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Database: UniProt
Entry: A0A177E3P9_ALTAL
LinkDB: A0A177E3P9_ALTAL
Original site: A0A177E3P9_ALTAL 
ID   A0A177E3P9_ALTAL        Unreviewed;       987 AA.
AC   A0A177E3P9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE            EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN   ORFNames=AA0117_g11890 {ECO:0000313|EMBL:RYN66176.1},
GN   CC77DRAFT_1015840 {ECO:0000313|EMBL:OAG26565.1};
OS   Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Alternaria; Alternaria alternata complex.
OX   NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG26565.1, ECO:0000313|Proteomes:UP000077248};
RN   [1] {ECO:0000313|EMBL:OAG26565.1, ECO:0000313|Proteomes:UP000077248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG26565.1,
RC   ECO:0000313|Proteomes:UP000077248};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000291422}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FERA 1177 {ECO:0000313|Proteomes:UP000291422};
RA   Armitage A.D., Cockerton H.M., Sreenivasaprasad S., Woodhall J., Lane C.,
RA   Harrison R.J., Clarkson J.P.;
RT   "Genomics, evolutionary history and diagnostics of the Alternaria alternata
RT   species group including apple and Asian pear pathotypes.";
RL   bioRxiv 0:0-0(2019).
RN   [3] {ECO:0000313|EMBL:RYN66176.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FERA 1177 {ECO:0000313|EMBL:RYN66176.1};
RA   Armitage A.D., Cockerton H.M., Sreenivasaprasad S., Woodhall J., Lane C.,
RA   Harrison R.J., Clarkson J.P.;
RT   "Genomics, evolutionary history and diagnostics of the Alternaria alternata
RT   species group including apple and Asian pear pathotypes.";
RL   J. ISSAAS 0:0-0(2019).
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 4-phosphate) + ADP +
CC         H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216;
CC         EC=2.7.1.67; Evidence={ECO:0000256|ARBA:ARBA00001686};
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DR   EMBL; KV441469; OAG26565.1; -; Genomic_DNA.
DR   EMBL; PDXD01000059; RYN66176.1; -; Genomic_DNA.
DR   RefSeq; XP_018391986.1; XM_018524102.1.
DR   STRING; 5599.A0A177E3P9; -.
DR   GeneID; 29109696; -.
DR   KEGG; aalt:CC77DRAFT_1015840; -.
DR   VEuPathDB; FungiDB:CC77DRAFT_1015840; -.
DR   OMA; TQDYVDV; -.
DR   OrthoDB; 147843at2759; -.
DR   Proteomes; UP000077248; Unassembled WGS sequence.
DR   Proteomes; UP000291422; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05168; PI4Kc_III_beta; 1.
DR   Gene3D; 6.10.140.1260; -; 1.
DR   Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR021601; Phosphatidylino_kinase_fungi.
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; IPR049160; PI4KB-PIK1_PIK.
DR   InterPro; IPR015433; PI_Kinase.
DR   PANTHER; PTHR10048:SF22; PHOSPHATIDYLINOSITOL 4-KINASE BETA; 1.
DR   PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF21245; PI4KB-PIK1_PIK; 1.
DR   Pfam; PF11522; Pik1; 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   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OAG26565.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077248};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..120
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          693..972
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   REGION          181..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          509..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          671..691
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..239
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..564
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   987 AA;  108611 MW;  5656994ECD4F2580 CRC64;
     MSWNLLERFI ESEHFNQDPS LAVAYLARYA DHVGIHYVLC SKLRQFAYEE LEFFLPQLCH
     LLISIDNESM ALEEFIIDLC EESVNGALLT FWLFQTYLHD LASAPNSIAF KTCRRIYNRV
     QRIVFGSAEP QRREKIKENV LPVTVLSSLV LASIAAPFLP AHAGPLAIAQ ARKPRPVEDI
     ISDNVQTAKV GRSKTVTGGS SRSKEKRVAA QHSDPEDGRS IKASSSRPRD PKELRKAAAR
     PPAAQRAPSM QHRPSLLSIA SEARLSSSSL PDFRDGKSSP LPTPPATAGL GPGPLQHGLR
     KSGLPPRPLT PTALTRTQKI RLLRSNYFRN ETQFLSALED ISNRLVVVPK PARLSALRAE
     LALIDQDLPA EVDIPLLSPP TLKDGIPSQS QHHRIVRINP AESTSLNSAE RVPYLLMVEV
     LEEDFDFDPD TEQNQQLLEK LMLEKGTSRR RLFDITNAEY LAFDRTPPNG SDSVFEPATG
     DLGSTSLIKD MDENDIASGM ARVTLPGATA NGKATAPRSS SGANTLSSVA TLSTPRTSDS
     QISRSNSPGP IRRMTIPANL NSRNQAVDQP DFSALATHMR TAAQMLAQLE ASGAKRPKGE
     VAAIKAKIIA SMQTLEEQNF LNEDQGPTFD TIMAESDPTA ITGEPEELED GLPVATNSGA
     GAARMENDLK TGGMRRKGDR DDPSAATFGE EWSAKRERIR RSSPYGHMKN WDLISVIVKT
     GADLRQEAFA CQLIDVCTKI WEEANVPVWT KRMRILVTGE SCGLIETITN GVSLHSLKRS
     LTLASIAAGT NPRKRIATLK DHWLKTFGEP DSEAYIAGVG CFARSLAAYS MICYVLQLKD
     RHNGNLLIDN MGHIIHIDFG FMLSNSPGSM GFEAAPFKLT QDYVDVLGGV TGSAFEEFKT
     LCKKAFQALR KDAERLIMLV DLMSKNSSMD CFKAGAQTVT NSLRARLMLH LSREEAEGFV
     EELVAKSVGS YYTRLYDTFQ YRTQGIY
//
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