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Database: UniProt
Entry: A0A264W247_9BACL
LinkDB: A0A264W247_9BACL
Original site: A0A264W247_9BACL 
ID   A0A264W247_9BACL        Unreviewed;       290 AA.
AC   A0A264W247;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Agmatinase {ECO:0000313|EMBL:OZS77668.1};
GN   Name=speB {ECO:0000313|EMBL:OZS77668.1};
GN   ORFNames=CF394_10690 {ECO:0000313|EMBL:OZS77668.1};
OS   Tetzosporium hominis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Tetzosporium.
OX   NCBI_TaxID=2020506 {ECO:0000313|EMBL:OZS77668.1, ECO:0000313|Proteomes:UP000217065};
RN   [1] {ECO:0000313|EMBL:OZS77668.1, ECO:0000313|Proteomes:UP000217065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VT-49 {ECO:0000313|EMBL:OZS77668.1,
RC   ECO:0000313|Proteomes:UP000217065};
RA   Tetz G., Tetz V.;
RT   "Tetzosporium hominis gen.nov. sp.nov.";
RL   Submitted (JUL-2017) 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:OZS77668.1}.
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DR   EMBL; NOKQ01000220; OZS77668.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A264W247; -.
DR   OrthoDB; 9788689at2; -.
DR   Proteomes; UP000217065; 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:SF43; AGMATINASE; 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:UP000217065}.
SQ   SEQUENCE   290 AA;  32216 MW;  D954697613F86D81 CRC64;
     MRFDEAYSGN VFIKSKQDYE NAQAVIYGMP MDWTVSYRPG SRFGPQRIRE VSIGLEEYSP
     YLDRELDDVN YFDAGDIPLP FGNAEKSLEL IGGFIRQLLQ DGKVPVGMGG EHLVSWPVMK
     EVAAVHKDLA IIHMDAHTDL RVEYEGEPLS HSTPIRKIAE HIGPHNVYSF GIRSGMKEEF
     EWAKENGMEI AKFEVLEPLK KVLPKLEGRP VYVTIDIDVL DPAHAPGTGT VDCGGITSRE
     LLASIHAIAN SGVNVVGFDL VEVAPIYDSS EQTANTASKL IREMLLGWVK
//
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