ID A0A1V9YAS9_9STRA Unreviewed; 1051 AA.
AC A0A1V9YAS9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Cyclin-F {ECO:0000256|ARBA:ARBA00019493};
GN ORFNames=ACHHYP_15524 {ECO:0000313|EMBL:OQR82806.1};
OS Achlya hypogyna.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Achlya.
OX NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQR82806.1, ECO:0000313|Proteomes:UP000243579};
RN [1] {ECO:0000313|EMBL:OQR82806.1, ECO:0000313|Proteomes:UP000243579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQR82806.1,
RC ECO:0000313|Proteomes:UP000243579};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
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}.
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:OQR82806.1}.
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DR EMBL; JNBR01002418; OQR82806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9YAS9; -.
DR STRING; 1202772.A0A1V9YAS9; -.
DR OrthoDB; 48263at2759; -.
DR Proteomes; UP000243579; Unassembled WGS sequence.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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:OQR82806.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000243579};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 726..744
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 765..785
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 805..824
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 864..883
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 895..917
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 929..949
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 969..989
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 133..426
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 1051 AA; 118390 MW; 42173B3D12880D2F CRC64;
MDVARLLSGE KDGEDEEMLL SIDPSERVEH RSTKLVRREI VIASPVSNED MEDVDEAKPA
PSTLPSRPEA LRLGFDLQPV DMILHVFSFL IDTEDLHNMQ LVSKRWRELT SHTSLYRHVP
DTTPEGTINW LNFRNLGIKN KGTEGTCYRC YQRSSGKVLA MKRARVFPKG EGVPYYMLRE
LAVLRGISHP HIASLEMISL AKDELHVFFP YVDKTLHEII NPTSDPNGGR VLPEHQIRRL
LHQLLDAIAY CHRRGVLHRN LKPKHLLIDT AVPDNYDEAT LRISDFALVR ATGIPRRQYT
MEVVTLWYRP PEILMGEKQY SPAVDVWSVG CIFAEMAQGK PLFTGISEID QLFQIFSKLS
TPTAATWPAF TSLPNYRFEF PNWKPRPLER LFPHISPLGL DLLGKLLTYN PDTRISAENA
LRHPYFDEHA SLPRLLPSIP MTSMAFGLRR AVEGEYLDLF HAHLRDAELQ LCKEVKYLSR
QKTLRPLHRS MLVDWLIEGA CGALQLAVTR DVVVDVFEMC LRTAFLAVNY TDRFLDVVMV
KKTKFQLLGA TCLHVASKCE DVSYIGVEDL SMCADNVYNS MEVLKMEEQL LNTLNFTLAV
PTALDFLNIY QKCMPELEQK TSMLAHYLSE LALQEYSFLK YLPSCVATCC LSLALYCCHG
YAMTPELKAA CRYSWEDLKE CMTTLQEVYS SSQFNVLTVV KKRYSEEDRC QRCTSYSYLE
MSSEQLAWKA APVAGSIATL LLASHTALHL LDRSRYFKST AVKRVFFGIA TLALGVAGVL
SFHVSQASAS SALACDGFLL LQPEWLLAAF GLGVAGSMVS LYVATQDPFF AGLGETVTLS
SLLNKRKTEL QIQFLAKFSQ LQPITGGAFV WSATLMGVRL LLVQTQMGLV TESPWWVLVW
ASGSTFFLGW LSFWGVFRLI TFRPHVYRFR WYATLLFSMT IALPHYLMVA LSTHQVGEVS
NIAGVSAPAF ASNLHIVSLL LLVSILLGLT HFESHALFDD SNPHAILPAG LPLPSSKAIV
TLQSSTHSFR FGSMRSLVAG RQRSSRIVSF K
//
