ID A0A1J7JZX6_9PEZI Unreviewed; 1938 AA.
AC A0A1J7JZX6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN ORFNames=CONLIGDRAFT_627035 {ECO:0000313|EMBL:OIW34996.1};
OS Coniochaeta ligniaria NRRL 30616.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX NCBI_TaxID=1408157 {ECO:0000313|EMBL:OIW34996.1, ECO:0000313|Proteomes:UP000182658};
RN [1] {ECO:0000313|EMBL:OIW34996.1, ECO:0000313|Proteomes:UP000182658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 30616 {ECO:0000313|EMBL:OIW34996.1,
RC ECO:0000313|Proteomes:UP000182658};
RG DOE Joint Genome Institute;
RA Jimenez D.J., Hector R.E., Riley R., Sun H., Grigoriev I.V.,
RA Van Elsas J.D., Nichols N.N.;
RT "Draft genome sequence of Coniochaeta ligniaria NRRL30616, a
RT lignocellulolytic fungus for bioabatement of inhibitors in plant biomass
RT hydrolysates.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR EMBL; KV875093; OIW34996.1; -; Genomic_DNA.
DR STRING; 1408157.A0A1J7JZX6; -.
DR InParanoid; A0A1J7JZX6; -.
DR OrthoDB; 147843at2759; -.
DR Proteomes; UP000182658; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00871; PI4Ka; 1.
DR CDD; cd05167; PI4Kc_III_alpha; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 1.25.40.70; Phosphatidylinositol 3-kinase, accessory domain (PIK); 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR045495; PI4K_N.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048:SF15; PHOSPHATIDYLINOSITOL 4-KINASE ALPHA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF19274; PI4K_N; 1.
DR SMART; SM00145; PI3Ka; 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 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000182658};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1368..1554
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1652..1922
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 1938 AA; 217026 MW; F52DECFA15870265 CRC64;
MARDIRQRAL QKIAALSASS STTSFDRSDL DKLCKAVPSY GQPRETTNGH RPNHFTSVGR
VPMAIREFEV LLALCKAAPM VKTPQSAQKL ARQLGPYLLE SHSQIFAASP FYRKIQPSPT
EALTYNVTAA LLSLGTRHDD VQQMASDNFR AFLNACAHAS EAVVPPGDDG GPEAVENAIR
VATITISLLG FLDAASAQAN FWRTGGRLAL IQRLRDLLSD DFFIAVETAF STIRNCESQE
RHVREWKRHL HHYDHIGRPL SAMLLQQSFM WLIVAATSLL VAEVDALRTT HVLDILMSGD
GLLRPLTAKS GDADFRSVET YATAVIDQMN YLESSADFVR LRSSAEQRIA SNIKVSALTS
FLNCSRLNED AADADILMNW LEDTLSDASS MADENLATTV LKTLALLCKV SPSYAVTVSR
LLPRFIVQGD ARSETVAVAA DCLVFVLRML STDAVITTLY TLGNVLSSAD QQSFANGLNG
NSPDRSDTHI YAGRQSTGSS ISLQITGEEE TAAVHGNVVQ AICRVAAASK DEKITALAQS
MLLQKYGKIN SLVDAHIVRG AAVLALDGAQ LEFRSLLKLY GRIAHSAIVE NREPVLVAVR
TARNHISANI PRESPLWDIY WEHLLDSIIS KGDAPADQHN HRKESEVELA AREIAQLLQP
LAVLMSTHDL ALDESTDDET HAMLRDAWFN IVVHGFVPNT ARGKEHLNEL RIIAIHSPAL
VLEDRGEEDE SDIELNTILR RGMSSERESL LKKQLIELIP SRESDIRALS YRKLTFLQSA
YVVETLRAET GDCTRVVTYF LEPSMRKGEV SRSMEGIANA VMDKYLKRTQ VAATPAFSAQ
YAAGQLARIL CNCCHRIERV QQAAFACADR LIRDIPSALC QRSSLFALLE LLSLMWTSCL
EAETDMYEPR TIFKSVRGQV QVQLSDDYAF RRYTLDNLNR KARVWLTNAI GLAPSDVKGL
LQTYLSEYDD DGAYGHISLG RSFAIEMGSV IPLTDQKLSS IDNVGDYNIN TASDFIAQYT
TRQEYRYTEA LPDHSLEWLS FMRLDRRSSF LPSSENESAD AVTALAHIEK RIVLKKTTPL
NDVRDILRRA AALLCRSDGD ECNTVHYLVS IPFAMFTKQS MKLGVSLWLG VMHENPRMES
RLLTEIAQQW EFSMQKNLGL FNPTITNPDP FFLREEFAPT DNAAMVKRRQ HVYNVLAPHS
RLLQFFASHY NATRLGNTDT QKTFLRLLNV TLDRVTSSTA HPMAREIRFQ IVLFGLKVLK
TSTTMTAVSQ LRLKDKILSA ALSWFNEAPR WSFGSNMLQL KTEIRLLSDV MVALKGTSMI
GANAAPGIKS LQPKEQLLIL LLESEQARLL VWVYPLAEPA KSQFAVGHTN KLAIETTLAP
LVRTAWAESP ALAIELTTRF QYPRIHKDVR WLLLNFPAKA VTEPEALPIL LGGSLPDDVS
FQLKYLLYWA PVNPITAVTF FLPQYRNNPF LLQYAVRALE SHSVDVTFFY VPQIVQTLRY
DALGYAERYI IETAQFSQLF AHQIIWNMKA NAYKDDDGEI PSDIKPTLDH VMGRMIESFS
AFDRGFYERE FSFFDEVTSI SGKLKPFIKK SKPEKKQKIE EELRKIKVEV GVYLPSNPDG
VVIGIDRKSG KPLQSHAKAP YMATFRIKKP KGGSVEEANE LLEDADMNKI EGKENTIEVW
QSAIFKVGDD CRQDVLALQM IAAFRGIFQN VGLDVYVFPY RVTATAPGCG VIDVLPNSIS
RDMLGREAVN GLYDYFISKY GNEDSLRFQQ ARNNFVKSMA AYSVISFLLQ FKDRHNGNIM
IDDAGHILHI DFGFCFDIAP GGIKFERAPF KLTSEMVAVM GGSTDHQSFK WFEELCVKAF
LASRQYAEKL SQIVLLMMDS GLPCFKPESV KHFKDRMVLE KSEREAADFM KDLIKKSYTS
YSTGVYDHFQ LLTNGIPY
//
