ID A0A1V9YNC8_9STRA Unreviewed; 2586 AA.
AC A0A1V9YNC8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Phosphatidylinositol kinase {ECO:0000313|EMBL:OQR87151.1};
GN ORFNames=ACHHYP_09470 {ECO:0000313|EMBL:OQR87151.1};
OS Achlya hypogyna.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Achlya.
OX NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQR87151.1, ECO:0000313|Proteomes:UP000243579};
RN [1] {ECO:0000313|EMBL:OQR87151.1, ECO:0000313|Proteomes:UP000243579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQR87151.1,
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 -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00879}.
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:OQR87151.1}.
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DR EMBL; JNBR01001463; OQR87151.1; -; Genomic_DNA.
DR STRING; 1202772.A0A1V9YNC8; -.
DR OrthoDB; 46300at2759; -.
DR Proteomes; UP000243579; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00821; PH; 2.
DR CDD; cd00891; PI3Kc; 2.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 2.
DR Gene3D; 1.25.40.70; Phosphatidylinositol 3-kinase, accessory domain (PIK); 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 4.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR002420; PI3K-type_C2_dom.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR000341; PI3K_Ras-bd_dom.
DR InterPro; IPR035448; PI3Kc.
DR InterPro; IPR015433; PI_Kinase.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048:SF14; LD28067P; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00169; PH; 4.
DR Pfam; PF00454; PI3_PI4_kinase; 2.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 2.
DR SMART; SM00233; PH; 4.
DR SMART; SM00145; PI3Ka; 2.
DR SMART; SM00146; PI3Kc; 2.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR SUPFAM; SSF50729; PH domain-like; 4.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS51547; C2_PI3K; 2.
DR PROSITE; PS50003; PH_DOMAIN; 4.
DR PROSITE; PS00915; PI3_4_KINASE_1; 2.
DR PROSITE; PS00916; PI3_4_KINASE_2; 2.
DR PROSITE; PS50290; PI3_4_KINASE_3; 2.
DR PROSITE; PS51546; PI3K_RBD; 1.
DR PROSITE; PS51545; PIK_HELICAL; 2.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OQR87151.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000243579};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 101..226
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 371..552
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 568..678
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 696..876
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 951..1228
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1374..1483
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1488..1586
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 1656..1835
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 1863..1978
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2040..2218
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 2293..2573
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 2586 AA; 288310 MW; B38F9BAB0F106436 CRC64;
MRLPPPELLN PCAAEPLLSQ PGLWLPFPDM RHSRESAEFF RAADAVLHDA HADLPDGDIA
AALPEFLAPT LDGDAPVVAL TATVVLQRSP AALELDEPDA ALGPSGWLWK KGDSHKAFQR
RFVVLHGREL SYYKAPVGPH GLYQKAASYR GSIPITDGTS ICPAAQRLDA GGGPRGLRAF
FVRQPTADAE RSLGIDIVTR TRTWSLVAPD ASAHAMWLRA LAVAAPECLH PLLTPPPPSV
PRRQSTEAWS IEFPSDALVA DVISLACAKL GVSAPESDDD GVGVVGGTLF ALKCVGHRAF
FRTPTRQMHE FAHVAAVVAT GGCHLPLVLV EYAPMAPPSA RPLDVPRPAR SLDAALSFPL
AMPALVESWR VSQSLRLAVH EVVNVPPHTT AGGLTPAGLT AVPLTYSHVV VRLTLWFGTT
LLEPWQETPP VKLQPTATPE LLAVWPSALK PLKSQLKINQ LPCETRLVCT LFGVKKDANG
HASCLGDDSD REPIVAAAIQ VFDQHGQLRQ GPQYAAMVTG PSLSPQFLDA AQPLLHMSFG
VADYRCYFER MPKNIFLKRS RTVATEAPPA HRGWLRKQGR GVGKAWAERW FVLEGRQLSY
AEDPAYPPTA TLDVSQAAVE PLDDLNETYT TFAVNKGTRK EQTTYCFQLV VDGRTYVLSA
TSKSARQAWM TALSAAASDP TYLLSPPSEL NGSDRSSTDS SLSDDFVDDI LSLVSRDPLA
VLTPSQKTRL WAHRIEFLGS FAMLPHVLSS ADWTSPVDVD HAATCLRVWQ PPAHSAEWLR
LLTPAFPMEY VRNFALGRLA EAPPQDWCRL LPQLVQALQS EAFHSSSLAL HLLAQAWRYP
EHAGVRLYWL LQVEAESPHA GVRERCAVVL NAYMAGVAPA VRTACRTQKH LFGSTGVFDA
LAGYVKMLKK KGISLGDIQL AMRANLEEIN ETLPPSVTLP LPDSAGVSKL IVAKCKVMSS
AKLPLWLVFE NADPGGDPVV VIFKSGDDVR QDCLTLQLME VMEDLWHTAG LNLNLEPYSC
VATGPSVGLL QVVLNAETTA QIHQRMGALG AFDDTSFSSW LRSHHPEPAQ YAAAVDLFRR
SCAGYCVATY VLGIGDRHND NIMMTTAGRY FHIDFGHFLG HFKYQFGIKR EKTPFVFTPE
MAHVLVADQL PEVFRSFVIV CGEAFNVLRR HAHVLVALLL LMIPAGMPEL RDQNDLNHLV
ESLLLAVDER TAAANFEAAI DFCLSSTFKR VDNTFHIIAH NRSSTMYGEM DVMSMAASGK
LPSFADLNPF AQYGSAATPT AAARWQPVPG LVHSKESLAL RQAVGGILKN VHEEVSSETL
EIRANTPEYR LEKDDWIAHR NSNKVLPPTL KTVARLPMSL LITNPNSVAV DKEKLNVAGW
LKKKGEKNTA MKKRYMELEN KVLTYYKKKP EHRGRPLSRE EKVPLMQGKI ELDKVSSVQP
TLVKGSQVKW GIDLVTTNRT WVLQAESDDD YLMWVHALCH SVRFHCVNII YRRMLQLAEV
SASAENEVRL VILPSYTVAE TVEHIFKCYE QMLDAVALRP YDPKDYVLKL TGYRDYMIDP
FREVNNYQHV RECLLTKKTL CLTLVHRSKI TEALQRGLSM RPTSGLLYNE AVCKMPPSAG
SVRNKLNFTT LGNEWQQADD VGNNNDAFAV GKSCHYREPL RFCVNRVLNV PRYTTHMRRT
AHDMAPEQKP LLFTNGIVVI ELYNGGKLLE PVVETMDVRM KAQASDDGLI AVWSEPKWYR
TKLKLHEIPR TARLVFTLYG VRKGIGGVVS NNSDGADRER ILTTGLNVFD VEGIIAQGEK
YMQMLDNLHH SHHGPVPHVI DPAKPIIHVS LSTYHSDIVF DWSAGNAVEN VAPTVNHGSR
SETLEKCGWL KKTGKSHALT AWQLRWFTLS QTTHSLSYAE DVNAPAKHTI DLLGANVMIA
DELNERYTTF AVSKGTRKEQ STWVFKLRAA DSSREFIMCA NTRQEREEWI MAIKMVASGE
TLSDEEDDDD VMGNQFDNDM HRMTLDPGSA DRSTILHGFS TNLLSERGRV MSGRQSSMNS
SVFSDGGTKA LDDLRETIRR DPLYRLSSFQ KAIMWKNRAD FMDKFEFLPR MLTCVNWFNA
KEVDEVISFL PRWAKASHPA AYIELLDMEF AHEGVRQFAV DKLAEMADTT FSVFLPQLVQ
ALKFENHHVS PLAKHLIERA IKNPNQIGFD LFWAMKVESY NEQYKERYGL LLNTYVDVCS
YKMRSILELQ DRLFTEKGVF EGICQEIKEL AHAGRSKDEM KGLLHTRLEE LNQSLPNAYQ
LPIDPRVEVS KIVVKKCKIM SSAKLPLWLE FENAEEGGDP VIIIFKAGDD VRQDCLTLQL
IRLMDEMWRE DGKDLAMEPY KCVSTGPMTG ILQVVQHAVT TADVHKRGGA MGGIFGAFND
QSFTDWIEAN NADPRSKKVA VDLFMRSCAG YCVATYVLGI GDRHNDNIMI TTGGRYFHID
FGHFLGFMKY QYGIKREKTP FVFTPEMAHV FGGIGTDEFR KFQALSAEAF NVVRRHLHLL
VSLLLLMIPA DMPELRKRDD INYIVEIMSS EKTDNEAAAY FADLIVQCTK NTFKRIDNTL
HILKHS
//
