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Database: UniProt
Entry: A0A3S3PF60_9ACAR
LinkDB: A0A3S3PF60_9ACAR
Original site: A0A3S3PF60_9ACAR 
ID   A0A3S3PF60_9ACAR        Unreviewed;       780 AA.
AC   A0A3S3PF60;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Phosphatidylinositol 4-kinase beta {ECO:0000256|ARBA:ARBA00039877};
DE            EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN   ORFNames=B4U79_01736 {ECO:0000313|EMBL:RWS11228.1}, B4U79_05867
GN   {ECO:0000313|EMBL:RWS04579.1};
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:RWS11228.1, ECO:0000313|Proteomes:UP000285301};
RN   [1] {ECO:0000313|EMBL:RWS11228.1, ECO:0000313|Proteomes:UP000285301}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UoL-WK {ECO:0000313|EMBL:RWS11228.1};
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).
RN   [2] {ECO:0000313|EMBL:RWS11228.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UoL-WK {ECO:0000313|EMBL:RWS11228.1};
RA   Dong X.;
RT   "Trombidioid mite genomics.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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 4-phosphate) + ADP +
CC         H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216;
CC         EC=2.7.1.67; Evidence={ECO:0000256|ARBA:ARBA00036767};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19878;
CC         Evidence={ECO:0000256|ARBA:ARBA00036767};
CC   -!- SUBCELLULAR LOCATION: Endomembrane system
CC       {ECO:0000256|ARBA:ARBA00004308}. Mitochondrion outer membrane
CC       {ECO:0000256|ARBA:ARBA00004450}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004450}. Rough endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00037860}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00037860}.
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:RWS11228.1}.
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DR   EMBL; NCKU01005431; RWS04579.1; -; Genomic_DNA.
DR   EMBL; NCKU01001796; RWS11228.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S3PF60; -.
DR   STRING; 1965070.A0A3S3PF60; -.
DR   Proteomes; UP000285301; Unassembled WGS sequence.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05168; PI4Kc_III_beta; 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; 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; IPR001263; PI3K_accessory_dom.
DR   InterPro; IPR042236; PI3K_accessory_sf.
DR   InterPro; IPR049160; PI4KB-PIK1_PIK.
DR   InterPro; IPR015433; PI_Kinase.
DR   PANTHER; PTHR10048:SF22; PHOSPHATIDYLINOSITOL 4-KINASE BETA; 1.
DR   PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF21245; PI4KB-PIK1_PIK; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Reference proteome {ECO:0000313|Proteomes:UP000285301};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..204
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          498..765
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   REGION          58..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   780 AA;  87901 MW;  B639A04AFDB0FFCC CRC64;
     MEVCANVDHC LHQKATSETS GEKSNGEIRT DVAVEETKLS SVSNSVIIPK IVENGIHAEN
     SEKSNENEAT TKKREQEEEN VRRAFGPSRE SWLLRLFECK LFDMSIAITY LFKSKEPGVL
     SYIGNRMFSF NPSDVDFYLP QIVNLYIHCS DVAEALQTYL ISRCRECPQF SLQLVWLLTS
     FCTDNRKKSL GVKLKNLILS EELKLKLPPL QNRVHVKKSH HRSYSDATGC LQVMPGSSAA
     NLLNPSKTLG DLSSGHAFDN GCICFKSCAG ICNDLRGEKI TCHCGAPRLT AEYEFVKHLI
     SIGARLQTFP SKDIKSQRLM AELSMLNLNL PARVWLPIHS FKHMIIRVPP GAAVLLNSKD
     KAPYLVYMEA VEVFGDINSI PIPTKLSNTL RQTRSEENLL NFSHHRSSSG NINLIPPVDD
     DNDCWTQEDD DISSQYRCAK NVNKDRDTIS QVSQDSSAGE AVFVAAGDIR RRLTESINAP
     KTNFALDPED PSAAVLKEPW DEKVMRIRES SPYGHLQEWR LIAAIVKCGD DLRQEMMAYQ
     FLVSLQKIWE QEGVPLWVRP YKILVTSSDS GLIEPIVNAI SVHQVKKHSK MSLLDYFLKE
     FGSTVSEAFL TAQRNFVQSC AAYSVVTYLL QVKDRHNGNI LLDSEGHIIH IDFGFILSTS
     PKNLGFENSP FKLTLEFVEV MGGIGSDMFE YFKILILQGL IAARKHHERL VTLVEILQTN
     SQLPCFKTGP STIKALRERF HMNLTEEQLQ LLVNNMVDDS LHSLTTRLYD GFQYLTNGIL
//
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