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Database: UniProt
Entry: A0A075NXI0_9ALTE
LinkDB: A0A075NXI0_9ALTE
Original site: A0A075NXI0_9ALTE 
ID   A0A075NXI0_9ALTE        Unreviewed;       474 AA.
AC   A0A075NXI0;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Arginase {ECO:0000313|EMBL:AIF97340.1};
GN   ORFNames=EP13_00765 {ECO:0000313|EMBL:AIF97340.1};
OS   Alteromonas australica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=589873 {ECO:0000313|EMBL:AIF97340.1, ECO:0000313|Proteomes:UP000056090};
RN   [1] {ECO:0000313|EMBL:AIF97340.1, ECO:0000313|Proteomes:UP000056090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H 17 {ECO:0000313|EMBL:AIF97340.1,
RC   ECO:0000313|Proteomes:UP000056090};
RA   Gonzaga A., Lopez-Perez M., Rodriguez-Valera F.;
RT   "Genomes of Alteromonas australica, a world apart.";
RL   Submitted (JUN-2014) 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; CP008849; AIF97340.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A075NXI0; -.
DR   KEGG; aal:EP13_00765; -.
DR   eggNOG; COG0010; Bacteria.
DR   Proteomes; UP000056090; 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   CDD; cd09990; Agmatinase-like; 1.
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   PRINTS; PR00116; ARGINASE.
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:UP000056090}.
FT   REGION          441..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..474
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   474 AA;  52348 MW;  3FF78889661D75D5 CRC64;
     MCSLGASVYA EDTDTPMPDS FKEKTKGISE EKLEILDSPL PTMLLGTMER FYKSMEGKSA
     EEIEAYLDGM IEVAEAGKFN PETDMASIPL NTEAKGFNGW KAKRPKSLNP EREPGPIHLS
     RYMSSRSGGV KTFANAPLAI YPEDLIAGNV DIAIVGAPLD MGSYYRGQKF GPQAMRNEYG
     AGGIDMSTMV NPSKVLSIVD YGDIAIDNMS TELSVQHVRE RVREIAETGT MPFIVGGDHS
     LEYPDIAALA DVHGKGSFGV VHFDSHYDAG KNQAHWLTHG QPVYRAVKEG HVKPENFIQI
     GLRGPWPGPE GFEWMRNNGM RYHTMAEVEK KGWKQVMDTA LKEARENVDK LYISFDVDVI
     DPAFIPGTGT PVPGGLTMRE AIPIVRGLCA QNDIIGFEIV ELDPLLDPTY RSALNSNFIL
     HACLTGVAMR KEGIEDPYYL SDLTTEHRQP EAGEKARKEG LREEVDPNYA KPKN
//
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