ID A0A0D2WMD5_CAPO3 Unreviewed; 832 AA.
AC A0A0D2WMD5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Phosphatidylinositol-4-phosphate 5-kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CAOG_008653 {ECO:0000313|EMBL:KJE91970.1};
OS Capsaspora owczarzaki (strain ATCC 30864).
OC Eukaryota; Filasterea; Capsaspora.
OX NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE91970.1, ECO:0000313|Proteomes:UP000008743};
RN [1] {ECO:0000313|Proteomes:UP000008743}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 30864 {ECO:0000313|Proteomes:UP000008743};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KE346363; KJE91970.1; -; Genomic_DNA.
DR RefSeq; XP_011270264.1; XM_011271962.1.
DR AlphaFoldDB; A0A0D2WMD5; -.
DR STRING; 595528.A0A0D2WMD5; -.
DR EnsemblProtists; KJE91970; KJE91970; CAOG_008653.
DR GeneID; 23302050; -.
DR eggNOG; KOG0229; Eukaryota.
DR InParanoid; A0A0D2WMD5; -.
DR OrthoDB; 5481504at2759; -.
DR PhylomeDB; A0A0D2WMD5; -.
DR Proteomes; UP000008743; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0052742; F:phosphatidylinositol kinase activity; IEA:InterPro.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00139; PIPKc; 1.
DR Gene3D; 3.30.810.10; 2-Layer Sandwich; 1.
DR Gene3D; 3.30.800.10; Phosphatidylinositol Phosphate Kinase II Beta; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR InterPro; IPR027483; PInositol-4-P-4/5-kinase_C_sf.
DR InterPro; IPR002498; PInositol-4-P-4/5-kinase_core.
DR InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR InterPro; IPR023610; PInositol-4/5-P-5/4-kinase.
DR PANTHER; PTHR23086; PHOSPHATIDYLINOSITOL-4-PHOSPHATE 5-KINASE; 1.
DR Pfam; PF05462; Dicty_CAR; 1.
DR Pfam; PF01504; PIP5K; 1.
DR SMART; SM00330; PIPKc; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS51455; PIPK; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Kinase {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Reference proteome {ECO:0000313|Proteomes:UP000008743};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 41..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 109..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 269..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..294
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT DOMAIN 415..831
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
SQ SEQUENCE 832 AA; 92503 MW; 553036BF34628B91 CRC64;
MNPLPLSTPL LLQAVGMLNH SNSSSLTTLS NEDTGDNNNH ALLYFIGGLL SALFCGLQVV
SYALFPRLRQ HPSQIASIRA MCDFIFNLGF IFVYIFGEPG GDSNACLTLA LVNQFMAFAS
NGWYLVLSID LFKAIRNPFF VPTDYMKVYH LFVWSTSLVT AIVLGVADRW GYSLFDFCWI
KVTGPSDLNT FSWVLFYIPI MIFYLASLVV LIVATFALRN GLPESHEARS RVLTQGRRYV
TQFFLYWTFA GAVWGAQYGY VSETSHKEYP LIVVFSLTIA VRGLADLVIL LWSSRLTPRD
YVTAIADLCR RGGKRKSART ASTHHERVTL TQSLLSSEAT SAASDLGTAA AAAPSAPATA
AAVASAAASD NINLALRKDI MLCTTWAIVD TVKYQHKLAH PRVTVSNTVE ETGTAADPEQ
DPADISPGGA VVDLYASTSD ENFSTTHLAS DSHILDFEQV VTSEMVKRRG HGKFYFKDYM
PAVFEQLRSL FGVSATKYLS SFVARDDLKE ERERQMLEKF TEGRSGSFFY FCQDARYIVK
TVTSSDLAVL CKILPAYYEH MLHNPDSLLA RFCGLHAICL SREQEWIHFV VMENSIFTPL
KLHERYDLKG SWIARRSLKE GKTLANVGTM KDTDLINNQR KVKLGAVRSR RMIQQLDTDA
TFLHSLGIMD YSFLLAVHSQ DPNDAKTRAA VARAREFEAA QVVPTASDVA THRPESMLVG
EDALNSSFIS HVSTASAGSA AGADSHRHAS HNIRRYTPFY RVDAGGMQGV DGAQPCLYFG
GVIDMLQQYD LSKKLEHFAK TKITCKDAHG ISAVEPHEYR DRFVRAMEQM FE
//
