ID A0A1V9XA88_9ACAR Unreviewed; 1017 AA.
AC A0A1V9XA88;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Phosphatidylinositol 3-kinase catalytic subunit type 3 {ECO:0000256|ARBA:ARBA00019787, ECO:0000256|PIRNR:PIRNR000587};
DE EC=2.7.1.137 {ECO:0000256|ARBA:ARBA00012073, ECO:0000256|PIRNR:PIRNR000587};
GN ORFNames=BIW11_11707 {ECO:0000313|EMBL:OQR70311.1};
OS Tropilaelaps mercedesae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Mesostigmata; Gamasina; Dermanyssoidea; Laelapidae;
OC Tropilaelaps.
OX NCBI_TaxID=418985 {ECO:0000313|EMBL:OQR70311.1, ECO:0000313|Proteomes:UP000192247};
RN [1] {ECO:0000313|EMBL:OQR70311.1, ECO:0000313|Proteomes:UP000192247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wuxi-XJTLU {ECO:0000313|EMBL:OQR70311.1};
RX PubMed=28327890; DOI=10.1093/gigascience/gix008;
RA Dong X., Armstrong S.D., Xia D., Makepeace B.L., Darby A.C., Kadowaki T.;
RT "Draft genome of the honey bee ectoparasitic mite, Tropilaelaps mercedesae,
RT is shaped by the parasitic life history.";
RL Gigascience 6:1-17(2017).
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|PIRNR:PIRNR000587};
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC {ECO:0000256|PIRNR:PIRNR000587, ECO:0000256|PROSITE-ProRule:PRU00880}.
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:OQR70311.1}.
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DR EMBL; MNPL01017937; OQR70311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9XA88; -.
DR STRING; 418985.A0A1V9XA88; -.
DR InParanoid; A0A1V9XA88; -.
DR OrthoDB; 10350at2759; -.
DR Proteomes; UP000192247; Unassembled WGS sequence.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd08397; C2_PI3K_class_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; 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; IPR008290; PI3K_Vps34.
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; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR PIRSF; PIRSF000587; PI3K_Vps34; 3.
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; PS00915; PI3_4_KINASE_1; 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 ATP-binding {ECO:0000256|PIRNR:PIRNR000587};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000587};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000192247};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000587}.
FT DOMAIN 21..197
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 302..621
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 735..1001
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 460..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1017 AA; 114520 MW; 6AEC81E0C6A47280 CRC64;
MNLLDGEPTS QLLRYVYSSD LDARFKIKVV NLEGDRPRPP YQDLVQNPLL RRNQLLLTWG
DSDRQSLVSD LVVTVEIFSD GRSLALPTQT SYKPFTTRYN WNEWLTLPLK FSDLPRDAQL
AFTVWDLHGP KTAVPVGGTT VSVFNKSGAM RQGMHDLKLW ANSKADGGSH TSTPGKISGA
KDELARLIKL TKKHHNGEMA RVDWMDRLTF REIEILNNNE KKKSQQMFLM IEFPRVVYRN
IEHMVVYFEK DLDTPCHYNG NSATSAADSK LATMFDPDVW FENLVEEKHH KLSRNQRTQL
IDKDLKPNAT IRDQLNRIVN KCSTTPLTAD EQDLVWKFRF YLKDQKKALA KFVHCVKWNA
EEETFHALEL MRQWEPMDVE DALELLGPQF KHTAVRRYAV TRLEQASDED LLLYLLQLVQ
ALKYEPSSQT SQHAESVSSS NTVFASVSSS PNFCGSVHQG GFSASSTHAQ QEQPLLSGSG
ELSESSQSSL SGATFASALD EDARRMEKGF DDQARSEERP PELRDAECRD SRLTIERSIS
ACGEGGALQD KELNSATSLA AATAITAALE DNRDLASFLI KRACRSDILS NYLYWYLTVE
SEGSHNYGSS AAGSLATSTG GGAGTQAVNN SGRKDNNSGC RSYAEMYADV LRRLVRCLKD
GNREQDLRRK MLAKQMSFVT NLVNVMKTVA AESGNRQKKI EKLKVLLNDP EQSKLALSES
LALPLNPKIR VKAIVADQAT LFKSALTPCR LTFLTDAGKE YVAIFKHGDD LRQDQLILQI
ISLMDKLLRR ENLDLQLTPY CVLATSTRHG FVEYVESRTV ADVLKEEGSI QNYFRKCAPC
DNGPYGIEPE VMDNYVKSCA GYCVITYLLG VGDRHLDNLL LTKRGQLFHI DFGYILGRDP
KPLPPPMKLS REMVEAMGGV SADHYNEFKK QCYTTFLHLR RHANLILNLF SLMVDASVPD
IALEPDKTAK KVQDKFMLEM SDEEAVSEMQ RLIDASVSAV MAVVVESLHK WAQYWRK
//
