ID N6UKF0_DENPD Unreviewed; 969 AA.
AC N6UKF0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=phosphoinositide 5-phosphatase {ECO:0000256|ARBA:ARBA00013044};
DE EC=3.1.3.36 {ECO:0000256|ARBA:ARBA00013044};
DE Flags: Fragment;
GN ORFNames=YQE_02479 {ECO:0000313|EMBL:ENN81111.1};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:ENN81111.1};
RN [1] {ECO:0000313|EMBL:ENN81111.1, ECO:0000313|Proteomes:UP000019118}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA Birol I., Jones S.J., Bohlmann J.;
RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT a major forest pest.";
RL Genome Biol. 14:R27-R27(2013).
RN [2] {ECO:0000313|EnsemblMetazoa:ENN81111}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JAN-2017) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178,
CC ChEBI:CHEBI:58456; EC=3.1.3.36;
CC Evidence={ECO:0000256|ARBA:ARBA00001786};
CC -!- SIMILARITY: Belongs to the synaptojanin family.
CC {ECO:0000256|ARBA:ARBA00008943}.
CC -!- SIMILARITY: In the central section; belongs to the inositol 1,4,5-
CC trisphosphate 5-phosphatase family. {ECO:0000256|ARBA:ARBA00009678}.
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DR EMBL; APGK01020351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB740193; ENN81111.1; -; Genomic_DNA.
DR AlphaFoldDB; N6UKF0; -.
DR EnsemblMetazoa; ENN81111; ENN81111; YQE_02479.
DR HOGENOM; CLU_003016_5_0_1; -.
DR OMA; HPCHELR; -.
DR Proteomes; UP000019118; Unassembled WGS sequence.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR CDD; cd09089; INPP5c_Synj; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR046985; IP5.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR002013; SAC_dom.
DR InterPro; IPR015047; SYNJ1/2_RRM.
DR PANTHER; PTHR11200; INOSITOL 5-PHOSPHATASE; 1.
DR PANTHER; PTHR11200:SF257; PHOSPHOINOSITIDE 5-PHOSPHATASE; 1.
DR Pfam; PF08952; DUF1866; 1.
DR Pfam; PF02383; Syja_N; 1.
DR SMART; SM01165; DUF1866; 1.
DR SMART; SM00128; IPPc; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50275; SAC; 1.
PE 3: Inferred from homology;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 1..302
FT /note="SAC"
FT /evidence="ECO:0000259|PROSITE:PS50275"
FT REGION 851..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..879
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ENN81111.1"
SQ SEQUENCE 969 AA; 108615 MW; BFFE85A5E0D6D21A CRC64;
MLHVHLVRFG VDCNSWLLKA MCGSVEIRTV YAGPKKAFAA VISRLSCERA GTRFNVRGTN
DEGHVANFVE TEQVIYLDNE VSSYIQTRGS VPLFWEQPGV QVITQLITVG SHKVRISRGY
EASKSAFDRH MSMIKERYGK QVIVNLLGTS LIGSKEGEAT LSQEFQKHHK ESAFNDIPHV
VFDYHQEIRG GNQANLQKLR SKVEQQLQDF SYFHADGNAI YSLQTGTIRT NCLDCLDRTN
CVQTFFGLER LSYKSSISSQ ILTTQLQVMQ MVDKKITISR FEEVFRQMWI NNGNEISKIY
AGTGAIQGGS KIMDGARSAA RTIQNNLLDS SKQEAIDIFL LGSTLSTELA DRARHLLPYN
TLHAPPHVLR EMCKRYTEYT EALPVRVAVG TYNVNGGKHF RSLVFKDIKL SDWLLDNHKN
NQNLVDTSHS DVNRMTPVDI YAIGFEEIVD LNAANIMNSS SDNAKAWAVE LQKVLSRDCP
YVLVTYQQLV GVCLYVFVRP EHVPYIKDVG IDSVKTGLGG HTGNKGAAAI RLVFHATSLC
FVCAHFAAGQ SQVNERNADY NEITRKIGFP MSRSLNSHEY LFWCGDFNYR VDMDKDEIKE
LIKQGNYDAV LENDQLRKQQ LEGNVFKNFI EGKITFPPTY KYDLFSDDYD TSEKCRAPAW
TDRILWKRRK HSPEINGCAD HWTAGNLIHY GRAELKQSDH RPVIAIVDIE CRILNLNKRQ
DVFYEVIKDM GPPDSTLIVH CEDVSDEDDG CIFDEHMVLI LLEEFAQFGE TILVRFVGDK
MWITFRDGQS VLEAMRKTNG TLRIQDYDLT LSLKTPDWVE KAKDEIGFCS SNTIPLYSSP
SLGIPEVQQK MLPPARPLPP SRPPPPSMKS NPTPSPTKKP QPRAGVISIP VKPAPPPPSH
ASPILVPTIC SGLPSCASGS SNGAVPSTAP PDIPPPDLPS MPSLDQDVGI YEEITDDVNI
TIPEPQAVY
//
