ID I7ZU14_ASPO3 Unreviewed; 527 AA.
AC I7ZU14;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Multiple inositol polyphosphate phosphatase {ECO:0000313|EMBL:EIT75539.1};
GN ORFNames=Ao3042_08531 {ECO:0000313|EMBL:EIT75539.1};
OS Aspergillus oryzae (strain 3.042) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1160506 {ECO:0000313|EMBL:EIT75539.1, ECO:0000313|Proteomes:UP000002812};
RN [1] {ECO:0000313|EMBL:EIT75539.1, ECO:0000313|Proteomes:UP000002812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3.042 {ECO:0000313|EMBL:EIT75539.1,
RC ECO:0000313|Proteomes:UP000002812};
RX PubMed=22933657; DOI=10.1128/EC.00160-12;
RA Zhao G., Yao Y., Qi W., Wang C., Hou L., Zeng B., Cao X.;
RT "Draft genome sequence of Aspergillus oryzae strain 3.042.";
RL Eukaryot. Cell 11:1178-1178(2012).
RN [2] {ECO:0000313|Proteomes:UP000002812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3.042 {ECO:0000313|Proteomes:UP000002812};
RA Zhao G., Hou L., Wang C., Cao X.;
RT "Comparative genomic analyses of Aspergillus oryzae 3.042 and A. oryzae
RT RIB40 for soy-sauce fermentation.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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:EIT75539.1}.
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; AKHY01000175; EIT75539.1; -; Genomic_DNA.
DR AlphaFoldDB; I7ZU14; -.
DR SMR; I7ZU14; -.
DR HOGENOM; CLU_020880_2_0_1; -.
DR Proteomes; UP000002812; Unassembled WGS sequence.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR016274; Histidine_acid_Pase_euk.
DR PANTHER; PTHR20963; MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE-RELATED; 1.
DR PANTHER; PTHR20963:SF43; PUTATIVE (AFU_ORTHOLOGUE AFUA_7G01240)-RELATED; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR PIRSF; PIRSF000894; Acid_phosphatase; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR000894-2};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..527
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003712853"
FT ACT_SITE 82
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT ACT_SITE 382
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT DISULFID 71..435
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 288..301
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ SEQUENCE 527 AA; 57281 MW; 41422F0AD5E53FEE CRC64;
MQQLLQSTAA LLAFQAVVGD AAPTSSSSAA ASGPTGASYP SGFDMSTSWG NLSPYKDQPG
FEVPNGVPRG CELSQVHVLH RHAQRYPTSW KLDGGVIEDF AQKLKNYTKR HDNATVGKGA
LSFLNEWEYV LGEDLLLVSG AATEATSGAN VWSKYGRALY HAPVGVASYD SSLNVYPNGT
ERPKPIFRTT DQARILESAR WWLSGFFGNT GANSSYSEYD LVITHEGTGF NNTLASDGSC
PGDLEEGDDS GEKFIPNLTK DALKRLSHFL PSDFNLTAYD VVGMFSLCPY ETAALGSSSF
CSLFTEQEWR DFEYFVDLQF YGNYGFGAPT GRAQGIGYVL ELAARLEGKR IETSDTSINA
TVDSKPATFP LNQPLYMDMS HDDVIVGVLA ALGLKYFNYG SKGLPDDVAH AVPRNFKLNE
VTPFGAHLIS EIWTCPEKTN FHELDGALYK NPDLSSTSDT TDVIRFVLNG SPVSQEGLDG
CETSINGFCS VEDFLKGVPK LKVKAEYQYA CFGNYTAGHQ VGDGRPE
//
