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Database: UniProt
Entry: S9QKK0_9RHOB
LinkDB: S9QKK0_9RHOB
Original site: S9QKK0_9RHOB 
ID   S9QKK0_9RHOB            Unreviewed;       392 AA.
AC   S9QKK0;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Agmatinase {ECO:0000313|EMBL:EPX81981.1};
DE            EC=3.5.3.11 {ECO:0000313|EMBL:EPX81981.1};
GN   ORFNames=Salmuc_00295 {ECO:0000313|EMBL:EPX81981.1};
OS   Salipiger mucosus DSM 16094.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Salipiger.
OX   NCBI_TaxID=1123237 {ECO:0000313|EMBL:EPX81981.1, ECO:0000313|Proteomes:UP000015347};
RN   [1] {ECO:0000313|Proteomes:UP000015347}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16094 {ECO:0000313|Proteomes:UP000015347};
RX   PubMed=25197501; DOI=10.4056/sigs.4909790;
RA   Riedel T., Spring S., Fiebig A., Petersen J., Kyrpides N.C., Goker M.,
RA   Klenk H.P.;
RT   "Genome sequence of the exopolysaccharide-producing Salipiger mucosus type
RT   strain (DSM 16094(T)), a moderately halophilic member of the Roseobacter
RT   clade.";
RL   Stand. Genomic Sci. 9:1331-1343(2014).
CC   -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00742}.
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:EPX81981.1}.
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DR   EMBL; APVH01000028; EPX81981.1; -; Genomic_DNA.
DR   AlphaFoldDB; S9QKK0; -.
DR   STRING; 1123237.Salmuc_00295; -.
DR   eggNOG; COG0010; Bacteria.
DR   HOGENOM; CLU_703764_0_0_5; -.
DR   Proteomes; UP000015347; Unassembled WGS sequence.
DR   GO; GO:0008783; F:agmatinase activity; IEA:UniProtKB-EC.
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   PANTHER; PTHR11358:SF26; AGMATINASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11358; ARGINASE/AGMATINASE; 1.
DR   Pfam; PF00491; Arginase; 1.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR   PROSITE; PS51409; ARGINASE_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:EPX81981.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015347}.
FT   REGION          211..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          273..332
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          357..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..241
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   392 AA;  42554 MW;  88D3C96D732EB752 CRC64;
     MHSYETGRLN LPFTGICTFA KKPYVEDWST LEADAAILGA PFDAGTQFRA GARFGPRAVR
     EASTLFSFGH AGAYDHEDDV TYLGPEVRIV DMGDADIVHT DTLKSHANIR TGVEAALAAG
     ALPVVIGGDH SVNIPCVEAY EGQKPFHILQ IDAHLDFVDE RHGVTRGHGN PMRRAAEKPW
     VSGLTQVGIR NVSSTARDGY EAARAMGSDI LSVRHGPRPS GPRRRRGAHP RGRPGLHHAR
     HRRFLPLHRA RHGHAQPRRV PLLRGAGTAA IGGARAPCRG HRPGRGRTGP RPHRIDGNPC
     GTGAYEPSRV HLPRPRHGRL TQAGPRSSAK EGAWHNCRLR RPSGIVQPVR DITSRSKALP
     CRHPSPTSRC WTSRGGSPGP TRAACWPISA PR
//
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