STT4_ENCCU
ID STT4_ENCCU Reviewed; 1412 AA.
AC Q8SQY7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Probable phosphatidylinositol 4-kinase STT4 homolog;
DE Short=PI4-kinase;
DE Short=PtdIns-4-kinase;
DE EC=2.7.1.67;
GN Name=STT4; OrderedLocusNames=ECU11_0450;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GB-M1;
RX PubMed=20003517; DOI=10.1186/1471-2164-10-607;
RA Peyretaillade E., Goncalves O., Terrat S., Dugat-Bony E., Wincker P.,
RA Cornman R.S., Evans J.D., Delbac F., Peyret P.;
RT "Identification of transcriptional signals in Encephalitozoon cuniculi
RT widespread among Microsporidia phylum: support for accurate structural
RT genome annotation.";
RL BMC Genomics 10:607-607(2009).
RN [3]
RP PREDICTION OF FUNCTION.
RX PubMed=17784954; DOI=10.1186/1471-2164-8-309;
RA Miranda-Saavedra D., Stark M.J.R., Packer J.C., Vivares C.P., Doerig C.,
RA Barton G.J.;
RT "The complement of protein kinases of the microsporidium Encephalitozoon
RT cuniculi in relation to those of Saccharomyces cerevisiae and
RT Schizosaccharomyces pombe.";
RL BMC Genomics 8:309-309(2007).
CC -!- FUNCTION: Acts on phosphatidylinositol (PI) in the first committed step
CC in the production of the second messenger inositol 1,4,5,-
CC trisphosphate. {ECO:0000250}.
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;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000305}.
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DR EMBL; AL590450; CAD25955.2; -; Genomic_DNA.
DR RefSeq; NP_586351.1; NM_001042184.1.
DR AlphaFoldDB; Q8SQY7; -.
DR SMR; Q8SQY7; -.
DR STRING; 284813.Q8SQY7; -.
DR GeneID; 860004; -.
DR KEGG; ecu:ECU11_0450; -.
DR VEuPathDB; MicrosporidiaDB:ECU11_0450; -.
DR HOGENOM; CLU_253125_0_0_1; -.
DR InParanoid; Q8SQY7; -.
DR OrthoDB; 1147978at2759; -.
DR Proteomes; UP000000819; Chromosome XI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.25.40.70; -; 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; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048; PTHR10048; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..1412
FT /note="Probable phosphatidylinositol 4-kinase STT4 homolog"
FT /id="PRO_0000385337"
FT DOMAIN 878..1055
FT /note="PIK helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT DOMAIN 1127..1396
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1056..1163
FT /note="Pleckstrin homology (PH) domain conferring
FT phosphoinositide binding specificity"
FT /evidence="ECO:0000250"
FT REGION 1133..1139
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1266..1274
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1285..1308
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
SQ SEQUENCE 1412 AA; 163616 MW; 044890C799A139FB CRC64;
MRIEVMIKGN SKEICIPLIK ETTLEDIREL SEVEVYDISS GLNAYAILKN STVCLEYSSK
LYEMYIAIFL KMLDDTATSK EIMSDMGGME PYSLLEVGLI NAFIEALIWR VEQGEVVGRY
EAFVEDLCRK MSSNLLCEIV SWKQEEDIMN TKFDYLLLSL RLIVMMVEYK TKEEGEIEKK
STFAFAKEYF YKAFALLGET KDLEDDMAFV FRASLTIDAL VTRQVAGRIS EVFPIVEDLP
ISKKNMFGIY IQMAEVCMSE DGALNDLLYS VFTTSCLVSL DTGYGNEFVE VLIAMVEQDG
GSGGKRIGNV METFRMIFHS LQDSESRGRE RLIWNFLSFL SRIRMGRDMG DLNSIFLKFI
VKYPETIELY SNFILINKID FPLHTLHGIS SFGFMKRFYS VLFNKVRKER HDKAHVDKLI
SEFLKFFLAT KNKELIGILP LVPYIPSKRE VLYVLYEIYS FLFEKEVIEH VGLFLLKTPA
LVGISSSIYY NVRYLRHLAT RLSLVDVEPR MVVFLGIVYY CESKKLYNFN YTGILEYIQD
EDGIRMSRDG LVGVIELIHS GYISRSHEFT LSYVNSLLTI ALKPKTIETT LVIIEIILRR
ILEKEEKIIF MKGIHQRFQE LFVLLSSKRF LSDEVSDSYR RLYRSIVERI KCAPNFYNYV
VLCLADISFF DGEFPRGHFK SFNDLYNHTL SRMGVVEGFP DIFMVDHGWS CSENTDKAVS
GPFLHRVCGS GKEEETKPRE TKSHNMYDII RTGTNDSVMS LESSTGSISL HSSAPMPSIS
RKAWLEMLDE GIRKREKSVS WLIDVIYTRR SQSSTIRTVL DLLKLRLRNK FEYEDLYILL
KAYNILSIRE NDSEEFLKHA LHRGLDFKTD PAICYKLSME TNGFYRFFFR ALHLAVSNLP
CNEDLSFPER TQLVSRFDTA DLVHIQNTFK QKMVQKLLER SRSPSYRTYF FNVDSLGVID
SLTIIRRLDD PSLVSRAFER LRESKNEMLF YVPQLVQMLR YKKVFEMAFS TLKELAKDEY
VAHQLIWNLK ANLYVDGRAA VNNYHGTFVR CIEEIMKEMP DGSRDIFLKE EEFISSLTKI
SSELTPHLRS SKDEKRRRIN EYLSRIKLHP GIYIPFYPDL KIIEIVNGSA RALQSHSKVP
FMASFRVQDP GGQISIKQLI FKSGDDCRQD MLALQIISMF ESIFKQANLD IFLYPYKVMA
TSSGTGIIEV IPNSKSRDQI GKENINNLLE YFEYKFGFKE SEGYLTAICN FASSLAGYSL
VGYFLNIKDR HNGNIMIDDQ GRMIHIDFGY MLEMSPGNLN IEAPLKLTKE IEELLGGTSG
KGFEIYQELM VKGFLALRRR SKDLVMMVDS FVDSELPCYR RNAVENFILR FRFELSDKNA
RRFVLSLIAE SSQKFRTWMY DQYQKITNNI AF
