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Database: UniProt
Entry: A0A2K3V104_9DEIO
LinkDB: A0A2K3V104_9DEIO
Original site: A0A2K3V104_9DEIO 
ID   A0A2K3V104_9DEIO        Unreviewed;       312 AA.
AC   A0A2K3V104;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Agmatinase {ECO:0000313|EMBL:PNY82464.1};
GN   ORFNames=CVO96_14900 {ECO:0000313|EMBL:PNY82464.1};
OS   Deinococcus koreensis.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=2054903 {ECO:0000313|EMBL:PNY82464.1, ECO:0000313|Proteomes:UP000236379};
RN   [1] {ECO:0000313|EMBL:PNY82464.1, ECO:0000313|Proteomes:UP000236379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SJW1-2 {ECO:0000313|EMBL:PNY82464.1,
RC   ECO:0000313|Proteomes:UP000236379};
RA   Choi A.;
RT   "Deinococcus koreensis sp. nov., a radiation-resistant bacterium isolated
RT   from river water.";
RL   Submitted (JAN-2018) 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:PNY82464.1}.
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DR   EMBL; PPPD01000001; PNY82464.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K3V104; -.
DR   OrthoDB; 9788689at2; -.
DR   Proteomes; UP000236379; 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   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:UP000236379}.
SQ   SEQUENCE   312 AA;  33088 MW;  26F821AFAE56FF6E CRC64;
     MTIPPHLPYG GIPTFARAPI VEPGGEWRAN VAVLGIPFDL ALGFRPGARF APRALREASL
     RWVPPLTGLD GVTRLSGVTF ADAGDVVLPS LEPELARQRI SAAAEQVRDQ CSLPVFLGGD
     HSVTYPILRA FAGVPDLHIL QLDAHLDFTD VRNDTSYSNS SPFRRASEAL PNLVHITTIG
     LRGLRFDPEA VAAARARGHA LIPMTDVGAD LPGVLAQLPR GKNLYLSVDV DGFDPGVLPG
     TSSPEPDGLT YAQGMAILAA AARHNTIVGL DVVELAPNLD PSGRSELLAA RLIMETLCAV
     DESDSAQPGW KP
//
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