ID A0A139I0K0_9PEZI Unreviewed; 1003 AA.
AC A0A139I0K0;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN ORFNames=AC579_7572 {ECO:0000313|EMBL:KXT08264.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT08264.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXT08264.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT08264.1,
RC ECO:0000313|Proteomes:UP000073492};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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};
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:KXT08264.1}.
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DR EMBL; LFZO01000468; KXT08264.1; -; Genomic_DNA.
DR EMBL; LFZO01000468; KXT08267.1; -; Genomic_DNA.
DR EMBL; LFZO01000468; KXT08269.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139I0K0; -.
DR STRING; 113226.A0A139I0K0; -.
DR Proteomes; UP000073492; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000073492};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..128
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 709..988
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 184..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1003 AA; 109983 MW; 94DE5E24787FAD24 CRC64;
MSWNLLERFI QSEHFNRDPS LTVSYLALTA IYTASRYAEH VGIHYVLCSK LRGFSYEEIE
FFLPQLCHLV ISIDNESMAL EEFILDLCEE SVNGALLTFW LFQTYLHDLS SKPASNAFQT
CRRLYNKVQH IVFGGGEPLR RPRIHENVLP VTVLSTLVLA GIGMPLLPQH AGPLAIAQAR
RPRPIEEGGA GSDATPSIQK QGLGRSATVT GNTSGAARAR PQTGDGRDLP RRKSRKPADI
VVNGAKFSAS TPNTPALATS GHAERKASGH VPRHSLAIAM SSQGMNSSSS LPEHQRKPSR
PALSLPDSPG VPRRIAGDRE LSRRHSQMLR PVTPSSMSRN QKIRALRQNY FRHESQFLTA
LEGISNRLVS VPKAARLSAL RAELGLIAQD LPAEVDIPLI CPATLVDGTA SRSRHHRIVR
LNPAEATSLN SAEKVPYLLM LEVIREDFDF DPESQQNRDL LAKLLSERGK QKRRLFDTTD
AARQAAITSP LEKTTSDSVL EPTGGDLSSA ALLEDLDNPA KSNSPKLQAA LANSKEPPRL
SSGVSTISTA TVPTPRNSDG LGVRPDSGGR SSPYLRPQQS TQADVSALAD HMRTASQMLA
QLDLSASKRP KAEVAAIRAK IIASMQSLEE QSFLSDEQGP SFETIMAKTG SDPANADDMG
ENLDEPTGTD LVNTGKGAAR MENDAMTAGI QRTGDRDDPS AATFGEAWEQ KKERIRRSSP
YGWIKHWDLI SVIVKTGADL RQEAFACQLI AVCSKIFAEH AVDVWVKNMR ILVTGETSGL
IETITNAVSL HSLKRSLTIA SIATGTNPKK RIATLQDHYA KTFGPADSPA YAKAIDCFIR
SLAAYSIISY VLQLKDRHNG NILIDSDGHA IHIDFGFMLS NSPGNMGFEA APFKLTLEYV
ELLGGPEGEA FVRFKELMKD AFQALRREAE RIITLVELMG RESKMPCYGG GLINVVSALR
ARFVLEKSKE EARDWVEELV NKSIGSYYTR LYDTFQYRTQ GIY
//
