ID A0A2T4H7P9_FUSCU Unreviewed; 2496 AA.
AC A0A2T4H7P9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=1-phosphatidylinositol-3-phosphate 5-kinase {ECO:0000256|ARBA:ARBA00012009};
DE EC=2.7.1.150 {ECO:0000256|ARBA:ARBA00012009};
GN ORFNames=FCULG_00002901 {ECO:0000313|EMBL:PTD11844.1};
OS Fusarium culmorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5516 {ECO:0000313|EMBL:PTD11844.1, ECO:0000313|Proteomes:UP000241587};
RN [1] {ECO:0000313|EMBL:PTD11844.1, ECO:0000313|Proteomes:UP000241587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV {ECO:0000313|EMBL:PTD11844.1,
RC ECO:0000313|Proteomes:UP000241587};
RA Schmidt R.;
RT "Fusarium culmorum secondary metabolites in fungal-bacterial-plant
RT interactions.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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:PTD11844.1}.
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DR EMBL; PVEM01000001; PTD11844.1; -; Genomic_DNA.
DR OMA; QEKVVEW; -.
DR Proteomes; UP000241587; Unassembled WGS sequence.
DR GO; GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd03334; Fab1_TCP; 1.
DR CDD; cd17300; PIPKc_PIKfyve; 1.
DR Gene3D; 3.30.810.10; 2-Layer Sandwich; 1.
DR Gene3D; 3.50.7.10; GroEL; 1.
DR Gene3D; 3.30.800.10; Phosphatidylinositol Phosphate Kinase II Beta; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR044769; PIKfyve_PIPKc.
DR InterPro; IPR027483; PInositol-4-P-4/5-kinase_C_sf.
DR InterPro; IPR002498; PInositol-4-P-4/5-kinase_core.
DR InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45748; 1-PHOSPHATIDYLINOSITOL 3-PHOSPHATE 5-KINASE-RELATED; 1.
DR PANTHER; PTHR45748:SF7; 1-PHOSPHATIDYLINOSITOL 3-PHOSPHATE 5-KINASE-RELATED; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF01504; PIP5K; 2.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00330; PIPKc; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52029; GroEL apical domain-like; 1.
DR SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR PROSITE; PS51455; PIPK; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE-
KW ProRule:PRU00781}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Reference proteome {ECO:0000313|Proteomes:UP000241587};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00781}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 412..471
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 2135..2465
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 40..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1612..1679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1698..1853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1898..2047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2153..2172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..592
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1082
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1614..1633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1640..1662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1663..1679
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1777..1793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1821..1844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1960..1976
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1995..2031
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2496 AA; 279389 MW; C6890E367D50807C CRC64;
MSPPRAGSIA SESPVRIRRD SISSITTGQL AHALDKIHTS ASQSDSLTTF NDFAPPPIAV
PTSDSKGLTG DLVQQGFSGL YSRLREAVGG GPKSPLEPTY GERSEPSSKR TSITANHGSK
ASIGSLSRAE TGASISTTSS QVIANDGAST QASGGTIEPR PQAQSSKPSS ISLMSNQKAS
STNRQSFSKK APSSIAADPT IAPITVHRDP SNTTLRTEDS GGVGSSRKSV SSRVDLQAHL
TTAESSASLF DAKDGKLPPR SKRDDTSSID ESLKSPTSPR SAHHHRTPSL QTLQTRSLRS
PSVTSSLLSP DSVRRKPAVI DRISRSKSPG DQNSRESSLD RGTAEPSHVS TSAHDSVCHD
SFSHNPKPQK MASGDFRIPG TVTSNEEASE QVNAQLDRMR KQVLSKEFWM KDDTVKECFL
CQTPFSAFRR KHHCRTCGCI FDSKCTTVIS GERFGVQGSL RVCKRCLEVI TRRFDGSGSD
DSGDEQSFMP RFFGSNHAKS PSNASQSKPR DIESGVASEG SEDSRTVSRP VTTPMMAIPA
TRRLGESRTA AILEIDAPQL SRPGSSRSLR SLSARPHSSA GHKRHHSKHS GFLNRFKPAP
EERAPFRRVV DDENTKKPKF PAFHDDNIID PELADYMSDE SSEDEQMSLF ATMTGDLQPG
SLGDDKSELT PYVNANRKYR HRAGEKSISG MSFASRSGID DLPGSLGAYR RPPRRRNTSN
VGGSIHYLPS PRPKSGVYKG PSQSSEMLFS LDTPHHSASQ ITRSDSLQHR KAPKVELNSS
SLRHVDKLLH QLLDDAEIPN PPAWQKALVP ILLRATDDVD PDVAKGEDMD IRHYVKLKRI
PGGKPGDTAY ISGVVFTKNL ALKSMPRRIT NPRVMLVTFP IEYQRHQQHF MSLQPVIEQE
KEFLRVVVQR ITNLRPQVLL AEKSISGVAL QYLSDSNISV AYNVKHTVIE AVSRCAETDI
ISSLDMLALP VQIGRCSNFE VRTFVNNDYP GRKKSYIFLS GCTPELGCTI ALRGANSTVL
SNVKHIMEFM VYVVYNLKLE SSLLRDESIE LPEGGESMAN SVQLPVESAR SQSVSSTDHS
RDGPAVVVNH PASESEQPSQ TTVDSSSITE ADDVGSLEQS GQLTEERVRS KSLPPQEQPE
PAVQDQTSQV PDDVPMPTYY SDMVAKYETK ILSASPYVKF TQPYLLMKAR EQERRLLYLR
RLRDHDNLTE NPNPEKTDHE KADPEKADPP RFQLIKPEMV EAIGHKAPKQ VTEILRAVHD
AEYDKALYNY QTQTRQWETY IQGNLDLFDP YSHQNIVVLY SVICTETKIP CTEPSLVAIN
FYDEQHIDTG MDPDCTLGQY IEDLAYTMNQ VCTSNGCERR MLGHHRTYVH DQSRITVFVE
NLPANSPMAD LDGITMWTYC KICKKDTEER TMSEATFKYS FGKYLELLFW GRGLKMKDMH
DCPHDHHRDH VRYFSLQGAR IRIHWDPIDL LEIVVPRARI TWKVTNDLKL KNEIFARMEE
RWAKFMTSVK SRLMCIRIDS VLPEKADLCK CEVDRLTAKA KEDQPLIVKR LQDIYVKSKY
YEVVPFNSIV REMLEKAGEW DQAFTKFEAD FLSDKDMRQL TIMQLKKMFT DNESKESLTS
NEGTPSTVDS EERPSQTFTE EEGKSTQPTD YTDNSMEASV TSSKPIDEKD VPDDDDGKVE
IPAEGAIERV EALDLACTPL TASNPPTEYF QPGDVLEDLD DQETPLAIDP EQTPKAPSKP
FDGASTDTAE PIPSPMDALP SPVPSLAEKV DQVRREQGPS SIPTPTGERA PSRKTGQAVS
PPMVRATSHP TRALARTQSG KGLATKDSKT NTSESTGSDS TTPEGSIRVD KKLSDRLGLR
NLKDRGKATA SGIPRFVHKK RETKVSTLAK HFEQLSREFE KERIRDRKKR AASMRQPRAM
LPRTTTKAIV EVYDDVNEAF EEPSPPADSV AEREASKRAG STASRMSESR QRTGPVSEPL
TPAEPPASIE EQQHGNQRQQ HEDDEQHQDL QDKEQEEKDE KMEKEDNDDH TIANTSQTFS
DDEERAADLE NSVTEEYLHD IKEIADSVDA SEIPLELPKH QKTSLMKYLT NFWAERGASG
WHQLEYPVNP SDHIFVDSDI IVREDEPSSV IALALNSEDY KGKLRNIRIE AQENMQRESD
SGMEGEPKSL PSESIDWVSE TDLEKSLLRV TGTHLKYQFR EGTATMTCKI FYAEQFDALR
RKCGVAERIV ESLSRCLKWD SKGGKTKSVF LKTLDDRLIL KSLSPIETSA FLRFAPGYFN
IMAEALFHDL PSVIAKMLGF FQVFIKNPVT GTDIKLDLLI TENLFYDRTA TRIFDLKGSM
RNRKIQSTGE QNEVLLDENM VEYIYESPLF AREHSKKLLR ASVWNDTLFL ARQNVMDYSL
MIAVDEARKE LVVGIIDCIR TYTWDKKLES WIKDRGFAGG GRNRPTVTSP KEYKSRFREA
MARYILQAPN CWHLFNNPQY PHYYGRARFE EPEMLR
//
