ID   A0A0F0I6Y5_ASPPU        Unreviewed;       416 AA.
AC   A0A0F0I6Y5;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Arginase family protein {ECO:0000313|EMBL:KJK63480.1};
GN   ORFNames=P875_00065075 {ECO:0000313|EMBL:KJK63480.1};
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:KJK63480.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK63480.1, 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:KJK63480.1}.
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DR   EMBL; JZEE01000559; KJK63480.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0I6Y5; -.
DR   STRING; 1403190.A0A0F0I6Y5; -.
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:SF26; AGMATINASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11358; ARGINASE/AGMATINASE; 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..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..416
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002443202"
SQ   SEQUENCE   416 AA;  45269 MW;  6313617F3AC44FDF CRC64;
     MKYTLGLLAL AGTALSHAHH DDTEVVPEHL REELLKKWDQ EWTFSGIASF AHLKPVKCLI
     EPDERYDIAV IGAPFDTAVS YRPGARFGPR AIRAASARQM AGTAYNTRAG INPYSSWATV
     KDCGDIPIIP FDNGVAERQM YEAFLELGSR SPITPADSKY GTKGISAGKA KLVTLGGDHS
     VALPALRALY QIYQKPITVL HFDAHLDTWN PVRYSAYWTS EQSAFNHGSF FHKASREGLI
     CNSTSAHAGL RTRLTGVTDS DYTNPGPEQG FMRIHADDID DLGPMGIVDK IIERIGLDSE
     QPVYLSVDID VLDPATAPGT GTPEPGGWTT REFIRIMRGI EKLNIVGADI VEVSPSYDNK
     GETTALAAAQ VAFEIITSMV KAGAGEDLGG WYGRKEEKID ASAKEGEAKK EGKDEL
//