ID A0A0N0U2V0_9HYME Unreviewed; 1881 AA.
AC A0A0N0U2V0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=WN51_07374 {ECO:0000313|EMBL:KOX68078.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX68078.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX68078.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX68078.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX68078.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KQ435955; KOX68078.1; -; Genomic_DNA.
DR STRING; 166423.A0A0N0U2V0; -.
DR OrthoDB; 5481504at2759; -.
DR Proteomes; UP000053105; 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:0035556; P:intracellular signal transduction; IEA:InterPro.
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; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR043548; PIKfyve.
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; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
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; PTHR46715; 1-PHOSPHATIDYLINOSITOL 3-PHOSPHATE 5-KINASE; 1.
DR PANTHER; PTHR46715:SF1; 1-PHOSPHATIDYLINOSITOL 3-PHOSPHATE 5-KINASE; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF01504; PIP5K; 1.
DR SMART; SM00049; DEP; 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 SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50186; DEP; 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053105};
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 127..182
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 280..354
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
FT DOMAIN 1532..1865
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 40..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1502..1533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1547..1582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1547..1576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1881 AA; 212885 MW; 28ED1DB749B80FE2 CRC64;
MNKNMNSPSK LTEFAPLSPE ESQPVVASLF SKFFNFTKSS QNVDDSTISP VTNEEQSSSD
SESWKQSEST EKSPEDDGSS MMNFPLDTRE GRSLPNVLKR ISNIVALKSN NLRSYKDSQL
RSYWMPDSVS KQCYECGERF TTFRRRHHCR VCGQIFCSKC CSDQIPGKIM GCTGDLRVCT
YCCKVVLSYL QSSDMRSDLS ADLKALQEDL QVKYGNDSPP ATQKCSHKSA EDETSICRKP
SVGYMEEKYA IGSYLTSQER SIVLQNSASL RMIYEELFRS SQAIVLQTHR VRLKCYHNCF
LANELVNWMI AQNKAATRVQ ATAIGEALLE AGFIEPVIVD NIFSDTATIF KPVKLLNMQS
IDLLTETQNT CDAQEPAWVK TIPQHDSTTD SESETKPSNS TQQTTGRLPS SSSSFYLDLN
LEASTVTLKR PTSEDLTTIS VDSSDGVIEQ KEVTVKSHKC NFKIADDLLN DTLQVQEFKE
KIGWHKPTNL RTMFGELHAY ECLISAYKQH EDSLIKQLLN KEGLSQSWLE VILPIAHQII
DFVRPDLNHN VDDLDIRQYI QIKKCSGGSR DDCEIVSGVV CTKNVAHRGM NAMIAHPKIL
LLQCGLMYQR VEGKLLSLEP VMLQENEYLG HTVARITALG PDVVLVHRSV SRLAQDRLRE
CGVTLVLNVK LSVLERIARC TGANIVNTID AHISARYMLG TCKKFYLRNF LSEKNGIKTL
MYFEGCANPH LGATILLRGG SQTELKKVKN VTSTMIFAAY SWRLEKSFLM DEFARPPSSK
DNPFLDDTYK DFKDFPETNK ILHNKASEGN DLLLSRSKEY ADKEKRIYGE SISDRSDPLH
QYLNEDEEDV FNQTSPNGQH LSVADLPLLN KFKKALEGTI LSVSPYLKFS IPYLETETGR
NCILRSFFPR EIFYSAQFED KVKEIKTVNV SSEQSVTESS LMKLKLKPQH PFVQARLTTD
VDSREVQALL ANFRACGSRL YPTNNVLSDQ QILIQSEASE QLPAWPDCLD PASHQRLSVL
FCSFSHTGNN DTPAFCVNPW VVNMDLYGRN DIALGRFLER YCLTYEYKCP AQACRAQIAH
HVRRFVHDGG CIHITLNEMS TDPFSQDSAN QILMWSKCMK CKGVSPVVPM SDDTWSLSFA
KYLELRFHGS AYTRRGTDTC QHSLHHDHCQ YFIKKNMLAV FKYTKISQWE ISLPPPVINI
MYDPKQHADV IEEMKGIALK GDEVFSCIRE KLTTLQTDLD ILNAVKQQLA KDQQYFKNKI
EEIQLKLTSP TLENKKLEGK VSEKQVQALM FRIEDGIVIL KRLISEVVFT WNAKILEISV
KKKDERPRRF TERSLTTGSN SIIDTDGYIT EDTASESQLE DLSPMSADYN AVDAIAAVQN
DLQGMEGLEN SDNEVLENNN PEDIVVIQGS PKMHQRSHSD VLPVTFDDIP DKKKKKKTIL
SQLLPSVPVI QPIPNPLGTL EHHLLPLGSV VPIVVYESEP SSIIAYALDS HDYKHTLHEL
MRSTKGPDLN PSPLNKRKFP ENKENVPDMT QSGEFKRPSV LSFFRGNSPN SASPLDSDKT
ISNVDSSTQN LSVTADTDED TKTKKQQNYI EVQFNDATTN FYCRIYFAAQ FATFRENVLP
CGEDGFTRSL SRSVQWAARG GKSGSTFCKS RDDRFIIKEM SRLEMQIFLD FAPNYFSYME
KCQQTKQPTL LGKIVGVYRV SFKNNTTNAA LRTSVLVMEN LFYKRTITDK FDLKGSVRNR
LVNPDDMCQE GELVLLDENL LNMSCDSPLY IRSHSKAVLN RAIEQDTKFL ADNSVMDYSL
LVGLEPNSDE LVLGIIDYIR TFTWDKKLET MVKKSGILGG QGKLPTIISP EEYRARFIAA
MHRYFLPVPD RWYGLGRGVE T
//
