ID E6ZVR0_SPORE Unreviewed; 2175 AA.
AC E6ZVR0;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN ORFNames=sr16726 {ECO:0000313|EMBL:CBQ71378.1};
OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ71378.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ71378.1, ECO:0000313|Proteomes:UP000008867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX PubMed=21148393; DOI=10.1126/science.1195330;
RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA Kahmann R.;
RT "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL Science 330:1546-1548(2010).
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR EMBL; FQ311443; CBQ71378.1; -; Genomic_DNA.
DR EnsemblFungi; CBQ71378; CBQ71378; sr16726.
DR VEuPathDB; FungiDB:sr16726; -.
DR eggNOG; KOG0902; Eukaryota.
DR HOGENOM; CLU_000893_0_0_1; -.
DR OrthoDB; 147843at2759; -.
DR Proteomes; UP000008867; Chromosome 21.
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; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CBQ71378.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1609..1797
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1894..2157
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 241..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1519..1546
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2175 AA; 238861 MW; 0BBF4430536E4132 CRC64;
MDSLDLPTHQ LILDSLALNL AEDIANVPSA RSHVRSLFAQ SATTSKVTTG SKLFLSASAA
RTQISLALFA SSISSALRST EHTTDIKNDE HLVPVLDDLE QLLRQLTLID YDQDMSWSQH
PLPDQLAHAL VSSFLRVAIN APHHRTRCVN AIFDLAAKLG DALGATSGDA HTVVVKLVPL
FNGLYRAIAT TSFAWKLHEF ARFADVLNPI LVSTQTVRRL NEALLLGDQL DIRQQAGRAT
RRAPKVATVR PTDDQSEASV DTFSGDEDED ADLVGPEGGF TFAVDAPSAQ DAQDYRISFL
GRYRLAGVPL SGHYVLLSSI DILATALAQA LAVNARPPIK DFSDFQKLGL DLDRIDPSRQ
SQADRFDLDS DFAQGDVEHI HSRSILAPGA TKNAWNSLLR YSVNPNFSTS LSTAAATNGH
TTGHANANAN ANANGGLLAA VPVIGALASS TDKSAAFGQA ASAQSERNSL FDLDETLYAV
LRASNKSFHD VQRFLLSEGL KSLEVLPELH VPEILAESLK LSALCSVARS LAGGANVDNN
VFVRIRSLLS ESAPIYDPRV QGAALQSVGV LVRNNSALAL PMTRVLRHFV TSPIPIFAPS
ARGASSPVLL AAARCLASCV TIAPGDDLVV STMYNLLNYL GRDTPGGLGV GGVAGSGVSV
RSGASRAVTA RDQVNGISMS GSQANISARS EDQRKLINLS TITVISRLAL EVGKSDVTAL
TISMLLQRLR NADVSTEAAI LDNVVPLALA GPRSAYIDVV RALSAVSRSA LTGGASRRAA
VAVESAQLKL ARGLGRLDER DERDSAASDD NEASGGRKEI FLVELLQLFA EKGMQLQTVA
SSGKSSAEEL AELNTDLATL LPAIAAVLEH KDIHPEVQPT TEMVSLFRNM WFLSVLFGFA
SPSNIKSHVS ADGKPIARPT SAAEAQAEIV GKSLSAISLK TPTLVPETAH NYLESDLEYN
SVLKREFSNQ TLDSQRKALS AVIPTHASDV RSFSYAQVTF LSTIYDLECL RSRMGRPSMV
LSYFTNEGLN SSALVGSMQA IADKVIDFFI RDLGTQVNRH TLDPRVANEV KALMLGCCHR
VPKVRQVSQG ILNKLVYALP SLLCDQDVVT TMLEILTLLR DACEAEYKDE FAPAYHYTSE
RANISFDLSD SYVQRNEILS QFLTKSREFL SLIIALAPLE LQGILERYLG SFDDSFLPDR
SELGKSVALE YARSMPVSAR KERLLPNLGG WRSDASSSFI GELSAKSTYL GEMTGIHLAL
TKGLVELSHD PTTTMTPASV AECRQQLAAL SDSVSSKRKV LPFAELRRLL YRTAALVVAL
PEPDYELLHF IVSIPFLVFT PEAISTACQV WTWVIGARPQ VETKIMVELT IGWAMTAKAR
KGIFSPNLTS KHPFLRKTEM GAFDREEITA EQEQAARLFT PHLTLIHLIS SRFQAFRYRD
PTMVLSLVRL LQHSGAAVDR MSTHPLSREA RFTLLNFGLR LIQTSQLEGL VEHHLREALY
KLAFGWFASS PQWSFGGNRL QLSADMQVLQ ETLNLLQRDV VRADQHVTSF PPTLSSVRLP
GGLTLQEAVK SFDEKKRVLQ LMVENEYARL SVWANPLNNS SRGSDFVGSL SKSMTEASWG
GLVESAWRVN PAVAVQLGLR FQSKALKSTL GRLIRSQPYK TVDIPAALKY LLEDHLKLAK
KENADLKWLQ YWAAVSPVEA IDLFQPEYEN HPMVLQYAMR SLEQHPVELT FFYVPQVVQA
LRTDEYGYVE HFIFETSKIS QLFCHQIIWN MKANSYRDDN AEEEDPMKPT LDRMVENIVN
ALSGEAQDFY EREFGFFNEV TSISGKLKPY IKKSKPEKKA KIDEEMAKIK VDPGVYLPSN
ADGVVVDLDR KSGRPLQSHA KAPFMATFKV HREVVKPGDE GDENTPPKKT GVDVWQAAIF
KVGDDCRQDV LALQVIAMFK NVYTTVGVDL YLNPYRVTAT GPGCGVIDVV PNATSRDEMG
RAKINHLLTF FIGKYGNTDS VAFQKARINF IQSMAAYSVV CHILQIRDRH NGNMMIDGDG
HLVHIDFGFL FDIGPGGMRF EPYSFKLSHE MIDVMGGPGS QGFRMFEELV VKAFLAARPF
CDEIVDTCKL MLGTELPSFK GMPTIDRLRD RFKPELTERE AAAHAQWLVK DAYGNRRAVL
YDKLQEVTND IPFAR
//