ID A0A165IID2_9BASI Unreviewed; 519 AA.
AC A0A165IID2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Arginase/deacetylase {ECO:0000313|EMBL:KZT60610.1};
GN ORFNames=CALCODRAFT_428997 {ECO:0000313|EMBL:KZT60610.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT60610.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT60610.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT60610.1,
RC ECO:0000313|Proteomes:UP000076842};
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).
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DR EMBL; KV423929; KZT60610.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165IID2; -.
DR STRING; 1353952.A0A165IID2; -.
DR InParanoid; A0A165IID2; -.
DR OrthoDB; 10780at2759; -.
DR Proteomes; UP000076842; Unassembled WGS sequence.
DR GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR47558; HISTONE DEACETYLASE HOS3; 1.
DR PANTHER; PTHR47558:SF1; HISTONE DEACETYLASE HOS3; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000076842}.
FT DOMAIN 184..487
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 33..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 519 AA; 55906 MW; 09025F2BE771F3ED CRC64;
MDRLIPVDVR ETSIDRTLSA ALDALTISHV SPGPFTEATP AEDPDLSHLP PLPPSPEKSR
TSASPPAAQP SKAQVALFSA PACSLHTYIR TSNSSTIVER PQRLRAVAVG LACALARLEE
VISGASTPVA GPSNSSVSVP DFIQLVDPAT YSDIDIRTHE ATAYVHNTLA ALEDERTPDS
VEKVYIDRLY DIVGACLDKV SLRESEIPAE WPQGDLYLSP GSMAAFQSSI ATVCAAVDTI
AAPLSTGPKL AFASVRPPGH HCSSAQPSGF CFLNNVAIGA VHAHLHHSIT HVAILDIDLH
HGNGTQAIAW AINAETNKRA ESEEQAGPDA KPGLQIYYGS IHDILSYPCE TGDLALTQAA
SISIHGAHGQ HIENIHLEPY MSDTDFWGRL YPEKYSQLLK KADDFFQTTG ADPEKSLIFV
SCGFDACSHE LASMSRHKRN VPPTFYGRFA ADAHTLAERR TKGKAITVLE GGYGDRALQS
GAMAYLTGMF LTAEGVMHTE PWWSVEELMK VRIFYGFGT
//
