ID Q0V5L7_PHANO Unreviewed; 2258 AA.
AC Q0V5L7;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 2.
DT 27-MAR-2024, entry version 112.
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=SNOG_00697 {ECO:0000313|EMBL:EAT92192.2};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT92192.2, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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DR EMBL; CH445325; EAT92192.2; -; Genomic_DNA.
DR RefSeq; XP_001791374.1; XM_001791322.1.
DR STRING; 321614.Q0V5L7; -.
DR EnsemblFungi; SNOT_00697; SNOT_00697; SNOG_00697.
DR GeneID; 5968194; -.
DR KEGG; pno:SNOG_00697; -.
DR VEuPathDB; FungiDB:JI435_006970; -.
DR eggNOG; KOG0230; Eukaryota.
DR HOGENOM; CLU_000480_0_0_1; -.
DR InParanoid; Q0V5L7; -.
DR OrthoDB; 5481504at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0010008; C:endosome membrane; IBA:GO_Central.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
DR GO; GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
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; 1.
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:UP000001055};
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 398..433
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1869..2189
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1393..1412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1439..1476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1517..1539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1574..1620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1715..1759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1771..1790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2212..2258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..534
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1451..1476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1517..1538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1585..1620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1720..1758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1774..1789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2258 AA; 252829 MW; B96C513EC0FB985B CRC64;
MADDPRSSLH DMHATASRSD TLTTFDDLTA PPAPAVDEPK GAELVSGGLS GLYSRLRASV
GGVKEQTAAD GDGAATATSK AAAKLGPAPR SPGGTALPSP VVFSGPSSRL QSPSVPSFPE
ALPPSRDSSS SVATLPGKHS LNASKTSLAT TRSRPSIAPS IEPGRSLKEE DAFAHSPTST
HSRVQSLSNH DLPKNTATKD SATGPPPANS PRFPSGKSFR DRKGDMDLVG QESDTSEDDD
VVGEGYKDAA GPAGNFKFPS DTPRQSLSKV SSRADNQYQT ARPASKAARD QPDNRGENTE
APRITSNARV PAGAQEPQRP PLLKVGPSHL PGFRPSRASS SDGLSSVITT STIRTPTVAP
IEEIQRVTQA RPAVSRMPTN AFSQMRRKIL DREFWMRDEN AKDCFNCGDT FTTWRRKHHC
RTCGQIFDSK CTSIISDDGD QASLYDHGES TRDFDDEVVE PTESDHTKIG TPTISIPMSR
KTGSDKKRRS HVIEVGPQTL ARPSSSRSLR SLGGRPRSSS HKRHPSRHQH MRHVKHDDRA
PFHQYLDNAR QPSLPAFHHD NIIDPDLAPF MSDEGSSEEE QASLFATLRN DTSESTQLEN
ERVGLGGLLA AMRKGKQRAG DRSVASGGHA RDTDNISITS RNPQRTNRRR NLSCTDDVNP
DVDRGDDIDI RNYIKLKKIP GGKPRDTAYV SGVVFSKNVA LRSMPRNILN PRLVIITFAI
EYARHQTHFM SLEPVIAQER EYLRNLVSRI AALRPQVLLV ERNVSGLALE FLEKEGIAVV
YNVKAAVLHA VARCTQSRMI SSVDKLAIDP NHLGRCGSFD VKTYLHKNIR KTYVFLSGCQ
KDLGCTIVLR GAENEELVKL KRITEFMSYV VYNLRLETCL MRDEFIDTPT TSITGTLSSS
QGEEDKAKHS QIAGGTHSQS KSGTESGTGN DQVTGNEGDI EDAAPSYYSD MVEDHRTKIL
SSSPFVKFMQ PYLLEQARQY EQKLGQLKKL KNQYTTEDGE EDIEDTEQQF ELVQPEMVHT
VVQKASKQVR EFLSAVHASE YDKALHHYIT QKRQWETYVS GNMDLYDPFN HQKIAVLYSV
VNTATSTPCI GPEIIALGFY QEHDYDDGFT PDCTLGQYVE DLCTSAGVVC EVDNCNRRML
DHSRQYVHGE GQMSVIVQKQ PPKLKGLYQT ILMWSCCRIC GQETQTFPMS EWSWKYSFAK
YLELTFWSTR LHPRADLCPH DINKDHVRYF GYNNVALRIQ YDPVPLYEVT VPKPNVTWKV
DSDLRLKNEQ YLKIEERLDC FMNSVLDRIQ DIHPDSVIPE KVDLCRKEVD RLVRRANEDH
AWMRHKLQDK YMNSKYYEII PMNRAIRAIQ EKAIAWDETF LDFEQQFFPS EKDIRRLATL
QLRKFFLERD ESTSSLTSVE EGAESGAEDV DMDEKDAALA LSPMPSNMSP EKAQDMLASV
VHEEHSVDSS STEKGPASPQ TPTPSTPSKG SSDLSIQTHR EAIERDDVRH LDLALSSNFS
DQPVSNEDLL KTPTLAAQTA QDAQYDQGSP TPTSVPKINP IDRSLAEAIE NMPTSPSPQP
NSNVPLESKI PRLVDNGRRE APQRPTSLIR TQSQPGNVPK HTPPSIASML PASSFNTPKP
AMSDSMRALE RMGERLGMGT MKQGKSASRI PRSIPFKQSS KVSKLAEHFE QLSREFQKER
MRERRADRSR QIRAYPLASS KPVVEVYRDV HEAVQEHNAS DEDMLSTSPP RTSMDDSTLG
DSAFHGTTPT TVESQSPVDE RYPHNVAVEY SEHEEQPLTS TNPPSVSDIE NDISDIDIAA
EDVPLPDSIA SSQLMNMSES QLESSLELPR HEKTTLLKML TNFWSERSSS GWAPLDYPFA
PMEHVWEDSD IIVREDEPSS IIALALSSPD YLTKLQSFRD DPWAAKKEFE NLETRDDSIE
RNLLHEVNSN IRYSFTNRGV RVQCKIFFAQ SFDALRRKCG VADRFVESLS RCSNAKSIFL
KTLDDRFVLK SLSPIEVQAF FRFAPNYFAF THQNLFKSLP SVIAKMFGLF QVQIKSPAGR
DFDWFMLVME NLFYDREPNR RYDLKGSMRN RKIQSTGERD EVLLDENLVD IIYSETPIFV
REHTKKLLKA SVWNDTLFLS QNNVMDYSLM AGFDDTNREI IVGIIDCIRT YTWDKKLESW
IKDRGKNKPT ITSPKDYRMR FRVAMEKYIL QAPNCWHQFS GRIVQQGNER SRGVLEGPGA
NTGAGGSGKV RGHKRNTSGS SAGGKMRRRG QGTVVALE
//
