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Database: UniProt
Entry: A0A1S8BBL5_9PEZI
LinkDB: A0A1S8BBL5_9PEZI
Original site: A0A1S8BBL5_9PEZI 
ID   A0A1S8BBL5_9PEZI        Unreviewed;      1931 AA.
AC   A0A1S8BBL5;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE            EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
DE   Flags: Fragment;
GN   ORFNames=BK809_0000669 {ECO:0000313|EMBL:OMP84917.1};
OS   Diplodia seriata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Diplodia.
OX   NCBI_TaxID=420778 {ECO:0000313|EMBL:OMP84917.1, ECO:0000313|Proteomes:UP000190776};
RN   [1] {ECO:0000313|EMBL:OMP84917.1, ECO:0000313|Proteomes:UP000190776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F98.1 {ECO:0000313|EMBL:OMP84917.1,
RC   ECO:0000313|Proteomes:UP000190776};
RA   Robert-Siegwald G., Vallet J., Abou-Mansour E., Xu J., Rey P., Bertsch C.,
RA   Rego C., Larignon P., Fontaine F., Lebrun M.-H.;
RT   "Draft genome sequence of Diplodia seriata F98.1, a fungal species involved
RT   in grapevine trunk diseases.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:OMP84917.1}.
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DR   EMBL; MSZU01000086; OMP84917.1; -; Genomic_DNA.
DR   STRING; 420778.A0A1S8BBL5; -.
DR   OrthoDB; 147843at2759; -.
DR   Proteomes; UP000190776; 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; 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:OMP84917.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190776};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1378..1552
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          1625..1915
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OMP84917.1"
SQ   SEQUENCE   1931 AA;  215509 MW;  985C5E487F54EE3D CRC64;
     SIRRSALEKL ATLSAASPAP DSSSTDFKRL YRLCPPHAQA NGGHDELDGA RGGAARVPMS
     LPELETLLAL CKAAPQVVDV ATAEQLLNQL TPYLPESFAQ AIAPSPFLRD LDPSPWEILT
     HNLAFAILSL GNNHEGLKEV AAAAVKKYVA EWSASARSLT GEHMSREDAV DNTADGDVGR
     VLCLAMSMLG FLSAASACAS IWNPTEMLDL IENLRTALSE KLMISVEASV SNVLYGSNSK
     RTLREWRRHA KHYAAMGRPL GALLLHHGLM QVVVACTATV ASPSERESGK PVLDRLQSAH
     ALQQPLDAGA ETLLASVAGI AEEELERINA DSEYVKRVGT VWQQHIAHAV LADALVTYLC
     CAVLNEEIAD SDKLMDLLES TLSDDILAAD EILACVVLKS MSILGKSSPD HASHLSKSLP
     RIIVQGGLKE GTSAVAADCL ASVLMHLPQD AVITTLYSLG NVLSGKQAPE RANTGLSQLN
     GGAKANGTLH TQHQTGSTIS LAPADVDEPS HVYGTVIQTI VGVACRCKDQ KISELALSML
     VQKIGRVSIS VDAKIIIESS LLGAHSGPGE LRALLKLYSK LARDAIVQDN SVLLDAVMRG
     RCHLSREFKV GQPLFEVYLQ YVLDDIVSKG DAHGPEATPM ADTEVAAQEI AQLLGPLAIL
     ISSNAEGPEE YIEDEAIVSL QRDAWFNVAV HGFSLTSPLG KRYLNELRIL AQHSKPLVSE
     SRADQLESDV ELNTVLRRGK SAEHIVEQKR RLQELLPACE VDIKSLGYPE VVFLNTVHLV
     EGLRASTGDC TKTLTYFLDP RLRNKEMGNC MVAIAEAGVR SYLKKTVSGG FQSFSAPYVA
     QQLAIFFTGC CHRVLQAQKV AIHCADIIIQ QVPSALCQRA SLFALLELLS MMWNSCLEKE
     IDEYGWSSTF TSTRENISIE LSDNYSFRRN TLIQLQNRAR VWVLSAMDIA PLDIKGLLQT
     YLSEYDDDGA YGHVSLGRSF ALEMGSVIPS TDQRLGAIDR ERELNINTAS DFVAQYTNRQ
     EYRYVEPMTD FNDDWIRFGN DSDPLMRRSK HYDRSVEDAR RVLLDLEQRT LSRKHVSIAE
     LRDALRRAAA LLCRSPKDEC AIAHHVVGIP FAAFNKQSIK LGISLWLSII KENPRMESRI
     LVEIAENFEK TVRRRLGLFD EHFHHPDPFF VKQEFAQSDR TAIMKRQQHA YNLIAPHFRL
     LQFLESHFSA TRLGSPHVER VYHRLMHITL SAMSHTTNHP LTREAHFHVV LLGLRILQYS
     TGSNTSGQWR LKDRILSAAL AWFKERPRWS FGGNRLQIKA EAQVLVDIHN ALQNVTGIGL
     NTNGPRKSLH AKQELLLLLL ASEHQRLMVW LFPLEQDRRL HLMPGHSGKA PTDAVLSGLL
     KTAWTEDPAI AVQLVFRFNS LRLATEVRFL VLNFPEKVLD QPDALEVLLG KSLPDDVSFQ
     LKYLMYWAPV NPMTAITYFL PAYGNHPFII QYAMRALESH SVDITFFYVP QVVQTLRYDV
     LGYVERYIIE TAKFSQLFAH QIIWNMKANA FKDEDSLIPD PVKPTLDVVM ASLENSFSPE
     DREFYEREFT FFNEVTGISG KLKPFIKKSK PEKKQKIEEE LRSIKVEVGV YLPSNPDGVV
     VGIDRKSGKP LQSHAKAPYM ATFRIRKEKT EIIPVVEDGN DEEKKEENYY EVWQSAIFKV
     GDDCRQDVLA LQMISAFRGI FNDVGLDVYV FPYRVTATAP GCGVIDVLPN SISRDMLGRE
     AVNGLYDYFV SKYGGEDSIR FQEARNNFVK SMAAYSIISY LLQFKDRHNG NIMIDDAGHI
     LHIDFGFCFD IAPGGIKFER APFKLTQEMV AVMGGSTDSQ PYRWFEELCI KAFLAARQHC
     EHLAHIVIVM LDSGLPCFKP ETVQHFRERF VLDKTEREAA EFMRFLIKKS YNSLSTGQYD
     RFQLLTNGIP Y
//
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