ID A0A087WLN3_ECHMU Unreviewed; 555 AA.
AC A0A087WLN3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
GN ORFNames=EmuJ_001102300 {ECO:0000313|EMBL:CDS43279.2};
OS Echinococcus multilocularis (Fox tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX NCBI_TaxID=6211 {ECO:0000313|EMBL:CDS43279.2};
RN [1] {ECO:0000313|EMBL:CDS43279.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23485966; DOI=10.1038/nature12031;
RA Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A., Sanchez-Flores A.,
RA Brooks K.L., Tracey A., Bobes R.J., Fragoso G., Sciutto E., Aslett M.,
RA Beasley H., Bennett H.M., Cai J., Camicia F., Clark R., Cucher M.,
RA De Silva N., Day T.A., Deplazes P., Estrada K., Fernandez C., Holland P.W.,
RA Hou J., Hu S., Huckvale T., Hung S.S., Kamenetzky L., Keane J.A., Kiss F.,
RA Koziol U., Lambert O., Liu K., Luo X., Luo Y., Macchiaroli N., Nichol S.,
RA Paps J., Parkinson J., Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M.,
RA Salinas G., Wasmuth J.D., Zamanian M., Zheng Y., Cai X., Soberon X.,
RA Olson P.D., Laclette J.P., Brehm K., Berriman M., Garciarrubio A.,
RA Bobes R.J., Fragoso G., Sanchez-Flores A., Estrada K., Cevallos M.A.,
RA Morett E., Gonzalez V., Portillo T., Ochoa-Leyva A., Jose M.V., Sciutto E.,
RA Landa A., Jimenez L., Valdes V., Carrero J.C., Larralde C.,
RA Morales-Montor J., Limon-Lason J., Soberon X., Laclette J.P.;
RT "The genomes of four tapeworm species reveal adaptations to parasitism.";
RL Nature 496:57-63(2013).
RN [2] {ECO:0000313|EMBL:CDS43279.2}
RP NUCLEOTIDE SEQUENCE.
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC subfamily. {ECO:0000256|ARBA:ARBA00006457}.
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DR EMBL; LN902844; CDS43279.2; -; Genomic_DNA.
DR AlphaFoldDB; A0A087WLN3; -.
DR STRING; 6211.A0A087WLN3; -.
DR eggNOG; KOG1342; Eukaryota.
DR OMA; GKIMEWY; -.
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 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 Repressor {ECO:0000256|ARBA:ARBA00022491}.
FT DOMAIN 26..315
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 450..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 555 AA; 62613 MW; 7541CA177EEBEBED CRC64;
MDPAVDKKVC YYYDGDIGNY YYGQGHPMKP HRIRMTHNLL LNYGLYRKME VYRPSKASAE
DMTKFHSDEY IRFLQSIRPD NMLDYTKQMQ RFNVGEDCPV FDGLFEFCQL SAGGSVAGAV
KLNKQQTDIA INWGGGLHHA KKSEASGFCY VNDIVMGILE LLKYHQRVLY VDIDIHHGDG
VEEAFYTTDR VMTVSFHKYG EYFPGTGDLK DIGAGRGKHY AVNCPLRDGM DDECYEKIFK
PVVSKVMETF RPGAAVLQCG ADSLSGDRLG CFNLSLKGHG KCVEFLRSFP IPLLMLGGGG
YTIRNVARCW TYETSIALNT EVPNDLPYND YYEYFGPDFK LHISPSNMTN LNTPDYIERI
KNKLFENLRM LPHAPSVQMV DVPPDTIDVE EQEKEAIENE DPDKRISIMA SDKAVHRDNE
FYDSGEEDGV GVQVAPKGIK TAKDVHSFRN QAKRARIEES GKGDVASMDT EESAEADKAR
TGGDKETVDT GATLADSNTT ASYIAHTTRQ YYIGCHWHLL CTERSGKRYF LVYGLPPCKI
LFFNGFLIIP WANST
//
