ID A0A179G4Q0_METCM Unreviewed; 1952 AA.
AC A0A179G4Q0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN ORFNames=VFPPC_00697 {ECO:0000313|EMBL:OAQ72832.1};
OS Pochonia chlamydosporia 170.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ72832.1, ECO:0000313|Proteomes:UP000078397};
RN [1] {ECO:0000313|EMBL:OAQ72832.1, ECO:0000313|Proteomes:UP000078397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:OAQ72832.1};
RX PubMed=27416025;
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT genome mining.";
RL PLoS Pathog. 12:E1005685-E1005685(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:OAQ72832.1}.
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DR EMBL; LSBJ02000001; OAQ72832.1; -; Genomic_DNA.
DR RefSeq; XP_018148915.1; XM_018280667.1.
DR STRING; 1380566.A0A179G4Q0; -.
DR GeneID; 28844661; -.
DR KEGG; pchm:VFPPC_00697; -.
DR OrthoDB; 147843at2759; -.
DR Proteomes; UP000078397; Chromosome 1.
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; 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; 2.
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:OAQ72832.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078397};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1367..1553
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1653..1936
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 1653..1681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1952 AA; 217357 MW; 1420ED121095C45C CRC64;
MTRDIRSRAL ERIAALSAES STTSFDKSDL DKLCRACHSA RGREYNHGGY STKQAGSLGR
IPMSIREFEV LLALCKTAPN IKSSQSAQKL SYRLIPYILE AHAQVFAPSP FFRKVEPSPT
ESLAFHLTAA LLSLGTNYID LKETVADGIW AFTNACGRAT ESVLSPQSGD PESLPVDDAI
RTVTIALALL GFLDAASAQA DFWNAGGRLG LIQKFNQLLS EPFLVAVETS LSTIRNTHSQ
TNEVREWKRL LRHYASHGRP LGAMIIQRSF MWLVLSSTSL MVADGPALRK QHVLDLLMSG
DGAAVMEQRH LLDGDVRSVE VYASITTDQM DYLEAGADFV RLGSPDQQKL AYDVKSAAMV
AFLNCSLLHE NGADSDVLMG WLQETLEDPL QMSDPSLASV VLRCMALICR ISPSYSSAVS
RALPRFLVQT APHGDSTKVA STSLAFVLKM LSKDAIISTL YTLGNVLSPD SDEIAHGLTN
GTTSNEEVAA GGYNRRHSTG SSISLLMNGE QETAIVYGNV VQAICTIATT SGDEKIIALA
QSMLLQKLDK VNASVDTKVI SGAAKLSLHG GQLEFRSLLK MYSRICHIGV VDHKDFLLTA
VMKARTYISA NLRRDSSLFN IYWEHLLDAV ISLGDAESPH HTKESDVQLA AQEIAELLHP
LAVFMASNDV ASNPIDVDET YSLLKDAWFN IVVHGFTTTT DRGKKYINEL RTIAVHSPPL
VAGERTEVVE SDIELNTVLR RANSGEREAA QKKLLTELIP SKASDIKGLS YRKVIFLQAA
YLVESLRADS GDCTKVLSYF LEPSMRKGEV SSTMEGIAAA VVEKYLKKTL GGSEPTFSAQ
YAAEQLATIF CICCHRIERV QQAAFTCADR IIRDVPSALC QRKSLFALLE LLSLMWSSCL
EAETDLYAPR SMFKSEIGKV MVELSDDYDF RRWTLDHLNR KAKVWVNAAI SLAPMDVKGL
LQTYLSEFDD EGAYGHISLG RSFALELGSI IPSTDNRLQS LERVGSCEIN TASDLIAQYT
TRQEYRYGET LPDRGTELIS FMNVNRRTSF SQSNVTESAN AATALAHVEA RILSKKATSL
NEVRDILRRA AALLCRTHRD ESAVARYLVS IPFALFTKQS IKTGVSLWLG VMNENPRLEP
KLLNSIAQQW EFTISRKVGL FSSALAHPDP FFLKEEFAPS DLELMAKKRQ AIHDVLSPHA
RLLHFFTSHF NATRLGSRDT QRVFLRMLDL TLTALKGTSS HPMSRELRFQ LVLFGLKVLR
SSTTIGATAQ WRLKDKILSA GLGWFRNAPK WSFGSNILQL KTEVRLIADV LVAMKVVSFI
GAHTVGNVKS LQAKEQLLQL LLENEQSRLA VWISPLSQQG LQLSAQNTSK SSIENALIPL
VKTAWQQDPS IAIELTTRFN FPRLHRDVRQ LVLSAPDKAV SDPEALPLIF GGHLPDDVNI
QLKYLLVWEP LNPLTAVTLF MPAYKHHPFI IQYAMRALES HSVDVTFFYV PQIVQTLRYD
ALGYVERYIL ETAQFSQLFA HQIIWNMKAN SYKDDDAQVP DEIKPTLDGV MTKMVDSFAA
LDRDFYEREF AFFDEVTGIS GKLKPLIKRP KPEKKQKIEE ELRKIKVEVG VYLPSNPDGV
VIGIDRKSGK PLQSHAKAPY LATFRIRKNK SGGNDVLNAD APEQAPKKGQ DEQGQQQQLQ
QQQQQYQDNI IEVWQSAIFK VGDDCRQDVL ALQMISAFRG IFHSVGLDVY VFPYRVTATA
PGCGVIDVLP NSISRDMLGR EAVNGLYDYF ISKYGNEDSL RFQRARNNFV KSMAAYSVIS
FLLQFKDRHN GNIMIDDAGH ILHIDFGFCF DIAPGGIKFE RAPFKLTSEM VAVMGGSTDH
QSFKWFEELC VKSFLASRQY CEKLSQIVLL MMDSGLPCFK PESVKHFKER FVLDKTEREA
ANFMKGLIKT SYSSYSTGVY DQFQLLTNGI PY
//
