ID   A0A1X2GSQ9_9FUNG        Unreviewed;       330 AA.
AC   A0A1X2GSQ9;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Agmatinase {ECO:0000313|EMBL:ORX59641.1};
GN   ORFNames=DM01DRAFT_318695 {ECO:0000313|EMBL:ORX59641.1};
OS   Hesseltinella vesiculosa.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Hesseltinella.
OX   NCBI_TaxID=101127 {ECO:0000313|EMBL:ORX59641.1, ECO:0000313|Proteomes:UP000242146};
RN   [1] {ECO:0000313|EMBL:ORX59641.1, ECO:0000313|Proteomes:UP000242146}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3301 {ECO:0000313|EMBL:ORX59641.1,
RC   ECO:0000313|Proteomes:UP000242146};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC       {ECO:0000256|ARBA:ARBA00009227}.
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:ORX59641.1}.
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DR   EMBL; MCGT01000005; ORX59641.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X2GSQ9; -.
DR   STRING; 101127.A0A1X2GSQ9; -.
DR   OrthoDB; 161483at2759; -.
DR   Proteomes; UP000242146; 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   GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR   CDD; cd11592; Agmatinase_PAH; 1.
DR   Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR   InterPro; IPR005925; Agmatinase-rel.
DR   InterPro; IPR006035; Ureohydrolase.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR   NCBIfam; TIGR01230; agmatinase; 1.
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:UP000242146}.
SQ   SEQUENCE   330 AA;  36550 MW;  EF4C94BE36466E67 CRC64;
     MPSFAGISTF AHLPYLQCFD EGVVEDYDVA VLGAPYDIGV TFRTGARFGP SAIRESSKRI
     KGYNNEIKIN PFKSWAKLVD CGDIPFEPFD SEHAIKQIED HAKYVLQRPP KPDEEVAVPP
     RLVTLGGDHT ILLPVLRALR ETYQRPITVI HFDSHLDTWA PEIYNVKAKG SRFNHGNPLY
     HAAKEGLTTN GTSCHVGIRS SLYDEEDIAR DQALGFNIVK ANDIFSMGID GMVDRIKSII
     GPMDDTLLYL SIDIDVIDPS MAPATGTPES GGLLTREMKY ILRGLNGYNI IGMDVVEVAP
     AYDTQAQLTS YLAADLIYEI LSMIVKRGEQ
//