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Database: UniProt
Entry: M2UHS1_COCH5
LinkDB: M2UHS1_COCH5
Original site: M2UHS1_COCH5 
ID   M2UHS1_COCH5            Unreviewed;       847 AA.
AC   M2UHS1;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037919};
DE            EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037919};
GN   ORFNames=COCHEDRAFT_1145200 {ECO:0000313|EMBL:EMD87492.1};
OS   Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) (Southern
OS   corn leaf blight fungus) (Bipolaris maydis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=701091 {ECO:0000313|EMBL:EMD87492.1, ECO:0000313|Proteomes:UP000016936};
RN   [1] {ECO:0000313|EMBL:EMD87492.1, ECO:0000313|Proteomes:UP000016936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [2] {ECO:0000313|Proteomes:UP000016936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on the
CC       N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone
CC       deacetylation gives a tag for epigenetic repression and plays an
CC       important role in transcriptional regulation, cell cycle progression
CC       and developmental events. {ECO:0000256|PIRNR:PIRNR037919}.
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:PIRNR037919};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR037919}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC       subfamily. {ECO:0000256|PIRNR:PIRNR037919}.
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DR   EMBL; KB445582; EMD87492.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2UHS1; -.
DR   STRING; 701091.M2UHS1; -.
DR   ESTHER; cocvi-w7ezb7; Arb2_domain.
DR   eggNOG; KOG1343; Eukaryota.
DR   HOGENOM; CLU_007727_4_3_1; -.
DR   OMA; FVSPACY; -.
DR   Proteomes; UP000016936; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0031078; F:histone H3K14 deacetylase activity; IEA:UniProtKB-UniRule.
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; IPR017321; Hist_deAcase_II_yeast.
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   PIRSF; PIRSF037919; HDAC_II_yeast; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|PIRNR:PIRNR037919};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037919};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR037919};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016936};
KW   Repressor {ECO:0000256|PIRNR:PIRNR037919};
KW   Transcription {ECO:0000256|PIRNR:PIRNR037919};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR037919}.
FT   DOMAIN          141..450
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   DOMAIN          504..767
FT                   /note="Arb2-like"
FT                   /evidence="ECO:0000259|Pfam:PF09757"
FT   REGION          1..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          771..810
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        778..793
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   847 AA;  95055 MW;  94FAE54AB409988A CRC64;
     MDDEDFPMGE DSIIISTEPN GDHAPETVVP SKIFGNSKGP LLSKQEQLPF HSPSKGPLLQ
     PNIHRSNPGS HRTTKSPSSW SDKMNTSRPT PAQHSSPQVR IPPKPRSTLV YPTSKTGLVY
     DPRMRFHAEL PDMNINPDDI HPEDPRRIHS IFEELKQAGL VASSTSEEDK EDHCWRIAAR
     FATRPEILLI HTEEHYDLVE SFQNMTSDEL KFEAERLDSI YLNNSTYECA KLAAGGAIEA
     CKAVVQGAVR NAIAIIRPPG HHAESDQPSG FCIFNNVPIA ARVCQDAYPE TCRKVLILDW
     DVHHGNGIQH AFYDDPNVLY ISLHVFKDGT FYPNLPDGNL DYCGEGRGEG KNVNIPWAEH
     GMGDSEYLYA FQQVVMPIAT EFNPDLVIIS AGFDAAEGDL LGGCFVTPAC YGHMTHMLMS
     LAKGKLVVCL EGGYNLRSIA RSALAVTKVL MLEPPDRLRD DLPAPKDSAV YIVENVKRQH
     SKYWKSLYPK HLDKTDSGYQ DAYRFHEIIR EWQSQRLAAE HSMVPLPPLQ INKAGLAQTF
     EHNIIATPKF MEQYPLLVIF HDPPSLQDHS DPMSGKREPH NTWLTDVTKR YIDWAIKNDF
     QVIDVNIPRV VAVEDPNIGF TKSDNSVVRA QQTRELASYL WENYIEPNEA TQVFLMGVGD
     AYLGLVDLLS HNENCTDPDS PVECLIGFVA ETTIQSIKRA TDDTISSWYH SHSMIFVKNS
     HFVWDPSRQR KMRKKLGNLI KSSQDTLDDM LEQHLEEVQE LLLEKKSEFE EMNDISSRTD
     EGPQTTSIGL QSSPLPRAPY DSKKFEPGAR QENAVNAVKS PKMPAVGLFA VSPKTSGTRS
     PMKRPSS
//
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