ID A0A397GAL2_9EURO Unreviewed; 1939 AA.
AC A0A397GAL2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 13-SEP-2023, entry version 16.
DE RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN ORFNames=CDV56_102102 {ECO:0000313|EMBL:RHZ48052.1};
OS Aspergillus thermomutatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ48052.1, ECO:0000313|Proteomes:UP000215305};
RN [1] {ECO:0000313|EMBL:RHZ48052.1, ECO:0000313|Proteomes:UP000215305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ48052.1,
RC ECO:0000313|Proteomes:UP000215305};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequence of azole-resistant Aspergillus thermomutatus
RT (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT aspirate.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:RHZ48052.1}.
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DR EMBL; NKHU02000206; RHZ48052.1; -; Genomic_DNA.
DR STRING; 41047.A0A397GAL2; -.
DR VEuPathDB; FungiDB:CDV56_102102; -.
DR OrthoDB; 147843at2759; -.
DR Proteomes; UP000215305; 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:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05167; PI4Kc_III_alpha; 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; IPR045495; PI4K_N.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048:SF15; PHOSPHATIDYLINOSITOL 4-KINASE ALPHA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF19274; PI4K_N; 1.
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; PS00915; PI3_4_KINASE_1; 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 Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000215305};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1340..1523
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1636..1923
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 1613..1655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1630..1655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1939 AA; 216289 MW; 89D2BBCC46401916 CRC64;
MDCFFTNIRR CALDKLATLS VTEAGCDDLS DLTRLSQQCP HPSSRSNVSP DGVVNNKTTI
SQLPMDSREL DVLLALCDAA PSVTEFEHAS KLATQLFPYL PESHSQCFRP SPFLNNMKPS
PWETLTRKLT SSLLSLGSNH PALRSTTLSA VNEYLYSCAD SIDAITPLQR YDSAGDNYGA
VQEHKRILSL AVSLVGFLEA SAQFPSLWSA SEKLQIVEHV RSMLSEGFMV AIETASSTVR
NASMADPTLR DWRRYTRRYA ANRRPLGAML LQQGFMRFVK SCATSLVGAQ SLSDEELLDD
YMNGVGIARS NDDAEITLID RITEIIADEI QLLEDGSDYL QLGSPWQKQL TFSVKSFALI
GYLNCVILSG NAANSGAFLS WLEDALADPN QMASLELATA TLKSIAIISR MSLASASSGS
RSLLRFIIEG CVLGEHTGSV AGKCLAQVLG ILSQDAIITT LYSLGNALSP GSGTDKYYHG
QLLNENAGHP DSVSSIPPPV GNGSVVSLSA IGDHDNATCR NILRAIVTIA TSSNDEKISA
LAQSMLLQKI GKVNIAVDSL IIRETASLSL STGQAEFQLL LKFYDRAYQD GITRNLCDVM
NAVKGAMTYI SLALRRDSPL FRVYLIHLLE CIVNKGDAIG EGERQKEVIL APEAISFLLR
PLALLISSDE EETGTQQTDV IFDEDITALF RDAWFNISVH GISTQSVVAQ SHIRELRLLA
KHSPPLIAES RMEMLESDVE LNTILRRGMS PQRLIELKRI LMAELPDCES GIKHLNYPKV
VFLNASLLVE SLRASSGNCT KVLSYFRDPA LTTADMANCM SSIADKVVAD YLSLTLSAND
ENFSVPYLSK ELAQFFMACC HRIERVQSVA MLCADKIIRE CPSALCDKHS LFALLELLTV
MWLSCLEEEL DEFEWKASCA SPMGIVKVDL ADNYNARKRT LNTLLERAKA WVAAVIDIAP
LDTYLSISND TVDGSHILLG RSFALDMGST IPRSDQRLGC IQSSGISRVN VASDFIAQYT
IRQQYRASDL LVTKYLEQGS IENNGEDCGK IARGLLESSE HVKNMLHRLH DQLKAGNGVV
LSEFRDTLRR AAAVLCGSDY FQPSILHYLV ILPFQLFSEE SMNVGVALWL GAIHENPKLE
PRILAEVIEA WEETIQRRRG LFDLSFDYVD PMYAKIELLP SDKALLLKKQ QKAQATFAPH
LIALRFFESH FNAVRLNSAQ NSRLFGRLID RTTVGLLQTS GHPLARELHF RIVLFGLRVI
QDSYQPDKVA LWKLSDQILS AALNWFKHPP RWSFGGNRLQ VKAEDQILDD VARALGRLST
VPSPTRGNFK PLQYKHDLLQ LLIEHERSRL RVWLFPLEGE RKHFQISGNR NSAEEAIHLL
RLAWTESPGL AIQLSSRYSS SKMKNDIRWL LLNFPEKALD EPSSLEVMLG AALPSDVSFQ
LKYAMRALES HPIDVRFYFV PQLVQALRYD ALGYVERYIL ETAKQSQLFA HQVIWNMKAN
SYKDEDSQIP DPLKPTLDRF MDTLISSFSD EERDFYEREF SFFNDITGIS GKLRPYIKKS
KPEKKAKIEE ELRKIKVEIG VYLPSNPDGV VVGIDRKSGK PLQSHAKAPY MATFRIQKTR
NRGDERDSQG PSRPNTSSHD DSTKTLSAPL HSPSSQETYE VWQSAIFKVG DDCRQDMLAL
QMIAAFRSIF ASAGLDVWVF PYRVTSTAPG CGVIDVLPNS ISRDMLGREA VNGLYDYFIS
KYGGEHSTRF QEARTNFVKS MAAYSVISYL LQFKDRHNGN IMIDDAGHII HIDFGFCFDI
APGGVRFERA PFKLTSEMVA VMSGTSHPHI HSHGGSNGGH SSNPTSTQPY RWFESLVIKA
FLASRPFCTK LSHIVSLMLD SGLPCFKPDT LKNFRDRFVL EKNEREAAEY MRDLIRKSYM
SVSTKGYDQF QLLTNGIPY
//