ID S3BUQ5_OPHP1 Unreviewed; 1139 AA.
AC S3BUQ5;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN ORFNames=F503_01497 {ECO:0000313|EMBL:EPE03161.1};
OS Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE03161.1, ECO:0000313|Proteomes:UP000016923};
RN [1] {ECO:0000313|EMBL:EPE03161.1, ECO:0000313|Proteomes:UP000016923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE03161.1,
RC ECO:0000313|Proteomes:UP000016923};
RX PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA Robertson G., Birol I., Bohlmann J., Breuil C.;
RT "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT a comparison with the bark beetle-associated pine pathogen Grosmannia
RT clavigera.";
RL BMC Genomics 14:373-373(2013).
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; KE148170; EPE03161.1; -; Genomic_DNA.
DR AlphaFoldDB; S3BUQ5; -.
DR STRING; 1262450.S3BUQ5; -.
DR VEuPathDB; FungiDB:F503_01497; -.
DR eggNOG; KOG0903; Eukaryota.
DR HOGENOM; CLU_002446_2_0_1; -.
DR OMA; TQDYVDV; -.
DR OrthoDB; 147843at2759; -.
DR Proteomes; UP000016923; 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:UP000016923};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..120
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 844..1123
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 170..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1139 AA; 122960 MW; 89BD55034ABB4A44 CRC64;
MSWDLLQRFL DSDVFNSNPF LSVSYLSRYA DHIGIHHVLC NKLRQFPYED IEFFLPQLCH
LIISVDNDSM ALEEFLLDLC EESVTAALLT FWLFQTYLYD LSSNPQTQAF QTCRRVYNKV
QHIVFGLPDA SRREKITENA LPVTVLASFV LASIGLPGLP KLAGPMAIAQ ARKPAPPGET
NTAGGLSDTE QNDPPRRPTR AQTVTAASSK SRRLKDATGG SVGSGIGTRS GSGPASIAVA
TMSTPALHNA PEIIRSLPPL ESVARSPKQR KQPSSSRPGS SSSQLASPLP LRSPEQPRRS
IPPIVHTHAE LISVEARLSS ASLPLPDMRS PRMATRPATP VSAGLGIQDS PAALSRRHSH
HTKPRIVSVG DMTSEQKTRL LRQNYFRCET QFLRALEDIS NRLVSVPKPA RLSALRAELA
LIGQDLPAEV DIPIICPPSL VNGVPSRSRH HRIVRLNPAE STVLNSAEKV PYLLMVEILR
EDFTFDPDSS DNQRLLATLI ADQGSRKRIF DLSDSARRPT TRTSDAASTT STAATLELPV
DSVFEPTSGD LGHSPLMKPA DDENGAAFSS PGTPRRTISS GSVIAIPPAA ATLPQRGQIL
HKHSSSSSLA NRHIIGGAGS APSVSGTASS TNTAVTANFS ESTPRSSAAS TSRSSSPGPL
LRKMTVPIMR GPNALDQPDF TALATHMRTA AQMLAQLEAT SGKRPRQEVA AIRAKIIASM
QSLEEQSFDL DDGQGQGPTF DTIMAKASTS SAPAAPLSGE NALADVSGSN SADTALGPRV
GGDDNEDPAA AAAVAAAAAS VSTDPAVDGH AGIARMENDF KTGGLQRKGD RDDPSAAVFG
EAWDIKRERI RRSSPYGWMK NWDLVSVIVK TGADLRQEAF ACQLIAVCDK IWEDAGTSVW
VKQMRILVTG ESSGLIETIT NGVSLHSIKR SLTLASIESG QNPRRRIATL RDYFVKAFGL
PESEAHRAGI DAFKRSLAAY SIISYVLQLK DRHNGNVLID NEGHIVHIDF GFMLSNSPGS
VAFEAAPFKL THEYVEVLNG VGSPDFDDYK RLCKQAFQAL RKSADNVVDL VSMMGRDSKM
PCFVAGVTQA TANLRQRFQL HLSAEDAEQF VETELIGKSL GSYYTRLYDT FQYRTQGIY
//
