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Database: UniProt
Entry: A0A0V0RX20_9BILA
LinkDB: A0A0V0RX20_9BILA
Original site: A0A0V0RX20_9BILA 
ID   A0A0V0RX20_9BILA        Unreviewed;      1015 AA.
AC   A0A0V0RX20;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=phosphoinositide 5-phosphatase {ECO:0000256|ARBA:ARBA00013044};
DE            EC=3.1.3.36 {ECO:0000256|ARBA:ARBA00013044};
DE   Flags: Fragment;
GN   Name=Synj1 {ECO:0000313|EMBL:KRX18996.1};
GN   ORFNames=T07_10414 {ECO:0000313|EMBL:KRX18996.1};
OS   Trichinella nelsoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX18996.1, ECO:0000313|Proteomes:UP000054630};
RN   [1] {ECO:0000313|EMBL:KRX18996.1, ECO:0000313|Proteomes:UP000054630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS37 {ECO:0000313|EMBL:KRX18996.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KRX18996.1}.
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DR   EMBL; JYDL01000065; KRX18996.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0RX20; -.
DR   Proteomes; UP000054630; Unassembled WGS sequence.
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   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; 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   PROSITE; PS50275; SAC; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000054630}.
FT   DOMAIN          140..466
FT                   /note="SAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50275"
FT   REGION          981..1015
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        988..1002
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRX18996.1"
FT   NON_TER         1015
FT                   /evidence="ECO:0000313|EMBL:KRX18996.1"
SQ   SEQUENCE   1015 AA;  114038 MW;  032CD95F1A408926 CRC64;
     LYSCGYLENY DAKVMPFGRT YSVYLNAAGK ENIILLENTR NKNCVLGFAN GVVLSLDQKK
     WLILKSDCNK ICDVHACLGV LSLPVVETEG SFVQYLIVVK NASLIGQLFN CEAYRITDVN
     CLPLWGDFNQ KPSDPRIIQI QKLLSCGLFL FGWSNAQNAF VDISLAMQRQ FLNNKKGDTR
     FHWNVTLRSH LQQFGIDAED WVTPCICGVI EVKTAYVGHQ QAKACIISRI SSERMGTRFN
     VRGVNDFGNV ANFIETEQVI FYNDNVVSHV QVRGSVPLFW DQPGIQVGSH KIKINRSLEA
     SLVAYEKHFQ QMKICYGSAA IINLLGTKND ENTLSESYQT IHSDSAFDSI IPFISFDLHS
     EAKGSSRSEC LKKLWPKLET LVNTHGFFHC SGSELLRKQT GVLRVNCLDC LDRTNSVQSL
     IGLKILQQQL AALGLSDKAN ICTRFVELFK ACWTLNGDHC SKLYTGTAAQ EGKSKFKDAS
     ISVTRTIQGN LMDKSKQQAM NFLLRNSKLG TDTVAQINCI VPNRNFHVYP SIGISLIEKV
     EEFVDPLQLR LFCGTWNVNG GQLTSSVVFR NETSLADWLI NLMPNFNGDA SHRKPYDIYA
     IGLQEMVDLN ASNVLNASVS YQNSWRDAFL KELNSISQYV LLETIQLVGI CLFVFVQPEL
     LVHIRDVSTA AVKTGFGGTI GNKGGTAISF TLGASSLCFI CSHFTAGHSQ VQERNDDYEG
     TCRRLRFPSG LNLFSHDFIF WFGDFNYRID MSGEEVKHLV DLRDFDSLRE ADQLVQQKMA
     GCVFIEFEEG LINFAPTYKY DAFSDNYDTS EKARVPAWTD RIFFRKRRPY FKAQDTCQLL
     VYCRAELKTS DHRPVGAVFN LHIGHTNVDK LRNAVEDIVS SMGPRDATVM VSVQSQRDMV
     PFVDSVLEKI RHLGIKALLT KCIGEHLFCT FGKSEDAIAA LSMDGVKIGQ NVLCVRLKTT
     DWETDCQNVV NQLFNDDFDK NSKNSSLNDR RNNEAAMSNS TAPVPQRPPP PKRYS
//
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