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Database: UniProt
Entry: A0A2J6PL23_9HELO
LinkDB: A0A2J6PL23_9HELO
Original site: A0A2J6PL23_9HELO 
ID   A0A2J6PL23_9HELO        Unreviewed;       328 AA.
AC   A0A2J6PL23;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   08-OCT-2025, entry version 27.
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=NA56DRAFT_583158 {ECO:0000313|EMBL:PMD14713.1};
OS   Hyaloscypha hepaticicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX   NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD14713.1, ECO:0000313|Proteomes:UP000235672};
RN   [1] {ECO:0000313|EMBL:PMD14713.1, ECO:0000313|Proteomes:UP000235672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD14713.1,
RC   ECO:0000313|Proteomes:UP000235672};
RG   DOE Joint Genome Institute;
RA   Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA   Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA   Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA   Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA   Martin F., Perotto S.;
RT   "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL   Submitted (MAY-2016) 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}.
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DR   EMBL; KZ613519; PMD14713.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6PL23; -.
DR   STRING; 1745343.A0A2J6PL23; -.
DR   OrthoDB; 9992747at2759; -.
DR   UniPathway; UPA00158; UER00270.
DR   Proteomes; UP000235672; 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   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:UP000235672}.
SQ   SEQUENCE   328 AA;  35321 MW;  DF462839555E73CC CRC64;
     MTTTSMVQPK FLSKADELGV VAVGFSGGQC KPGVDAAPSA LIANGLLTQL REDLGYKLFH
     DDTVHSYKEL LPASDPDYRG MKNPLAVSAV TKKLCEQVYS HAKEGRCVLT LGGDHSIAIG
     TIAGTAKAIR ERLGREMAVI WVDAHTDINT PETSESGNVH GMPVAFLSGL AKDDREDTFG
     WLKSENMISL KKLVYIGLRD VDRGEKLILR EQGIKAFSMH DIDRHGIGRV MEMALGHIGN
     DTPIHLSFDV DALDPMWAPS TGTPVRGGLT LREGDFIAEC VHESGCLVAM DLVEVNPTLE
     PGIDDIGAQQ TVRSGCSLVR CALGESLL
//
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