ID A0A2P6V787_9CHLO Unreviewed; 652 AA.
AC A0A2P6V787;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
GN ORFNames=C2E20_6642 {ECO:0000313|EMBL:PSC69949.1};
OS Micractinium conductrix.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Micractinium.
OX NCBI_TaxID=554055 {ECO:0000313|EMBL:PSC69949.1, ECO:0000313|Proteomes:UP000239649};
RN [1] {ECO:0000313|EMBL:PSC69949.1, ECO:0000313|Proteomes:UP000239649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 241.80 {ECO:0000313|EMBL:PSC69949.1,
RC ECO:0000313|Proteomes:UP000239649};
RX PubMed=29178410; DOI=10.1111/tpj.13789;
RA Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA Barney B.M.;
RT "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL Plant J. 93:566-586(2018).
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|ARBA:ARBA00001028};
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC subfamily. {ECO:0000256|ARBA:ARBA00006457}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PSC69949.1}.
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DR EMBL; LHPF02000023; PSC69949.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6V787; -.
DR STRING; 554055.A0A2P6V787; -.
DR Proteomes; UP000239649; Unassembled WGS sequence.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd09991; HDAC_classI; 1.
DR CDD; cd00202; ZnF_GATA; 2.
DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 2.
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 InterPro; IPR000679; Znf_GATA.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR10625:SF11; HISTONE DEACETYLASE 19; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR Pfam; PF00320; GATA; 2.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PRINTS; PR01270; HDASUPER.
DR PRINTS; PR01271; HISDACETLASE.
DR SMART; SM00401; ZnF_GATA; 2.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2.
DR PROSITE; PS00344; GATA_ZN_FINGER_1; 1.
DR PROSITE; PS50114; GATA_ZN_FINGER_2; 2.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00094};
KW Reference proteome {ECO:0000313|Proteomes:UP000239649};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00094};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00094}.
FT DOMAIN 545..603
FT /note="GATA-type"
FT /evidence="ECO:0000259|PROSITE:PS50114"
FT DOMAIN 599..652
FT /note="GATA-type"
FT /evidence="ECO:0000259|PROSITE:PS50114"
FT REGION 400..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 652 AA; 69434 MW; A61E38E8EAECF71D CRC64;
MEGSAPAVGP ARKARVAYFY DPEIGQFYYG QGHPMKPHRV RMANSLVLHY GLHSKLDGFY
TPTRAGEEDM AAFHSEDYVQ FLRTVTPDNQ AQFTRELRTF NIYEDCPVFD GLWEYCQIAA
GGSLGAAVKL NYQTADIAIN WTGGLHHAKR AEASGFCYVN DIVLGVLELL KYHQRVLYLD
IDVHHGDGVE EAFLTTDRVM CVSFHKFGNG YFPGTGDIGN MGHGPGRGYS LNVPLRDGVT
DEAYQSLFKP VMAKIMEVYR PEAIVLQCGT DSLAGDRLGV FNLSSRGHAA CVAYMKSFGL
PLMLLGGGGY KIINVARCWA LETGLAVGAD MSEQLPPNEY YDYYGPVGFK LTVQPRAGLN
NYNSSEYLQN LRTTILQRLS QLGGAPSVAF HERAPDGMAL DDIQDVDMRD PSRSPQRLWD
GELDPEGDQE GGGGGGGGPS GGGSGGGGPS GGGGGPRRRR ADTHFRDAPA FKPQSPSMLR
PASASRLTGG GSADGDAVPA ESGLTAATQG TVGTAGTAGT AGTAGAAEPS GGTGAASPSF
GPPGGSGGKC CTNCGTANTS SWRKDPQNGS TLCSACGQYK KMNGTDRPVK LRQRQAAQDE
QPRVCTNCAI TETSNWRRHP LTREMLCNAC GNYLKLHGVM RPLVTAQSEG GY
//
