ID A0A1G8VS52_9RHOB Unreviewed; 414 AA.
AC A0A1G8VS52;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:SDJ68697.1};
GN ORFNames=SAMN04488026_102215 {ECO:0000313|EMBL:SDJ68697.1};
OS Aliiruegeria lutimaris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Aliiruegeria.
OX NCBI_TaxID=571298 {ECO:0000313|EMBL:SDJ68697.1, ECO:0000313|Proteomes:UP000199382};
RN [1] {ECO:0000313|EMBL:SDJ68697.1, ECO:0000313|Proteomes:UP000199382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25294 {ECO:0000313|EMBL:SDJ68697.1,
RC ECO:0000313|Proteomes:UP000199382};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00742}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNEK01000022; SDJ68697.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8VS52; -.
DR STRING; 571298.SAMN04488026_102215; -.
DR OrthoDB; 9788689at2; -.
DR Proteomes; UP000199382; Unassembled WGS sequence.
DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd09990; Agmatinase-like; 1.
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 PRINTS; PR00116; ARGINASE.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000199382}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 414 AA; 46063 MW; 3028A95E6F9162B3 CRC64;
MFPSPRDRSR PHNPRHMRRE EKRFHHPDLT KLLGWKAMQK EGELPEGRWD EERRWALRMG
LTGADSIEDK SIPTFARGEL PHYAGINTFL KAPYAEDVLE VANYDATVLG IPFDGGTTYR
PGTRFGPQGV RKISALYTPY NYEIGVDLRE QMTLCDAGDV FTIPANIEKS FDQISRAVSH
VFSSGSLPIM IGGDHSIGFP CVRGIAECTS KKIGIVHFDR HADIQEKDLD ERMHTTPWFH
STNLPNVPAK NLVQVGIGGW QVPREAVKVA RERQTNIITM SDMERMGVDK TAEMALEMAW
EGVDMVYMSF DIDSIDCGFV PGTGWPEPGG FLPREALALA SKVAAQGICG MELVEVSPPY
DTSDITALMG TRVIVDVFGA MVSNGTLGKH KRHIDRPVAI PHGEFVGKRW SNAT
//