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Database: UniProt
Entry: A0A085NQX8_9BILA
LinkDB: A0A085NQX8_9BILA
Original site: A0A085NQX8_9BILA 
ID   A0A085NQX8_9BILA        Unreviewed;      1923 AA.
AC   A0A085NQX8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFD71874.1};
GN   ORFNames=M514_08131 {ECO:0000313|EMBL:KFD71874.1};
OS   Trichuris suis (pig whipworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichuridae; Trichuris.
OX   NCBI_TaxID=68888 {ECO:0000313|EMBL:KFD71874.1};
RN   [1] {ECO:0000313|EMBL:KFD71874.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DCEP-RM93F {ECO:0000313|EMBL:KFD71874.1};
RX   PubMed=24929829; DOI=10.1038/ng.3012;
RA   Jex A.R., Nejsum P., Schwarz E.M., Hu L., Young N.D., Hall R.S.,
RA   Korhonen P.K., Liao S., Thamsborg S., Xia J., Xu P., Wang S.,
RA   Scheerlinck J.P., Hofmann A., Sternberg P.W., Wang J., Gasser R.B.;
RT   "Genome and transcriptome of the porcine whipworm Trichuris suis.";
RL   Nat. Genet. 46:701-706(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-
CC         [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC         COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:61930; EC=3.5.1.98;
CC         Evidence={ECO:0000256|ARBA:ARBA00001028};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-
CC         phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC         inositol-3,4-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:18373,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57658,
CC         ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.154;
CC         Evidence={ECO:0000256|ARBA:ARBA00029297};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18374;
CC         Evidence={ECO:0000256|ARBA:ARBA00029297};
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-3-phosphate) + ADP +
CC         H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216;
CC         EC=2.7.1.137; Evidence={ECO:0000256|ARBA:ARBA00023985};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710;
CC         Evidence={ECO:0000256|ARBA:ARBA00023985};
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00879}.
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DR   EMBL; KL367480; KFD71874.1; -; Genomic_DNA.
DR   Proteomes; UP000030758; Unassembled WGS sequence.
DR   GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0008193; F:tRNA guanylyltransferase activity; IEA:InterPro.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR   Gene3D; 3.30.70.3000; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 2.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 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   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
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; IPR002420; PI3K-type_C2_dom.
DR   InterPro; IPR001263; PI3K_accessory_dom.
DR   InterPro; IPR042236; PI3K_accessory_sf.
DR   InterPro; IPR000341; PI3K_Ras-bd_dom.
DR   InterPro; IPR015433; PI_Kinase.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR025845; Thg1_C_dom.
DR   InterPro; IPR024956; tRNAHis_GuaTrfase_cat.
DR   InterPro; IPR038469; tRNAHis_GuaTrfase_Thg1_sf.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR   PANTHER; PTHR10048:SF14; PHOSPHATIDYLINOSITOL-4-PHOSPHATE 3-KINASE; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF00794; PI3K_rbd; 1.
DR   Pfam; PF00613; PI3Ka; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF04446; Thg1; 1.
DR   Pfam; PF14413; Thg1C; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00144; PI3K_rbd; 1.
DR   SMART; SM00145; PI3Ka; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS51547; C2_PI3K; 1.
DR   PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR   PROSITE; PS51546; PI3K_RBD; 1.
DR   PROSITE; PS51545; PIK_HELICAL; 1.
DR   PROSITE; PS50195; PX; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          414..503
FT                   /note="PI3K-RBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51546"
FT   DOMAIN          666..829
FT                   /note="C2 PI3K-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51547"
FT   DOMAIN          849..1028
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          1072..1370
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   DOMAIN          1409..1524
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   DOMAIN          1538..1683
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
SQ   SEQUENCE   1923 AA;  219143 MW;  5A27088F2B2F4099 CRC64;
     MTVSLHLQEP GFYPCSGDLT DFGVGRGKNY AVNVPLRRGL NDEQFIEIFD NILPRLKINF
     DPHAIVVQLG VDGLTGDPNQ AFNLTPTSYC VSLQRILALN LPCLLLGGGG YRPVNFAKCW
     AQLLSTVVGK PLLEDIPEHP FFPLYGPDFV LTIQAAERRS EHPMSIGDKE QVNDDDLISW
     VDPAILAREQ KIIEIKRLLA ASNQATPAFQ SRVPFTVFPS SYFASCRLEP LPQYGHLVQP
     RALPETPSNW NHSKTSALSR AVTCFENYDV PTRLPLGRSI SFENVTLLAP HPRREGSVPA
     PQISVRDESS SDLGFLSEFD PLIKADSSLG QDSSTVHLLV ASTSLDAEQE SKGHVPRPVI
     PFTCDSSFKI IDRTPVWLQQ ATELGSRVVA LRQDCTVFDQ LVIGERLSGY QPTVNSLKMT
     VHTKLGKPSP VVFTCDIASS VEQIIGCVLC SVGIQQEPLP IGQYALKLFN SDEYIAPFTS
     LCNYAFVHEC IKLGQDPELE LVSLPKAEPF PEWTSKLRHY VHCSSVKRDD VQVVLTTLAA
     ELEKLLQRAK NSQFSSRSVS QSIMALCALL QVEPVWLVRS VKSLQAACKS MSESRHVNCG
     CSEPTSDSKL SHDCGLFREL TSSVSSVVAS VTHMCAVYCQ SSDADFTVVC QKEADDSRET
     KDIVDMEENF TLTIESLHGI PQAWTTKYMR FSIKCHLIHG LREVGPSIRT SCGVAQHNFY
     DYLLFDSLIS FPLPVSALPR EVQLCLVLCG ERMEPCQPDG AQSQCQSSDD RLVEEQLCFS
     LLCLFASDGL LVEGARFVPF YEGSRVRPWL PPAPSFRSRQ GPICVVTFPT KNYRLKFPAL
     QASDDNVEPM DFHQLPPDSQ MLLEDIIENR GFRELDADEK DFVWEKRVYL TAMPEALPLV
     LSSAICWDWA CLTNLYSLLN VWTSLPAPLA IELLLPNFPD IRVREKAVQW LSRSDVDSMV
     DLLPQLVEAL WFEKSEHSAL AEQLLSYALQ SRRFAFALYW ELERRIRLLD RGTRCYLLQM
     VLVALLGEKF RSEAELQNQL VTKLECAGAL VKREAKDDRK MARQVIVMTH RDSYRFYFPE
     GIGGPIEPNR FLVASKSYLS ARQIFQAGDD LRQDFLVLQM IRLMDRLWLT DGIDLRMIVY
     RIIPLQARKG LIEIVRGAKT LREIQTEDGG VTGVLRGDSI QRWLQKQNPS ELEYHIVWLR
     KFACPLIGCD CNLKALKNFR CSCAGWSVGT YVLGVGDRHN DNVMITPRGH LFHIDFGKYL
     GDAQMFGSFK RDRVPFLLTD EMLYAINSSE SSSSSYFHEL VDLCCHALNV IRKHSTLFLN
     LMKLMLYADV PGLTPESIAY MRGNLWLECT DSEASVRFTR MIEETLRSKF PKLNFLVHAV
     VQSGRRSIST PSQQVLTFVP RVYTMQTDGV IKSVEIVGCE KWHTPEKIYM YKLRVDRENV
     KVPSYLYRSY NEFLELLEAV YYRFPLVKVH SLPRGRSLRS NVRVVALRRQ LEIRFFLRSL
     FMHAEEVAHS DLVYTFFHPI FRDERADIMS KTVQGTKPMN QSTVSGEIKV QVAFCQGMLE
     VFINHARNLV YKLIDVSFDR MMSLYYQSLI NGSHLPDTYV KCYLRPDRRR WSKKKTRIVR
     GTRDPTFNEM FIYRCLSSQL VTKALEITVW HHDILKENTF LGGIVIPMEN LCTISGFKIN
     EWFRLENRPT WKFEHLDTCL LDTWIVVRLD GCGFKGFSAE HNFSKPNDAR ALNLMSAAAK
     HVMSNHKDIR IAYGQSDEYS FVFWKRTNMW NRRMSKIISI LTSLFTSAYV FNWPNFFPDC
     TLKRPPCFDG RAVLYPNDAT MMDYLKWRQA DCHINNLYNT AFWKLVLELG WTCAEAQARL
     RGSTSADKNE LLFSMFNTNY NNEPQLFRKG TVLWRGQDGE TILSDNISLI ADSFWQDNEH
     LLR
//
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