLL QQRSNELFKY QTAIENDLAR MRKQKKNLTA KRRQLNKNNQ
KFDANGLRID VELNDTDKSC LAMLINAIPI RQKDLENCKR DIKEHSSSVR DFEVKNNIPS
DFANQMASQA ASLNMNNIRS PNVTSSGLRP PPPYSFVSDQ RQNIAHNYQV SIGTHRFSST
RPDIDGSQFG SGSSTPSNSR RESVGSADWT KQRLGRKRKT EDDLFEEYER PAKLGDVYAS
SITSQIELDV FDVVDHLLTQ VAIMVHGAEA AKKSGILKRL LEPLSGKLCS PQKTFTSDDL
FKENCLLELH HFENIKPKKK RSQQKKLPVG SSNEYELLLE RISTQLRLCP PLPRRALEPV
PRIDRSSLSM FGVTDLPDRT EKCSIAGDKI GSLRLLFMHD YYTRMFECPI EEKSLYPSMS
FFCNDVKMTS LAQITNTNFL WLEDSELDRS SMKMKSLSVD RRSRSPPLRT ISRIPEAISP
QPPHRSSFLK PPNLIDQVAV SIIMEGEDGF DPEYSYRQLM KLLDINPCPD FKMDTPPDTP
INCKGEIQEQ SKIDIHNEIS HCRNCNSIIK HSVVPQSKLI DEEKEGEASF CSMSCYYNFI
VNAGIALSTD DLQKAERFVD EETLSKLRQI SAENFAKYLH LGKMKSENIS TPVGGDGSPL
DSRLAISDPD SQSYKLQTIY ARELSALIES KVQKVTDQKW KGRLWMQYDA ELLESFQHLA
SQVRQKHMAI QLQSSEGMRA ARKDDARTCA FCGIRGDGDI DVCGRLINAD ANTWVHVNCA
IWSQEVYENS SGALSNVDEA LRRSTDVLCL VCKRSGASLR CYKLNCESHF HLACAKSANG
HFMKDKTFIC SLHDDIRPEL SIDRLDALRR IYIDRNENKV LAKLFHSNGN QLILRIGTLI
FHQLGQLLPD QLKSFHNSDY IFPIGYRITR IYWSPLNRME KIRYNCSIAD NRSGPQFIIT
YEGGKEIREF SCTNAWNRIV TMVQNLRQKQ NNDVLKLFPV QIIGETLYGL NETAISKMIE
SLPGIDQLAT YSFKHGGSPL MDLPLAVNPC GCTRSERRFR TLIKHKRRNQ PAVAASIHSN
IGLDIVSRDT RNRGGPAASL EQICSRSLSL CAFSNDLWNP YARWETGPLS SSYYSQYQKM
KKEWKNTVYL ARSRIQGLGL FASRDIEMNA MIIEYKGELI RTEVGEMREK RYEAQNRGVY
MFRIDDERLI DATMAGGPAR YINHSCDPNC STRLVDSGPT GDDKKIIIIA NRPISAGEEL
TYDYQFDIED TNDKIACLCG APNCQKWMN
//
