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Database: UniProt
Entry: B7PIF4_IXOSC
LinkDB: B7PIF4_IXOSC
Original site: B7PIF4_IXOSC 
ID   B7PIF4_IXOSC            Unreviewed;      1142 AA.
AC   B7PIF4;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   SubName: Full=Phosphatidylinositol 3-kinase class, putative {ECO:0000313|EMBL:EEC06376.1, ECO:0000313|EnsemblMetazoa:ISCW004026-PA};
DE            EC=2.7.1.154 {ECO:0000313|EMBL:EEC06376.1};
GN   ORFNames=IscW_ISCW004026 {ECO:0000313|EMBL:EEC06376.1};
OS   Ixodes scapularis (Black-legged tick) (Deer tick).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX   NCBI_TaxID=6945;
RN   [1] {ECO:0000313|EMBL:EEC06376.1, ECO:0000313|Proteomes:UP000001555}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wikel {ECO:0000313|Proteomes:UP000001555}, and Wikel colony
RC   {ECO:0000313|EMBL:EEC06376.1};
RG   Ixodes scapularis Genome Project Consortium;
RA   Caler E., Hannick L.I., Bidwell S., Joardar V., Thiagarajan M., Amedeo P.,
RA   Galinsky K.J., Schobel S., Inman J., Hostetler J., Miller J., Hammond M.,
RA   Megy K., Lawson D., Kodira C., Sutton G., Meyer J., Hill C.A., Birren B.,
RA   Nene V., Collins F., Alarcon-Chaidez F., Wikel S., Strausberg R.;
RT   "Annotation of Ixodes scapularis.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:ISCW004026-PA}
RP   IDENTIFICATION.
RC   STRAIN=wikel {ECO:0000313|EnsemblMetazoa:ISCW004026-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00879}.
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DR   EMBL; ABJB010091313; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DS718559; EEC06376.1; -; Genomic_DNA.
DR   RefSeq; XP_002404927.1; XM_002404883.1.
DR   AlphaFoldDB; B7PIF4; -.
DR   STRING; 6945.B7PIF4; -.
DR   PaxDb; 6945-B7PIF4; -.
DR   EnsemblMetazoa; ISCW004026-RA; ISCW004026-PA; ISCW004026.
DR   KEGG; isc:IscW_ISCW004026; -.
DR   VEuPathDB; VectorBase:ISCI004026; -.
DR   VEuPathDB; VectorBase:ISCP_022067; -.
DR   VEuPathDB; VectorBase:ISCW004026; -.
DR   HOGENOM; CLU_002191_0_1_1; -.
DR   InParanoid; B7PIF4; -.
DR   OMA; CWNSANI; -.
DR   Proteomes; UP000001555; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IBA:GO_Central.
DR   GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IBA:GO_Central.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IBA:GO_Central.
DR   GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; IBA:GO_Central.
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; cd00864; PI3Ka; 1.
DR   CDD; cd05166; PI3Kc_II; 1.
DR   Gene3D; 3.10.20.770; -; 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   Gene3D; 3.30.1520.10; Phox-like domain; 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; 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   PANTHER; PTHR10048:SF14; LD28067P; 1.
DR   PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 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   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); 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   SUPFAM; SSF54236; Ubiquitin-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; PS51546; PI3K_RBD; 1.
DR   PROSITE; PS51545; PIK_HELICAL; 1.
DR   PROSITE; PS50195; PX; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EEC06376.1};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001555};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EEC06376.1}.
FT   DOMAIN          42..140
FT                   /note="PI3K-RBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51546"
FT   DOMAIN          300..454
FT                   /note="C2 PI3K-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51547"
FT   DOMAIN          460..636
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          704..978
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   DOMAIN          1015..1130
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
SQ   SEQUENCE   1142 AA;  130144 MW;  DA9C62FC17323D89 CRC64;
     MSHFFKFVQA RLVKKQPNHH SQRLLRKLQH LVCDVQPEDS PYSGLLISPT LQNNSEETFD
     VKLKIFSEQL HKPVCFSCPA ATRVGYLVES IQPFLGSPGK YVFKVTGLDE YLSNDTLLSD
     YAYICACRRV GKVAWLTIVN LDNVQKPWTL VTSESCDLDI DVSEKITFVA VRDALETFES
     QVEELIGVAL SVGGDLVKAA GDIRASVTEL CQLLNHTETS ELYQTTTDLL NFFRDTLSEN
     RDGVDAPRKV FLVTRFVEDI ELAIARFLAM HSQRRSVEFT VEFLDESLRR RRTVDANELF
     SPKVEMLVQL QKAWVQNYDS YSVDCALTYG ERLFSYQTTR RLYVTQRIFQ CVNFDEYISF
     KNIQIRSLPR ETRMYLTVVG HRDGADHVLG WTGLNIFADR EHFNGGEFLL GLWSPEMLST
     RGPVSASEQN KGCLLVTLPH VKNQAVLAKS ITRNVREVVR KPFHELSADV QQTFLDLTVT
     DVSTPLPTYV RDLIWEHRHH LCDFSSLLPH LLKLPVCWNS ANIEETYTLV RSWCPLSPEE
     SLTLLSPAFP DSLVKKYAVQ SLQSVGSDEL SLYLAQLVES LRFQNWDDSF LATFLLRRAR
     QSVRLAHQLF WWLTGMINEP LMRDRALIMR KALFFVAGEK VTASLLTQIV ADEMLAETAR
     SVKQAADSQK EEVMRRELAK LNSSLQVLKL RLPLDPAISV ESVDVDTCCV FPSKTLPVKL
     VFRSSEEAAE KIETIYKAGD DLRQDVLILT VIRLMDKLWL ESGMDLKMLT FKCTTTGESR
     GFLEAVRDVS TLRTIQTNHS GVTGAFSNRT IADWLWKHNS CRPQYQAAVD NFIKSCAGCC
     VATYVLGVGD RHNDNILLAT SGHMLHIDFS KVLGHAETFG GIRRDRAPFA LTQDMVYVIR
     RNGGEAQFVR LCCEAYNVLR RNSSLFLALF SIMKHSGLPD VDQDALAYLR RSMSLEATDE
     QAARHFEKRI RESVMTLATS FNFFIHNLAS LGANTRECAL RLSFNPRDFS IAAEGKIVQL
     TVEDIRLRYH PERYYVYVVN VEREFPPAQS VIRTYKNFLE LYTKMSRKFP ACDFHPLSRG
     SVFSSEGDES LALKRKRDIQ QFLDTVMAQP EDVSHYRLVY SFFHPLPRDL ELLNGVPITI
     AT
//
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