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Database: UniProt
Entry: V5HFX5_IXORI
LinkDB: V5HFX5_IXORI
Original site: V5HFX5_IXORI 
ID   V5HFX5_IXORI            Unreviewed;       514 AA.
AC   V5HFX5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Putative phosphatidylinositol 3-kinase vps34 involved in signal transduction {ECO:0000313|EMBL:JAB72403.1};
OS   Ixodes ricinus (Common tick) (Acarus ricinus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX   NCBI_TaxID=34613 {ECO:0000313|EMBL:JAB72403.1};
RN   [1] {ECO:0000313|EMBL:JAB72403.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Salivary gland and midgut {ECO:0000313|EMBL:JAB72403.1};
RX   PubMed=25765539;
RA   Kotsyfakis M., Schwarz A., Erhart J., Ribeiro J.M.;
RT   "Tissue- and time-dependent transcription in Ixodes ricinus salivary glands
RT   and midguts when blood feeding on the vertebrate host.";
RL   Sci. Rep. 5:9103-9103(2015).
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DR   EMBL; GANP01012065; JAB72403.1; -; mRNA.
DR   AlphaFoldDB; V5HFX5; -.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05166; PI3Kc_II; 1.
DR   Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
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; IPR015433; PI_Kinase.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   PANTHER; PTHR10048:SF14; LD28067P; 1.
DR   PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR   PROSITE; PS50195; PX; 1.
PE   2: Evidence at transcript level;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:JAB72403.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          76..350
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   DOMAIN          387..502
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
SQ   SEQUENCE   514 AA;  58235 MW;  AAAA1EA8878F9B90 CRC64;
     MRKALFFVAG EKVTASLLTQ IVVDEMLAET AQSVKQAADS QKEEVMRREL AKLNSSLQVL
     KLRLPLDPAM SVESVDVDTC CVFPSKTLPI KLVFRSSEEA AEKIETIYKA GDDLRQDVLM
     LTVIRLMDKL WLESGMDLKM LTFKCTTTGE SRGFLEAVRD VSTLRTIQTN HSGVTGAFNN
     RTIADWLWKH NSCRPQYQAA VDNFIKSCAG CCVATYILGV GDRHNDNILL ATSGHMLHID
     FSKVLGHAET FGGIKRDRAP FALTPDMVYV IRRNGGEAQF VRLCCEAYNV LRRNSSLFLA
     LFSIMKHSGL PDVDQDALAY LRRSMSLEAT DEQAARHFEK RIRESVMTLA TSFNFFIHNL
     ASLGANTREC ALRLSFNPRD FSVAAEGKIV QLTVEDIRLR YHPERYHVYV INVEREFPPA
     QSVVRTYKNF LELYTKMSRK FPACDFHPLS RGSVFSTEGD ESLALKRKRD IQQFLDTVMA
     QPEDVSHYRL MYSFFHPLPR DLELLNGVPI TIAT
//
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