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Database: UniProt
Entry: G3AZ67_CANTC
LinkDB: G3AZ67_CANTC
Original site: G3AZ67_CANTC 
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
//
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