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Database: UniProt
Entry: A0A316UTM7_9BASI
LinkDB: A0A316UTM7_9BASI
Original site: A0A316UTM7_9BASI 
ID   A0A316UTM7_9BASI        Unreviewed;       683 AA.
AC   A0A316UTM7;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Arginase/deacetylase {ECO:0000313|EMBL:PWN26445.1};
GN   ORFNames=BDZ90DRAFT_233088 {ECO:0000313|EMBL:PWN26445.1};
OS   Jaminaea rosea.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Microstromatales; Microstromatales incertae sedis;
OC   Jaminaea.
OX   NCBI_TaxID=1569628 {ECO:0000313|EMBL:PWN26445.1, ECO:0000313|Proteomes:UP000245884};
RN   [1] {ECO:0000313|EMBL:PWN26445.1, ECO:0000313|Proteomes:UP000245884}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 5214 {ECO:0000313|EMBL:PWN26445.1,
RC   ECO:0000313|Proteomes:UP000245884};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(2018).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KZ819671; PWN26445.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316UTM7; -.
DR   STRING; 1569628.A0A316UTM7; -.
DR   OrthoDB; 124800at2759; -.
DR   Proteomes; UP000245884; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR   InterPro; IPR019154; Arb2-like_domain.
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; PTHR10625:SF4; HISTONE DEACETYLASE 6, ISOFORM G; 1.
DR   PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR   Pfam; PF09757; Arb2; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   4: Predicted;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245884}.
FT   DOMAIN          71..380
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   DOMAIN          436..675
FT                   /note="Arb2-like"
FT                   /evidence="ECO:0000259|Pfam:PF09757"
FT   REGION          19..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   683 AA;  75262 MW;  3F711144E33A2430 CRC64;
     MQSPQRPLDL ATIPAIVEED GNGLDAVEDS PSSSSSSSSP PAFALATGLV YSTVMMLHSY
     PTTIVKPSDD HPEAPERISR AFIVLKENGC VKRMKRIQPR EITRDEVALV HDKGVWEGVY
     RSQFYTRSDL AEITALFGER SSLYLNEHTF LSARLSCGGV MELCDAVCSG RIHNGFAIVR
     PPGHHAEPDK SMGFCLFNNV AVAARWIRQR YGGQDVPKEQ RVRKILILDW DVHHGNGTQR
     AFEEDDDVLY ISLHRYDDGE FYPCGTYGAS ASMGSGKGRG FSVNIPWPCG DMGDGEYIYA
     FHQVVMPIAA EFGPDLVIIS AGFDAAMGDP LGGCDVTPIG YAQMTWMLMG LAKGKVVVAL
     EGGYNIEALA LSALAVTRTL LGDPVPSHES LAPACTAAVD VLRLVKRDVA PYWKCIESNP
     LDPRPDIEDG LTRYSLSELL KAHRQQEIAR HFQLSELPAG DRKWDSHALC SSDLMDTPRT
     VVLFAHDMGS LRAGNERPNL ALIPESEGAY IIDSSKVVLD WIQQRRFGIV DVNLYSGSLH
     GADATDFLEF IWDTYLDLCP ATDIVLFAHA GAAKSVLSLI SSRRLDKDSR VISTCLTMGH
     EAVPMVPKDE VDLRKWYIKN GRVFLPETHS WWSQDDDKRR KMKRAGKVVS VAERRPIQVL
     TAALGEVAAF VDARLAAKQE IVA
//
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