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Database: UniProt
Entry: L0A780_DEIPD
LinkDB: L0A780_DEIPD
Original site: L0A780_DEIPD 
ID   L0A780_DEIPD            Unreviewed;       305 AA.
AC   L0A780;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Arginase family hydrolase, arginase/agmainase/formiminoglutamate hydrolase {ECO:0000313|EMBL:AFZ69042.1};
GN   OrderedLocusNames=Deipe_3614 {ECO:0000313|EMBL:AFZ69042.1};
OS   Deinococcus peraridilitoris (strain DSM 19664 / LMG 22246 / CIP 109416 /
OS   KR-200).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=937777 {ECO:0000313|EMBL:AFZ69042.1, ECO:0000313|Proteomes:UP000010467};
RN   [1] {ECO:0000313|Proteomes:UP000010467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19664 / LMG 22246 / CIP 109416 / KR-200
RC   {ECO:0000313|Proteomes:UP000010467};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Lu M.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Pukall R., Steenblock K., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "Complete sequence of chromosome of Deinococcus peraridilitoris DSM
RT   19664.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00742, ECO:0000256|RuleBase:RU003684}.
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DR   EMBL; CP003382; AFZ69042.1; -; Genomic_DNA.
DR   RefSeq; WP_015237338.1; NC_019793.1.
DR   AlphaFoldDB; L0A780; -.
DR   STRING; 937777.Deipe_3614; -.
DR   KEGG; dpd:Deipe_3614; -.
DR   PATRIC; fig|937777.3.peg.3626; -.
DR   eggNOG; COG0010; Bacteria.
DR   HOGENOM; CLU_039478_0_2_0; -.
DR   OrthoDB; 9788689at2; -.
DR   Proteomes; UP000010467; Chromosome.
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   Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR   InterPro; IPR006035; Ureohydrolase.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   InterPro; IPR020855; Ureohydrolase_Mn_BS.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010467}.
SQ   SEQUENCE   305 AA;  33492 MW;  9BC322FF332CDA09 CRC64;
     MAHLPFSGIA SFARAPIVES GGEWRSDVAV LGVPFDIALG YRPGARFAPR AIREASLRYA
     LTEEGFYDLE SGRTRLAGLR LADAGDVELP SLETELAHAR IEEAARQLRA RCSLPVFLGG
     DHSVTYPLLR AFDDVPDLHV VQLDAHLDFT DLRNDTRLSN SSPFRRACED LPNLTHITTL
     GLRGLRFDRE AVDAARSRGH QLVTMRRLTE NLDEVLAVLP TEKAVYLSLD VDAFDPSVLP
     GTSSPEPDGL TYGLAMGLIR EVVRRNHLLA YDVVELAPNL DSSGRSSLLA ARLIMETLVE
     ALDAR
//
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