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Database: UniProt
Entry: X6MF16_RETFI
LinkDB: X6MF16_RETFI
Original site: X6MF16_RETFI 
ID   X6MF16_RETFI            Unreviewed;       728 AA.
AC   X6MF16;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   13-SEP-2023, entry version 51.
DE   RecName: Full=phosphatidylinositol 3-kinase {ECO:0000256|ARBA:ARBA00012073};
DE            EC=2.7.1.137 {ECO:0000256|ARBA:ARBA00012073};
GN   ORFNames=RFI_24906 {ECO:0000313|EMBL:ETO12469.1};
OS   Reticulomyxa filosa.
OC   Eukaryota; Sar; Rhizaria; Retaria; Foraminifera; Monothalamids;
OC   Reticulomyxidae; Reticulomyxa.
OX   NCBI_TaxID=46433 {ECO:0000313|EMBL:ETO12469.1, ECO:0000313|Proteomes:UP000023152};
RN   [1] {ECO:0000313|EMBL:ETO12469.1, ECO:0000313|Proteomes:UP000023152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24332546;
RA   Glockner G., Hulsmann N., Schleicher M., Noegel A.A., Eichinger L.,
RA   Gallinger C., Pawlowski J., Sierra R., Euteneuer U., Pillet L.,
RA   Moustafa A., Platzer M., Groth M., Szafranski K., Schliwa M.;
RT   "The Genome of the Foraminiferan Reticulomyxa filosa.";
RL   Curr. Biol. 0:0-0(2013).
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC       {ECO:0000256|PIRNR:PIRNR000587}.
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:ETO12469.1}.
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DR   EMBL; ASPP01021379; ETO12469.1; -; Genomic_DNA.
DR   AlphaFoldDB; X6MF16; -.
DR   EnsemblProtists; ETO12469; ETO12469; RFI_24906.
DR   OMA; LHKFAQY; -.
DR   OrthoDB; 10350at2759; -.
DR   Proteomes; UP000023152; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00896; PI3Kc_III; 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; 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; IPR001263; PI3K_accessory_dom.
DR   InterPro; IPR042236; PI3K_accessory_sf.
DR   InterPro; IPR008290; PI3K_Vps34.
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; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF00613; PI3Ka; 1.
DR   PIRSF; PIRSF000587; PI3K_Vps34; 2.
DR   SMART; SM00145; PI3Ka; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR   PROSITE; PS51545; PIK_HELICAL; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR000587};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000587};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000587};
KW   Reference proteome {ECO:0000313|Proteomes:UP000023152};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000587};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        433..452
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          129..300
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          436..713
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   REGION          53..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          403..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..425
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   728 AA;  82563 MW;  BC9A82243C361A70 CRC64;
     MGIDDKDEHR FTATINGSNG MSAARGAAST TTSIVSSTTT SAATTPIATM ATTTTTTTTT
     TSSAVNTPSS TTPTTGTTTT TTTMPMTVVM DRDKGMNQSV WNLLTVYDPE AQLSNPVAMK
     DKKLLKHFED PHIKPNPEER ERLEKIINSP SRVLTEVDKQ LLWRFRNQLI SNNKALTKFL
     RCVSQSSEEE VDTAMELHLF RIGLLGGQFE NPKIRSYGIE VLRKADDIEL ESFIMQLTQA
     IRFESSHTAD LPQFLLDRSL LSKDFRLLNF FYWSVRVQSQ AEEESQANIY QELLKDIESK
     LKLRRPVFAM EIDRQKWLVA ELTDLSETIS KDKGRAEDKK ARLIALLSDP VGRFSCLKQF
     PYPVRMPVRP EYLVDGIIHD KCSVFKSALC PFLLCFRRVR EETPNQSETN GPTSSSIDSM
     DESRSATTAT TTITTTIKTI IIIITIIIII IIKNNNNNNN NNNNNNNNNN NNNDYHDTYR
     IIWKNGDDLR QDQLIIQMIK VMDDLLKRVN LDLCLTPYPV LATGLENGML EFVENSKAVA
     TILRDNDNDI SRYLLDNQKG KRFISQSVDT FVRSCAGYCV ITFLLGIGDR HLDNLLMTKD
     GRLFHIDFGF IYGEDPKPWP PPMKICKPMI DAMGGNTSQN YKLFTEHMCS CYLLLRKSAN
     LLLNLLSLMG QGDMETMEKN LNFVHQKFRL DLDDQQAAKS LLDLVKRSVS ALFPKAVDII
     HDWATYWR
//
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