ID A7RRA6_NEMVE Unreviewed; 1310 AA.
AC A7RRA6;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDO45977.1};
GN ORFNames=NEMVEDRAFT_v1g90881 {ECO:0000313|EMBL:EDO45977.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO45977.1, ECO:0000313|Proteomes:UP000001593};
RN [1] {ECO:0000313|EMBL:EDO45977.1, ECO:0000313|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
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; DS469531; EDO45977.1; -; Genomic_DNA.
DR RefSeq; XP_001638040.1; XM_001637990.1.
DR STRING; 45351.A7RRA6; -.
DR EnsemblMetazoa; EDO45977; EDO45977; NEMVEDRAFT_v1g90881.
DR eggNOG; KOG0905; Eukaryota.
DR HOGENOM; CLU_002191_0_0_1; -.
DR InParanoid; A7RRA6; -.
DR OMA; QMAAGFR; -.
DR PhylomeDB; A7RRA6; -.
DR Proteomes; UP000001593; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IBA:GO_Central.
DR GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IBA:GO_Central.
DR GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04012; C2A_PI3K_class_II; 1.
DR CDD; cd08381; C2B_PI3K_class_II; 1.
DR CDD; cd05166; PI3Kc_II; 1.
DR CDD; cd06883; PX_PI3K_C2; 1.
DR Gene3D; 3.10.20.770; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
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; 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; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048:SF14; LD28067P; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00142; PI3K_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; 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; PS00915; PI3_4_KINASE_1; 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 Reference proteome {ECO:0000313|Proteomes:UP000001593};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 60..150
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 311..462
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 480..656
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 723..1001
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1046..1162
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 1183..1303
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
SQ SEQUENCE 1310 AA; 149057 MW; 73A6672A8C4DB57A CRC64;
MFLGGGLFEV AKERDAEVIA FGEMLSEVRS NFHWYESSNR GYVLSPALPS RFGKTICNRE
TEVVVVIFTE GRRDTFRFAI DTWASVKEVL ELTLSCLSNS DVNIEHASTT HVLKICGRSE
YLEAQRKLVE YEYIQECLKF QKEVQFVLLE NEKVSRHLAR TASDDEIDLV PRSYKDFFNL
SHTTAVSQYG LTVLVESFTE ETSRLLQEAT SLVNPKFEPS PIIQLTKAIC STLASIETAD
IHVAVDALNL FHEVNKNSAV LNVTILKNLL SNLTDSVFLL IEMYCDAFDT EFASSQISRP
GLSGTLDVSS MTDKLKVHIS SAHRIPLYWK QDFENFSVDG GVYYGGCLLC PIETTTQSKL
TRKFSELLQW GDWLKFDIPV KRLPRESRLC LTLYGTKPSS KGNPSARSAL GWVALQLFNF
NGVLLTGTQI LGLWPDSKAN PVGSCTSNLL HPNSVLLLVT FERYLSEIVF PDCSDFPGFD
DMDHCIPEAD YGLFEEILMK DLFNELKPNE RSILWEHRFY CRSVPRALPL VLSSAPSWEI
QSLPEIYKLL HTWSPMSPVD AMELLKVNFP DRHVRSMAVR WMANFSDDEL CDYLPQLVQA
LKYEIYHDSA LTRFLVRRAL GNVRLMHLLF WFLKDKISEP QFGQRFQVIL GGLLNICGEA
QKEEFTFQDD LVTELIKVAR KVKSAKDSAR NNILQQELAA LAGKLCCVFR LPITPSLEVV
GMDVRSCGYF TSNSAPLRLV FRNVDPFGEN VNVIFKMGDD MRQDTLTMQL VGIMNKIWLQ
EGLDLKIITY QCMATGPGMG MIEIVSDSQT LREIHTEFGL TGSFKDESIN RWLLKFNPDE
KEYRRAVENF TASCAGYCVA TYVLGICDRH NDNIMIHRSG HLFHIDFSKI LGHAQMFGNF
KRDRAPFVLT PDMAYVINGG YRPSPRFQHF IDLCSRAFNL IRRHSNLFLN LLSLMLNSGI
GSLGNVSDLR YIRDSLLPQE SEAEATAAFT RLIESSLSSW FTQVNFFIHN VAQIRDVSQL
KRTSSGNASI SLLSFALKTY TLEMDGFIES ARVVDYQKRY NTEKYYIYVI NICRANSDQA
TFVFRRFGHF IELHAKLSEL YPDIALPRLP ARIYLGRSQI RTVAERRRAE LDTFLRHLLM
MPQEISESDV LYTFLHPIPE VKSSSSCVID VLIVFSLWRS PCVSGQIKLS IRHERGALRV
MVMHAKDLSS RNSSTAGDPY VKLYLLPDPS KTTKLKTKIA KKSQNPTYNE TLVYSNLSAA
DLKTRHLQVT VWDHDRVGEN DFMGGVVINL ADMDSSINIT NWYPLKDIRS
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