ID B9T3Y2_RICCO Unreviewed; 1838 AA.
AC B9T3Y2;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 81.
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=RCOM_0417950 {ECO:0000313|EMBL:EEF29435.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
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DR EMBL; EQ974441; EEF29435.1; -; Genomic_DNA.
DR RefSeq; XP_002532951.1; XM_002532905.2.
DR STRING; 3988.B9T3Y2; -.
DR eggNOG; KOG0230; Eukaryota.
DR InParanoid; B9T3Y2; -.
DR OrthoDB; 5481504at2759; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0010008; C:endosome membrane; IBA:GO_Central.
DR GO; GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
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; 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 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:UP000008311};
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 36..102
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1481..1805
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 153..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1247..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1100..1131
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 189..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..346
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1838 AA; 203922 MW; 589947FAE99795F4 CRC64;
MDSSDKTFSE LVGLLKSWIP WRSEPSSVSR DFWMPDQSCR VCYECDSQFT IINRRHHCRL
CGRVFCAKCT TNSVPVPSSD PNTAREEWEK IRVCNYCFKQ WQQGITTFDN GIQVPSLDLS
SSPSAASLAS SKSTGTANSS SFTLGSMPYS AGTYQRAQQS AGPSPHQTSE MDVNSDNQIE
VTLGRSNGHV ADMSYQSPNP YAFSRNRSYD DDDEYGVFRA DSEARRFPQV NEYFHRDEFD
DMSNDEGSHK AHLDGENIDS KSLSSSPINP SFGSHGLEGG QQLGEKIEHG MDDEEETSSM
YPGDNRDAEP VDFENNGLLW LPPEPEDEED EREAGLFDDD DDDDEGHAAG EWGRLRTSSS
FGSGEFRNKD KSSEEHKKAI KNVVDGHFRA LVSQLLQVEN IPVGDEDDKD SWLEIITSLS
WEAATLLKPD MSKGGGMDPG GYVKVKCIAS GRRSESVVVK GVVCKKNVAH RRMTSKIEKP
RLLILGGALE YQRVSNHLSS FDTLLQQEMD HLKMAVAKID AHQPDILVVE KSVSRFAQEY
LLAKDISLVL NVKRPLLERI ARCTGAQIVP SIDHLSSPKL GYCDMFHVER CLEDLGTAGQ
GGKKLVKTLM YFEDCPKPLG FTILLRGANG DELKKVKHVV QYGVFAAYHL ALETSFLADE
GASLPELPLN SPITVALPDK PSSIERSIST VPGFTVPANE KLQGPQTSSE PQRSNNVPVA
YLDSTISSIG HVGRKPLADG PIFQSTAPTT SCISPTSFLS TVPFTVKVVS DSYRTFEQKN
KFEYGGSPVS ETTAANIKVA AIDEHLTVNG FGVSEGIIEK HSQNNLSKMV ASQSNIAVLP
SAPENKNNLE APGSLKEEFP PSPSDHQSIL VSLSSRCVWK GTVCERSHLF RIKYYGSFDK
PLGRFLRDHL FDQSYTCQSC EMPSEAHVHC YTHRQGTLTI SVKKLSEILL PGEKDGKIWM
WHRCLRCPRT NGFPPATRRV VMSDAAWGLS FGKFLELSFS NHAAASRVAS CGHSLHRDCL
RFYGFGNMVA CFRYASINVL SVYLPPLKLD FNSENQEWIQ KETDEVVNRA ELLFSDVLNA
LSQIAQKKSS LGPGNSGMKL PESRRQIGEL EAMLQNEKTE FEDSLQRALN KEAKKGQPVI
DILEINRLRR QLVFQSYMWD HRLIYAASLD NNSLQDDLNC SNTGHEEKAF ASTEQLNEMN
VNDKAGKGFG SFDSLPVGAK LLKIDRQGGL GINSDQSETV HREIDMSQDP NHEKNDRAEL
SGAMPTCDQP HGLEHSGNVR RTLSEGQVPI VSNLSDTLDA AWTGENHPGI GLVKDDSSVL
SDSAVADLST TSTAMEGLDL YSQLQDPNGS KVSNALSPAL STKGSDNMEE VGGYLRTPFL
NFYRSLNKTF YASPEKLETM GEYSPVYVSS FRELELQGGA RLLLPMGVRD VVIPVFDDEP
TSIIAYALLS PEYEDQLADD GERIKEGGDA NYSSNLSDHL TSQSFHSADE VTIDSHRSLG
YTDESILSMS GSHSPLVLDP LSYTKTMHAR VSFGDEGPLG KVKYSVTCYY AKRFEALRNR
CCPSELDFIR SLSRCKKWGA QGGKSNVFFA KTLDDRFIIK QVTKTELESF IKFAPEYFRY
LSESISSRSP TCLAKILGIY QVTSKHLKGG KESKMDVLVM ENLLFGRNVT RLYDLKGSSR
SRYNPDSSGS NKVLLDQNLI EAMPTSPIFV GNKAKRLLER AVWNDTSFLA SIDVMDYSLL
VGVDEQTHEL VLGIIDFMRQ YTWDKHLETW VKATGILGGP KNASPTVISP KQYKKRFRKA
MTTYFLMVPD QWSPPLLIPS KSQSDLCEEN TQGGTSVE
//
