ID   A0A0M0BJM3_9ARCH        Unreviewed;       301 AA.
AC   A0A0M0BJM3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Agmatinase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AC481_01110 {ECO:0000313|EMBL:KON28521.1};
OS   miscellaneous Crenarchaeota group archaeon SMTZ-80.
OC   Archaea; Candidatus Bathyarchaeota.
OX   NCBI_TaxID=1685135 {ECO:0000313|EMBL:KON28521.1, ECO:0000313|Proteomes:UP000037599};
RN   [1] {ECO:0000313|EMBL:KON28521.1, ECO:0000313|Proteomes:UP000037599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMTZ-80 {ECO:0000313|EMBL:KON28521.1};
RA   Lazar C.S., Baker B.J., Seitz K.W., Hyde A.S., Dick G.J., Hinrichs K.-U.,
RA   Teske A.P.;
RT   "New insights into the roles of widespread benthic archaea in carbon and
RT   nitrogen cycling.";
RL   Submitted (JUN-2015) 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:KON28521.1}.
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DR   EMBL; LFWY01000004; KON28521.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M0BJM3; -.
DR   PATRIC; fig|1685135.3.peg.1241; -.
DR   Proteomes; UP000037599; 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; cd11593; Agmatinase-like_2; 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:SF42; ARGINASE 1, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11358; ARGINASE/AGMATINASE; 1.
DR   Pfam; PF00491; Arginase; 1.
DR   PIRSF; PIRSF036979; Arginase; 1.
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}.
SQ   SEQUENCE   301 AA;  33666 MW;  A1B4EDAEBD7ED6A1 CRC64;
     MYKESKKIFQ FYCSLNSKNF AGCNTSFDDA KYVILGVPYD KTSTYRPGSR FAPSHIREAS
     LNIETYSFKT NLDLEEIKIC DLGDLNIVDS LEETLKRLKI VVTEIVNADK IPIVIGGEHT
     ITTGVFKSLK ENSALMIFDA HLDFREEYMG SNFSHATFVR HLMNALGPEK IILAGTRAVS
     KVEVEYAKKI GLFYITTNEI QQNEANVIIN KIKSKISDLK KVYISLDMDV LDPAYAPAVG
     NPEGFGINIK DLMEIIYGLR DIPLSGFDLV EVVPHYDQGV TAIQAAKIIF EIISLTESVA
     K
//