ID A0A024TMY3_9STRA Unreviewed; 1391 AA.
AC A0A024TMY3;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=H310_10976 {ECO:0000313|EMBL:ETV95510.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV95510.1};
RN [1] {ECO:0000313|EMBL:ETV95510.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETV95510.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KI913980; ETV95510.1; -; Genomic_DNA.
DR RefSeq; XP_008875704.1; XM_008877482.1.
DR EnsemblFungi; H310_10976-t26_5; H310_10976-t26_5-p1; H310_10976.
DR EnsemblProtists; ETV95510; ETV95510; H310_10976.
DR GeneID; 20088026; -.
DR VEuPathDB; FungiDB:H310_10976; -.
DR OrthoDB; 5481504at2759; -.
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; 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 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 3..63
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1049..1377
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 648..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1391 AA; 154539 MW; B2B41A982DBD22CA CRC64;
MPDKVCKVCS DCGESFNIFR RRHHCRGCGH IFCHSCSPYA VESIEQGVKT HVRICKRCHM
NHSSSAINTT EVAMDFPPGL MSPIVSQTVF DYGNVAGFDL EFDPSDTVLP SVVDTSDTAQ
RSNSLYAHLF RRPSSELASA LKAIHDAEEH LEKSASSMLD MVDEESGGRG SMSQDQHWHR
DHLDCQSPPL SSTKSRLSAR HSFTEGMDGC QGLWADHPDH IEAPVEPTPC TPFEAHQMAG
RRQLRKLLVR GLDTAVDSLL PDAKDRVAVQ DELERVIDET TDLLIRATYN RNAADGMFNH
QDMLHIKTIA EVPDDVPSTD TRSTYTGQVI HGIVCRKNVS HKKAPRMLEN PRVLLLGGSI
VTDRESLKLT KFEDLLNDEA VYAQQLVDKI LAVKPSVVFV EQSVSRLAQD QLQLHNIALV
LKVKEATLRR LERLTRAKMV PSIDTMQPDD TSVVGTACGS FAVMPMRVAD LTKEPGGWKR
DSILIVDGCD ASAGCTILLK GPNKAVLRAL KALVLQLVPR AYDLMLRAEA LADLAYPVRS
NLADDEPDDK WTFQVIKYML KHRDEVHKPK FSQCSRPQPH EVAFYSKHDK ALGSYLQKEG
IDSSTKCQVP NCKVPLIEHL EAYSFFNGTV LISTEHLPDV ARTEIERTEG QHAAAAASDN
QPLERSGTCM DDDSTGPTIF FWRHCRECSK MVMPPRLLPV TTLKFSFARF LETIFNVPGP
QSMPGHGPSE LCTVYESIPL ESSDDSAATT LLANKGQASE TSRHDQDPRD CICPHDGQTQ
HLLYFKCGKR AIRVEYMHDE PWSIKHDKCL HFDQNWYVAH QRQQAADLKQ AMANHFAVLY
AKLRTLPPSS REVMCLELLM KTAQKTYMNE LTDLMEHGEV VHASSVVDAN TVRRAFYHSC
CDWSVMVHKI TKSLSANATP LDTSPPSNDI APVGDVDGMP ATPLAQSARV ELDALGLDTS
STEGAPVEGD LPPLPPISVK ELSTGEMTPP VTMSSPSPMS WTTALSNSLG AILLGDKKPM
DTLALDPHHA VPDVFAGGHP FLPVGANDRV VYVYDHLRFS FVTYALNSSE YLNETTAIRA
ALEHDHVGEF LTSPVDTTVK LKVSSSDVEF TCQVHYALQF EALRCMFYGG LVDFVRSLAT
SQHWSAKGGK SGATFFRTSD DRFVIKYISQ VELQSFLASA LSYFAYIGKV EAESANSVLC
KLVGVYTVTT KKWTEHLVVM ENIFCNAPHV DQVFDLKGST RNRYLVTHDA HPDVLLDGNF
LERHLGLPCP LHCRSYTKLV DAIRNDARFL SDNNIMDYSL VIGYASNVPV ANDDKTVTTT
NRVLLVGIID YLRHFDFLKR MESVGKSVTM IAGQAAPTVV QPKQYARRFV DAIEQTYFMP
VPSFTESVET P
//
