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Database: UniProt
Entry: A0A094ZI85_SCHHA
LinkDB: A0A094ZI85_SCHHA
Original site: A0A094ZI85_SCHHA 
ID   A0A094ZI85_SCHHA        Unreviewed;      1107 AA.
AC   A0A094ZI85;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Phosphatidylinositol 4-kinase beta {ECO:0000256|ARBA:ARBA00039877};
GN   ORFNames=MS3_00752 {ECO:0000313|EMBL:KGB32614.1};
OS   Schistosoma haematobium (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6185 {ECO:0000313|EMBL:KGB32614.1};
RN   [1] {ECO:0000313|EMBL:KGB32614.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22246508; DOI=10.1038/ng.1065;
RA   Young N.D., Jex A.R., Li B., Liu S., Yang L., Xiong Z., Li Y.,
RA   Cantacessi C., Hall R.S., Xu X., Chen F., Wu X., Zerlotini A., Oliveira G.,
RA   Hofmann A., Zhang G., Fang X., Kang Y., Campbell B.E., Loukas A.,
RA   Ranganathan S., Rollinson D., Rinaldi G., Brindley P.J., Yang H., Wang J.,
RA   Wang J., Gasser R.B.;
RT   "Whole-genome sequence of Schistosoma haematobium.";
RL   Nat. Genet. 44:221-225(2012).
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}.
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DR   EMBL; KL250510; KGB32614.1; -; Genomic_DNA.
DR   RefSeq; XP_012792387.1; XM_012936933.1.
DR   AlphaFoldDB; A0A094ZI85; -.
DR   STRING; 6185.A0A094ZI85; -.
DR   EnsemblMetazoa; XM_035733903.1; XP_035590295.1; MS3_0019993.
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   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; 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; PS50290; PI3_4_KINASE_3; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KGB32614.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1076..1101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          878..1107
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   REGION          523..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..537
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1107 AA;  124134 MW;  886050E62813A56C CRC64;
     MPDISEYRLG SACRINNSDQ FSEKAGSEAS ILDPSGSNAL KLEECIVSVQ ELHHVVNDKA
     SSDDNGSNNN NPNMEDVTCC CHDSRNECGI LNDSNSSSWL RRLFTSSLFN LDMTIQYLFK
     SEDVNVQMYL ADRLFGFPES DVDFYLLQLV SLYEKSPSLA EHLTNYFIYR CTKSVSFAIN
     LVWLLDSFSS HSYNPLKRVS SILLNRPSSV PIFSYVSNQL YLMNSSDNSQ SINSNSNNSK
     FIKLKSSSSA ITPLQELDYH NSNNGDENYN TNVVPTPNTT TTNNSTELSN DNRFVYTAQT
     LRDLLLPIDE TTWGSFIPQS IVNGSYNMGS YNNVNTHYTH NTSSPSSNCK LSPNIHHNIG
     HKRSTSDVTN KSRHRVVMDQ LDLMNNTETN QTITTITSNP NRWSSSQDSA VCLSTIDDVV
     NNPITTISNI TNQISLNSIC PIINHLSNQT NPLLNENRHS LHQLHLNNLN QNPIKSSMSM
     NKIITKEILP QSCLPKHSRS SVNLQQLNSS LCIMNDDNSA QIKSSSSLNQ TATVRGENNH
     RNDVDRNLSS YSTNNITSDL MLGSLEGVPV LTTITLTKTK SINEARNNPT HTMESCSSTT
     ESSSPLDSVP RIIPEWDFVD GLLRIARRLV PISPKEQRTA YLQAELANLN LHLPARVWLP
     VNKAGHIVLR IPPTAAVCLN SKDKAPFLIY VEILCCDDPS IISLPSRPIT AASSKSSNSL
     SAVYPWNPNS HTGCFSSNEI TENHEINVNT RTSDELSLRS SSISSNVSLS EELINPIEFN
     HHQHQHPHYH LTIDEMDERK EHTTKCTHDQ FELNETIMKD DSFTATDSIT VTNANRSKSP
     IYIGAGEIRN RLKEQCELQP HKSFRCDPED PSAAVLKEPW HVKCERIRAT SPWGSLPGWI
     LTSAIVKVGD DLRQEQLAYQ LLTVLKNIWS MEYVPLWLRP LTVVVISSDS GFIEPVPDTV
     SFHQIKRHAH LSLLDYMHRE HGGDNSEEFL TAQRNFLHSC AAYCLVGYLF QVKDRHNGNI
     LLDNQGHVIH IDYGFILSSS PGKNLGFETS PFKLTLEQID VIGGLNSDLF EYFKFLLLRG
     LLAALVYSFI EFPFFSFFFG WGGMGSI
//
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