ID J7RWD4_KAZNA Unreviewed; 2243 AA.
AC J7RWD4;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=1-phosphatidylinositol-3-phosphate 5-kinase {ECO:0000256|ARBA:ARBA00012009};
DE EC=2.7.1.150 {ECO:0000256|ARBA:ARBA00012009};
GN Name=KNAG0C01990 {ECO:0000313|EMBL:CCK69312.1};
GN OrderedLocusNames=KNAG_0C01990 {ECO:0000313|EMBL:CCK69312.1};
OS Kazachstania naganishii (strain ATCC MYA-139 / BCRC 22969 / CBS 8797 / KCTC
OS 17520 / NBRC 10181 / NCYC 3082 / Yp74L-3) (Yeast) (Saccharomyces
OS naganishii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071383 {ECO:0000313|EMBL:CCK69312.1, ECO:0000313|Proteomes:UP000006310};
RN [1] {ECO:0000313|EMBL:CCK69312.1, ECO:0000313|Proteomes:UP000006310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-139 / BCRC 22969 / CBS 8797 / CCRC 22969 / KCTC 17520
RC / NBRC 10181 / NCYC 3082 {ECO:0000313|Proteomes:UP000006310};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN [2] {ECO:0000313|Proteomes:UP000006310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-139 / BCRC 22969 / CBS 8797 / CCRC 22969 / KCTC 17520
RC / NBRC 10181 / NCYC 3082 {ECO:0000313|Proteomes:UP000006310};
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Kazachstania naganishii.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE978316; CCK69312.1; -; Genomic_DNA.
DR STRING; 1071383.J7RWD4; -.
DR eggNOG; KOG0230; Eukaryota.
DR HOGENOM; CLU_000480_3_1_1; -.
DR OMA; QEKVVEW; -.
DR OrthoDB; 5481504at2759; -.
DR Proteomes; UP000006310; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0044249; P:cellular biosynthetic process; IEA:UniProt.
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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE-
KW ProRule:PRU00781}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Reference proteome {ECO:0000313|Proteomes:UP000006310};
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 225..284
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1902..2231
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 167..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1483..1526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1560..1613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1708..1746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1767..1812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1887..1937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1088..1118
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 169..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1483..1503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1504..1521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1560..1594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1595..1610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1781..1797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1798..1812
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1887..1915
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2243 AA; 255006 MW; 60E8FFB9DF5CECF5 CRC64;
MDKVVEPDEK PRISVPLIPA GLSNGAAVPT TSTTEDFVPR AVLPTTATIG TTSAATTPTI
QLDENPLTAS GVSLAPNFDA SSKEGHQGQI PTILNEHTDF PDDHHQAHPV SPLIKQDSIS
FLPPANGVSP NVVHDKPRFN LASNAMNAQR SSIYASKSTV TAIPIRNPKS HRLVDEEEGR
SSRSRSSSIT TSLSKSFLFG FYHDKKKGGK QPSNYLISKE YWMKDESAKE CFACGKAFNT
FRRKHHCRIC GQIFCHSCTL IIDGSKFGYM EKMRVCYHCF EHADTWQDSS DEEDTEDELD
VHAHEHLNED IGHTWEERTQ DGNTNSLDDT HSILEQNDNH EIPNSILPAD QFTSKSISNK
SLFERTLIAK RQREFILLNK DDAQSIMTSG EDSKLFVSTP SPPPKMAIPA TRQGESLEIS
FTANDLDRPR LKDGNIDSYS SHLSKPTQSN ERYSIRDVDM IPANYLHRQN RHRKTTSSHS
PAPDSNYQRR SMNSLKRSIF NYVGNKTQSS SERSRGLNDE SASAIPLRKS TPLSAGQESG
DSYMDQSDRV IGNFTNKNFK FQFNFSKENG HKKIERTSSL PKHPLDSSEN EEVGNDQDSL
EDEGTMSIYS SLNDASKSTN PIRSTRNSSK SFQRAQASLQ RIKTRRKSRS KAGTSSLYKD
ITKLTHSTPN LLSVVTDNGD NSNDYTLSGI EPLTGDNVAV SDSPSSSKTN PVQKLTPDPH
QSPTKNLTMK YSTTQFGSDQ WRRLSSTFST RQLRTESFNN GKKNELSDVA ILHLEALLHQ
VLDDQNIGAM EAWTHFLKTI TLARLQNIEL SARDSNTLDY RQKYVKIKRI PGGRVEQSEY
IHGIVFSKAL PSKSMPRHID NPRILLVMFP LEYEKNGKHF LSIESVFAQE KEYLNKLISR
LTSLNPDIVY VGANVSGYAL ELLINANIVV QYNLKPQVIE RIARLTEADI VVSIDNLTAN
VKMGECESFS VKTFVYGNLS KTFTYLRGCD PKLGGSILLR GDTAENLEKI KHVTEFIVYV
VFSLKLESSF FNDNFIQISM PFYLERQANM AQLQCTGYFS DFLEKFNNRI LTVSPTVEFQ
IPFLLKKARE LEEIILRNEE QNKTLKDEDI SIDNLEVKDL HIESTITFKD MKYITKFIRQ
RNIEELRKEF IRRSRQWEVL YASTHNMLGT GSHQSINVLY SMVSTKTATP CIGPQVVAID
YFWDTDISIG QLIENIVSAA WYPCHQGCKG NLFDHYRSYV HGSGKVDILT EKFQTKLPKL
KNIILTWSYC KQCGTSTPIL QISEKTWNYS FGKYLEIMFW SKQGSLSDIG NCVHDFTKDH
VKYFGYNDLV IRMEYSELEV HELMTPPTKL KWQPSVDIKF KVENYYGILD KINRFYDSIV
DRLDRVKIDS IITAKQLSAK IKIDQLKELV YTEKRALCTE LEKVYQDYPG DQHLQMNVVI
RKVYDKAVSW DSEFDTFERQ YLPSETDITR ITSSQLRKLF KDTDKEQEKK VHSLDREKLS
KSNDVSGIDS NNGSGSKHQD DGSRQCSIRK DGSLQKLELA SSLKSSNSLA ASKLSTFKVP
TKENIPHQDT TVNQNEGDNA SGIRTVIHPR NTQLDSRRSS SDHDSTLTVG RGQRDSRVSQ
LANFFDKIHF DAISKEFELQ REFERLRLNK GNVQSYKVQT STPIVEIYRD VKDAVDEPLH
DPAKQAKNPR ESTRTLDEFE LGKFNDQKLK SGEERQIGTG FMNPEEFIDR RRNGNNKSSI
GKEVNKNLES ELENSINSWG ERVLNSHRQG EEDNDLKIDS KSNRSASSGT LKKQQLSKPT
KAIDKDEDDT QPDKSLLMKA LANFWADRSG YLWKPLVYPT LPSEHVFADN DVIIRDDEPS
SLIAFCLNMP DYKQKMVDMG SIIAQSMNSS TRRNPSQSVS GGDQETNTTL ETDGGLPGSL
PNPVLPRDQT QSTLPISLDT PEVLEATMTK KTAVHLRYQF QDNMTVMSCK IFFTEHFEAF
RKVCNAGDKY VQSLSRCVKW DSSGGKSGSS FLKTLDDRFV IKELSHSELD AFIKFAPSYF
EYMTQVMFHE LPTALAKVFG FYQIQIKNPN TAKSFKLDVI IMENLFYNKK PTRIFDLKGS
MRNRHVEQTG KKNEVLLDEN MVEYIYESPI HVREYDKKLL RASLWNDTLF LAKMNVMDYS
LVVGIDNENF LLTVGIIDFI RTFTWDKKLE SWVKEKGLVG GGGNGGVIKQ PTVVTPRQYK
NRFREAMERY ILMVPDPWYQ ENT
//
