ID A0A0M0BNB5_9ARCH Unreviewed; 292 AA.
AC A0A0M0BNB5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Agmatinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AC482_04950 {ECO:0000313|EMBL:KON30028.1};
OS miscellaneous Crenarchaeota group-15 archaeon DG-45.
OC Archaea; Candidatus Bathyarchaeota; MCG-15.
OX NCBI_TaxID=1685127 {ECO:0000313|EMBL:KON30028.1, ECO:0000313|Proteomes:UP000037210};
RN [1] {ECO:0000313|EMBL:KON30028.1, ECO:0000313|Proteomes:UP000037210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG-45 {ECO:0000313|EMBL:KON30028.1};
RA Lazar C.S., Baker B.J., Seitz K.W., Hyde A.S., Dick G.J., Hinrichs K.-U.,
RA Teske A.P.;
RT "New insights into the roles of widespread benthic archaea in carbon and
RT nitrogen cycling.";
RL Submitted (JUN-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:KON30028.1}.
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DR EMBL; LFWZ01000044; KON30028.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0BNB5; -.
DR PATRIC; fig|1685127.3.peg.1318; -.
DR Proteomes; UP000037210; 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 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: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}.
SQ SEQUENCE 292 AA; 31483 MW; 742F1509D203D771 CRC64;
MQPFLDADTP VQEARHVIVG APLDQTMSHR RGARFAPTAI RQASLHMETY SLRTGLDWRD
VEVADAGDVE IPAGVEGAVG NIEEAVRRIR EAGRVPALLG GEHTVTLGAL RALRPDLVVD
LDAHLDLRRR LLGLELSHGT FMRRGLEELG HRVVVLGCRA LSEEEWEFAM ANPDRVTAVT
AAELRREGVK SGVEAVRRGL ADASTAYLSI DMDVLDPASA PAVGNPSPEG IGVTMLLDLV
GGMVDARFVG FDLTEVTPHY DSGLTAAQAA YIFLETIYSF EAARRASGAQ QP
//
