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Database: UniProt
Entry: A0A1V6RFL0_9EURO
LinkDB: A0A1V6RFL0_9EURO
Original site: A0A1V6RFL0_9EURO 
ID   A0A1V6RFL0_9EURO        Unreviewed;      1201 AA.
AC   A0A1V6RFL0;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Inositol polyphosphate-related phosphatase domain-containing protein {ECO:0000259|SMART:SM00128};
GN   ORFNames=PENVUL_c054G02785 {ECO:0000313|EMBL:OQE00330.1};
OS   Penicillium vulpinum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=29845 {ECO:0000313|EMBL:OQE00330.1, ECO:0000313|Proteomes:UP000191518};
RN   [1] {ECO:0000313|Proteomes:UP000191518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 29486 {ECO:0000313|Proteomes:UP000191518};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQE00330.1}.
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DR   EMBL; MDYP01000054; OQE00330.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6RFL0; -.
DR   STRING; 29845.A0A1V6RFL0; -.
DR   OrthoDB; 996872at2759; -.
DR   Proteomes; UP000191518; Unassembled WGS sequence.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
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; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_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   SMART; SM00128; IPPc; 1.
DR   SMART; SM00320; WD40; 3.
DR   SUPFAM; SSF56219; DNase I-like; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000191518}.
FT   DOMAIN          813..1151
FT                   /note="Inositol polyphosphate-related phosphatase"
FT                   /evidence="ECO:0000259|SMART:SM00128"
FT   REGION          1..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..137
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..160
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..181
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..320
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..406
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..440
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..460
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1201 AA;  133508 MW;  F40F31C5B7AB8A26 CRC64;
     MAMAGTGKQP DNNEDPPTPQ RPVSSLLSHF ENLSHRRAPS AAAASPRTST THLLATPEPS
     DDLRSSTRAS LDLPRPHVPW TPDEERPNVL QQLNAEHSRD RGFSGRRYGR PISMNFHRSS
     PQLPPTLTVQ SPQSPPRGQD RDEVWTPQGD GRKTRSPGHR PRESMSVSPA PPRPLSPIPK
     FGPPINAGGT IPRTSPGSLR VNLTGSPADR KLKSASLPPP ANRTPKPKIP AKPAMFSHRD
     GASSLTPRPE RASPDRSVSP FRTPPGSPDK PIKPQSTGKI SDRPIPARPT TEPPTRCSFD
     ERSPIPSANA RHDAREMGFS RIRPGPEPSR VSKPLMVQIP SIPVRPDDPM SAATAPPLSA
     QRFRASDIPY DRPGLPPRPS GVLRRSGVSP ARDSLGLNSA AQLTPIARSA PSFPRASESS
     APKPIQRQPS VAQESHLSSS LPERRVVRTD TEEEEQVEGP AISRTDYPDA SKANRRPPCF
     KSGPQDILTK YDTRLLAVCG KYVCTTGYLT RVWDLTTGDQ VMSLSHGETV KSLSLAFKPG
     KGLEDEGERI WLGTSAGDIH EVDIPSQSIV ATRAYPSRRE VIQILRHKKE MWTLDDEGRL
     LVWLPDETGA PNLQYSYHSP SERVARGHTF SMVVDDKLWL AAGKDVHIYR PHAQDDVPFK
     VFKRPLGLQH SGDVTSGSYT TREGGRVYLG HADGKVTVYS STDFTCLAVV NVSVYKINCL
     AFVGDYLWAA YKTGMIYVYD VSTNPWTVKK DWRAHDSPVS SFVLDMSSVW TMNRLQVTSL
     GTDNCIRLWD GMLEDDWLDA RMQARDVEFC KFREIKAAVV TWNAGASTPG SLRTSDFIRN
     VVTPDDPPDI VVFGFQELVD LENKKITAKS LLLGSKKKEN GEKEHMSRQY RVWIDHLTRA
     LHECMPLEES YVLLHSANMV GLFTCVFVKH KERHNIKNVS ASEIKRGMGG LHGNKGALVL
     RFVLDDSSIC FVNCHLAAGQ TQTTNRNNDI AAILEAESLP AENNMTLRTD QFASGGDGSM
     IMDHEICILN GDLNYRIDAI PRNVIIDAIR QNNLPKLLDR DQLLASRRKN PGFRLRSFIE
     SPITFAPTYK YDVGTDEYDS SDKKRSPAWC DRVLYRGLGR VKQIDYRRHE VRASDHRPVS
     AAFKIRVKTV LSKERNATWE ACNTEFQDEK RRLASETSIE YLITVLGTDP RQARTLILGK
     Q
//
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