ID A7EB46_SCLS1 Unreviewed; 2434 AA.
AC A7EB46;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 104.
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=SS1G_02532 {ECO:0000313|EMBL:EDN99674.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN99674.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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DR EMBL; CH476623; EDN99674.1; -; Genomic_DNA.
DR RefSeq; XP_001596312.1; XM_001596262.1.
DR STRING; 665079.A7EB46; -.
DR EnsemblFungi; EDN99674; EDN99674; SS1G_02532.
DR GeneID; 5492396; -.
DR KEGG; ssl:SS1G_02532; -.
DR eggNOG; KOG0230; Eukaryota.
DR HOGENOM; CLU_000480_0_1_1; -.
DR InParanoid; A7EB46; -.
DR OMA; QEKVVEW; -.
DR OrthoDB; 5481504at2759; -.
DR Proteomes; UP000001312; 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:UP000001312};
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 467..501
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 2086..2416
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1101..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1614..1635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1691..1722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1740..1834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1691..1711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1740..1789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2434 AA; 268781 MW; 52B6A8CDDD45EFE4 CRC64;
MSSHGSPRPS AGVPLLIPLR TRSRRGSLGS LASGTPVDKE QLAQALDKIH STACQSETLT
TFNEFAPPPP SSSNTESKGL AGDIMQNGLS GLYSRFKGAV GVGKDKAGSS SVKGDSESFD
ATSVKSQNAS NATPSSKGSS GPAREDSGIT ASPVQLSTAS SQLQSPTVSS FMGTSSEMQS
QAMKSSKTSL SSVPKTARSA SRPPLNPMAK TTLSSAIVPT VAPVNAVAFK EGEKTRLGSS
DGNILEKANK KSVSDRSEPV SASDYTHPGT FGSASASESR RFTGHPSVLD DPESVEFDSM
KSESAGRMSL SNLDSKKDSQ DLPLRISDSS NAGRAKSMSN PKTASATLSS IKTSDSRPNA
PPRLTILETA RRTPAVERIT QSHLPGYQAS RTSSTDRSTA EASPINTSAH NHVRHDSFGT
DERSSRTYSG RSRIPGTTTN GGSAEVVSAR LEQMRKQVLS KEFWMADDIC KECFLCGDPF
TAFRRKHHCR TCGCIFDSKC THTISGQRFG VQGSLHDESG LPTFFHSQQA KFDSSTSTKI
DLPEGPGADP MKIGDESRPL ATPMMAIPAT RRIGDSSNRR SAILEIDAPQ LSRPSSSRSL
KALSAATRPP SSSHRRHQSK HNFLGRFKSP VGDRAPFHRG LTDDIAKATR LPAFHDDNII
DPDLAPYMSD EGSSADEQMS IFATLHNSNT ATPPFENDRA GFGSLLNATK RHRARTGDKS
VSGISFTSRG LEDASATVGA FTRPNRRRNL SIASNTLHHT RPSPRQTKPT SLAKGFGNVS
EDVTAPENPS DPTTPAGMSS KMTRSASMRD AKAPAVELNN ASLHHVRRLL HQLLEDADIP
NVASWEKALI PILLQCTDDV NPDVRRGDDI DIRHYVKLKK IPGGKPGDTS YVSGVVFTKN
LALKSMPRSI ASPRIVIVSF PIEYQRHQSS FMSLEPVIAQ EKEFLRNMVN RIASLRPQLL
LVQKHISGLA LQYLAEANIA VIYNVKPSVI EAVSRCAQTE VISSIDMVAL KPVHIGKCSG
FDVKTYVHGD IPGKKKTYIY LSGCPKELGC TIALRGASMP ILAKMKQITE FMVYVVYNLK
LETCLMRDEF VLIPSVAESG NLSPARQTSQ TSKSTVSNAP PHQDTVVAAS NVLQAAAASE
KVKSFSQDGI GSSEGISADQ VLVTPETVTE AQKAISTEQK PEVSRMISAH ESHVHSSHDD
HLPEDVPMPT FYSDMVAKHQ TKILSASPFV KFVQPYLLVK AREQERRLVY LKRLRDQDMF
EEQTDTEKSK PQKFQLIKPD MVHESIKNAP RQIMEVLHAV HDAEYDKALH NYQTQTRQWE
NYIQGNLNLF DPYGHQNITV LYTVVCTETS IPCAGPDLLT LAFYTEHEIS AEIDPDCTLG
QYVEDLCLTI NTTCTFNGCD RKMSEHHRTY VHGEARITVF VERSPCKIKG LQDSILMWSY
CKKCQKETQV MPMSESTWKY SFGKYLELSF WSSDLHLRAG FCPHDLHRDH LRYFGFRNVA
IRIHYDPIDL LEIVVPRTRI TWKVDNDLRL KNELFTKIEE RWNRFMASVM SRIKGINIDS
VAPEKAEACK AEIDRLTKRA QEEHTALLRK LQDKYMESKY YEIIPLNRAK SFIPTSPEAT
FEPSPDTEES PEGHPAVVDD SLVADLTTIN SQSASNTESS MNEDQVQMPR HEGVEHLDLA
ISETADQQLT SKTLTPAETS DFLTSSPPDL ESPSDADIPT TPLEASLSEK IERLRRANQS
FSAENGQLQS ETSGIPRPTE RTSSRRSGAS PPLNRTQSQP ANTLRRMQPI STKAYHRLGD
TRKSSDSQIP LLEPLKPSTT EPVRPTDKRL SERLGLGSLK QNRKAGHSFI PRSVQPKRKE
SKVTTLAKHF EQLSREFEKE RLRDRRRMAA KVTQSRAFPK ASSKPIVEIY KDINEAVEER
GPPDEVPLDA EPTHINTEST SMTEGLAKLN MEPSSIETQP SSPDDTVAMG GAIADIEADD
THQNFSQTGS DDEGVTSDAE HSLLGDLLPG AEELAESLRV GKPDADLPME IPKHEKSSLM
KMLTNFWAER SASGWTQLEY PINAGEHIFV DSDVIIREDE PSSLIAFTLS SEHYRAKLND
LRQQGPVCAK PEEHDSMPTS DTPDLCEDGI NQAEVETSLL RATGTHLAYS FVDSSARMQC
KIFFAEQFDA VRRKCGVADR IVESLSRCLK WDSKGGKTKS VFLKTLDDRL VLKQLSPIET
QAFLKFAPAY FNIISEALFH ELPTAIAKML GFFQIVIKNP ATGTEIKWDV LVMENLFYDR
SPTRIFDLKG SMRNRKIQST GEQNEVLLDE NMVEFIYESP LFAREHSKKL LRSAIFNDTL
FLQRNDVMDY SLMVAVDEAR KELVVGIIDV VRTYTWDKKL ESWIKDRGFA GGGRNRPTVT
SPKLAPTSRW TAERGFKTDS AGGENTGFMI DPTL
//
