ID A0A0V0XJS4_TRIPS Unreviewed; 1523 AA.
AC A0A0V0XJS4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha {ECO:0000313|EMBL:KRX88216.1};
DE Flags: Fragment;
GN Name=kin-18 {ECO:0000313|EMBL:KRX88216.1};
GN ORFNames=T4E_1400 {ECO:0000313|EMBL:KRX88216.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX88216.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX88216.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX88216.1};
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=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 -!- 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:KRX88216.1}.
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DR EMBL; JYDU01000245; KRX88216.1; -; Genomic_DNA.
DR Proteomes; UP000054815; Unassembled WGS sequence.
DR GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0008193; F:tRNA guanylyltransferase activity; 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 GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR CDD; cd04012; C2A_PI3K_class_II; 1.
DR Gene3D; 3.10.20.770; -; 1.
DR Gene3D; 3.30.70.3000; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
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; 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; IPR025845; Thg1_C_dom.
DR InterPro; IPR024956; tRNAHis_GuaTrfase_cat.
DR InterPro; IPR038469; tRNAHis_GuaTrfase_Thg1_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048:SF14; LD28067P; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00168; C2; 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 Pfam; PF04446; Thg1; 1.
DR Pfam; PF14413; Thg1C; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00144; PI3K_rbd; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM00312; PX; 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; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRX88216.1};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 208..296
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 469..634
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 821..1113
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1083..1198
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 1215..1335
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX88216.1"
SQ SEQUENCE 1523 AA; 173597 MW; AA16EBE486CC042D CRC64;
LVMENDDDLI AWVDPDLLAR EKKITAIKKM LYASNAVSNG LPPLLTGLST PATTEHAATT
SGRLSLSALT DSVAQLRFTS SNNSVGGNEN DANISTVERS RSFGSCSFVE FDPLSEHHST
SSNTPVESVG VTVTKSTPTE GDDNRRCSGG GDGGGQEFFH LIDCCSNASS QARRLFDYSK
SMVDLFDQLD IYRQLIISRR RFDLLSPDTS LKVTVHTSFD QRAPVLFACH IRSSIGQIIG
CVLCSFNSAR LLPIEQYAIK RFGIDEYLLP DSALADYVFV HDCLKLGHDP ELELVDLPKI
IEIAKSEESL LPTLINNNNN NNNNTIIINS TTIGSLKRDD LKVVLNTVRQ ECEKLLDESA
TAFHRKVNSK FVVQSVKALC SLFHRVENLP LIKAVKKFIT ACNMEVNGEI QSEMAFKKYK
NVKNAINCLV DAIEKLCSFE TNFTVALSAN CGTDFPCSFS PVRQDITDSE ENFHFMIETV
HNLPQNWMTK YSQFYLACHL IYGEKELCSV LKTNCGRSDR HFYEYLLFDA WITLPVPLCA
MPRETKLCLA LYGQHVDLNA CEQNSNTADV ACLIDEQLCF SVTPLFDMDN ILLNGTKLVT
FYPGSELKSW LPQLSEWSES PVSFPYNEPK MHFPDILPNT GLSIGRFDQL DCNIKLLLED
MIENRGLKDY ADEFVRKYAV SCLRCNPVDS LMDILPQLVE VLRFERFECS SLAECLLKFA
VESRAFAELE SHKMHPGWGL RCHLLQSVLV TVVGPGMPTE VRLQVQLLSS LDSISELVKR
ESRDDKKTKA LLVQLHLLDS WLLQTHVRVP LNPSVLAVGV FTENSKVYRS LTCPVKVSFR
TVSSNFDIMY KSGDDLRQDS LVLQMIRLMD YLWLKENLDL RMVVYRILPL QDKKGVIELV
KNAKTLREIQ VEEGGMTGVL RDDLIQKWLQ KQNPSELEYQ IALKNFRLSC AGWSVGTYVL
GIGDRHNDNV MITSKGHLFH IDFGKYLGDA QMFGSFRRDR MLYSSIPGLT RDSIAYMYQN
FWLECTDSEA SMRFTRLIEE TLRSKFPKLN FLVHTVVQGQ RKTGHLSNGQ ILSFVPQTYT
AQTDGTIQSV QVIDCEKWHV PAKMYKMKVE RENVKVPSFV YRSYDEFCEF AESIYFRFPL
IKMHSLPRGV TLRSNVRGVA VRRQSEIAQF IRLLFHYAEE ISHSDLVYTF FHPIFRDEQA
DIKSKTLNLH HPENVSGEVK VQVEFRQGLL EIFINHARNL SLINGINLPD SYVKCYILPD
KRGWSKKKTR VVRGTRDPTY NEMFVYRVPA SQLKCKVLEI SVWHYDLLKG NNFLGSITIP
MADICDIPAG LRLMSSAAKS VLHNYKDIRI AYGHSDEFSF VFCKRTNLWN RRLQKLLSTI
TSLFTSSYIF QWNLHFSDDR PLIWAPCFDG RVVLYPTDEN LTDYLKWRQA DCHINNLYNT
VFWKLVNEGG LKPDEAEKRL CGSTAADKNE ILFSQFNTNY NNEPVIFRKG TVLYRNVDGE
TVDTFHGSII DDKFWQSNAH LLK
//
