ID A0A1V9XLV6_9ACAR Unreviewed; 1189 AA.
AC A0A1V9XLV6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Phosphatidylinositol 4-kinase beta {ECO:0000256|ARBA:ARBA00039877};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN ORFNames=BIW11_09050 {ECO:0000313|EMBL:OQR74466.1};
OS Tropilaelaps mercedesae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Mesostigmata; Gamasina; Dermanyssoidea; Laelapidae;
OC Tropilaelaps.
OX NCBI_TaxID=418985 {ECO:0000313|EMBL:OQR74466.1, ECO:0000313|Proteomes:UP000192247};
RN [1] {ECO:0000313|EMBL:OQR74466.1, ECO:0000313|Proteomes:UP000192247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wuxi-XJTLU {ECO:0000313|EMBL:OQR74466.1};
RX PubMed=28327890; DOI=10.1093/gigascience/gix008;
RA Dong X., Armstrong S.D., Xia D., Makepeace B.L., Darby A.C., Kadowaki T.;
RT "Draft genome of the honey bee ectoparasitic mite, Tropilaelaps mercedesae,
RT is shaped by the parasitic life history.";
RL Gigascience 6:1-17(2017).
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:OQR74466.1}.
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DR EMBL; MNPL01007929; OQR74466.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9XLV6; -.
DR STRING; 418985.A0A1V9XLV6; -.
DR InParanoid; A0A1V9XLV6; -.
DR OrthoDB; 147843at2759; -.
DR Proteomes; UP000192247; 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 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; 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; 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, ECO:0000313|EMBL:OQR74466.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000192247};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 352..526
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 892..1174
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 719..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1189 AA; 130302 MW; 826E4EC0BDFDA574 CRC64;
MELASVHRRG HHRVASLDVR STQTLGSTLK VKNFSPATNV TEADQNSSVG HHQQTCPITN
HESHQARTAN ITCLETRVHG LGGPAKVPKA GVCDICKTSI TSSYNSESLS CSTAGTSSCV
QCGHLGTTVL LTPVPIRSAS QQHQHMRNLS LDSALQQQRQ LQQLQYQQLP LHATQLNVGH
PLLLQETDGN SLASDDSGIC AAAEMPDAEH HRIMGSGHGP FFKATDEEEK SSSRLETPFC
RLGRPESYTG NSPYFMPSTA SNGDRQDTLE CSLADNKREV GFAQAERSTT EVNLVESSFL
STDTMASIKY NQRVAQWTSG QQIEERPVDS EDTDGELGSC CRNGQYSREA RNREACSYND
KRIFILATGQ QSEPPSSTEF NSSQMLFSRE TVSCNQVTAD LVQEVPVLPS SQSGLLRLFE
SRLFTMRFAV QYLSQSREAG VLAYIGNRMF GFDDVDVAFY LPQLVCLYVH HADVAEAIKP
YLVLRCRRDA DFSLQLSWLL SAFCEDSNAP SRKTSQGLRL KNIIQSEELG LGAVRSLGLS
INHLEVTSNN PSSRLASESQ GKFQVTYHHH RRTTGHYRSY SDATGLQQPK LSNLLQHLGN
LSSGHAFDSG CRCHSRCECG APRLRAQNEF IKALIQLGSM LASIPTKDLK TQRLQAELTR
LNMNLPARVW LPVHSRPHLV VRIPPQAAVV LNSKDRAPYL IYVEVVAVDD IATSPVPSKT
IQNSIKASRS EENLERDPDN SNGSPSNPPS GFLSSSSSCQ QLHLQGASSG SGGGSSNLGV
PLNGIGTPAN GTSGSSATTV ASSGMLLSGD PVDGGCLFSF AGDEWSVEDD EISAPFAVSV
SMNNLYKRDR DTLSVDSGVG LLTVGAGDIR RRLSEQQGGN GAAGGRRPAL QRDPEDPSAA
ALKEPLDDKI ERIRDGSPYG GLNSWKLISA IVKCGDDLRQ ELMASQLLSL LQMIWAEEKI
PLWIRPYRIL VTGHDSGMLE PILDTMSLHQ LKKLHNNCSL VVYFEREFGP RTSEPFLAAQ
RNFVESCAAY SILSYLIQIK DRHNGNILLD GEGHVIHIDF GFILSASPRN LGFEASPFKL
TQEFVQVMGG TDGDMFEYFK MLMLKGLLAT KKHQERLVTV VETLQADAQL PCFQGGKGAS
ALRAFKDRFL MHMTEEEIAI KVETMVESSL HSLTTRLYDG FQYFTNGIH
//
