ID I2JZ28_DEKBR Unreviewed; 597 AA.
AC I2JZ28;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 2.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Phosphatidylinositol 3-kinase Pdd1p {ECO:0000313|EMBL:EIF48230.1};
GN ORFNames=AWRI1499_1818 {ECO:0000313|EMBL:EIF48230.1};
OS Brettanomyces bruxellensis AWRI1499.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Brettanomyces.
OX NCBI_TaxID=1124627 {ECO:0000313|EMBL:EIF48230.1, ECO:0000313|Proteomes:UP000004997};
RN [1] {ECO:0000313|EMBL:EIF48230.1, ECO:0000313|Proteomes:UP000004997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI1499 {ECO:0000313|EMBL:EIF48230.1,
RC ECO:0000313|Proteomes:UP000004997};
RX PubMed=22470482; DOI=10.1371/journal.pone.0033840;
RA Curtin C.D., Borneman A.R., Chambers P.J., Pretorius I.S.;
RT "De-Novo Assembly and Analysis of the Heterozygous Triploid Genome of the
RT Wine Spoilage Yeast Dekkera bruxellensis AWRI1499.";
RL PLoS ONE 7:E33840-E33840(2012).
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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:EIF48230.1}.
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DR EMBL; AHIQ01000098; EIF48230.1; -; Genomic_DNA.
DR Proteomes; UP000004997; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.150; C2 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; IPR002420; PI3K-type_C2_dom.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048:SF7; PHOSPHATIDYLINOSITOL 3-KINASE CATALYTIC SUBUNIT TYPE 3; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR PROSITE; PS51547; C2_PI3K; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:EIF48230.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004997};
KW Transferase {ECO:0000313|EMBL:EIF48230.1}.
FT DOMAIN 16..232
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 369..597
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT UNSURE 220
FT /note="I or L"
FT /evidence="ECO:0000313|EMBL:EIF48230.1"
SQ SEQUENCE 597 AA; 67948 MW; 8A1A245927495123 CRC64;
MMQTKMFINF CLSKDLHIPF RLKLIGLSGF TRQLFDIIYK TTTDGLDDAT ANVVRAKIEN
TLDERCSLIA TISIESGIGK GLTCSVVSTI KFDSSIYVGT NIXKSGXKXX XTNKEQXRXE
WINLPIDYSK LPLDSRLLIK LYSSEPRSGK XLFIGYAAID LFDVNGGYTL QTGYQSLKVT
IIGGSNVKSE TDGISPRTKN LSSTLSRLEE KLGERRKGNL PSTDWLNNMT FEAIEKLNSE
EIERIKEFSG NISMAELPRQ GALFVDIELV KFEMPIVFSD IKYAPLHIPA LVSTLEKGEI
TGNNGNKVNN LKAGTNDFNR ITYDNREEFN KNPSFSVFDP EQYRVNISED PIEYKFRKLE
RTHQLSSLDK DLKPTLKVRA KLDAILKKQF FEKLSQQEKN LIWKFRFFLL NGLVINGSNE
QYNNFIINFI KCIDWDGDFE VKEFLTIIRD LDTRSGGSNL FIQELTIVDC LELLSKVYXN
KIVRGMAIKR LRMASDEDLE LFMVQLVHSI QNEQEIRIND SDGDGGASES KYDDFVDEFE
AQLLQGAANG GYQLVEKEXE IADDPIXRLL YSPRLFELSK KVAKVPRTNI SAKRFHH
//
