ID A0A168JN54_CORDF Unreviewed; 1943 AA.
AC A0A168JN54;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 13-SEP-2023, entry version 39.
DE RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN ORFNames=LEL_00195 {ECO:0000313|EMBL:OAA80650.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA80650.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA80650.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA80650.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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:OAA80650.1}.
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DR EMBL; AZHF01000001; OAA80650.1; -; Genomic_DNA.
DR STRING; 1081108.A0A168JN54; -.
DR OrthoDB; 147843at2759; -.
DR Proteomes; UP000076881; 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:0048015; P:phosphatidylinositol-mediated signaling; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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, ECO:0000313|EMBL:OAA80650.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076881};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1369..1555
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1664..1927
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 1652..1675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1652..1669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1943 AA; 217519 MW; 5495C1B16BB4638F CRC64;
MTGNIRAKAL DKIASLAASS TNTSFDKSDL DRLCRACNVS GRGREYNHGA YNSKQTGSLG
RIPMSIREFE VLLALCKTAP SILSAQSAQK LSYQLIPYVL EAHSQTFVPS PFFRKINPCP
TESLSFHVTA ALLSLGINYN ELKETVTDGI WAFTNACSRT TESVLSPRTG DPENLNIDEA
IRTLNIAVAI LGFLDAAAAQ SDFWKAGGRL GLIQKVKQLL SEPFLVAVET ALSTIRNAHS
DDRDVREWKR HLRHYSAAGR PLGAMLLQRS FMWLVLSSTS LMITDGSQLR KKHVLDVLMD
NDGALPRPDG FVADVDLRSI DLHANFAIDQ MNYIEAGADF ARLGSPSQQK LAYAVKSAAM
ISFMNCTMLN EDAAEPELMM NWLQQTLDDP QQMSDDTLAS TTLRCMALLS RIAPSFSQTV
IRSLPRFIVQ DVTSTGTGAV ASRSLAFVLK KLSKDAVIST LYSLGNVLSP DTQERLVNGH
TNGSVDGENG LNPVYQRRQS NASSISVDMN GEEEAAIVYR NVVQAICGIA TAYKDEQITA
LAQSILLQKL DKVNATVDVQ VISGAADLAL SGGQLEFRSL LKMYNRLGHI GVIDKKDFFS
EAVFKGRTHI SANLRRDSPL FDIYWEHLLE SIIALGDAYS QGQTKQVDVD LAAQEIGELL
HPLAVLMSAN DLAARPLDND ESYALLRDAW FNIVVHGFST STERGKRYLN ELRIIAIHSP
PLAAEQRGEQ VESDIELNTV LRRGNSGERE SLQKKLLTEL IPSKASDIKG LSYRKVIFLH
SAYLVEILRA DSGDCTKVLS YFAERSMLQR EVCSVMDGIS NAVVDKYVKK TISGTEPAFS
AQYAAKQLAT IFSRCCHRIE RVQKAAFASA DKIVRDVPSS LCYRTSLFAL LELLSLMWSS
CLEAETDMYG HRSTFTSLRG NVTVRLSDDY DFRSLTLKHL HQRARAWVYA AINLAPLDVK
GLLQTYLSEF DDEGTYGHIS LGRSFAVELG SAIPNTDNRL QSLDQVNEYG INSASDLIAQ
YTTRQEYRYG ETLPDRGTEL MSFMQTNRRP SFPQSSGVDS ANAATALAHV EARILSKKAT
PIDEVRDIMR RAAALLCRSE HDESAVARYL VSIPFALFTK QSIKLGTSLW LGVMNENPHL
ESKLLNAIAQ QWEFTISRRV GLFDPALEHP DPFFLKQEFS PSDWDMINQQ KQKVHDMLSP
HTRLLQFFTS HFNATRLGSP DIQRVFLRLL DLTLDALKDC SPHPMAREIR FQIILFSTKV
LRNSTTIGPT AQWRLKDRIL SAGLSWFRHS PRWSFGSNML SLKTEIRLLS DIIASLNLVA
HIGSHTVGNI TSLQSKDSLL KVLLENEQSR LVVWANPRNL SGTQFPSHHN SKNASENVLL
PLVRTAWYQD PAIAVELATR FHFPRLRSDV RRLILTSPEK VIDEPEAIPL MVGGQLPDDV
NSQLKYLLFW EPVNPITAVT LLSPAFRDHP LVIQYAMRSL ESHSVDVTFF YVPQIVQSLR
HDNLGYVERY ILETAQFSQL FAHQIIWNMK ANSYKGDDAE VPDEIKPTLD TVMTKMVDSF
MPEDRDFYER EFSFFDEVTG ISGKLKPYIK RPKPEKKQKI EEELMKIKVE VGVYLPSNPE
GVVIGIDRKS GKPLQSHAKA PYMATFRVRK NKHPGDAPTD LEEEQQLAKQ QDGVPESQEN
YIEVWQSAIF KVGDDVRQDV LALQMISAFR SIFHNVGLDV YVFPNRVTAT GPGCGVIDVL
PNSISRDMVG REAVNGLYEY FKAKYGNEDS LRFQAARSNF VKSMAAYSVI SFLLQFKDRH
NGNIMIDDAG HILHIDFGFC FDIAPGGIKF ERAPFKLTSE MVAVMGGATD HQSFHQFEAL
CVKAFLAARQ YRDKLAQVVE LMMDSGLPCF KPESVRHFKD RFVLDKSERE AADFMRDLVK
KSHSSYSTGI YDQFQLLTNG IPY
//