ID A0A165DUL7_EXIGL Unreviewed; 397 AA.
AC A0A165DUL7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 28-JUN-2023, entry version 20.
DE SubName: Full=Arginase/deacetylase {ECO:0000313|EMBL:KZV85393.1};
GN ORFNames=EXIGLDRAFT_726155 {ECO:0000313|EMBL:KZV85393.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV85393.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV85393.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV85393.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00742, ECO:0000256|RuleBase:RU003684}.
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DR EMBL; KV426190; KZV85393.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165DUL7; -.
DR STRING; 1314781.A0A165DUL7; -.
DR InParanoid; A0A165DUL7; -.
DR OrthoDB; 161483at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
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; cd11592; Agmatinase_PAH; 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:SF30; AGMATINASE 1-RELATED; 1.
DR PANTHER; PTHR11358; ARGINASE/AGMATINASE; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003684};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..397
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007856840"
SQ SEQUENCE 397 AA; 42529 MW; C9372C75BE2B3017 CRC64;
MLLSLVLLAV SFAAAAAHEH DTLEQIPVGY VKYPWQATYP GDNEVTADSI FSGITTFARL
PWVQCLGKDA DEAFDIAFIG APFDTGTSYR PGARFGPSGI RAGSRRLTLY GGYNVPLGVN
PFMSGLKIVD CGDVPVTPYD NKHAIAQIES GHKTLLHRTP FSPLGNDSVT GEALVPVSKD
GKHHPRLITL GGDHTIVLPL LRSVHSAYGA ISVIHFDSHL DTWKPSVFGG APSHQAEINH
GTYFYWAAQE GLVKNGSSIH GAIRTTLSGP ADYENDDTIG FQRIEAREID TLGTDGIIKK
IRDVVGTDPV YLSIDIDSID PAFAPATGTP ETGGWSTREL RTILRGLDGL HIVSADIVEV
APAYDTNAEL TTMAAADVLF EVLSVMAKTP LGKVAKK
//