ID A0A2G9H241_9LAMI Unreviewed; 1809 AA.
AC A0A2G9H241;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=CDL12_15803 {ECO:0000313|EMBL:PIN11587.1};
OS Handroanthus impetiginosus.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Bignoniaceae; Crescentiina; Tabebuia alliance;
OC Handroanthus.
OX NCBI_TaxID=429701 {ECO:0000313|EMBL:PIN11587.1, ECO:0000313|Proteomes:UP000231279};
RN [1] {ECO:0000313|Proteomes:UP000231279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. UFG-1 {ECO:0000313|Proteomes:UP000231279};
RX PubMed=29253216; DOI=10.1093/gigascience/gix125;
RA Silva-Junior O.B., Grattapaglia D., Novaes E., Collevatti R.G.;
RT "Genome assembly of the Pink Ipe (Handroanthus impetiginosus,
RT Bignoniaceae), a highly valued, ecologically keystone Neotropical timber
RT forest tree.";
RL Gigascience 7:1-16(2018).
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:PIN11587.1}.
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DR EMBL; NKXS01002909; PIN11587.1; -; Genomic_DNA.
DR STRING; 429701.A0A2G9H241; -.
DR OrthoDB; 5481504at2759; -.
DR Proteomes; UP000231279; 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; 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:UP000231279};
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 37..103
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1458..1784
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 1156..1181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1281..1317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1809 AA; 201408 MW; B682576953168C8A CRC64;
MGSTDNTKLS EIVDIVKSWV PRRAEPANMS RDFWMPDASC RVCYECDSQF TIFNRKHHCR
LCGRVFCAKC TANSIPAHSD EPKSGREDAD RIRVCSYCFK QWKQGSATGN NMMFESSPGL
SLSSSSSSLV STQSSCCTCN SGSSGGSAGY STGSFQLVSS AVGLSPHLST QMDSKSAKQD
QARSPGKLEY LNAGDVNEQF GPCSRSDDED DDYTICGSQS EATTISPGLT YGNNDSQIDH
IYESQEVHPN EGTAHPTYNS SLLPENFETQ GSDYATRLGE AANQRDDHVQ SGPPPLYGLN
DVDIDAVDYE NNSLIWLPPE PEDEEDEREA IISYDDDDDN AGKDATGEWS YLRSNSFLVG
ECRNRDRSNE EHRKAMKRVV DGHFRALITQ LLQAENLPAT EHESWLDIIT SLSWEAATLL
KPDTSRSGGM DPGGYVKVKC IARGHRNEST VVKGVVCKKN VAHRRMTSKI ENARLLLLGG
ALEYQRVANH LSSVDTLLQQ EMDHLKMAVA KIDAHHPNVL LVEKSVSRYA QEYLLAKNIS
LVLNVKRPLL ERIARCTGAQ IVPSIDHLSA PKLGYCDSFH VEKFLEDLGT AGHDGKKLTK
TLMFFEGCPR PLGCTILLKG ASGDVLKKVK HIFHYSVFAA YHLALETSFL ADEGASLPQL
PLTSPIKVAL PDKPSSIDRS ISMIPGYCAP SSETSQAQQQ PSNAFQPRND LFLDIRQSPG
TVPKAVSCSN AQTPNAEPAI RKMDVTDSCT NFSGPQWEQL SAVNFSQVDS ELDPSGRSVA
RTLGYLHEVE GNDDLDSNNF FKSEASGQGF SISPDEGNRL SSKLEGSQLV SPAHHNIDHP
DELGTLKEEF PPSTSVHQSI LVSLSTRCVW KGSVCEHAHL CRIKYYGNFD KPLGRFLRYH
LFEQDYQCRS CGMPSEAHVH CYTHRQGSLT ISVKKLQEVL PGEREGKIWM WHRCLRCPRT
NGFPPATRRV VMSDAAWGLS FGKFLELSFS NHAAATRVAS CGHSLHRDCL RFYGFGRMVA
CFRYAPIKVH SVYLPPSKLE FNHCKEEWIQ NEFDEVRSRA DLLFTEVLEV LRQISGKTKN
ETVKKAPEYG QQIAELDLML QKEKKEFEES LWSLLKKEGK SGEPEVDILE INRLKRQLIF
HSYVWDQRLI HVSKSNSQGL SSSIPREKPV NSRDKRTEMD VVSRSGRGFS SWDSSLVNFN
SDMVQSDVEH CQINSSKGIH EGEDISHTLS NRQDTDRYHS SRTNLSNQSY VLEFGKSVRR
ARSEGQFPVM ENISDNLDAA WTGNPQPETV TSKDMAAASP NTLPQESSSG RISTSAEPVV
GNCTNDRFVA EEACPVHSGL PAKGPSDMEN PSNWLRIPFS ALYRSFIRNS SAFAQKLGKI
ANYSPVYISS LRELVHQSGA RLLLPMASSD TIVPIYDDEP TSIITYAVVS PDYQDLMSGE
PDKQKESLES STSFSILDSV NLLALHSFDE SPSESLRNLG SADESILSSV SRNFSGLDSL
LFLNPLHARV SFIDDGPPGK AKFTVTCYFA KQFEAFRRTC CACELDFIRS LSRCKKWGAQ
GGKSNVFFAK TLDDRFIIKQ VTKTELESFI KFAPAYFKYL SESINSGCPT CLAKILGIYQ
VTSKHLKGGK ESRMDVLVME NLLFRRNITR LYDLKGSLRA RYNPDSSGSN KVLLDQNLIE
AMPTSPIFLG TKAKRLLERA VWNDTSFLAS IDVMDYSLLV GVDEEKHELV LGIIDFMRQY
TWDKHLETWV KASGILGGSK NMSPTVISPK QYKIRFRKAM SAYFLMVPDQ WPSSVIPSSG
SQSDLCEEN
//
