ID A0A090MXK2_STRRB Unreviewed; 1050 AA.
AC A0A090MXK2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=phosphatidylinositol 3-kinase {ECO:0000256|ARBA:ARBA00012073};
DE EC=2.7.1.137 {ECO:0000256|ARBA:ARBA00012073};
GN ORFNames=SRAE_2000025600 {ECO:0000313|EMBL:CEF65579.1,
GN ECO:0000313|WBParaSite:SRAE_2000025600.1,
GN ECO:0000313|WormBase:SRAE_2000025600};
OS Strongyloides ratti (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF65579.1};
RN [1] {ECO:0000313|EMBL:CEF65579.1, ECO:0000313|Proteomes:UP000035682}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_2000025600.1}, and ED321 Heterogonic
RC {ECO:0000313|EMBL:CEF65579.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SRAE_2000025600.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00880}.
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DR EMBL; LN609529; CEF65579.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090MXK2; -.
DR STRING; 34506.A0A090MXK2; -.
DR EnsemblMetazoa; SRAE_2000025600.1; SRAE_2000025600.1; WBGene00260449.
DR WBParaSite; SRAE_2000025600.1; SRAE_2000025600.1; WBGene00260449.
DR WormBase; SRAE_2000025600; SRP06443; WBGene00260449; -.
DR eggNOG; KOG0906; Eukaryota.
DR eggNOG; KOG3856; Eukaryota.
DR OMA; EPMEPPM; -.
DR OrthoDB; 10350at2759; -.
DR Proteomes; UP000035682; Chromosome X.
DR GO; GO:0000123; C:histone acetyltransferase complex; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00870; PI3Ka_III; 1.
DR CDD; cd00896; PI3Kc_III; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 1.25.40.70; Phosphatidylinositol 3-kinase, accessory domain (PIK); 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR015418; Eaf6.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048:SF7; PHOSPHATIDYLINOSITOL 3-KINASE CATALYTIC SUBUNIT TYPE 3; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF09340; NuA4; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 2.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51547; C2_PI3K; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CEF65579.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035682};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 221..404
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 498..695
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 771..1034
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT COILED 10..44
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 82..116
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1050 AA; 121563 MW; 96A859B2AC8B4A21 CRC64;
MVSKKKTTII DNSKKKQDQL LKDLKKLEEQ LYKYETELLA KELNCDPKDI PDNFRIYSGS
SATYMKDQET IKSIHSAEGN ELLQMIKRRR ECIENLVNLE NEITKLESKY FEESHDYGNM
INGFHKMTST STSRGVNIRY DKRKKNVQTL DRIISLSSLT SPLSIKTSVA IPKNLMEQGS
SNSNNPILLA DGDNDSIRSM PINILDKLMQ REFNYVLSND LDIPLSINIL SLECAKERSS
YMRMYPNILN EITGQMFLKV SLFSNGRLVG TTMPTKYVTN TKESTSGKSE SLSSGKIQTW
NEWMKFPIKY SQLTRDAFVH FSVWDISSSD CKEIFIGETI MTLFSKRGTF RSDIIDLRLD
PAKKGETKDN PWKMSPKNAF KLAKYPHGDE KMNELMKKSK MHLNGLMKRV HFLDKISLNE
IEQIKADKKR KCNWLYLSIK LPTFTYDTNP FTLVFYQEEP ILSHPFMPFV SAYVDPEQDL
ENLYESRHHE MTRNCQGDDR NLKPSAQMKH YLERIIKKPS CVPITSEERD LIWKFRYWLM
KFPSALTKFV RCINWEIENE VKHAIKFINE WALCDAADAL ELLSDQFIHP FVRSYAVARL
QEADDSIILL FLPQLVQSIR YEVNVFLILT SKDLNIEQTF EDHGLASFLV DKCTKNREIA
ILLYWYLKVE IEANERVDKA VSDLFKDVLD KMLLALDELG STGREIKMTI EHQLKLVNGL
ENLGKNIADE NGRLDYKRDL CIQRLSEDET FTKLHSLSLP LDPKVTVYGI IPEDTKLFSS
KQMPMKLTFA TNSHYLHEIN SANDNYTLLY KRGDDLRQDQ LVVQMIKVMD MLLKKEKLDL
CLTPYSVLAT SPTEGFVQFI KAYPFREVNN QGGIRAMLKK YRPAKTPEDI EIEALNNYTK
SLAGYSIICY ILGIGDRHMD NLLLCENGRD PKPFPPPMKL NSDIMNALGV ENSDRRKMFV
TYCYSAFCIL RRNANLILNL FQLMLDAGIP DIAVEKDKAV EKVLHRFHLD LEDDEEKIYS
KINSLINEST SDRFAAIMDV AHDFKQNYLN
//
