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Database: UniProt
Entry: A0A0C3CUQ6_HEBCY
LinkDB: A0A0C3CUQ6_HEBCY
Original site: A0A0C3CUQ6_HEBCY 
ID   A0A0C3CUQ6_HEBCY        Unreviewed;      2274 AA.
AC   A0A0C3CUQ6;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 47.
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=M413DRAFT_439251 {ECO:0000313|EMBL:KIM47586.1};
OS   Hebeloma cylindrosporum h7.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Hymenogastraceae; Hebeloma.
OX   NCBI_TaxID=686832 {ECO:0000313|EMBL:KIM47586.1, ECO:0000313|Proteomes:UP000053424};
RN   [1] {ECO:0000313|EMBL:KIM47586.1, ECO:0000313|Proteomes:UP000053424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG   DOE Joint Genome Institute;
RA   Kuo A., Gay G., Dore J., Kohler A., Nagy L.G., Floudas D., Copeland A.,
RA   Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000053424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN831769; KIM47586.1; -; Genomic_DNA.
DR   STRING; 686832.A0A0C3CUQ6; -.
DR   HOGENOM; CLU_000480_3_0_1; -.
DR   OrthoDB; 5481504at2759; -.
DR   Proteomes; UP000053424; 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; cd03334; Fab1_TCP; 1.
DR   CDD; cd15725; FYVE_PIKfyve_Fab1; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000053424};
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          219..279
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   DOMAIN          1905..2246
FT                   /note="PIPK"
FT                   /evidence="ECO:0000259|PROSITE:PS51455"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          90..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          339..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          433..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1387..1506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1534..1691
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1716..1817
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..115
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        377..393
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1424..1440
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1441..1459
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1482..1496
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1610..1629
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1630..1652
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1729..1745
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1746..1760
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2274 AA;  254554 MW;  CC0EC5BC3A4B72B0 CRC64;
     MESPNAVESL SGHSSRSRSS TKLADDVTSL TSFNPFSEED EHDQSSYTLV TSIFSRMKNT
     LSAPLSSAVG VSANTSVSNN TNVTTVVGPE ARRPSYTTAQ TGSSTFSSRT NASDRPNPLA
     AAPAQAAPPL VSLTPAESEL PTFTVEYDRS PQIHNKVPYS PAFDVGENVP FGTSIPGFPI
     QDDARSVKTA TSVHRSGSVS KVIRRLRGEG LSRDYWMDDE NCKECYDCKS IFTTWRRKHH
     CRICGQIFCS RCASNIIKGA RFGSEGMVRV CNLCLEKLAK VEEDDDDDRR SVISSVTNFP
     AHQFGMDPFT NLAHPQSPFA ASQLFGRTDE PFNLYSVAET RRPLHSQDGS PSRAETSLMR
     EGENDVWEPV RDNPAPFRRG LSDEEKDVGQ PPSSFDHDHL APGPEGKSHI QFPTTQPINI
     DAPTSSIQFP LGSPEHIGTP RPLNRTKTSS TPYGEFEVAT PFIRSRVQSR LDPTFEAEPG
     WRTRRESTAY AQELNLASML HLKIMLRQML TIEGIPNIRE WEETLLRLAL RIAREMTFTA
     LPHRQGQDMD VRRYVKIKKI PGGMPKDSEY VTGAVITKNV AHKQMSRLQA NPRVMLVTFP
     LEFSRIEGQY MHFGQIVRQE KEYLGNLASR IAALRPHVVL VEKSVSRLAL DALAKHNIAV
     ARAVKPSAIQ TIARMTQGDI FSSMDKLALE PRLGHCARYC IQTYDHPLIP GRRKTYMRFE
     GCNRDMGCTI ILRGGDIETL KRIKKVTRFL TFIVRNLKLE THLWKDSVIS VPSFNALAIP
     SSTSRLLGLD ATAPSLLLGS SSLLPPRFFT SGLGLTSPPK DYDSSKNIGE EDLPNEDAEQ
     LRLSRRIDES LGHYTKTFIS VSATLRFPPP YPIQRMKELD NMLLEAKRAW EDEVVRKEER
     LQSLHRQEET ITAATVTSDI QTPELQPDMK REDIFAQIEA LPVLSLPSTP LPMDGFPSTS
     KLDDDLSYFT LGTLSPNPST PSTAVTPLYR VLAAEEPETM KTATDIYQQS HYTLLKWQHE
     EFRRIWEWYL RKNPDDFVVE KYQCIHLREY TIPATNIGQH RPCFAPRLQN IKFYGENDMT
     LGQFIEKSVN DTLVQFLDPK AVCTGKGCDQ PLARHCKVFV HNEATLFVAV EQWDGQIIGR
     SAYYPSPDLV TTWSACRVCG SATPFIPVSE EMQRYSFAKF LELHFYPADV KLVQGAGCQH
     NIYQHHIRYF ASKGMTVRFQ ANPIVLHEVV YPPFRIRVRP ETQLDLKNSD FERLHFRNML
     WYTQLIDDLK LISIDAATGD EETDALLLAD INVLITRAEA EREDISRLIN QIYRDSPPTD
     TLALNQVHAA RQDKIVAWEM DFDRLPKPRP AQTIVNRNSR SSAFDSMRAI WPSRKYDLAG
     AFDNPYIPPS SVSEAEEDPV KSRKTTIADS ASDASENEST EKGKQASDVS PASETKAISN
     NEATSDEHVR SDPDSDSTIG ATREDGGSQE IAPLPPQMPD EKEEILSTEE PGQRVSRLPR
     RTTQNMSVAE LVKKYQDFLP AQGVHDLAQT AFAPRPVMSE SEQEYPSQVT PRPGIRSKGR
     HRLPVRKAST SDFEQGYAAN VAPRYLPHSR KPIPAPSTSR IPAPKGPVFE SHESSRRASP
     DKRSFSNQGK EVRFSRPPSP HSTRSTVPGI KQPKNRVISR SKDKIAPRPP SIPNRSTFRR
     PPAGAGNKVS NIAKHFERLG RDAEKSKGRY AVIRGKRARP VASARAKVEV LDSVKDAIRD
     DSESSDSSSE ADDEDEGNDE EHPAPTAQPD LLEPKPNSLE SDLKIVPPSD SFPATNLDMG
     TQEGGATVPL PPPGHISLPS SPFLSSMKSK QETALTPPAS DIELGGPERN SILKALSGFW
     PQPARHSIEG DDPMNDPLHI FRDSSMVVRL DEPTSIIALA LDSPTYRDTL AKSRKIAREA
     KLTEGSEAFM PDECSIADSS STWNVVNVDS TETVDPTGEL RVPSSKLPLA ITFESNGLTI
     SCTVLYPEQF DALRRTYDCE KSMVESLSRC VKWNASGGKS GSAFLKTRDD RFIAKELSKP
     ELQTMETFAP AYFDYMSSSV SANRPTLLAK VFGCYKLTFR KTGKDKGPGK SKSTQMNLLV
     MENLFYDKRF TKIYDLKGST RNRHVRSTGR ENEVLLDENL VEAAHDKPFY LREHSKRILR
     GALYNDSKFL ADINVMDYSL VCGVDSENNE LVVGIVDYIR TYTWDKKLES WVKESAFLGG
     AGKGEPTIVT PKQYRQRFLG AMERYFPLVP DRWMKQTDTP EEDSIVLSEL WPDW
//
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