ID C1G6D2_PARBD Unreviewed; 1255 AA.
AC C1G6D2;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 2.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Inositol polyphosphate-related phosphatase domain-containing protein {ECO:0000259|SMART:SM00128};
GN ORFNames=PADG_02737 {ECO:0000313|EMBL:EEH46639.2};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH46639.2, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH46639.2, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH46639.2,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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DR EMBL; KN275959; EEH46639.2; -; Genomic_DNA.
DR RefSeq; XP_010758107.1; XM_010759805.1.
DR AlphaFoldDB; C1G6D2; -.
DR STRING; 502780.C1G6D2; -.
DR GeneID; 22582167; -.
DR KEGG; pbn:PADG_02737; -.
DR VEuPathDB; FungiDB:PADG_02737; -.
DR eggNOG; KOG0565; Eukaryota.
DR HOGENOM; CLU_002027_1_1_1; -.
DR InParanoid; C1G6D2; -.
DR OMA; CVFVKHK; -.
DR OrthoDB; 996872at2759; -.
DR Proteomes; UP000001628; Unassembled WGS sequence.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IEA:UniProt.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR046985; IP5.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR11200; INOSITOL 5-PHOSPHATASE; 1.
DR PANTHER; PTHR11200:SF240; INOSITOL POLYPHOSPHATE 5-PHOSPHATASE C9G1.10C-RELATED; 1.
DR Pfam; PF19056; WD40_2; 1.
DR SMART; SM00128; IPPc; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001628}.
FT DOMAIN 864..1202
FT /note="Inositol polyphosphate-related phosphatase"
FT /evidence="ECO:0000259|SMART:SM00128"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..179
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1255 AA; 138950 MW; E2A688229E54918F CRC64;
MEHRNNNGND GADDDSIKPV SSLLSHFENL ARLKPNSHHA CPTPASHELR DSPSTFLETP
HVVLGRASLD LPRPDTSIWT ASHSHSPSSS GWLQTPRRDS GIATQNADGS PGRRIPARPV
SMNVSSASWK APALTANTPH SSSQKNVIPA AENRTREAQQ APELSIPERP PPRRPPSNQS
RPSSRPSTPL VDSAGSKPGG SPRQKEHWAR DSKSNSKSSS HPPPVNRAEK PKIPATKRSI
AAPRLEASSS LAPESRRTSF DDKISPFTTP PNTPDKTPPG SIATNGHASA ALIREPISAI
EPGPRSALHD PTPLSNPCRS AALEVKTTGF SAVKSATAAL NREVKQPPPP PPLKRSNTGF
ARPRNARETI DTHDASDNLE DRPGLPLRSQ PRMSPKGVVP SWTGGREVPP RSKPPPRPSF
DISSSKTAPP PSSSLRIGSG ESSTNFLPPR RDSAAIVGRI PSEPVLSNPT QFARSPMRSV
ESLSSSPISN QRQIGRSALV ESDESEYTFD DAPIPHTDYP DFSNTNRRPP VFRSGTRGIH
TKHDTRVFDV CGNYACTTGY FTRVWDLVSG EQVLGLNHGE TIKGLSIAFK PGNTMHDEGK
LLWLGTSAGE IHEVDIQTQS IVSSRTSPSR REVIKIYRHK KELWTLDDDG KLLLWPPDES
GAPNLQYSYS HPYDRVVRGH TFSMVVGDQL WLVCGKEIHI YRPSAKDTSF QVLKGPLGKS
DAGEITSGTT STKDDDLVYF GHADGKVSIY SSKDYSCRAT LNVSLYKINC LAMVGDYLWA
GYKTGMIYVY DTSTKPWTVK KDWQAHDHAV CGLILDSSSV WTVNRLQVVS LGVDNYIRLW
DAMLEDDWLE TRMHSRDIEY CQFREISAAV VTWNAGAAIP GNLRDNKFIR DAIHPENPPD
ILVFGFQELV DLENKKITAK SILMGSKKKD SSDKEHMSRQ YRVWKDYLAT CIQAIMPLDQ
PYVLLHTSTL IGLFTCVFVR EAERERIRSL NAVEVKRGMG GLHGNKGALI LRFILDDSSL
CFVNCHLAAG QNHTAHRNND IAAILESSSL PMETNYSSRI DLFVGGGDGT LILDHEICIL
NGDLNYRIDS MPRNTVIDAV KANNLPKLLD RDQLLASRRK NPGFRLRSFN EAPITFAPTY
KYDVGTDQYD TSEKKRSPAW CDRLLYRGFG RIKQLEYRRH EVKVSDHRPV SGLFKMRVKT
ILPDKRTYVW ESCLEEFLEE KRRLASDASI DYLVRILGLN PQEARSLIAS GTGPK
//
