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Database: UniProt
Entry: A0A1Y2IFN0_TRAC3
LinkDB: A0A1Y2IFN0_TRAC3
Original site: A0A1Y2IFN0_TRAC3 
ID   A0A1Y2IFN0_TRAC3        Unreviewed;       317 AA.
AC   A0A1Y2IFN0;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   08-OCT-2025, entry version 33.
DE   RecName: Full=Arginase {ECO:0000256|ARBA:ARBA00018123, ECO:0000256|RuleBase:RU361159};
DE            EC=3.5.3.1 {ECO:0000256|ARBA:ARBA00012168, ECO:0000256|RuleBase:RU361159};
GN   ORFNames=PYCCODRAFT_1470304 {ECO:0000313|EMBL:OSC99413.1};
OS   Trametes coccinea (strain BRFM310) (Pycnoporus coccineus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Trametes.
OX   NCBI_TaxID=1353009 {ECO:0000313|EMBL:OSC99413.1, ECO:0000313|Proteomes:UP000193067};
RN   [1] {ECO:0000313|EMBL:OSC99413.1, ECO:0000313|Proteomes:UP000193067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRFM310 {ECO:0000313|EMBL:OSC99413.1,
RC   ECO:0000313|Proteomes:UP000193067};
RX   PubMed=26692083; DOI=10.1186/s13068-015-0407-8;
RA   Couturier M., Navarro D., Chevret D., Henrissat B., Piumi F.,
RA   Ruiz-Duenas F.J., Martinez A.T., Grigoriev I.V., Riley R., Lipzen A.,
RA   Berrin J.G., Master E.R., Rosso M.N.;
RT   "Enhanced degradation of softwood versus hardwood by the white-rot fungus
RT   Pycnoporus coccineus.";
RL   Biotechnol. Biofuels 8:216-216(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginine + H2O = urea + L-ornithine; Xref=Rhea:RHEA:20569,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:32682,
CC         ChEBI:CHEBI:46911; EC=3.5.3.1;
CC         Evidence={ECO:0000256|RuleBase:RU361159};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR036979-1,
CC         ECO:0000256|RuleBase:RU361159};
CC       Note=Binds 2 manganese ions per subunit.
CC       {ECO:0000256|PIRSR:PIRSR036979-1, ECO:0000256|RuleBase:RU361159};
CC   -!- PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-
CC       arginine: step 1/1. {ECO:0000256|ARBA:ARBA00005098}.
CC   -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00742, ECO:0000256|RuleBase:RU003684}.
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DR   EMBL; KZ084128; OSC99413.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2IFN0; -.
DR   STRING; 1353009.A0A1Y2IFN0; -.
DR   OrthoDB; 9992747at2759; -.
DR   UniPathway; UPA00158; UER00270.
DR   Proteomes; UP000193067; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR   GO; GO:0004053; F:arginase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030145; F:manganese ion binding; IEA:TreeGrafter.
DR   GO; GO:0006525; P:arginine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000050; P:urea cycle; IEA:UniProtKB-UniPathway.
DR   CDD; cd09989; Arginase; 1.
DR   FunFam; 3.40.800.10:FF:000009; Arginase; 1.
DR   Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR   InterPro; IPR014033; Arginase.
DR   InterPro; IPR006035; Ureohydrolase.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR   NCBIfam; TIGR01229; rocF_arginase; 1.
DR   PANTHER; PTHR43782; ARGINASE; 1.
DR   PANTHER; PTHR43782:SF3; ARGINASE; 1.
DR   Pfam; PF00491; Arginase; 1.
DR   PIRSF; PIRSF036979; 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   Arginine metabolism {ECO:0000256|ARBA:ARBA00022503,
KW   ECO:0000256|RuleBase:RU361159};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003684};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRSR:PIRSR036979-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR036979-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193067}.
FT   BINDING         114
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT   BINDING         137
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT   BINDING         139
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT   BINDING         141
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT   BINDING         241
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT   BINDING         243
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
SQ   SEQUENCE   317 AA;  34047 MW;  16500BBA3B5C53AE CRC64;
     MSSRVASSSS RFLPNPKSVA IVGCPFRGGQ TKSGVEKGPM HLIESGLPQQ LAKIGWKVQF
     DGELQFEHIL AEDDPPIGNL KNPRSVSRVS ELVAKVVGEH AKNGQLPLTL GGDHSLAMGT
     ISGTLEKYPD ACVVWVDAHA DINTAETSDS GNIHGMPLSF LLGIGTKLKE FSWIKPLLTP
     QRLVYIGLRD VDAGERRILR EHGIKAFSMH DVDKHGIGRV VEMALDHVNP GRTLPIHMSF
     DVDGLDPSVT PSTGTPVHGG LTLREGRYIC EAIYETGCLV ALDIVEINPS LVDEEAAKKT
     VAVGCSLVRS ALGESLL
//
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