ID   A0A0F8TZC5_9EURO        Unreviewed;       313 AA.
AC   A0A0F8TZC5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Agmatinase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ARAM_006327 {ECO:0000313|EMBL:KKK12668.1};
OS   Aspergillus rambellii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK12668.1, ECO:0000313|Proteomes:UP000034291};
RN   [1] {ECO:0000313|EMBL:KKK12668.1, ECO:0000313|Proteomes:UP000034291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK12668.1,
RC   ECO:0000313|Proteomes:UP000034291};
RA   Moore G.G., Beltz S.B., Mack B.M.;
RT   "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT   Species Obtained from the Cote d'Ivoire.";
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:KKK12668.1}.
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DR   EMBL; JZBS01004006; KKK12668.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F8TZC5; -.
DR   STRING; 308745.A0A0F8TZC5; -.
DR   OrthoDB; 161483at2759; -.
DR   Proteomes; UP000034291; 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   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:UP000034291}.
SQ   SEQUENCE   313 AA;  33668 MW;  5358E1A9F835C53D CRC64;
     MAGTAYNTRA GINPYSSWAT IKDCGDIPIT PFDNGLAERQ MYEAFLELGT RAPITTTPAA
     TSSAQGGSKG ISAGRAKLVT LGGDHSVALP ALRALYRIYQ KPITVLHFDA HLDTWNPVRY
     SAYWQSEQSA FNHGSFFHRA SREGLICNAT SAHAGLRTRL TGVDDADYTA PGPEQGFMRI
     HADDIDELGG PMGVVDAIIR RIGLDPEQPV YLSVDIDVLD PATAPGTGTP EPGGWTTREF
     IRILRGLEKL NIVGADIVEV SPSYDNNAET TALAAAQIAY EIITSIVKAG AAENLGGWYG
     RKEVPESVYK DEL
//