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Database: UniProt
Entry: A0A2G4SS38_RHIZD
LinkDB: A0A2G4SS38_RHIZD
Original site: A0A2G4SS38_RHIZD 
ID   A0A2G4SS38_RHIZD        Unreviewed;       479 AA.
AC   A0A2G4SS38;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Histone deacetylase {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037913};
DE            EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037913};
GN   ORFNames=RHIMIDRAFT_255565 {ECO:0000313|EMBL:PHZ11583.1};
OS   Rhizopus microsporus ATCC 52813.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=1340429 {ECO:0000313|EMBL:PHZ11583.1, ECO:0000313|Proteomes:UP000242254};
RN   [1] {ECO:0000313|EMBL:PHZ11583.1, ECO:0000313|Proteomes:UP000242254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 52813 {ECO:0000313|EMBL:PHZ11583.1,
RC   ECO:0000313|Proteomes:UP000242254};
RX   PubMed=27956601; DOI=10.1073/pnas.1615148113;
RA   Lastovetsky O.A., Gaspar M.L., Mondo S.J., LaButti K.M., Sandor L.,
RA   Grigoriev I.V., Henry S.A., Pawlowska T.E.;
RT   "Lipid metabolic changes in an early divergent fungus govern the
RT   establishment of a mutualistic symbiosis with endobacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:15102-15107(2016).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-
CC         [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC         COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:61930; EC=3.5.1.98;
CC         Evidence={ECO:0000256|PIRNR:PIRNR037913};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR037913}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD Type 1
CC       subfamily. {ECO:0000256|PIRNR:PIRNR037913}.
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DR   EMBL; KZ303851; PHZ11583.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G4SS38; -.
DR   STRING; 1340429.A0A2G4SS38; -.
DR   OrthoDB; 1327607at2759; -.
DR   Proteomes; UP000242254; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR003084; His_deacetylse_1.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   PANTHER; PTHR48252; HISTONE DEACETYLASE 2-RELATED; 1.
DR   PANTHER; PTHR48252:SF69; HISTONE DEACETYLASE 3; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037913; His_deacetylse_1; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   PRINTS; PR01271; HISDACETLASE.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW   ECO:0000256|PIRNR:PIRNR037913}; Hydrolase {ECO:0000256|PIRNR:PIRNR037913};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR037913-3};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR037913};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242254};
KW   Transcription {ECO:0000256|PIRNR:PIRNR037913};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR037913}.
FT   DOMAIN          58..349
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   REGION          456..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..471
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        171
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-1"
FT   BINDING         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT   BINDING         179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT   BINDING         206
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT   BINDING         208
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT   BINDING         295
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT   BINDING         334
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
SQ   SEQUENCE   479 AA;  55154 MW;  878C145643DED169 CRC64;
     MPRKGFVDDD SMSTFSEDYY STQKYMQPGK RRLASHSKKR VAYFHDEGVG NYHYGERHPM
     KPHRLTLTNH LVLKYGLHEK MEIFQPRKAT DNEIRNFHSA DYVDFLKRVT PDNADQYENL
     FQRFNVGDDC PIFDGIYDFC QRYAGATIEA SRKLIADGAD ICINWSGGLH HAKKSEASGF
     CYVNDIVLGT LELLRYFPRV LYIDIDIHHG DGVQEAFYST DRVMTVSFHK YNGDFFPGTG
     HIDEIGSSLG KYYSVNVPLR DGIDDDAYVW LFKEVIDAVI GTYQPSAIVL QCGADSLGCD
     RLGCFNLSIR AHGRCVQLVK NFNIPLLVVG GGGYTVRNVA RCWTYETSVL VDTELSENLP
     PNEYRDFFKP DYKLHPDLKG RVENQNDRTY LLKVRERVME QLRYLDAAPS IQMQEIPPDI
     QGFLDGEEEQ RDAEEDSEKG KDTRLYRGRR IIHDNEWYSD DDDNDSVGRW SDTMEDDDD
//
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