ID G3AZ67_CANTC Unreviewed; 2201 AA.
AC G3AZ67;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
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=CANTEDRAFT_119090 {ECO:0000313|EMBL:EGV66020.1};
OS Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC
OS 10315 / NRRL Y-1498 / VKM Y-70) (Yeast) (Yamadazyma tenuis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Yamadazyma.
OX NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN [1] {ECO:0000313|EMBL:EGV66020.1, ECO:0000313|Proteomes:UP000000707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 /
RC NRRL Y-1498 / VKM Y-70 {ECO:0000313|Proteomes:UP000000707};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
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DR EMBL; GL996512; EGV66020.1; -; Genomic_DNA.
DR RefSeq; XP_006684594.1; XM_006684531.1.
DR STRING; 590646.G3AZ67; -.
DR GeneID; 18248680; -.
DR KEGG; cten:CANTEDRAFT_119090; -.
DR eggNOG; KOG0230; Eukaryota.
DR HOGENOM; CLU_000480_3_1_1; -.
DR OrthoDB; 5481504at2759; -.
DR Proteomes; UP000000707; 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; 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}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Reference proteome {ECO:0000313|Proteomes:UP000000707};
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 273..346
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1866..2189
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1524..1564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1594..1636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1734..1776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1676..1728
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..534
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1536..1552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1601..1617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1746..1776
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2201 AA; 249678 MW; 0F555B1A6C1D85FE CRC64;
MNNSNVSVYG SDSTNIDNDD RQDANDEVKN PGLQKPQDQT SKVTSDSKTL RFSKQSVPVL
EATTESVTSS VINVNALANT EPDSTSKTNT PSLKDTSVTA SNRVTKKRSL KNLPNRISSI
FTNLPNDIEL SDDSASDTET VNDTSFLGGI PENSSLNQAG AVPPPELAMY RETSVKSSPV
KARQVRSPTA GTDASPTMNS FNTLKQYNMK KKSSNLSASL IDNARSIINQ NFHGNISSAS
SFVEKVTKKK RKTRPSQNPL KSGGIPKKYW MNDAFVSECL NCFKPFTAFR RKHHCRFCGQ
IFCSRCTLFI SYQEHKEQRK TGVINPDKRS YKDKLRVCRP CYSDVIVYLS DSDSSSSESE
QEVEDDAVSF ETLDKFKDDN LPQHPFVKSR SRSLSTSRRD FPFEGNKSFL KPALHDDKTT
VKSPLSLAIP SARKGDLLEV QYSKSNVNSS FSRSTSQEPS GASWLKNYPH LRRSKTQQNT
GLSRSNSFDN SSSLHGFISG KTDVSKKGKS MIFGDTNGDD PDDEDDEFES ENEDEQVMSL
YTSLNHSGFN GNANSSTISP RAPITRPLAN VSANAVPTLG EFPTMLVNEK LYPKNMSSGL
RSSPAGAVFP VFIPNNTKTD IDISADGGSV PRSVLEENPK SNLRSHERAH ASLLRMRSRR
RAKTARNLSL LTQNPTRLPQ LEFSDLRDSS SPISTPTSPT PGSGPSGAYF KDLITNEGFS
PLDKSPSDPQ TRHQISYGSL NNFDADDSDS ITRGLSGKAS REGLFDEIER QLDSVYLELF
KKILDQCLKD CDIKDDTQRW SNALTMSINF VNGLKLTDTL DIKQYVKIKK IPGGRIEDTQ
MINGLFMTKN IDSKKMSSRL SNPKIALLMF PIEYLKQKEQ FISLRIVQSQ QDVYISNLVS
RLISLEPDII VVGDTVCQLA KDFLEDANIT VISNTKPQVI ERISRYTRAD IFQSVNDLFF
KKGTLGTCQK FEIKKHLHGN VLKTFACFTG TDTELGFTIT LRGGDEETLN SIKYATENLL
STQINAKFEK SYFEDSKLVY LEDLPNESVS SLSSKLNQIK SEAEIENMGI EIIPDEKEVF
GYIAMFINRH ISTSPAAKFS LPTPLVNAVE AFFVFHNFNE RNKLLKSNES LDDVEMSLIE
ELKLNIGLEN MPNKAQDLLK FVKHAAEVKS KILLNQFQSR ARTWANYLKL PSYQLYPIFH
RNIHLLYSSV SKKFNTPCSG PNIIVVDFYT DNDKFLGLQL DQMFSESLTD CDECGEPMID
HYRNYVHGTG KLDMVVEKYE ALSAEHKNFP NQRTMWSVCK QCNYKTPVVL MSDDTYYFSI
GKYFEIAFWG RNVTLNNQGE CRHDFFKEHI RYFGFNDMAI KVEYFPIDTY EVVVPKKQTE
YDTSVEINLK VEAFDTIRTK SANFFDSISK RLNRVKVDTF DKAEDGAKVI EQMKERLDQQ
RSILEEDLLN IYNSTPSTYY LPMNSILREL QELGVAWDAD FNDFETQFLP SENEITRITQ
FHLRNFLIDK YNIDNAKEVE MNDMSKSVDS VGSEKEGLSS KSDEKTVKQQ DKDSELVQNL
NESPRKEIGK LIPRALEGPG SNVVDKVNKI EQKLEHERIQ NTGSRVSSGT GSMTDERKSG
FSPPKKASSK LLGRKSSDLS ISSVNSQLGV NSNKPVTKVS QLTNFFDQMS FDQISMEFKK
QREQELRKNL NKFRALPIVA SKPIVEMYNK IEDVVNADEL EVEKANRRLP RRLTSDSLIG
KRPDESTAPD LTRARPSDVN DSKDRDKQGE KLKEKDAKAI ENLKSKEKDK LLDIPQPERV
SLLKSLTNFW ADRSASLWDP LDYPLDSTEH TFADSDIIVR EDEPSSLVAF CLSTNDYKQK
IKSLAQEPDD DIKLDSEVNN KKFNSFAKIE KKFKNRFDNS KKPSELENIL TKNKSTHLKY
QFADGSTTLS CKIFYSEQFE ALRKACGKED RFLQSLSRCI KWNSSGGKSK SNFLKTLDNR
YIVKELSKSE LESFVPIAPF YFKYIGQSMF NTLTTALAKI FGIYQIQIKN IITGKTFRME
FLIMENLFYN NKTTRIFDLK GSMRNRHVTQ TGKEDEVLLD ENMIEYIYES PLFVKEHSKK
LLRGSLFNDS SFLSAMDVMD YSLIIGIDDQ TKKLYIGIID WLRTFTWDKK VENWVKGNNL
IGGNKGKDPT IITPKQYRIR FREAMERYIL EVPDIWYEGK N
//