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
//