ID V9FCA4_PHYPR Unreviewed; 1497 AA.
AC V9FCA4;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=CMGC/CDK protein kinase {ECO:0000313|EMBL:ETI48756.1};
GN ORFNames=F443_07264 {ECO:0000313|EMBL:ETI48756.1};
OS Phytophthora parasitica P1569.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI48756.1, ECO:0000313|Proteomes:UP000018721};
RN [1] {ECO:0000313|EMBL:ETI48756.1, ECO:0000313|Proteomes:UP000018721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1569 {ECO:0000313|EMBL:ETI48756.1,
RC ECO:0000313|Proteomes:UP000018721};
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., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P1569.";
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:ETI48756.1}.
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DR EMBL; ANIZ01001210; ETI48756.1; -; Genomic_DNA.
DR EnsemblProtists; ETI48756; ETI48756; F443_07264.
DR eggNOG; KOG0600; Eukaryota.
DR eggNOG; KOG4442; Eukaryota.
DR HOGENOM; CLU_002722_0_0_1; -.
DR OrthoDB; 49323at2759; -.
DR Proteomes; UP000018721; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0042054; F:histone methyltransferase activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00590; RRM_SF; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR006560; AWS_dom.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR PANTHER; PTHR22884:SF413; HISTONE-LYSINE N-METHYLTRANSFERASE CG1716-RELATED; 1.
DR PANTHER; PTHR22884; SET DOMAIN PROTEINS; 1.
DR Pfam; PF17907; AWS; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF47954; Cyclin-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS51215; AWS; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ETI48756.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018721};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 61..122
FT /note="AWS"
FT /evidence="ECO:0000259|PROSITE:PS51215"
FT DOMAIN 125..241
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 248..264
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT DOMAIN 900..1339
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1369..1497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1369..1401
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1402..1419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1497 AA; 169233 MW; 4EDCA7653033A3E8 CRC64;
MASNSPSPSS SPDALPETTS FDQLQALRNV QLIERNEYPL KHLARDKVRR RSRRDEDEDE
EEGALCFCTF PDAAEREEAE QKGEPVRRCD DVSCLNFATY VECTASCPTG QYCRNQRLQH
PERYPHLEPF KTEHKGYGVR TRQHIPQLSI VGEYVGEIID QKELARRLKS VPRHELNFYY
LLLAPGVYID ARNKGSFTRF VNHSCEPNCK TEKWTVKGET RIAVSALRDI EVGEELTFDY
KWKALGSRQI KCFCGAPSCK GVIGTQNETL QNAEAQTGYF RDPEKQEIGN ALVGRRVRVF
LSPEDKTEYD VQLIKGYDEQ KDRYEVEDLL EPGGYETDEN DTEEEQDATE KQYVQLKENG
WQLYCPPGDK EGGQVFAIPK RRIPVTNADS RDPSPKKETM TPSPVRTPSP VATARLENNF
NTQKRNEYGE LLDREGKVVS NKLLVKFLPK EYDERGLRSL FISRKHPHAL VSADVFHFLD
GTGWALVELE NYELASSFRR TLDRRNLLDK MLRVYQAGTK ELDNFRHQKT KVQMMRQAGI
TSSSLASEEK ENVQEKKIDP YCFGRKLNWL VTEDELKNLS VQQVLSASLE ETLRVKYVKS
IFHIAKGLRL DREDATSAII ALNRYFTFHT MPMEVDIYAA TMLHLFLKAH ARKVPWTAFV
KEVYKAKHGL SAAERLTAAS PELGVLKRHL VKAESELLEG LHYDVTGEDP YALLDLLTTR
KSSKKLVALS QNGYGHHMTP FLSSLPPPEV QKEAKHLVAE ALPLPIWRHT PVECVMLSVV
YVSAAVTEAL SSRPAPFICK IPDFLPQLDL QTNASEARML LDCSLSICTQ LKDRWVRLEK
QSKSAQQKQP KDANATDFDM TQFDVSKDKK DVDISERIAR LLKQWINLPA PSLSSALGAV
STVSATGMGN FPTVSPSHNT GKRCITFKEM GSSVPIPSST SQTSDNLGIV SALSISPKKS
AAGTNDSNVG DVRIHTDEIV KVESIRKRAF LGVISSDVGF DLAGKPVYLQ SWPYLEQELF
FMEEKGINEA CLRELSAATT LSSLLPDRFM KLHGIIFPAD RKDRQASESK TGKNSDVDEL
DLLAATIDDD GNPLPEGIDR LARQKHYLAF EQPLHMFSGI FEAHVPLSST LRKKAIFDML
QSLAAVHDQG YVHRFIAPSH LLVFKNGIKL GGFHSMRKIA NIKPKDGEGS TIAGYEMSDS
ERKEHCYGAW LYVTAPEVLL GETKYTWRSD VWSAGCVVLA ILLEKIPFLQ GQDVKVQLDL
IYRLCGTPSM SWEGAHKLPL YNAFRPKHEY KMRLRKTLLE QRSKFPDFPE DAVEVLEAML
QLDPARRSTV KKLLDMRYFD SVRSGERTFD FSDLPSTFPV QKKKLVQHLL KAKAKKHRSA
GSRSTSSRSS HHHRHSEHRH KRSLSTHDGL VEKSSHHDRH KSRSDKRKSR SLSTSRRDVK
HADTEDSEMQ DVSEYVPLPA SFTASAGSSP SRSTDDSLPP REKRMKLGWG MGLNSVS
//
