ID W2ZIP1_PHYPR Unreviewed; 993 AA.
AC W2ZIP1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Histone-lysine N-methyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=F442_06801 {ECO:0000313|EMBL:ETP47168.1};
OS Phytophthora parasitica P10297.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317064 {ECO:0000313|EMBL:ETP47168.1, ECO:0000313|Proteomes:UP000018948};
RN [1] {ECO:0000313|EMBL:ETP47168.1, ECO:0000313|Proteomes:UP000018948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P10297 {ECO:0000313|EMBL:ETP47168.1,
RC ECO:0000313|Proteomes:UP000018948};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P10297.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETP47168.1}.
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DR EMBL; ANIY01001392; ETP47168.1; -; Genomic_DNA.
DR AlphaFoldDB; W2ZIP1; -.
DR EnsemblProtists; ETP47168; ETP47168; F442_06801.
DR Proteomes; UP000018948; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042054; F:histone methyltransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd20104; MBT_PHF20L1-like; 1.
DR CDD; cd15565; PHD2_NSD; 1.
DR CDD; cd15566; PHD3_NSD; 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); 2.
DR InterPro; IPR006560; AWS_dom.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR003616; Post-SET_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; PTHR22884:SF413; HISTONE-LYSINE N-METHYLTRANSFERASE CG1716-RELATED; 1.
DR PANTHER; PTHR22884; SET DOMAIN PROTEINS; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00249; PHD; 3.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS51215; AWS; 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 Reference proteome {ECO:0000313|Proteomes:UP000018948};
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 343..395
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 596..655
FT /note="AWS"
FT /evidence="ECO:0000259|PROSITE:PS51215"
FT DOMAIN 653..776
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 783..799
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..987
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 993 AA; 110235 MW; A8CA992FA11C7B31 CRC64;
MDRAIGAPAG GTDHSPQQAQ TTAGQPAIAT ASKMGGDTAV SSATPVISST ANGRIETTGA
DPASSKPAVE QSDKLEGTVS TGVEGKAPAA AVAALAPFDT LIVNENVEAA ETASANHKRA
HEEDTEDTAS QESHPRKRTA IANGENTVLS SGQTTDETVG DSSDDVEMIE AKDEEDVLGN
DTTHANGEAN EEFYRNLEVN QQVDVYDVGT KDWLAAKIVR VDDEGCSVHY MGWNSKRDEK
IDITSSYRIQ PRATKATKAW TKHQAKIDKR NVVKKVEATP STDDNLGRLG AEQHELVPAF
VQTGLTRSGR AITKRVENGA LKPKAPPKKK KDAAAVESGF PEEDLCGVCG EIEDDDLTDM
ILCDGGCLKS YHFSCLGIDS APDGEEWLCE QCRTNEQLCF ACGRNGTINE KGGVFRCSAP
SCGKFFHQAC VDANKMSRRA GGKAKPGSAT VEELLESDAS FRCPRHVCFV CEGKKKSSDL
MCCLKCPESY HPQCVPPSAR YNSVGLLCWR HSEEELPKIP SFYLSDRNID TVTVDSSLHL
PWMFLPKRDP DTSNPNDCHH FRLLKSIIED VRLQPPTYRK LGRSIYTFKQ PKVSLEDAPT
CVCKEKCGDD CINRLSFTEC FGPAPTPGMK FNKHNRESNC MLGENCGNRA LHQKVYPRFQ
KFHTVEKGWA LRLLEPVKAG QLVIEYVGEV INEEEKERRL LDHAKNSPED KNMYIMELGK
GEYIDARFKG SVSRFINHSC DPNCHLLKWR VKGVNRIAIT ALKDIEPGTE LSYDYQFHTK
QAMEWKCHCK SKNCRGTMAP EKINQALESP AKKLTKKEQI KQRKRALMQE KIQQDKEIKS
TARRLSLTAQ ISMGDRTTMD KMVVRTGPAA RELQWAKYYH LFNIRDAKHG FNFKLRKEMR
DLRIARQEQV KQEHVSVSGS TTAASSRSVS PVRLLGDEIE PNQQKETKEQ SLSKGDPAKD
RQEFAQELVV SEPKKRESTK EDSVGTEPEE IPA
//
