ID R1EF34_BOTPV Unreviewed; 746 AA.
AC R1EF34;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN ORFNames=UCRNP2_6882 {ECO:0000313|EMBL:EOD46383.1};
OS Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS (Neofusicoccum parvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Neofusicoccum.
OX NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD46383.1, ECO:0000313|Proteomes:UP000013521};
RN [1] {ECO:0000313|Proteomes:UP000013521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA Blanco-Ulate B., Rolshausen P., Cantu D.;
RT "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT vascular pathogen associated with grapevine cankers.";
RL Genome Announc. 1:E0033913-E0033913(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216;
CC EC=2.7.1.67; Evidence={ECO:0000256|ARBA:ARBA00001686};
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DR EMBL; KB916463; EOD46383.1; -; Genomic_DNA.
DR RefSeq; XP_007586139.1; XM_007586077.1.
DR AlphaFoldDB; R1EF34; -.
DR STRING; 1287680.R1EF34; -.
DR KEGG; npa:UCRNP2_6882; -.
DR eggNOG; KOG0903; Eukaryota.
DR HOGENOM; CLU_002446_6_0_1; -.
DR OMA; TQDYVDV; -.
DR OrthoDB; 147843at2759; -.
DR Proteomes; UP000013521; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05168; PI4Kc_III_beta; 1.
DR Gene3D; 6.10.140.1260; -; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR021601; Phosphatidylino_kinase_fungi.
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; IPR049160; PI4KB-PIK1_PIK.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048:SF22; PHOSPHATIDYLINOSITOL 4-KINASE BETA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF21245; PI4KB-PIK1_PIK; 1.
DR Pfam; PF11522; Pik1; 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 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EOD46383.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000013521};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..124
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 452..731
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 179..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 746 AA; 82864 MW; F691BA157D8C47A9 CRC64;
MSWNLLERFI ESDHFNEDPS LSVAYLSCVL PRYADHVGIH YVLCSKLRRF SYDEIEFFLP
QLCHLLISVD NESMALEEFI IDLCEESVNA ALLTFWLFQT YLHDLAGNPQ SNDFKTCRRL
YNKVQRIVFG ASEPANRDRI RGNVLPVTVL SSLILATVAA PFLPRHAGPL AVAQARKPRM
STETISDASQ TQTQKLVRSN TVAGGSPRPR KPRPQIVRLN PAEATSLNSA ERVPYLLMVE
VLREDFDFNP DSEVNQTLLT RLLAEKGTNK RRLFDLSDSS RQAIPDKPPD PGVDSVFEPT
DGDLGSKDLL IKDPAEEELA NGMAKTALAS NGYTAVRINP APQMLAQLEA SGSKRPKTEM
AAIKSKIIAS MQNLEEQSFY MDETPTFDSI MAEPKPTALT AEPEDLDDAA VDPNASNSAG
AARMENDSKT GGIQRKGDRD DPSAATFGED WTAKKERIRR SSPYGWMKNW DLISVIVKTG
ADLRQEAFAC QLIQVCCKIW QDAEVPVWVK RMRILVTGES SGLIETITNG VSLHSLKRSL
TLASIAAGTN PRKRIATLRD HFVQTFGEAD SETNGAAVDA FARSLAAYSI ISYVLQLKDR
HNGNILIDNQ GHIIHIDFGF MLSNTPGSMG FEAAPFKLTQ EYVDVLGGVG SPGYNLFKML
CKQAFQALRK EAERIVMLVE MMGKSSQMPC FAAGVQQAVA ALRSRFMLQL SKEEAEYFVD
DLIGKSVGSY YTRLYDTFQY RTQGIY
//
