ID A0A200QCU5_9MAGN Unreviewed; 1828 AA.
AC A0A200QCU5;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=BVC80_209g12 {ECO:0000313|EMBL:OVA08293.1};
OS Macleaya cordata.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Macleaya.
OX NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA08293.1, ECO:0000313|Proteomes:UP000195402};
RN [1] {ECO:0000313|EMBL:OVA08293.1, ECO:0000313|Proteomes:UP000195402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BLH2017 {ECO:0000313|Proteomes:UP000195402};
RC TISSUE=Root {ECO:0000313|EMBL:OVA08293.1};
RX PubMed=28552780; DOI=.1016/j.molp.2017.05.007;
RA Liu X., Liu Y., Huang P., Ma Y., Qing Z., Tang Q., Cao H., Cheng P.,
RA Zheng Y., Yuan Z., Zhou Y., Liu J., Tang Z., Zhuo Y., Zhang Y., Yu L.,
RA Huang J., Yang P., Peng Q., Zhang J., Jiang W., Zhang Z., Lin K., Ro D.K.,
RA Chen X., Xiong X., Shang Y., Huang S., Zeng J.;
RT "The Genome of Medicinal Plant Macleaya cordata Provides New Insights into
RT Benzylisoquinoline Alkaloids Metabolism.";
RL Mol. Plant 10:975-989(2017).
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:OVA08293.1}.
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DR EMBL; MVGT01002328; OVA08293.1; -; Genomic_DNA.
DR STRING; 56857.A0A200QCU5; -.
DR InParanoid; A0A200QCU5; -.
DR OrthoDB; 5481504at2759; -.
DR Proteomes; UP000195402; 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 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:UP000195402};
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 1468..1795
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 112..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1223..1242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1805..1828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1097..1128
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 326..341
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1828 AA; 202942 MW; 0B30DE42650CEE1C CRC64;
MDTPDKPRAE LVDIVKSWIP RRTEPANFSR DFWMPDHSCR VCYECDSQFT IFNRRHHCRL
CGRVFCAKCT ANSIPAPSPE QKTGREDCER IRVCTYCFKQ WEKESATGHN GIHVSSQGLS
PSPSTTSLAS TKTSGTGNSN CSIIGSVPYS TGNYQFVAYG SGLSLDQSVQ MELGADKQDR
IASTSSTGPV ADIGDPSPDP FEYCMNRSDD DEDEYSVYRS DSESRHFPQV DDYYGPLEFD
EIDHAYGPHK LHSDEENIIA KDLRGSLLNG ELDSQGLEGN KEHEEETEGQ NNGDECEAAS
LEGTDAEPVD FENNGLLWLP PEPEEGENDG ICDDDDDEEA TGEWGYLRSS SLGSGEYRSR
DRSSEEHKKA MKNVVDGHFR ALVAQLLQVE NLPVGEEDDK ESWLEIITSL SWEAATVLKP
DTSKSGGMDP GGYVKIKCLA CGRRSESLVV KGVVCKKNVS NRRMTSKIEK PRFLILGGAL
EYQRVSNHLS SFDTLLQQET DHLKMAVAKI DAHHPNVLLV EKSVSRFAQE YLFAKDISLV
LNIKKPLLER IARCTGAQIV PSIDHLSSQK LGYCETFHVE KFLEAHGSAG QGGKKLVKTL
MFFEGCPKPL GCTILLKGAN GDELKKVKHV LQYGVFAAYH LALETSFLAD EGASLPELPL
KSPITVALPD KPSSIDRSIS TIPGFAAPAT AKPQGPQPNG DPQRPNRTLA PELNFPTDPC
NSNMEIAQSS GLSKSPTSQY RGATSSFMKS SSFSFLSTPE NFVSNPLHNE PYHPYEEKNK
LGIGDSIETN TSTSNISKDI VGDPLVKNVE ASGGDGALTN DAHIDHNDMP VDESTTFKLA
SLQQDGNNYL DEPGSSKEEF PPSPSDHQSI LVSLSTRCVW KGTVCERSHL FRIKYYGSFD
KPLGRFLRDH LFDQSYCCRS CEMPSEAHVH CYTHRQGSLT ISVKKLPELL LPGEREGKIW
MWHRCLLCPR INGFPPAIRR VVMSDAAWGL SFGKFLELSF SNHAAASRVA SCGHSLHRDC
LRFYGFGNMV ACFRYASIDV HSVCLPPSKL DFSHDNPEWI QKEANEVVDR AELLFTEVLN
ALRQIAVKRL GTSSLKVAES RRRIADLEEM LQKEKAEFEE SLQKTLSREV KKGQVDIDIL
EINRLRRQLL FHSYVWDQRL IYASSSDSSS LQEGISSSIP NCKENSLSST EKLVGTNSAS
KQGKGFASCD SFLMDAKCDE NSNLEGSGEH HHQTRLTHQG VDGDPFPNHP KVSEPCLSSS
ISLGVPSDPL ESGIHVRRAL SEGQFPIVAN LDAAWTGENN PGNTTPKENG YAHPEVADSS
IKVEAALVRL QLEERSEDLG RAEVTASPTP AVKVTYNMED YTGWVGMPFL NFYRSFSKSS
SGSNSKLDTL SDYNPVYVSS FYELERQGGS RLLLPVGVND TVVPIYDDEP TSIISYALVS
PDYLVQMSDE RERPKDGGES SVLLPLYDSM SLQSFHSFDE TASESFRSLG SVDSGILSMS
GSRSSLILDP LMYTKASHAR VSFADDGPLG KVKYTVTCYY AKRFETLRRT CCPSELDFVR
SLSRCKKWGA QGGKSNVFFA KSLDDRFIIK QVTKTELESF IKFAPAYFKY LSESIGTRSP
TCLAKILGIY QVTSKHLKGG KEYKMDVLVM ENLLFKRNVT RLYDLKGSSR SRYNPDSSGS
NKVLLDQNLI EAMPTSPIFL GNKAKRLLER AVWNDTSFLA SIDVMDYSLL VGVDEEKHEL
VLGIIDFMRQ YTWDKHLETW VKASGILGGP KNESPTVISP KQYKKRFRKA MSAYFLMVPD
QWSPPTIIPS ESQSDLCEEN TQGGTSHE
//
