ID A0A2B4S5G5_STYPI Unreviewed; 1039 AA.
AC A0A2B4S5G5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform {ECO:0000313|EMBL:PFX24040.1};
GN Name=Pik3cb {ECO:0000313|EMBL:PFX24040.1};
GN ORFNames=AWC38_SpisGene11379 {ECO:0000313|EMBL:PFX24040.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX24040.1, ECO:0000313|Proteomes:UP000225706};
RN [1] {ECO:0000313|Proteomes:UP000225706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA Tambutte S., Allemand D., Aranda M.;
RT "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT digitifera provides evidence for extensive differences between species of
RT corals.";
RL bioRxiv 0:0-0(2017).
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00879}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PFX24040.1}.
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DR EMBL; LSMT01000188; PFX24040.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B4S5G5; -.
DR STRING; 50429.A0A2B4S5G5; -.
DR EnsemblMetazoa; XM_022937487.1; XP_022793222.1; LOC111332193.
DR OrthoDB; 10350at2759; -.
DR Proteomes; UP000225706; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05165; PI3Kc_I; 1.
DR Gene3D; 3.10.20.770; -; 1.
DR Gene3D; 2.60.40.150; C2 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 InterPro; IPR016024; ARM-type_fold.
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; IPR003113; PI3K_ABD.
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; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR PANTHER; PTHR10048:SF118; PI-3 KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF02192; PI3K_p85B; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00143; PI3K_p85B; 1.
DR SMART; SM00144; PI3K_rbd; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 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; PS51544; PI3K_ABD; 1.
DR PROSITE; PS51546; PI3K_RBD; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PFX24040.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000225706};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 15..104
FT /note="PI3K-ABD"
FT /evidence="ECO:0000259|PROSITE:PS51544"
FT DOMAIN 186..281
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 321..482
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 497..674
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 744..1023
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 1039 AA; 119453 MW; B66AC4F88C1D6E5F CRC64;
MPPGLRRNFW DDYEPASVVN VDCFLPTGVV IQLQVRIEAP LSEIKSRLWR EASNYPLFNF
LKDGTNYIFV CVNQRGKQEE LLDETRQLID VRPFRPLLKL IQKQGDNEEK LFNSHIGNLI
GKSLHEFDQM QNTEVDDFRR KYRQFAERIA CERRQLDWIG RAMYAYPPEV ESTDPPECIE
KNLMENRRFL VNVAIKNNRA SIKDMHAFNV PADAYPDELL VLVLRKRGAI MGVLDLDKPC
DYVLKIVGQE SYLLGNYPLL QYTYIRTCVS KGIRPMLSLV LRSSLQVEVL DVSDLCRRVQ
GTRAPRLPDK PQSASLSLWS IEQQVRIKIT SAKNVNAGDL MRVGVRAGIY HGGEALCDIK
STRPENGANA TWNEFLDFDL RVADIPRMAR LCLVIYGVTS SPQKKSKKKK EETIPVAWVN
TTLFDYQGKL RQGPMKLFAW PVPETMADQL NPVGTVVSNI DTVTSVSLEI AFSSYSHPVI
YPTFDKIAEL AANVTDYDIF GGANDSVLQQ LRQIVNREPL APIFEQEKEL VWQRRIDCRE
HFPHALAKLL CCAKWNSNKD VAMMQILLQT WPKLEPEVAL ELLDYTYADK EVRKIAVRCI
EKMSDSEIQQ YLLQLVQVLK YESYLDCDLA EFLLGRALKN QHFGHELFWL LRAEMENPEV
SVRFGLMLEA YCRGAPTHMK SLQHQAQALS KMKAVTELLQ LIDREKKEKG LATMKELLRQ
KTYQGALSKI SSPLNPRYKL RNLNVDQCKF MDSKMRPLYL VFENMDELGD LVRIIFKNGD
DLRQDMLTLQ LFKIMDRIWQ NEGLDLGMIP YGCLSTGSSI GMIEVVHQAE TIAKLQKKKG
MTAVFAKECI WNWFKDYHST EDELNEAVRL FTLSCAGYCV ATYVLGVGDR HSDNIMVKNT
GQLFHIDFGH ILGNFKSKFG VRRERVPFVL TDHFVHVISL GKGKETDEFR EFKQLCEDAF
LILRRKGPLL INLFVMMLSA GLPELRSLDD IGYLRKTLLL PVSEEDALRD FRSKFDHAIN
NSFSTTMNWF AHNVKRDNP
//
