ID W2L171_PHYPR Unreviewed; 890 AA.
AC W2L171;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Cyclin-F {ECO:0000256|ARBA:ARBA00019493};
GN ORFNames=L917_10269 {ECO:0000313|EMBL:ETL91156.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL91156.1};
RN [1] {ECO:0000313|EMBL:ETL91156.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHvinca01 {ECO:0000313|EMBL:ETL91156.1};
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 CHvinca01.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000256|ARBA:ARBA00004114}.
CC Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily.
CC {ECO:0000256|ARBA:ARBA00006485}.
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DR EMBL; KI680154; ETL91156.1; -; Genomic_DNA.
DR EMBL; KI680154; ETL91157.1; -; Genomic_DNA.
DR EnsemblProtists; ETL91156; ETL91156; L917_10269.
DR EnsemblProtists; ETL91157; ETL91157; L917_10269.
DR VEuPathDB; FungiDB:PPTG_12384; -.
DR Proteomes; UP000054423; Unassembled WGS sequence.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20537; CYCLIN_CCNO-like_rpt2; 1.
DR CDD; cd09917; F-box_SF; 1.
DR Gene3D; 1.20.1280.50; -; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR013763; Cyclin-like_dom.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1.
DR PANTHER; PTHR24056:SF254; CYCLIN-DEPENDENT KINASE 2; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SMART; SM01332; Cyclin_C; 1.
DR SUPFAM; SSF47954; Cyclin-like; 2.
DR SUPFAM; SSF81383; F-box domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW Cyclin {ECO:0000256|ARBA:ARBA00023127};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ETL91156.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 247..294
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT DOMAIN 308..601
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 890 AA; 100421 MW; 64FCCFFEF6FA8ADA CRC64;
MDTQSSASRT SSSSDTTPSK KRRATTGASN QGLGVAVPAR TEPQRKRSGL PLLLCTPGAE
NPILAALGGT PRSQVAVANG FPEPEPLDLS QCSAVTSMDS VKEEKVEETR MKEEKRDILV
KEEKVNVMDL KQEHKPHTVK TESAGVETKY RVDAAPFVGK RKRDDESDED KTTDFVAYAR
EHIHSQEAGE EGFSIDPSER AVEHRASKVV RREILIASPA ANDDEDWEGN APLEVKMEEV
EAVLTPSEHF DLQPIDIILH VFSFLVTAKD LENMAQVSKK WKELTSRRSL YRSLPSVTPE
GSVNWINFKN LGIKNKGTEG TCIKCCQRST GKILAMKKAR VFPKGEGVPY YMLRELAVLK
GIKHDHIASL ELISLAKDEL HVFFPYVDKT LHEIINPSGD PNGGRVLPEA VIRKLLHQLL
DAIAYCHRRG VLHRNLKPKH LLIKTSDTEN LSDATLQISD FALVRATGIP RRTYTMEVVT
LWYRPPEILM GVRGYSSAVD IWSVGCIFAE MAQGKPLFTG ISEIDQLFQI FSKLSTPTSE
TWPGFSSLPN YHFEFPHWKR RPLNRLFPGI SDLGIDLLTK LLVYNPDQRI TAEDALRHPY
FSSEAPSFLP LTPKIPMDQM CYTMSRARIG PTPEHVELFH AYLRQTELDS WKEIKYLSRQ
KTLRPAHRSM LVDWLIEVVD VFEMCLRTAF LAVNYTDRYL DIVMVKKTQF QLLGATCLHV
ASKCEDVSYI GVEDLAMCAD NVYTSVEVLE MEEKLLNTLN FTLSVPTALD FLNIYERMIP
PIQKKTSMLA HYLLELALQE YQFLKYLPSV VAACCLSMAM YTMDGFPMTK ELVDACQYNW
SDLKECMGEL QTLYSNSPSN NLAVIKKRYS KAERCQVANV LPPTSFSMAF
//
