ID A0A081CNR8_PSEA2 Unreviewed; 534 AA.
AC A0A081CNR8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Arginase/deacetylase {ECO:0000313|EMBL:GAK68314.1};
DE SubName: Full=Related to histone deacetylase {ECO:0000313|EMBL:SPO47338.1};
GN ORFNames=PAN0_066d6559 {ECO:0000313|EMBL:GAK68314.1}, PSANT_05026
GN {ECO:0000313|EMBL:SPO47338.1};
OS Pseudozyma antarctica (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=84753 {ECO:0000313|EMBL:GAK68314.1, ECO:0000313|Proteomes:UP000053758};
RN [1] {ECO:0000313|Proteomes:UP000053758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10317 {ECO:0000313|Proteomes:UP000053758};
RA Saika A., Koike H., Hori T., Fukuoka T., Sato S., Habe H., Kitamoto D.,
RA Morita T.;
RT "Draft Genome Sequence of the Yeast Pseudozyma antarctica Type Strain
RT JCM10317, a Producer of the Glycolipid Biosurfactants, Mannosylerythritol
RT Lipids.";
RL Genome Announc. 2:e00878-e00814(2014).
RN [2] {ECO:0000313|EMBL:GAK68314.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 10317 {ECO:0000313|EMBL:GAK68314.1};
RA Morita T., Saika A., Koike H.;
RT "Draft genome sequence of the yeast Pseudozyma antarctica JCM 10317 known
RT as a producer of lipase B which used in a wide range of industrial
RT applications.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SPO47338.1, ECO:0000313|Proteomes:UP000325008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34888 {ECO:0000313|Proteomes:UP000325008}, and ATCC34888
RC {ECO:0000313|EMBL:SPO47338.1};
RA Guldener U.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DF830133; GAK68314.1; -; Genomic_DNA.
DR EMBL; OOIQ01000013; SPO47338.1; -; Genomic_DNA.
DR RefSeq; XP_014653490.1; XM_014798004.1.
DR AlphaFoldDB; A0A081CNR8; -.
DR GeneID; 26307361; -.
DR HOGENOM; CLU_007727_7_6_1; -.
DR OrthoDB; 5478215at2759; -.
DR Proteomes; UP000053758; Unassembled WGS sequence.
DR Proteomes; UP000325008; Unassembled WGS sequence.
DR GO; GO:0006325; P:chromatin organization; 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; 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:SF13; HISTONE DEACETYLASE HDAC1; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR Pfam; PF00850; Hist_deacetyl; 2.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000053758}.
FT DOMAIN 100..252
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT DOMAIN 274..437
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 52..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 534 AA; 57390 MW; 43B37212FDA3B52D CRC64;
MAVVPDPPRV AYVVSGDLVH YADLLPSNKG RSSHVHSLVH HLDLLDLSTL DDGSDDADDD
NLKRGKPAGS SERERFLAAI SADESAASPP KSDRRRAAVY LPLPATRQQL TTFHGEPFVD
HLTRGKSAQA QDSKPPRKRQ RTANDAGTSE SDPNSDSDSD VSRTSHGKRT ASVKNQFGLQ
DDCPTFDGLE KHVSLIAGAS ITAAELLATG QADIAIAWDG GRHHAKKHAA SGFCYINDAV
LAILALRKPR KVTVTTTVPR EAGDEATVRK TTIKRVQRVL YLDLDLHWGD GVEEAFHTSA
SVLTLSIHHY APGFFPCYTA SSDSRYGAPG SLGADPGAAD TTINIPLAMG TSDASLERVM
EATVQPVVEA WQPEMVVVQC GVDGLAADPM AVWNLSAAAY VAAIQRVLGW KRPTLLLGGG
GYDTANAARC WSLITAAALG RYEDTTKRRA AAPSFEPHTL VDRESVEAKP EDNVQTQSIS
LETGVPDHAF WPAYAPHYTL NVPAGEMIDH NPPAYFDEIH VSLAARIESF TKSS
//
