ID A0A448YNQ7_BRENA Unreviewed; 1048 AA.
AC A0A448YNQ7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=phosphoinositide 5-phosphatase {ECO:0000256|ARBA:ARBA00013044};
DE EC=3.1.3.36 {ECO:0000256|ARBA:ARBA00013044};
GN ORFNames=BRENAR_LOCUS3247 {ECO:0000313|EMBL:VEU22516.1};
OS Brettanomyces naardenensis (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Brettanomyces.
OX NCBI_TaxID=13370 {ECO:0000313|EMBL:VEU22516.1, ECO:0000313|Proteomes:UP000290900};
RN [1] {ECO:0000313|EMBL:VEU22516.1, ECO:0000313|Proteomes:UP000290900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tiukova I., Dainat J.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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; CAACVR010000023; VEU22516.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A448YNQ7; -.
DR STRING; 13370.A0A448YNQ7; -.
DR InParanoid; A0A448YNQ7; -.
DR Proteomes; UP000290900; 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; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR046985; IP5.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR002013; SAC_dom.
DR PANTHER; PTHR11200; INOSITOL 5-PHOSPHATASE; 1.
DR PANTHER; PTHR11200:SF257; PHOSPHOINOSITIDE 5-PHOSPHATASE; 1.
DR Pfam; PF02383; Syja_N; 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:UP000290900}.
FT DOMAIN 78..428
FT /note="SAC"
FT /evidence="ECO:0000259|PROSITE:PS50275"
FT REGION 851..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..892
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..946
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..986
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1048 AA; 117488 MW; 80AE81BDC7B55676 CRC64;
MGTDVFLCVI TGRIEVASPM AGERINRIYD VEFPCLTKDV WDFLDINGNG YPVTDSDSDS
SAPGGFTPRI EQNPCYELRK ILSDGSFYYS TDFDLTSTLQ GRGIRKSQQQ LSVDRYHMDY
MWNAFMMKEI IHFRNNLDDE PKQALDSNRF LTTVIRGFAE SVKTTVGGKN ARLTIVSKQS
WKRTGTRFNV RGIDDDGNVA NFVETECILN DGLHAFAYTQ IRGSIPLFWE QDTALVSPKV
QVTRSFDASQ PVFEKHFANL NGKYGPVHIV NLLSKTKSSE VTLSRAYKEH FRALKEKTPD
SLYFTDFDFH QETSKTYADA DRVLRPLKPS LQDFGYFCYD LKENETIMEQ QGVFRTNCLD
CLDRTNVVQQ VISRAALDEY MADFNMSKDD YSSPYVSNTG DVIESPVHAK HSVLWADHGD
QISQIYTGTN ALKSSFSRSG KMGFAGALSD ATKSLSRIYI NNFVDKGKQV VIDTLLGKNS
NQMPVLIFDP VTEYLTDRLH QAEPEFTTFR DISIFAGTFN LSGASQGTSL AEWLFPEQLG
TSYPDIYLVG FQEVIELNAS SILKNDGSAG QYWKNAVQKQ LDQGPGPHYV LLRSEYMSSI
LLLLFVKEDE MTNVTQVEGK SKKTGLGGMT ANKGSVAIRF NYGSTSFCLF NSHLASGVTN
TEERFNDFLT CWNGIRFSRN RLIKHHDNVV WTGDLNYRVS LPNEDTRALI EQGMLAKLLS
YDQLGYEMKR HPELQGFTEL PITFPPTYKF DKLSDNYDTS EKQRVPSWTD RIMFQGDEIS
QLYYQRAAGI RFSDHRPVFG SFSARVKLVN SERKHSLTRK FLQEYKSTAA KSSGSVLIEL
NVYSGDEDSF ASSTWSSTNS APTLIDLSAP SEDSERQSSE PPPPIPRRLP RRVPPPFDAR
EVSEMVRNEP ELSGISSPIP MTDVASAGSS TSSTPISYSV MRPTRSRAGT SLPPLPPRES
TTTATLSTAN RPVPPVPRKS TSSSLVPPVL ASNKEAHKVP PLVPVKPKSL NVFYSELETD
TANEASQAVQ QNSPPPNQWM PMAPTKRR
//