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Database: UniProt
Entry: Q4T0M8_TETNG
LinkDB: Q4T0M8_TETNG
Original site: Q4T0M8_TETNG 
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
//
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