ID A0A369GNF5_9HYPO Unreviewed; 1426 AA.
AC A0A369GNF5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=PI3K/PI4K catalytic domain-containing protein {ECO:0000259|PROSITE:PS50290};
GN ORFNames=CP532_0969 {ECO:0000313|EMBL:RDA84493.1};
OS Ophiocordyceps camponoti-leonardi (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2039875 {ECO:0000313|EMBL:RDA84493.1, ECO:0000313|Proteomes:UP000252748};
RN [1] {ECO:0000313|EMBL:RDA84493.1, ECO:0000313|Proteomes:UP000252748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 80369 {ECO:0000313|EMBL:RDA84493.1,
RC ECO:0000313|Proteomes:UP000252748};
RA Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA Luangsa-Ard J.-J., Giraud T.;
RT "A genome scan of diversifying selection in the zombie-ant fungus
RT Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT coevolution and host-specificity.";
RL Submitted (OCT-2017) 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:RDA84493.1}.
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DR EMBL; PDHP01000117; RDA84493.1; -; Genomic_DNA.
DR STRING; 2039875.A0A369GNF5; -.
DR Proteomes; UP000252748; Unassembled WGS sequence.
DR GO; GO:0005681; C:spliceosomal complex; IEA:InterPro.
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:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; 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; 1.10.20.10; Histone, subunit A; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003958; CBFA_NFYB_domain.
DR InterPro; IPR006973; Cwf_Cwc_15.
DR InterPro; IPR009072; Histone-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; 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; PF00808; CBFD_NFYB_HMF; 1.
DR Pfam; PF04889; Cwf_Cwc_15; 2.
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; SSF47113; Histone-fold; 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.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000252748};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 961..1237
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1322..1369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..952
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1323..1362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1426 AA; 155630 MW; 8E463057F980DE5E CRC64;
MAAEENYAPK SPDLSSFDSP GPTLPASQIA PYPAFSPPLL SSSFPSPVAA AAAAAAAAAA
AAAAGRAPDG YSPGAYRSFS AYPPPSPPVK AEFRSHSTSS QYLPPSPLRP APFGLHSPPQ
YQTAHHQQRL HRPLPPYLQS AYQHPAPPLA SETDMPPRRA VEAAPPPVAE PSPVKTKFPT
ARIKRIMQAD EEVGKVAQQT PIAVGKALEL FMIQLVTKSA DVAKEKGSKR VTAPMLKHVV
ETDDQWDFLR DIVSRHESSE KEGSRAKAKT ESESDEEFVE PRKRGRGAGR KKKARYADHV
GIHHVLCNKL RQFPYEDIEF FLPQLCHLII SVDNESMALE EFLLDLCEES ATAALLTFWL
FQTYLHDLSQ NPQSGPFQTC RRVYNKVQHI VFGLADTARH GKIKENVLPV TVLSSFVLAS
VALPLIPRWA GPLAVAQARK PQPVTDVAPD SAYSPKPVRA QTVSVSTTKS KRAKELRKST
APEAAGSSDL RSHSSRTHSQ SATSTAKRAK TPTGTKRPSV LNLESLEARA SSASLPLPSP
KPTTRPATPA SADMPPADGI YRRHSHHIKA SRNADDLTLV QKTRLLRSHY FRSQTQFLTA
LEGISNRLVI VPKPARMSAL RAELALVSRH LPAEVDVPVI CPPTLVNGSP GKSRHHRIVR
LNPAEATVLN SAEKVPYLLM VEVLRDDFTF DPDTADNRRL LAMLLDGGGT SRRLFDLSSE
TPKMSPTVAR APEPIVDSVF EPTSGDLGSS PLLKAEDEVP ARYGTTSRQQ TQAHTHTGQR
LSSGATTQAS STMLEVVSPR TSGGASTSRS SSPSSRRKMT VSLPRNVAAA ADQPDFSALA
THMRTASQML AQLDATSGKR PKHEVAAIRA KIIASMQSLE EQSFEMDDQG PTFDAIIAKT
GGGGGAPDSA DLDEEDGGPL DSAPNASAGR ERMENDIKTG GVQRRGDRDD PSAAVFGEAW
EAKKERIRKS SPYGWMKNWD LVSVIVKTGA DLRQEAFACQ LIDVCHRIWV DAGVDVWVKL
MRILVTGESS GLIETITNGV SLHSLKRSLT LDSAPSARQR IATLRDHFLK AFGQPESEPY
RAGVDAFKRS LAAYSIISYI LQLKDRHNGN VLIDSEGHII HIDFGFMLSN SPGSVGFEAA
PFKLTHEYVD VLGGIGSPDF EDYKKLCKQA FQALRRSADN IIDLVAMMGR DSKMPCFSVG
VAHATNSLRQ RFQLHLSAVE AEQFVETDLV GKSYGSYYTR LIGRDGLWHA RGKEALRGPA
YHQRLLPAHK QLKYRQAGQG GDADDDGSRR DLAAELLAAE AEAAAARRPG GKPLAGLVEA
VNEATREADD ENGDDEGGNR RSDGDDGKRQ RDEARAQAEA QERERSIALG NPLLNKQDFS
IKRRWDDDVV FKNQARGTEE KGKKKEFVND LLRSDFHRRF MSKYVR
//
