ID A0A091ITT3_CALAN Unreviewed; 1588 AA.
AC A0A091ITT3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=phosphoinositide 5-phosphatase {ECO:0000256|ARBA:ARBA00013044};
DE EC=3.1.3.36 {ECO:0000256|ARBA:ARBA00013044};
GN ORFNames=N300_07309 {ECO:0000313|EMBL:KFP03071.1};
OS Calypte anna (Anna's hummingbird) (Archilochus anna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC Trochilidae; Calypte.
OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFP03071.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFP03071.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFP03071.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL218200; KFP03071.1; -; Genomic_DNA.
DR STRING; 9244.A0A091ITT3; -.
DR Proteomes; UP000054308; 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; 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; IPR000504; RRM_dom.
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; 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:UP000054308};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT DOMAIN 119..442
FT /note="SAC"
FT /evidence="ECO:0000259|PROSITE:PS50275"
FT DOMAIN 919..974
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 1033..1317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1548..1588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1099
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1131
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1235
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1243..1274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1275..1289
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1290..1317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1558..1588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1588 AA; 176153 MW; 4FD54A6786B4E384 CRC64;
MAFSKGYRVY HKLDPLPFSV IVETRNREEC LMFESGAVAV LSSAEKDTIK NTYSKVMDAY
GLLGVLRLNL GDTLLHYLVL VTGCMSVGKI QDSEVFRVTS TEFVSLRIDS TDEDRISEVR
KVLNSGNFYF AWSATGVSLD LSLNAHRSMQ EHTTDNRFFW NQSLHLHLKH YGVNCDDWLL
RLMCGGVEIR TIYAAHKQAK ACLISRLSCE RAGTRFNVRG TNDDGHVANF VETEQVIYLD
DSVSSFIQIR GSVPLFWEQP GLQVGSHRVR MSRGFEANAP AFDRHFQTLK NLYGKQIIVN
LLGAKEGEHM LSKAFQSHLK ASEHSADIKM VNFDYHQMVK GGKAEKLHSV LKPQVQKFLE
CGFFYFDGKE VKRSQSGTVR TNCLDCLDRT NSVQAFFGLE MLTKQLEVLG LAEKPQLVTR
FQEVFRSMWS VNGDSVSKIY AGTGALEGKA KAGKLKDGAR SVTRTIQNNF FDSSKQEAID
VLLLGNTLNS DLADKARALL TTSSLRVSEQ SLQSASVKVL KSMCENFYKY AKPKKIRVCV
GTWNVNGGKQ FRSIAFRNQT LTDWLLDAPK LAGIHEFQDR KSKPVDIFAI GFEEMVELNA
GNIVNASTTN QKLWAAELQK TISRDNKYVL LASEQLVGVC LFVFIRPQHA PFIRDVAVDT
VKTGMGGATG NKGAVAIRML FHTSSLCFVC SHFAAGQSQV KERNEDFVEI ARKLSFPMGR
MLFSHDYIFW CGDFNYRIDI PNEEVKELIR QQNWDALIAG DQLINQKNSG QIFRGFLEGK
INFAPTYKYD LFSDDYDTSE KCRTPAWTDR ILWRRRKWPF DRSAEDLDLL NASFHNDRDV
PYTWTPGTLL HYGRAELKTS DHRPVVALID IDIFEIEAEE RQKVYKEVIA TQGPPDGTVM
VSIRGSSAEE NYFDDNLIDD LLQKFASYGE VTLIRFVEDK MWVTFLEGSS ALNVINLNGT
ELLGRTINIS LKNPDWIRSL EDEMNLEKIN IGLPSSTSST LLCEDAEVTA DYDMEGDIDD
YSAEVEEILP QHLQPTSGSG VGTSPSSSPR SSPCQSPTLS DGPALPVRPS RAPTKTPGPP
VSTHTEFQLG TQQKEPSQSL EPKRPPPPRP VAPPARPAPP QRPPPPSGGR SPAPARKEFG
GLGAPPSPGV ARREVEAQKS PGTQRKDNLV RNQPPPSTGI SSTGTAGYGT TRPTIPPRAG
VISAPQSHVR PSGGRPAPET QTKPAEPPRG SPLLPEPLKP QAAGSAQPTT QPQPVLKMQE
PLIPTSSQPS QTSAPPQSLE PPQPPPRSRS SHSLPSESPP PQQQIKTNGI YGTKLETQFN
SDPFEDLSFK LLVSKMQTSA RTSPVPTSNQ KEFIQLPLAT QQNADPLNTV NCMPSMPPIP
TFNSSQEHKR SSPNPFISRL NCTNPFTERT PNAGNPFRVE TQQSEITSHF LEGRAACSPF
PPLNTPSCNT SKPVFPVDAS ENTFCSRSNS LMVKNVQPKG WVTFDDDEDN FSVKLKPSKS
VPDFKRISSR NSAGSPDLLG TEQNTFLSSD FNFDNDWNRS STDCFYTMPA QRAPAPPIPS
RITSNRSPAD PFTSLAPKVS PTQDVTER
//
