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Database: UniProt/TrEMBL
Entry: A8N0K6_COPC7
LinkDB: A8N0K6_COPC7
Original site: A8N0K6_COPC7 
ID   A8N0K6_COPC7            Unreviewed;       590 AA.
AC   A8N0K6;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 2.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE            EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
GN   ORFNames=CC1G_04427 {ECO:0000313|EMBL:EAU93448.2};
OS   Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS   (Inky cap fungus) (Hormographiella aspergillata).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX   NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU93448.2, ECO:0000313|Proteomes:UP000001861};
RN   [1] {ECO:0000313|EMBL:EAU93448.2, ECO:0000313|Proteomes:UP000001861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC   {ECO:0000313|Proteomes:UP000001861};
RX   PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA   Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA   Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA   Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA   Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA   Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA   Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA   Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA   Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA   Zolan M.E., Pukkila P.J.;
RT   "Insights into evolution of multicellular fungi from the assembled
RT   chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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:EAU93448.2}.
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DR   EMBL; AACS02000001; EAU93448.2; -; Genomic_DNA.
DR   RefSeq; XP_001828456.2; XM_001828404.2.
DR   AlphaFoldDB; A8N0K6; -.
DR   STRING; 240176.A8N0K6; -.
DR   GeneID; 6004879; -.
DR   KEGG; cci:CC1G_04427; -.
DR   VEuPathDB; FungiDB:CC1G_04427; -.
DR   eggNOG; KOG1342; Eukaryota.
DR   HOGENOM; CLU_007727_0_2_1; -.
DR   InParanoid; A8N0K6; -.
DR   OMA; EHRWDKH; -.
DR   OrthoDB; 1327607at2759; -.
DR   Proteomes; UP000001861; Unassembled WGS sequence.
DR   GO; GO:1902494; C:catalytic complex; IEA:UniProt.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
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; 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:SF13; HISTONE DEACETYLASE HDAC1; 1.
DR   PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR   Pfam; PF00850; Hist_deacetyl; 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   Reference proteome {ECO:0000313|Proteomes:UP000001861}.
FT   DOMAIN          34..322
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   REGION          377..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          489..590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..456
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        503..517
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..590
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   590 AA;  63864 MW;  A444581ABBE13AA4 CRC64;
     MGDKWTPVEG ESQKKRVCYF YDSDIGGFHY GPGHPMKPTR IRMCHSLVMN YGLYKKMEIF
     RAKPATKREM TQFHSDEYVE FLSKITPNNM NSFVKEQHKY NVGDDCPVFD GLFEYCSISA
     GGSMEGAARL SRDKCDIAIN WAGGLHHAKK SEASGFCYVN DIVLGILELL RYHNRVLYID
     IDVHHGDGVE EAFYTTDRVM TVSFHKYGEY FPGTGELRDV GIMKGKYYSL NFPLRDGISD
     ENYKSVFEPV IRSVMETYDP SAIVLQCGTD SLSGDKLGCL NLSMKGHANC VKFVKSFNKP
     LLLLGGGGYT MRNVSRAWAY ETGLAAGVEL NPEIPVNEYY EYFGPDYQLD VKSSNTDDLN
     TPAYLDRVKR IVLENLRHTQ GPPSVQMTDI PSMPIDADID DPNQDEDMVD PNDRRPMRLL
     DSRRQADGEL SDSDDEGEGG RRDIASHKDR ESNGEGAGHK FGMGVGIMAS SSAATHGAGP
     SGHTTAAQIL SAPKADAPMD VDTPTSETGS APVTEGKSSE VNGGGGASAG AVAASAGPSS
     ASGQPAAPAA EPAKEDKDTA MAVEEPSEPK PSEPASSTAA AAPAPTTSTT
//
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