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Database: UniProt
Entry: A0AA39D373_9EURO
LinkDB: A0AA39D373_9EURO
Original site: A0AA39D373_9EURO 
ID   A0AA39D373_9EURO        Unreviewed;       351 AA.
AC   A0AA39D373;
DT   24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2024, sequence version 1.
DT   28-JAN-2026, entry version 9.
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   Name=CAR1 {ECO:0000313|EMBL:KAJ9646908.1};
GN   ORFNames=H2204_000600 {ECO:0000313|EMBL:KAJ9646908.1};
OS   Knufia peltigerae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Trichomeriaceae; Knufia.
OX   NCBI_TaxID=1002370 {ECO:0000313|EMBL:KAJ9646908.1, ECO:0000313|Proteomes:UP001172681};
RN   [1] {ECO:0000313|EMBL:KAJ9646908.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TK_35 {ECO:0000313|EMBL:KAJ9646908.1};
RA   Kurbessoian T., Stajich J.E.;
RT   "Culturing micro-colonial fungi from biological soil crusts in the Mojave
RT   desert and describing Neophaeococcomyces mojavensis, and introducing the
RT   new genera and species Taxawa tesnikishii.";
RL   Submitted (OCT-2022) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00047391,
CC         ECO:0000256|RuleBase:RU361159};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU361159};
CC       Note=Binds 2 manganese ions per subunit.
CC       {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}.
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:KAJ9646908.1}.
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DR   EMBL; JAPDRN010000002; KAJ9646908.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0AA39D373; -.
DR   Proteomes; UP001172681; 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   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   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|RuleBase:RU361159};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361159};
KW   Reference proteome {ECO:0000313|Proteomes:UP001172681}.
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   351 AA;  37597 MW;  D50CD13A2E273E69 CRC64;
     MQPKAVEKNT PANGQSTNGH SNGDDMATPS TIRQKFLTSP SDLGVVLVGF SGGQCKPGVD
     AAPTALVSAG ILDQMRDELG YTLHGDESVQ DYNQLRPQSD PDHRGMKNPR AVSAVTQGLS
     QQVYNQAREG RMVLTLGGDH SIAIGTIAGT AKAIRERYNG RKEIGVIWVD AHADINTPET
     SDSGNVHGMP VAFLTGLAKS EERDIFGWLE EDQRLSTAKL VYIGLRDVDR GEKKILRDNG
     IKAFSMHDID RHGIGRVVEM ALAHIGADTP IHLSFDVDAL DPMWAPSTGT PVRGGLTLRE
     GDYIAECVHE TGQLVAMDLV EVNPSLEVAG ASETVRAGVS LVRCALGDTL L
//
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