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Database: UniProt/TrEMBL
Entry: E9EYY3_METRA
LinkDB: E9EYY3_METRA
Original site: E9EYY3_METRA 
ID   E9EYY3_METRA            Unreviewed;       649 AA.
AC   E9EYY3;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   22-NOV-2017, entry version 34.
DE   RecName: Full=Histone deacetylase {ECO:0000256|SAAS:SAAS00894283};
DE            EC=3.5.1.98 {ECO:0000256|SAAS:SAAS00894283};
GN   ORFNames=MAA_05232 {ECO:0000313|EMBL:EFY99174.1};
OS   Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS   anisopliae (strain ARSEF 23)).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC   Metarhizium.
OX   NCBI_TaxID=655844 {ECO:0000313|EMBL:EFY99174.1, ECO:0000313|Proteomes:UP000002498};
RN   [1] {ECO:0000313|EMBL:EFY99174.1, ECO:0000313|Proteomes:UP000002498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z.,
RA   Hu X., Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W.,
RA   Wang S., Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y.,
RA   Feng M.G., Xia Y., Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(2011).
RN   [2] {ECO:0000313|EMBL:EFY99174.1, ECO:0000313|Proteomes:UP000002498}
RP   GENOME REANNOTATION.
RC   STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX   PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA   Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA   St Leger R.J., Wang C.;
RT   "Trajectory and genomic determinants of fungal-pathogen speciation and
RT   host adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC       {ECO:0000256|SAAS:SAAS00894227}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|SAAS:SAAS00894298}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EFY99174.1}.
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DR   EMBL; ADNJ02000002; EFY99174.1; -; Genomic_DNA.
DR   RefSeq; XP_007821421.1; XM_007823230.1.
DR   ProteinModelPortal; E9EYY3; -.
DR   EnsemblFungi; EFY99174; EFY99174; MAA_05232.
DR   GeneID; 19259518; -.
DR   KEGG; maj:MAA_05232; -.
DR   KO; K06067; -.
DR   OrthoDB; EOG092C1END; -.
DR   Proteomes; UP000002498; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.800.20; -; 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; PTHR10625; PTHR10625; 2.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037913; His_deacetylse_1; 2.
DR   PRINTS; PR01270; HDASUPER.
DR   PRINTS; PR01271; HISDACETLASE.
DR   SUPFAM; SSF52768; SSF52768; 1.
PE   4: Predicted;
KW   Chromatin regulator {ECO:0000256|SAAS:SAAS00894233};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002498};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00870288};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR037913-3};
KW   Nucleus {ECO:0000256|SAAS:SAAS00894277};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002498};
KW   Transcription {ECO:0000256|SAAS:SAAS00894309};
KW   Transcription regulation {ECO:0000256|SAAS:SAAS00894290}.
FT   DOMAIN       43    333       Hist_deacetyl. {ECO:0000259|Pfam:
FT                                PF00850}.
FT   COILED      514    535       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    156    156       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR037913-1}.
FT   METAL       191    191       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR037913-3}.
FT   METAL       193    193       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR037913-3}.
FT   METAL       279    279       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR037913-3}.
FT   BINDING     114    114       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR037913-2}.
FT   BINDING     164    164       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR037913-2}.
FT   BINDING     318    318       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR037913-2}.
SQ   SEQUENCE   649 AA;  72218 MW;  7EE5D74FAFA7CA20 CRC64;
     MGDSNLAQAQ AQLGSVALNG SSAKKVAYFY DSDIGNYAYV TGHPMKPHRI RLAHSLIMQY
     NLYQKMEIYR AKPATRGEMT QFHTDDYIDF LQKVTPDNMD SYMREQGKYN VGDDCPVFDG
     LFEFCGISAG GSMEGAARLN RQKCDIAVNW AGGLHHAKKC EASGFCYVND IVLGILELLR
     FMKRVLYIDI DVHHGDGVEE AFYTTDRVMT VSFHKYGEYF PGTGELRDIG IGQGKNYSVN
     FPLRDGITDQ TYKSIFEPVI ESVMKYYQPE AVVLQCGGDS LSGDRLGCFN LSMDGHANCV
     NYVKSFGLPT LVLGGGGYTM RNVARTWAYE TGVLVGQEMD RTLPYNEYYE YYAPDFELNV
     RASNMENSNS REYLDKITAA VIDNLRQTGP APSVQMQDVP RKPFGGMTDE EEAELDDLDE
     DENKDVRMTE HRWDKHVENG AEFEASDDDE MAAANGATRS NGNKGTFNDF KSADAAEDSR
     SKSPREKHDD NSKEAVEAET HDVNDDTIED VGAMEEQENQ AAEQEEKEDQ DLKKNKVDAD
     GDVGMTYSSV ADEATIKKEE GEPESVPEDE KEPERPTEEK PSVAEPDKPA EAEGATEVKA
     SDKPAVDQVS EEPAEKEGEA QATTEAETEP MEVDDKEKSE DKAEDDSSK
//
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