ID   A0A0F0IBL8_ASPPU        Unreviewed;       376 AA.
AC   A0A0F0IBL8;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   22-FEB-2023, entry version 19.
DE   SubName: Full=Arginase family protein {ECO:0000313|EMBL:KJK64127.1};
GN   ORFNames=P875_00138461 {ECO:0000313|EMBL:KJK64127.1};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK64127.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK64127.1, ECO:0000313|Proteomes:UP000033540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC   {ECO:0000313|Proteomes:UP000033540};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00742, ECO:0000256|RuleBase:RU003684}.
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:KJK64127.1}.
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DR   EMBL; JZEE01000523; KJK64127.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0IBL8; -.
DR   STRING; 1403190.A0A0F0IBL8; -.
DR   Proteomes; UP000033540; Unassembled WGS sequence.
DR   GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd11592; Agmatinase_PAH; 1.
DR   Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR   InterPro; IPR006035; Ureohydrolase.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR   PANTHER; PTHR11358; ARGINASE/AGMATINASE; 1.
DR   PANTHER; PTHR11358:SF28; HYPOTHETICAL ARGINASE FAMILY PROTEIN (EUROFUNG); 1.
DR   Pfam; PF00491; Arginase; 1.
DR   PIRSF; PIRSF036979; Arginase; 1.
DR   PRINTS; PR00116; ARGINASE.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR   PROSITE; PS01053; ARGINASE_1; 1.
DR   PROSITE; PS51409; ARGINASE_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003684};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033540};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..376
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002443046"
SQ   SEQUENCE   376 AA;  40282 MW;  36094B9093FE675E CRC64;
     MIPYSLLTLI VSTAAVAREI VFPPIAAIQG SGQVPLGKDD TVDIVTDSQF SGLTTFGHLP
     YVNCLMDDQA HSTPYDIAIL GAPFDTGVTA RPGARFGPVG IRLGSRRLQG WSIYTGVNVF
     ESWAKMVDCG DAPLTPLDNT VALKQLDLAH KVISSRPTNS TERGHTPRIL TLGGDHTTTL
     SALRSTYDKW GPVSVIHFDS HLDTWDPKVL GGGVSHYAGV NHGTFLHIAH EEGLIRNTSL
     HVGIRAPVIR PKGDIRNDIR CGFEIIKARD LDRVGITGIV EQIKARVGDS KVYISVDIDV
     LDPAYAPATG TAEPGGFTTR ELLSILDALH GLPVIGADVV EVAPIYDTTA ETTTLAAAEV
     AHSLLYLMVE TPVDDN
//