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
//