ID Q4T0M8_TETNG Unreviewed; 903 AA.
AC Q4T0M8;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 24-JAN-2024, entry version 80.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
DE Flags: Fragment;
GN ORFNames=GSTENG00009245001 {ECO:0000313|EMBL:CAF93554.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|EMBL:CAF93554.1};
RN [1] {ECO:0000313|EMBL:CAF93554.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|EMBL:CAF93554.1}
RP NUCLEOTIDE SEQUENCE.
RG Genoscope;
RG Whitehead Institute Centre for Genome Research;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC subfamily. {ECO:0000256|ARBA:ARBA00007738}.
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:CAF93554.1}.
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DR EMBL; CAAE01010929; CAF93554.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4T0M8; -.
DR KEGG; tng:GSTEN00009245G001; -.
DR GO; GO:0000118; C:histone deacetylase complex; IEA:InterPro.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd11681; HDAC_classIIa; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 2.
DR InterPro; IPR046949; HDAC4/5/7/9.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR017320; Histone_deAcase_II_euk.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR45364:SF9; HISTONE DEACETYLASE 7; 1.
DR PANTHER; PTHR45364; HISTONE DEACETYLASE 9-RELATED; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037911; HDAC_II_euk; 2.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; Arginase/deacetylase; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR037911-2}; Zinc {ECO:0000256|PIRSR:PIRSR037911-2}.
FT DOMAIN 425..703
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 223..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 554
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 417
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 419
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 425
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 502
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT SITE 788
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
FT NON_TER 903
FT /evidence="ECO:0000313|EMBL:CAF93554.1"
SQ SEQUENCE 903 AA; 97962 MW; 56B4550E39D80611 CRC64;
GIDSSGNILE TDRRDAAFHT LEDHSKNNIN PQKPSINLKY SKRLGVFDVK TESVSELLLW
RQDQNCHPRL KGQKAHLYAE QTHPPAAVAP LSLDVVPRTT VCPVTTACCH LQAQKLLLRD
GTLANFTIQS PSTLPTITMG LPANTKAEGE LSSLKVTRVP VVTGPGSPVF LPLSREDQAG
QLSPHLPVII LEPSGLVHTP LLTVPGLDTV QLQFSSHIDH LATGSAQPHK PLSRTRSEPL
PQSQRALHTH LLQQQHSTQL LERLKQQTHL GKLMSKSSEK PRLHQIPSEE MDSEDSGATS
PTEPTHLSRL RAESLREAES ATSTGQEEQI NLQHALILNQ QLHRQMETLA VPMLCTSGGA
GSGLGVHRPL SRTQSSPAST SLTLPEKSLS LAAPDTSIKP RFTTGLVYDS QMLKHQCTCG
DNSSHPEHAG RIQSIWSRLQ ERGLRGQCES IRGRKATLEE LQSVHTERHV LLYGTNPLNR
LKLDNRKLAG ILSQRMFVML PCGGVGVDND TIWNESHTST ASRMAAGSVV ELAFRVAKGE
LKNGFAVVRP PGHHADPSNP MGFCYFNSVA IAAKQLQHKL SVSKILIVDW DVHHGNGTQE
VFYSDPSVLY ISLHRYDNGN FFPGSGSPAE VGTGAGEGFN VNIAWTGGLD PPMGDAEYLA
AFRSVVMPIA QEFSPDVLLV SAGFDAAEGN PALLGGYKVS AKCKHRSPTA GCALRPPGPG
RLCAFDFAAE MPARTSRFVS LRQLDSGTHD GFWFFSVFFF SAAGFSFLTR QLMSLAGGRV
VLVLEGGHDL TAICDASEAC VSALLGMQDP LTEEVLLQKP NANAVRSLQT VIKIQSQYWQ
SVKAHSGSAC LSYLAAQRRD CEETDAVNAL ASLTVGVLSN ERYDTQAEAE AKMQSFTRPA
TLQ
//