ID A0A1R3H9U7_COCAP Unreviewed; 1841 AA.
AC A0A1R3H9U7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=CCACVL1_20796 {ECO:0000313|EMBL:OMO67101.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO67101.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO67101.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO67101.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMO67101.1}.
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DR EMBL; AWWV01012453; OMO67101.1; -; Genomic_DNA.
DR STRING; 210143.A0A1R3H9U7; -.
DR EnsemblPlants; OMO67101; OMO67101; CCACVL1_20796.
DR Gramene; OMO67101; OMO67101; CCACVL1_20796.
DR OMA; SWIPRRT; -.
DR OrthoDB; 5481504at2759; -.
DR Proteomes; UP000188268; 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:SF21; 1-PHOSPHATIDYLINOSITOL-3-PHOSPHATE 5-KINASE; 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 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:UP000188268};
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 1477..1804
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 132..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1208..1281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1335..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1817..1841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..343
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1242..1262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1841 AA; 203598 MW; 41082067D49D95A9 CRC64;
MGTPDNKLSD LVDIVKSWIP RRSEPPNVSR DFWMPDHSCR VCYECDSQFT VFNRRHHCRL
CGRVFCAKCT ANSVPAPSDE PRAGREDWER IRVCNYCFKQ WEQGVAAVDN GTNAPSPGLS
PSPSATSLAS TKSSCTCNSS SSTVGSTPYS TGPYHRVNYN SGLSPRESAQ MNASPTEQNN
ETSEMSTNPS SAAVDSSSNH FGFCGDRSDD DDDDYGAYRS DSESRHYAHA EDYYGAINID
DIDHVYGSDK VHPDGENSDA KSLSCSPLPE NFDTKSGDGI KNCEELNERE NADDGEATGY
DGTDVEPVDF ENNGLLWLPP EPEDEEDERE AALFDDDDDD EGARGEWGYL RSSNSFGSGE
FRSRDKSIEE HRQALKNVVE GHFRALVSQL LQVENLPVGD EDGGESWLDI ITSLSWEAAT
LLKPDTSKGG GMDPGGYVKV KCIASGHRNE SAVVKGVVCK KNVAHRRMTS KIDKPRFLIL
GGALEYQRIS NHLSSFDTLL QQEMDHLKMA VAKIDAHHPN VLLVEKSVSR FAQEYLLAKD
ISLVLNIKRP LLERIARCTG AQIVPSIDHL TSPKLGYCDV FHVEKFLEEH GSAGQGGKKS
MKTLMFFEGC PKPLGYTILL KGANGDELKK VKHVVQYGVF AAYHLALETS FLADEGATLP
ELPLKSPITV ALPDKPSSID RSISTIPGFT VPSSGKPLAS QPTNELQKSD NVIILNRPSS
ANVEPSSKFT GASLSSLSKG PHTQNMFKES TSGSIEAIVS LDSLSVWKDI SSNNNVSSVN
DVFREVHRMD PKESVQTKTA SGEAVMDDRF HSLRQSLSNA PEQGGGSNHA DGNTLAAHHL
GGPELASSKQ DTIINNEEVG SSKEEFPPSP SDHQSILVSL STRCVWKGTV CERSHLFRIK
YYGSFDKPLG RFLRDHLFDQ SFRCRSCEMP SEAHVHCYTH RQGSLTISVK KLPELPLPGE
REGKIWMWHR CLRCPRANGF PPATRRVVMS DAAWGLSFGK FLELSFSNHA AASRVASCGH
SLHRDCLRFY GFGRMVACFR YASIDVHSVY LPPSKLEFNY DNQEWIRNEA NEVSTRAEFL
FSEVYNALQK FSEKVLGSGS QEGCVKAPER NICIKELEAM LQKDREEFQE SFQEMLSKEV
KVGQPVIDIL EINKLRRQIL FLSYVWDQRL IHAFSSINNI QEVMSSSIPK LGLNSVSSVD
KLVEMNISPK PSKSLTSSNS ALVETKPDIN INQGGNTGEI SEPGGDHKER GMEQELNNRK
EAEPSISDAN TSEKSDSLES GKVVRRALSE GEFPIMANLS DTLEAAWTGE SHPASTVPKE
NGYSVPDSVV ADTSTALNSD MGNHTSDRGE AETAPSPQSA LPTKGSENLE KSMSWASMPF
PNFHSSFNKN ASFNAQKLSI SEYNPVYVSS FRELERQSGA RLLLPVGVND TVVPVYDDEP
TSIIAYALVS SDYHSQMSDL ERPKDAADSA VSSSIFESMN LLSLSSFNDS SSDTYRSFGS
GDESILSLSG SHSSLASDPL LYTKDFHARV SFTDDGPLGK VKYSVICYYA KRFESLRRTC
CPSELDFIRS LSRCKKWGAQ GGKSNVFFAK TLDDRFIIKQ VTKTELESFI KFGPAYFKYL
SESISTRSPT CLAKILGIYQ VSSKHLKGGK ESKMDVLVME NLLFRRNVTR LYDLKGSSRS
RYNPDTSGSN KVLLDQNLIE AMPTSPIFVG SKAKRLLERA VWNDTSFLAL IDVMDYSLLV
GVDEEKHELV LGIIDFMRQY TWDKHLETWV KTSGILGGPK NAPPTVISPQ QYKKRFRKAM
TAYFLMVPDQ WSPPTIVPSG SQTDLCEENQ NTQPGSISVE S
//
