ID A0A0M8MYM0_9HYPO Unreviewed; 957 AA.
AC A0A0M8MYM0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Phosphatidylinositol 4-kinase pik1 {ECO:0000313|EMBL:KOS19507.1};
GN ORFNames=ESCO_001274 {ECO:0000313|EMBL:KOS19507.1};
OS Escovopsis weberi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS19507.1, ECO:0000313|Proteomes:UP000053831};
RN [1] {ECO:0000313|EMBL:KOS19507.1, ECO:0000313|Proteomes:UP000053831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA Currie C., Gerardo N.M.;
RT "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT ant agriculture.";
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:KOS19507.1}.
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DR EMBL; LGSR01000020; KOS19507.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8MYM0; -.
DR STRING; 150374.A0A0M8MYM0; -.
DR OrthoDB; 147843at2759; -.
DR Proteomes; UP000053831; 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 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; 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.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KOS19507.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053831};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 668..957
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 157..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 957 AA; 105647 MW; A67EFC46F37C7B29 CRC64;
MSWDLLQRFL ESDVFNSNPF LAVSYLSRYA SHVGIHYVLC NKLRQFPYED IEFFLPQLCH
LIISDDNESM ALEGFLLDLC EESVTAALLS ISFQTCRRVY NKVQHIVFGL SDTARPEKIK
ENVLSVTVLS SFVLASVALP MIPRWAGPLA IAQARKPQPW TDSTLENAET SKLQRANTIS
STGSKTRRAK ELKLQSAPLP NATTASRHAA SHSALPTPTT PSQPNPKPGK DSKRPPILEM
RSLEARLSTA SLPLPSPKPP SRPNTPASSG SSSRTMDNFQ RRHSHHAKVL HNPLVNMTHI
QKTKLLRQHY FRSQTQFLSA LEGISNRLVA VPKAARMSAL RAELALIARD LPAEIDIPVI
CPPTLVDGAP GKSRHHRIVR LNPAEATVLN SAEKVPYLLM VEVLRDDFTF DPDTPDNQRL
LTSLSASGAS KRLFDLSSEL PRMTQSRAPE PVVDSVFEPT SGDLGSSPLL TAYDDYPIAS
PNSKQSSDQR HSSGTTTTST TFDVATPRTS ETLTSRSNSP GSRRLVAGMG RNTFPDQPDF
SALATHMRTA SQMLAQLEAT SGKRPRHEVA AIRAKIIANM QSLEEQSFDQ DEQGPTFDTI
IAKATTSGAV SGMGATLDEE APETPPIDPN INARAGRERM ENDIKTGGVQ RRGDRDDPSA
AVFGEAWETK KERIRKSSPY GWMKNWDLMS VIVKTGADLR QEAFACQLIS VCHKIWVDAK
VDVWVKLMRI LVTGESSGLI ETITNGVSLH SLKRSLTLAS IESGNLPRHR FATLKDHFVK
AFGQPDSEPY KAGIDAFKRS LAAYSIISYV LQLKDRHNGN VLIDSEGHII HIDFGFMLSN
SPGSVGFEAA PFKLTHERHS HHAKVLHNPL VNMTHIQKTK LLRQHYFRSQ TQFLSALEGI
SNRLVAVPKA ARMSALRAEL ALIARDLPAE IDIPVICPPT LVDGARFLIR LMRRSAE
//
