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Database: UniProt
Entry: A0A1F5BSQ5_9BACT
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ID   A0A1F5BSQ5_9BACT        Unreviewed;       338 AA.
AC   A0A1F5BSQ5;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   13-SEP-2023, entry version 16.
DE   RecName: Full=Arginase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A2V45_04280 {ECO:0000313|EMBL:OGD33612.1};
OS   Candidatus Aminicenantes bacterium RBG_19FT_COMBO_58_17.
OC   Bacteria; Candidatus Aminicenantes.
OX   NCBI_TaxID=1797275 {ECO:0000313|EMBL:OGD33612.1, ECO:0000313|Proteomes:UP000178644};
RN   [1] {ECO:0000313|EMBL:OGD33612.1, ECO:0000313|Proteomes:UP000178644}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGD33612.1}.
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DR   EMBL; MEYD01000218; OGD33612.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F5BSQ5; -.
DR   STRING; 1797275.A2V45_04280; -.
DR   Proteomes; UP000178644; 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:InterPro.
DR   Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR   InterPro; IPR006035; Ureohydrolase.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   PANTHER; PTHR43782; ARGINASE; 1.
DR   PANTHER; PTHR43782:SF3; ARGINASE; 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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..338
FT                   /note="Arginase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009517949"
SQ   SEQUENCE   338 AA;  36308 MW;  EDBD76C6DD54003A CRC64;
     MNHFAVYAGL LAVSALAFPL LASSVAPLGS QAKLKVAVVQ NDSDGPKYMA EGGLLPLLEN
     LGCDVQKIDT VALTPEEQRE YGEWNRDALE SRRIGYLASK NRVGEGLIIG LLTNCTDLLG
     MLAGLQHLRP SGERAGADER GLQREGLTGL KPLRVGLIYF DAHADFNTPE TTLSGMLGGM
     DVAVAAGMCL TRLRIKTGLD PALPTKYVVF GGLRDVDPLE QELLDRSDCE YLSVGDIRAA
     SDAVGSQMKR LSRLTDVIYI HVDMDVLEPS EVSGHPLTAP EGPTSRELAT AIQKMFTWPK
     AAAIGIASIP SGERDKEGHS LRASYRLIEA AVRGVKSR
//
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