ID G1X9A4_ARTOA Unreviewed; 2016 AA.
AC G1X9A4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN ORFNames=AOL_s00076g211 {ECO:0000313|EMBL:EGX50447.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX50447.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX50447.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
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:EGX50447.1}.
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DR EMBL; ADOT01000123; EGX50447.1; -; Genomic_DNA.
DR RefSeq; XP_011121066.1; XM_011122764.1.
DR STRING; 756982.G1X9A4; -.
DR GeneID; 22891967; -.
DR eggNOG; KOG0902; Eukaryota.
DR HOGENOM; CLU_000893_0_0_1; -.
DR InParanoid; G1X9A4; -.
DR OMA; TIEVWQS; -.
DR OrthoDB; 147843at2759; -.
DR Proteomes; UP000008784; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000008784};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1458..1633
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1706..2000
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 19..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2016 AA; 225434 MW; 898662F232D7146A CRC64;
MDSLDRDLRR SALSRLAKLA AASPAPPVPD YSNNISIPSS PTRRNQQPPP PPPPATDFEK
LEEEIQGGTR FTNGGGAAFM NGGPRSSFIK SSPQTLNARD IEIILALCGS VEFVNSTEAA
SKLARLLSPY LIDSSILQVE QSPQLRHFNP SPWESLTTSI TDSLALVGTL FPSQRDSIVS
TLNSYLRRIK SQAGGTPDFS DDRAAIPVAT LVVSLLGFFN SAAKRMDLWN HEERVELIKT
VREILSPNFL LSAETAFSTI RNSHGRELKL WKRYTRQYAA SGRPLGAMLL QQGFTCLLAA
STSLLVVDPK LLRDRDVLDV LLARTNKTKE TIITPGSASP STRKARLNRL SSHSDALTNG
HDQNDLVSSL VDMITEILAL VEDGADYLQV GSAWQQRLAF SVKAYAFISF CNCVEYRRRH
PTLNHLEDVE SRDEHADLLI GLLEASLEDP IQMVDQDLAR TVLKIMAIVG KNDPSFAVAV
IRLFPRYIVR SGAEKETIRV AGKCLARVLQ TLSQDAMITT LYTLGNVLSS GNPERALTAN
TREKIHPELL DVNALGSSIS LSLNSEEEKF LVYERVIEAI VGVACEMKDE KMVELAASIL
GQKVGKINGA VDAKIIVELA VLALAGGPLE LKTVLKLLDR LGTNAVGIRD VNIAGAVLEA
RIHMSTNLKP DHPLYDTYLT GLLECIINKG DIHEQDTRKQ ADPDSRTSPV EPPKLRFLAG
SQLFLHLDIV QLAAREISQF LQPLAILLNA TTPEKTEMPP YNIHSNKDIQ QLFRNAWFNC
VVHGFLRQSE LVQTHESFLR IIARHTPPLV AETRINHMES DMDLNTILRR GMNTQNIAEQ
KRKLSSAIPT HDSEIRGLSY PKVIFLQAAL LLESLRALEG DCSKILTYFV DPSFKHGDEA
TCMSSIAAEV ISIYLKNVQQ GNLEAFQAPY VSKQLVEFFT GCCHRVEKVQ FVAAICANNI
ITAVPSALCQ KSSMFALLEL LTLLWNSCLE AETDEYGWHS VYRSTVANIQ IELSDSFPLR
KKTLKTYHER AKGWLLRVLD IAPLDVKGLL QKYLAKFNDE NVFGHVALGR SLAYDIGAAV
PKSDPRLSTL ADINLASDFM AQYTIRQAYR YDDNMPEHAP DWIHDSDRPD HTAEIYGKHG
DAQAFLTHLE TRAVNGKFVA ISEVRDILRR TAGLLCQSHT EESILIQHFV GIPFAIFTKQ
SIKLGISLWM GVLNENKNIA PRILCEIARN WELTVRKKQG LFNPSFDAPD AFNTKMEYVP
SDKGLLTKHQ TAAINMLSPH LTLLKFLSSH FHASRHGDPN VIRMFLRLIR ISLVGLKNAS
PHPLAREARF QFILFSLQVL KYTPGIMPAV MQWKLKDEIF SAALSWFTYQ PRWSYGGNKM
QLRAEGLVMR EVALAIQGLS AVGNATVKSL ELKQELLLLL LENEQARVST WITPLDAPRK
QAPVPGIVPR QVSDVTLVTL LQTAWNENPA LAIQMIGRFP SKRYEAEVRK MMLAFPEKVV
KIPEALYYIF GDKLPLDVNF QLRYLLYWAP LNPISAATYL LPSYANNPFL LQYAVRALEN
HSIDVTFFYV PQFVQTLRYD ALGYVERWIL ETGKFSQLFA HQIIWNMKAN AYKDEDSEIP
DPIKPTLDKV MDHLISSFSP ADRSFYEREF SFFGEVTAIS GKLRPFIGQP KEEKKQKIEE
ELRKIKVDVG VYLPSNPDGI VIGIDRKSGK PLQSHAKAPY MATFRVRKKA NASVAGDDVG
SPRAESRVSG GLIGEEKWQA CIFKVGDDCR QDMLALQLIS AFRSIFNSVG LDVFVFPYRV
VATAPGCGVI EVLPDSISRD MLGREAVNGL YDYFTTKHGG EDSIKFQEAR SNFVQSMAAY
SVISYLLQFK DRHNGNIMID GSGHIIHIDF GFCFDIAPGG ITFERAPFKL TAEMIAVMGG
SLESQSYRWF EELCVKSFLA CRPYCEQLAH LVVLMLDSGL PCFKPETIQN FKARFVMERS
EREAADYMRG LVKRAYGSYS TRGYDQFQLL TNGIPY
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