ID A0A0V0V343_9BILA Unreviewed; 1873 AA.
AC A0A0V0V343;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha {ECO:0000313|EMBL:KRX57892.1};
GN ORFNames=T09_11297 {ECO:0000313|EMBL:KRX57892.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX57892.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX57892.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX57892.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-
CC [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:61930; EC=3.5.1.98;
CC Evidence={ECO:0000256|ARBA:ARBA00001028};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-
CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:18373,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57658,
CC ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.154;
CC Evidence={ECO:0000256|ARBA:ARBA00029297};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18374;
CC Evidence={ECO:0000256|ARBA:ARBA00029297};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216;
CC EC=2.7.1.137; Evidence={ECO:0000256|ARBA:ARBA00023985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710;
CC Evidence={ECO:0000256|ARBA:ARBA00023985};
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00879}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC subfamily. {ECO:0000256|ARBA:ARBA00006457}.
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:KRX57892.1}.
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DR EMBL; JYDN01000094; KRX57892.1; -; Genomic_DNA.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
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; cd04012; C2A_PI3K_class_II; 1.
DR CDD; cd10000; HDAC8; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 3.40.800.20; Histone deacetylase 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 Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR003084; His_deacetylse_1.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
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; IPR000341; PI3K_Ras-bd_dom.
DR InterPro; IPR015433; PI_Kinase.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR10048:SF14; LD28067P; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF00787; PX; 1.
DR PRINTS; PR01270; HDASUPER.
DR PRINTS; PR01271; HISDACETLASE.
DR SMART; SM00239; C2; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50004; C2; 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; PS51546; PI3K_RBD; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRX57892.1};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 594..683
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 863..1040
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 1055..1245
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1295..1572
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1611..1726
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 1743..1864
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
SQ SEQUENCE 1873 AA; 211924 MW; 06FDBF1B0FD3F6B3 CRC64;
MSSGRIEGMP ILKKEEVCVA FSVDYNKICD SFERLEKRSS IVFSLLQAYG LLDQVRLFKP
LIADESTVGV FHSDDYMSFV KNASAGLIAE VEDVESEPMR DYGLGYDCPI FPALYEYGRA
TVGATVHCAQ LLVDGKAKLA VNVNGGWHHA RRSAAAGFCY FNDCVIGILK LRERFKRVLY
IDLDAHHGDA VEDAFCSTRS VLTVSLHCYE AGFYPCSGSV DDVGVGSGKY YAVNVPFRQG
LVDEQLLSTF DALVPKIVHL YRPEVVFLQL GTDGLAGDPV AAFNLTPSAY AGVVCRVLGF
GKPCLLVGGG GYKPTNVSRC WALVLGALLG QNLDDDIPEH AFFSAYGPDF VLCNRHSTGT
IPNLNTDHQL NELYILERNK KNKNGTRRKN CPKLWLVMEP DDDLIAWVDP DLLAREKKIT
AIKKMLYASS GISNGLPSST SSTRTTINDG RLSLSSLADS VAQLRFVNSS DSGNNNENAS
STAVERSRSL DSCLFVEFDP LNDEHYSSTS ANPAEVESGP DLVVEESKKP TEGDNHAACG
QQFFHLVDYC SNASLQARRL VDYSKSVIAD LVDQSDIYRK LVVSRRRFDL VSPDTSLKVT
VHTPFDQTAP VLLFACHIRS SIGQIIGCVL CSFNSTRLLP IEQYAIKRFG VDEYLLPDSA
LADYVFIHDC LKLGHDPELE LVDLAKIIQT AKIDESSLLP TLINNNNNNN IISTTGIGSL
KRDDLQVVLN TIRQECEKLI DESAAVDAVH RKVNSKFVVQ SVKALCSLFH RVENLSLIKA
VKKFITACNM EIVVNGEMQS EMAIRKKYKN VKNAISYLVD AIEKFCINFC QSFEVDFSVE
LSANFRTDPS TSCPFRPLDI TDSEVNFHFM IETVHSLPQN WTTKYSQFYL ACHLIHGDRE
LCSAFKTNCG RSDRHFYEYL LFDAWITLPI PLCALPRETK LCLALYGQRI DSNPSSCDQN
SSTTAGIVAC LIDEQLCFSV TPLFDIDKKK QQLLFFSILL NGTKFVTFYP GSELKSWLPQ
LSSQWSESPI CVVSFPYNEP KMRFPHILPN ATLNIGKFDQ LDCNVKLLLE DMIENRALKE
LDRDEKDFIW EKRIYLTNFD EALPLVLSSA ISWDWACLSN IYALVQLWRP VPTGIAMELL
LPNCPDEFVR KYAVSCLECN PVDSLMDILP QLVEVLRFER FECSSLAECL LKFAVESRAF
AELESHKTHP GLGLRCRLLQ NVLVTVVGPG MPTEVRLQVE LLSRLDSISE MVKRESRDDK
KSKALLVQLH LLDSWLLQTH VRVPLNPSVL AVGVFTENSK IYRSLTCPVK VSFRTVNSNF
DVMYKSGDDL RQDSLVLQMI RLMDHLWLKE NLDLRMVVFR ILPLQDKKGV IELVKNSKTL
REIQVEEGGM TGVLRDDLIQ KWLQKQNPSE LEYQIALKNF RLSCAGWSVG TYVLGIGDRH
NDNVMITSKG HLFHIDFGKY LGDAQMFGSF RRDRVPFLLT NDMLYAINAG ESTKSAFFQQ
FVDCCCNAFN IIRKHSTLFV NLMQLVMLYS SIPGLTRDSI AYMYQNFWLE CTDSEASMRF
TRLIEETLRS KFPKLNFLVH TVVQGQRKTG HLSSGQILSF VPQTYTAQTD GTIQSVQVID
CEKWHVPAKI YMYKMKVERE NVKVPSFVYR SYDEFCEFAE SIYFRFPLIK MHSLPRGVTL
RSNVRGVAVR RQSEIAQFIR SLFHYAEEIS HSDLVYTFFH PIFRDEQADI KSKTQNLHHP
ENVSGEVKVQ VEFRQGLLEI FINHARNLSL INGINLPDSY VKCYILPDKR GWSKKKTRVV
RGTRDPTYNE MFVYRVPASQ LKCKVLEISV WHYDLLKGNN FLGSIAIPMA DICDIPGLKM
SDWFRLENRR FKT
//
