ID A0A093HXX7_STRCA Unreviewed; 1328 AA.
AC A0A093HXX7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=N308_14947 {ECO:0000313|EMBL:KFV87613.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV87613.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV87613.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV87613.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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}.
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DR EMBL; KL206965; KFV87613.1; -; Genomic_DNA.
DR STRING; 441894.ENSSCUP00000025307; -.
DR Proteomes; UP000053584; Unassembled WGS sequence.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR CDD; cd09099; INPP5c_Synj2; 1.
DR CDD; cd12720; RRM_SYNJ2; 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; IPR000504; RRM_dom.
DR InterPro; IPR002013; SAC_dom.
DR InterPro; IPR015047; SYNJ1/2_RRM.
DR InterPro; IPR034973; SYNJ2_RRM.
DR PANTHER; PTHR11200; INOSITOL 5-PHOSPHATASE; 1.
DR PANTHER; PTHR11200:SF148; SYNAPTOJANIN-2; 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; PS50102; RRM; 1.
DR PROSITE; PS50275; SAC; 1.
PE 3: Inferred from homology;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053584};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT DOMAIN 77..401
FT /note="SAC"
FT /evidence="ECO:0000259|PROSITE:PS50275"
FT DOMAIN 848..926
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 1003..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1181..1328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1025
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1073
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1248..1287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1306..1328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV87613.1"
FT NON_TER 1328
FT /evidence="ECO:0000313|EMBL:KFV87613.1"
SQ SEQUENCE 1328 AA; 149002 MW; 29F6A60E782A625B CRC64;
PEEKDAIKGQ YEKLLDAYGC LGELQLKCGN SRLHFLVLVT GCTSVGKILD AEVYKITATD
FCPLQEETKE EERVTALKKI LNSGMFYFSW PNAGSNFDLT VRAQKQGDNH YESGNSFFWN
QLLHVPFKHY QVNCSDWLLK VICGVVDIRT VYASHQKAKA CLISRISCER AGARFHIRGV
NDDGHVSNFV ETEQTIYLDD DVSSFVQIRG SVPLFWEQPG LQVGSHHLRL NRGLEANAPA
FDRHMMLLKE QYGKQVIVNL LGSRGGEEVL NRAFKKLLWA SSHAEDTPMI NFDYHQFAKG
GKAEKLENLL RPQLKLHWED FGIFTKGKNV NPRLQTGTFR MNCLDCLDRT NSVQSFIALE
ILLAQLESLR LNSKSIVERF VESYKAMWTL NGHNLSRVFT GSRALEGKHK VGKLKDGARS
VSRTIQSNFF DAVKQEAINL LLMGDFFSEE YADKGKMLMD HTALLVTPSI LKAMSERQFE
FTSFKRIRVA MGTWNVNGGK QFRSNILGTS ELTDWLLDSP KLSGVSEFQD DENCPPDIFA
VGFEEMVELS AGNIVNASTT NRKMWGEQLQ KAISRTHRYI QLTSAQLVGV CLFIFVRPYH
VPFIRDVAID TVKTGMGGKA GNKGAVSIRF QFHSTSFCFI CSHLTAGQTQ VKERNEDYKE
ITQKLSFPMG QNVFSHDYVF WCGDFNYRID LTYEEVFYFL KRQDWKTLLE FDQLQQQKSS
GKIFKDFHEG TINFGPTYKY DVGSEAYDTS DKCRTPAWTD RVLWWRKKLP FEKTAGEMNL
LDSDLNAETK VRHTWTPGAL MYYGRAELQA SDHRPVLAIV EVEVQEVNEA ARESVFQEVS
SFQGPLDATV VVNLLSPMPE EKNEFPEDLR TELMQMFEHY GTVVLVRICG GQMLVTFADS
KSALRVMDID GIKVRGRTVK IRPKTKDWLK GLQEEIARKR DSFAPKSPTA NSCLLEENFD
FSSLDYDSEG DIVEDEDDYL DDALCQHLVA DITDDLPERS GHFPSIALSN KSPLLTGQNP
QQCKDDTDLA DLKRELEASR ECHRRSPSRS LSVPNRPRPL HPPQRPPPPA GTSGKNSPSD
DSLPPGSQPA CSILATAKLL PGAPQQPPKV RTGISKPYNV KQIKTTTAEE AEEAIRCLME
AKGGLQEDAL KPAPARNQMF TKSEALPSIT KSLSFQGSQV GPVLVPHRPP PKVPTTKKPV
PLQRTGVKVE NAMSTEEQSD QQTMHSPFGL PEPCPEAGAI LSPTRITPVP KPRTSQPGKS
QESRGSSERQ PLSPSVAEAS ALPPQNTSFA PKVPPRRKKS APAALHLQVL QSSDNPLFRG
LMFSSNKN
//
