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Database: UniProt
Entry: A0A165DUL7_EXIGL
LinkDB: A0A165DUL7_EXIGL
Original site: A0A165DUL7_EXIGL 
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
//
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