ID A0A0W1SRL1_9EURY Unreviewed; 270 AA.
AC A0A0W1SRL1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:KTG29024.1};
GN ORFNames=AUR66_11335 {ECO:0000313|EMBL:KTG29024.1};
OS Haloferax profundi.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=1544718 {ECO:0000313|EMBL:KTG29024.1, ECO:0000313|Proteomes:UP000053157};
RN [1] {ECO:0000313|EMBL:KTG29024.1, ECO:0000313|Proteomes:UP000053157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB29 {ECO:0000313|EMBL:KTG29024.1,
RC ECO:0000313|Proteomes:UP000053157};
RA Zhang G., Stingl U., Rashid M.;
RT "Haloferax profundi sp. nov. isolated from the Discovery deep brine-
RT seawater interface in the Red Sea.";
RL Submitted (DEC-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:KTG29024.1}.
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; LOPV01000118; KTG29024.1; -; Genomic_DNA.
DR RefSeq; WP_058571644.1; NZ_LOPV01000118.1.
DR AlphaFoldDB; A0A0W1SRL1; -.
DR OrthoDB; 7186at2157; -.
DR Proteomes; UP000053157; 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}.
SQ SEQUENCE 270 AA; 29577 MW; E264BBDF056C3426 CRC64;
MFPGAIADRE VADYVLLGAP LDISTSFQPG TRFGPNRIRQ FAESFDDYDR RTDQFFTELA
VHDAGDVRAW DDAPDYVDWL TGSVRDAVWD DAVPVVLGGE HTVTAAGVTG VDPDVFVCLD
AHLDLRREYD GNEWSHATIT RRVLDELDVD EAVILGARTG SPDEWERAEA DDVTVVAPED
VPEWDPDFGD ESVYLSVDID AADPAFAPGT GTKEPFGLTS REMRDVVHAV APHTDGFDVV
EVNDRDDGQA ASLAAKLLRE FVFSHAAAHD
//