ID A0A3S3PMS4_9ACAR Unreviewed; 1068 AA.
AC A0A3S3PMS4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Phosphatidylinositol-4:5-bisphosphate 3-kinase catalytic subunit alpha-like isoform {ECO:0000313|EMBL:RWS15774.1};
GN ORFNames=B4U79_01193 {ECO:0000313|EMBL:RWS15774.1};
OS Dinothrombium tinctorium.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC Trombidioidea; Trombidiidae; Dinothrombium.
OX NCBI_TaxID=1965070 {ECO:0000313|EMBL:RWS15774.1, ECO:0000313|Proteomes:UP000285301};
RN [1] {ECO:0000313|EMBL:RWS15774.1, ECO:0000313|Proteomes:UP000285301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UoL-WK {ECO:0000313|EMBL:RWS15774.1};
RA Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT transferred genes associated with secondary metabolism.";
RL Gigascience 0:0-0(2018).
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:RWS15774.1}.
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DR EMBL; NCKU01000368; RWS15774.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S3PMS4; -.
DR STRING; 1965070.A0A3S3PMS4; -.
DR Proteomes; UP000285301; 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; cd05165; PI3Kc_I; 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; IPR003113; PI3K_ABD.
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; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048:SF111; PHOSPHATIDYLINOSITOL 3-KINASE AGE-1; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF02192; PI3K_p85B; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00143; PI3K_p85B; 1.
DR SMART; SM00144; PI3K_rbd; 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 SUPFAM; SSF54236; Ubiquitin-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; PS51544; PI3K_ABD; 1.
DR PROSITE; PS51546; PI3K_RBD; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RWS15774.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000285301};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 16..105
FT /note="PI3K-ABD"
FT /evidence="ECO:0000259|PROSITE:PS51544"
FT DOMAIN 186..284
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 334..488
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 519..696
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 767..1054
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 1068 AA; 124551 MW; 9538F92D41665958 CRC64;
MVPRPTSDEL WGHHLMPQTL PLDILMPNGT LIQIQSHRES SIETIKSEIW SEAKNHVLYR
LLNEPSSYIF IAVTQDAKLE EFYDESRRLC DLRLFYPILK LVEPKGNKEE KILNSDISLA
IGRPINEIEN KKEPEIVEFR RNVLSLCKSV VEERESLSNE QKLYYAFPPE LEPDYESERE
VRDENSQMIK LSVYFSFQKP DDCQVSEINY EIEIAYTRKP KEVISEMSKL LASKDFDSSG
MPDNFLLKVS GLNQYLFGDH PLFKFKYIKH CLSHGKCPKL SLESKENVFR SIPEAEFLVP
SFLRRLPSQP SKEQQLESIN QAFMNLQLMS LWRVETMLRV KILSATYVNV RDVERIYVKC
GIYHGPEALC PPKETQQVTP INPKWDCWLE FDLYVPDVPR SARVCLSICS ISYRKKREEH
CALAWGNFTL FDYNDNLLSD RVHIHLWPVP KGHDELLNPL GMIGSNFNKD SPCLQIEFDR
YSCPVIFPTK EQITDYSRFV RKQEENGRST GCKDFQQSRL LCNSPTQSDR ELLLEIIKRD
PLSEMSLQEK DLVWKFREIC LEIPDSLPKL LDAVKWNSRD EVCQLYTLLE RWTPVKAETA
LELLDCKYAD LTVRNYAVKW LNQNLSDDLL SQYLLQLVQV VKYESYLDND LSRFLIRRTL
MNRKIGHYFF WHLKAEMHDS IFSLRCQLLL EAYCRGIGKR VLKSTIRQVE ALEKLTKLTD
TLKERKDDTQ KERLKFLSAQ VKQADYLETL QNFPSPLNHN IILGELVVEE CRIMDSAKRP
LWLVWTNPDK HCDLSNQSNA IIFKNGDDLR QDMLTLQVIG IIDLIWKREN LDLKMLPYTC
LSTGKQVGMI EVVMRAKTVM NIQRTGGRMA AFQVDSTQLH KWIKEKNNTK ENYDRAVDIF
TKSCAGYCVA TFILGIGDRN PDNIMINEEG QIFHIDFGHF LGHFKKKFGI NRERVPFVLT
DDFLYVISKG AENPHKSPEF EEFTKLCGAA YLSLRKHANL LITLFTMMLS TGIPELQSID
DIGYLRKTLQ VEKSEKEALQ YFNSQFFEAY GGAWTTKIDW FFHSVKHM
//
