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Database: UniProt
Entry: W7UBL6_RUMFL
LinkDB: W7UBL6_RUMFL
Original site: W7UBL6_RUMFL 
ID   W7UBL6_RUMFL            Unreviewed;       283 AA.
AC   W7UBL6;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Agmatinase {ECO:0000313|EMBL:EWM52481.1};
GN   ORFNames=RF007C_08055 {ECO:0000313|EMBL:EWM52481.1};
OS   Ruminococcus flavefaciens 007c.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1341157 {ECO:0000313|EMBL:EWM52481.1, ECO:0000313|Proteomes:UP000019365};
RN   [1] {ECO:0000313|EMBL:EWM52481.1, ECO:0000313|Proteomes:UP000019365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=007c {ECO:0000313|EMBL:EWM52481.1,
RC   ECO:0000313|Proteomes:UP000019365};
RX   PubMed=24992679;
RA   Dassa B., Borovok I., Ruimy-Israeli V., Lamed R., Flint H.J., Duncan S.H.,
RA   Henrissat B., Coutinho P., Morrison M., Mosoni P., Yeoman C.J., White B.A.,
RA   Bayer E.A.;
RT   "Rumen cellulosomics: divergent fiber-degrading strategies revealed by
RT   comparative genome-wide analysis of six ruminococcal strains.";
RL   PLoS ONE 9:E99221-E99221(2014).
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:EWM52481.1}.
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DR   EMBL; ATAX01000035; EWM52481.1; -; Genomic_DNA.
DR   RefSeq; WP_019680839.1; NZ_ATAX01000035.1.
DR   AlphaFoldDB; W7UBL6; -.
DR   PATRIC; fig|1341157.4.peg.2856; -.
DR   eggNOG; COG0010; Bacteria.
DR   OrthoDB; 9788689at2; -.
DR   Proteomes; UP000019365; 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: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   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019365}.
SQ   SEQUENCE   283 AA;  31553 MW;  7F538F84F73EF0F0 CRC64;
     MLNKNIQTFI ACDSEYEDSK IVLFGAGFDG TTSFRPGTRF APSAIRNESF GIETYSPYQN
     KDMTDYSYFD SGDLELPFGS TDSAIDDIAA RADQILKDGK LPFMIGGEHL VTLGTVRAVS
     DRYKDLCIVH FDAHADLRDD YLGQKMSHAC VLRRCHEIVG DDHIFQFGIR SGDREEFFFA
     DEHTEMHRFS FDGLEETVEK LRGRDVYFTL DLDVLDPSIF PGTGTPEAGG VTFDELRKAV
     TLVCSRLNIV GCDVNELSPV YDQSGVSTAV ACKIIREMLL ALS
//
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