ID A0A091RK62_9GRUI Unreviewed; 1597 AA.
AC A0A091RK62;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=phosphoinositide 5-phosphatase {ECO:0000256|ARBA:ARBA00013044};
DE EC=3.1.3.36 {ECO:0000256|ARBA:ARBA00013044};
GN ORFNames=N332_08640 {ECO:0000313|EMBL:KFQ28922.1};
OS Mesitornis unicolor (brown roatelo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Mesitornithidae; Mesitornis.
OX NCBI_TaxID=54374 {ECO:0000313|EMBL:KFQ28922.1, ECO:0000313|Proteomes:UP000053369};
RN [1] {ECO:0000313|EMBL:KFQ28922.1, ECO:0000313|Proteomes:UP000053369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N332 {ECO:0000313|EMBL:KFQ28922.1};
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; KK801308; KFQ28922.1; -; Genomic_DNA.
DR Proteomes; UP000053369; 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; cd09098; INPP5c_Synj1; 1.
DR CDD; cd12719; RRM_SYNJ1; 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 InterPro; IPR034971; SYNJ1_RRM.
DR PANTHER; PTHR11200; INOSITOL 5-PHOSPHATASE; 1.
DR PANTHER; PTHR11200:SF158; SYNAPTOJANIN-1; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000053369}.
FT DOMAIN 119..442
FT /note="SAC"
FT /evidence="ECO:0000259|PROSITE:PS50275"
FT REGION 1044..1317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1557..1597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1073
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1141
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1231..1269
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1299..1317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1571..1597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1597 AA; 176845 MW; 66A3C20863192E81 CRC64;
MAFSKGYRVY HKLDPLPFSV IVETRNREEC LMFESGAVAV LSSAEKDTIK NSYSKVMDAY
GLLGVLRLNL GDTLLHFLVL VTGCMSVGKI QDSEVFRVTS TEFVSLRIDS TDEDRISEVR
KVLNSGNFYF AWSATGVSLD LSLNAHRSMQ EHTTDNRFFW NQSLHLHLKH YGVNCDDWLL
RLMCGGVEIR TIYAAHKQAK ACLISRLSCE RAGTRFNVRG TNDDGHVANF VETEQVIYLD
DSVSSFIQIR GSVPLFWEQP GLQVGSHRVR MSRGFEANAP AFDRHFQTLK NLYGKQIIVN
LLGAKEGEHM LSKAFQNHLK ASEHSADIKM VNFDYHQMVK GGKAEKLHSV LKPQVQKFLE
CGFFYFDGKE VKRSQSGTVR TNCLDCLDRT NSVQAFFGLE MLTKQLEVLG LAEKPQLVTR
FQEVFRSMWS VNGDSVSKIY AGTGALEGKA KAGKLKDGAR SVTRTIQNNF FDSSKQEAID
VLLLGNTLNS DLADKARALL TTSSLRVFSR TILNKNNIFS NVFAASVKVL KSMCENFYKY
AKPKKIRVCV GTWNVNGGKQ FRSIAFRNQT LTDWLLDAPK LAGIHEFQDR KSKPVDIFAI
GFEEMVELNA GNIVNASTTN QKLWAAELQK TISRDYKYVL LASEQLVGVC LFVFIRPQHA
PFIRDVAVDT VKTGMGGATG NKGAVAIRML FHTSSLCFVC SHFAAGQSQV KERNEDFVEI
ARKLGFPMGR MLFSHDYIFW CGDFNYRIDI PNEEVKDLIR QQNWDALIAG DQLINQKNSG
QIFRGFLEGK INFAPTYKYD LFSDDYDTSE KCRTPAWTDR ILWRRRKWPF DRSAEDLDLL
NASFHSDSNV PYTWNPGTLL HYGRAELKTS DHRPVVALID IDIFEIEAEE RQKVYKDVIA
TQGPPDGTVM VSIRSSSAEE NYFDDNLIDD LLQKFATHGE VILIRFVEDK MWVTFLEGSS
ALNVMNLNGT ELLGKIINIS LKNPDWIRSL EDEMSLEKIN IGLPSSTSST LLCEDAEVTA
DYDMEGDIDD YSAEVEEILP QHLQPTSSSG LGTSPSSSPR SSPCQSPTLS DGPTLPVRPS
RAPTKTPGPP VSTPTEFQLG SQQKDSSQSL EPKRPPPPRP VAPPARPAPP QRPPPPSGGR
SPAPARKEFG GLGAPPSPGV ARREVEAQKS PGTQRKDNLV RNQPPPSAGI SSTGTAGYGT
ARPTVPPRAG VISVPQSHVR PSGGRPAPEA QTKPAEPPRG SPLLPEPLKP QAAGPAQPTT
QPPPVLRMQE PLIPVTSHPS QTNAPQSLEP PQPPPRSRSS HSLPSESPPS QQQIKTNGTH
GTKLETQLNS DPFEDLSFKL LVSKMQTSAR TSPVPTLNQK ELIQLPSATE RNADILNAVN
CMPAMPPMPT FNTSQEHKRS SPNPFITGLN CTNPFTERTP NAGNPFRMET QEPEVTSHLL
EGRAACNPFP SLNPPSCNTS KPAFSVDASA NTFCLRSKSL MVKNVQPKGW VTFDDDEENF
NVKLKPSNSV PDFKQISSTK SAGSPDLLGT EQNTFLGSDF NFDNDWNKGS SDCFYTMPAR
RPPAPPIPSR ATSNRSPADP FTSLAPKVSP TQDFTER
//
