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Conserved domains on  [gi|767903932|ref|XP_011539611|]
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histone deacetylase 1 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Arginase_HDAC super family cl17011
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
1-181 1.42e-133

Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily includes metal-dependent enzymes that belong to Arginase-like amidino hydrolase family and histone/histone-like deacetylase class I, II, IV family, respectively. These enzymes catalyze hydrolysis of amide bond. Arginases are known to be involved in control of cellular levels of arginine and ornithine, in histidine and arginine degradation and in clavulanic acid biosynthesis. Deacetylases play a role in signal transduction through histone and/or other protein modification and can repress/activate transcription of a number of different genes. They participate in different cellular processes including cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and post-translational control of the acetyl coenzyme A synthetase. Mammalian histone deacetyases are known to be involved in progression of different tumors. Specific inhibitors of mammalian histone deacetylases are an emerging class of promising novel anticancer drugs.


The actual alignment was detected with superfamily member cd10010:

Pssm-ID: 354294  Cd Length: 371  Bit Score: 382.88  E-value: 1.42e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   1 MTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGC 80
Cdd:cd10010  191 MTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGADSLSGDRLGC 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932  81 FNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQ 160
Cdd:cd10010  271 FNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDSEIPNELPYNDYFEYFGPDFKLHISPSNMTNQ 350
                        170       180
                 ....*....|....*....|.
gi 767903932 161 NTNEYLEKIKQRLFENLRMLP 181
Cdd:cd10010  351 NTNEYLEKIKQRLFENLRMLP 371
 
Name Accession Description Interval E-value
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
1-181 1.42e-133

Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme that catalyzes hydrolysis of N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. HDAC1 is involved in regulation through association with DNA binding proteins to target specific chromatin regions. In particular, HDAC1 appears to play a major role in pre-implantation embryogenesis in establishing a repressive chromatin state. Its interaction with retinoblastoma tumor-suppressor protein is essential in the control of cell proliferation and differentiation. Together with metastasis-associated protein-2 (MTA2), it deacetylates p53, thereby modulating its effect on cell growth and apoptosis. It participates in DNA-damage response, along with HDAC2; together, they promote DNA non-homologous end-joining. HDAC1 is also involved in tumorogenesis; its overexpression modulates cancer progression. Specific inhibitors of HDAC1 are currently used in cancer therapy.


Pssm-ID: 212534  Cd Length: 371  Bit Score: 382.88  E-value: 1.42e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   1 MTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGC 80
Cdd:cd10010  191 MTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGADSLSGDRLGC 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932  81 FNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQ 160
Cdd:cd10010  271 FNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDSEIPNELPYNDYFEYFGPDFKLHISPSNMTNQ 350
                        170       180
                 ....*....|....*....|.
gi 767903932 161 NTNEYLEKIKQRLFENLRMLP 181
Cdd:cd10010  351 NTNEYLEKIKQRLFENLRMLP 371
PTZ00063 PTZ00063
histone deacetylase; Provisional
1-194 2.24e-111

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 328.69  E-value: 2.24e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   1 MTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGC 80
Cdd:PTZ00063 191 MTVSFHKFGDFFPGTGDVTDIGVAQGKYYSVNVPLNDGIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGR 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932  81 FNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALD--TEIPNELPYNDYFEYFGPDFKLHISPSNMT 158
Cdd:PTZ00063 271 FNLTIKGHAACVEFVRSLNIPLLVLGGGGYTIRNVARCWAYETGVILNkhDEMSDQISLNDYYDYYAPDFQLHLQPSNIP 350
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767903932 159 NQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPED 194
Cdd:PTZ00063 351 NYNSPEHLEKIKVKILENLRYLEHAPGVQFAYVPPD 386
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
1-125 1.60e-46

Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. Regulation of transcription is caused in part by this mechanism. Histone deacetylases catalyze the removal of the acetyl group. Histone deacetylases are related to other proteins.


Pssm-ID: 334285  Cd Length: 300  Bit Score: 157.77  E-value: 1.60e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932    1 MTVSFHKYGEY-FPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLG 79
Cdd:pfam00850 170 LTLSIHQYPGGfYPGTGAADETGEGAGKGFTLNVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAGFDAHAGDPLG 249
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 767903932   80 CFNLTIKGHAKCVEFVKSFNL----PMLMLGGGGYTIRNVARCWTYETAV 125
Cdd:pfam00850 250 GLNLTTEGYGELTRLLLELADehcgRVVSVLEGGYNLDALARSATAVLAA 299
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Chromatin structure and ...
1-147 6.97e-44

Acetoin utilization deacetylase AcuC or a related deacetylase [Chromatin structure and dynamics, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 223201  Cd Length: 340  Bit Score: 152.14  E-value: 6.97e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   1 MTVSFHKYGEY-FPGTGDLRDIGAGKgKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLG 79
Cdd:COG0123  180 LTVSLHQDGRPfYPGTGGADEIGEGK-EGNNVNIPLPPGTGDDSYLEALEEIVLPLLEEFKPDLVIVSAGFDAHRGDPLG 258
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767903932  80 CFNLTIKGHAKCVEFVKSFNL----PMLMLGGGGYTIRNVARCWTYETAVALD---TEIPNELPYN-DYFEYFGPD 147
Cdd:COG0123  259 RLNLTEEGYAKIGRAVRKLAEgyggPVVAVLEGGYNLDALARSLVAFLAGLAGlveEELEEPLPEDlELRRAFRAD 334
 
Name Accession Description Interval E-value
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
1-181 1.42e-133

Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme that catalyzes hydrolysis of N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. HDAC1 is involved in regulation through association with DNA binding proteins to target specific chromatin regions. In particular, HDAC1 appears to play a major role in pre-implantation embryogenesis in establishing a repressive chromatin state. Its interaction with retinoblastoma tumor-suppressor protein is essential in the control of cell proliferation and differentiation. Together with metastasis-associated protein-2 (MTA2), it deacetylates p53, thereby modulating its effect on cell growth and apoptosis. It participates in DNA-damage response, along with HDAC2; together, they promote DNA non-homologous end-joining. HDAC1 is also involved in tumorogenesis; its overexpression modulates cancer progression. Specific inhibitors of HDAC1 are currently used in cancer therapy.


Pssm-ID: 212534  Cd Length: 371  Bit Score: 382.88  E-value: 1.42e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   1 MTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGC 80
Cdd:cd10010  191 MTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGADSLSGDRLGC 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932  81 FNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQ 160
Cdd:cd10010  271 FNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDSEIPNELPYNDYFEYFGPDFKLHISPSNMTNQ 350
                        170       180
                 ....*....|....*....|.
gi 767903932 161 NTNEYLEKIKQRLFENLRMLP 181
Cdd:cd10010  351 NTNEYLEKIKQRLFENLRMLP 371
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
1-194 2.60e-120

Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that catalyzes hydrolysis of N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. In order to target specific chromatin regions, HDAC3 can interact with DNA-binding proteins (transcriptional factors) either directly or after forming complexes with a number of other proteins, as observed for the SMPT/N-CoR complex which recruits human HDAC3 to specific chromatin loci and activates deacetylation. Human HDAC3 is also involved in deacetylation of non-histone substrates such as RelA, SPY and p53 factors. This protein can also down-regulate p53 function and subsequently modulate cell growth and apoptosis. This gene is therefore regarded as a potential tumor suppressor gene. HDAC3 plays a role in various physiological processes, including subcellular protein localization, cell cycle progression, cell differentiation, apoptosis and survival. HDAC3 has been found to be overexpressed in some tumors including leukemia, lung carcinoma, colon cancer and maxillary carcinoma. Thus, inhibitors precisely targeting HDAC3 (in some cases together with retinoic acid or hyperthermia) could be a therapeutic drug option.


Pssm-ID: 212529  Cd Length: 381  Bit Score: 349.39  E-value: 2.60e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   1 MTVSFHKYGEYF-PGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLG 79
Cdd:cd10005  186 MTVSFHKYGNYFfPGTGDMYEVGAESGRYYSVNVPLKDGIDDQSYLQLFKPVIQQVIDFYQPTCIVLQCGADSLGCDRLG 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932  80 CFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHIS-PSNMT 158
Cdd:cd10005  266 CFNLSIKGHGECVEFVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVDEEISNELPYNEYFEYFAPDFTLHPDvSTRIE 345
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767903932 159 NQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPED 194
Cdd:cd10005  346 NQNSKQYLDQIRQTVFENLKMLNHAPSVQMQDVPPD 381
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
1-180 6.13e-118

Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme that catalyzes hydrolysis of N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. HDAC2 is involved in regulation through association with DNA binding proteins to target specific chromatin regions. It forms transcriptional repressor complexes by associating with several proteins, including the mammalian zinc-finger transcription factor YY1, thus playing an important role in transcriptional regulation, cell cycle progression and developmental events. Additionally, a few non-histone HDAC2 substrates have been found. HDAC2 plays a role in embryonic development and cytokine signaling important for immune response, and is over-expressed in several solid tumors including oral, prostate, ovarian, endometrial and gastric cancer. It participates in DNA-damage response, along with HDAC1; together, they can promote DNA non-homologous end-joining. HDAC2 is considered an important cancer prognostic marker. Inhibitors specifically targeting HDAC2 could be a therapeutic drug option.


Pssm-ID: 212535  Cd Length: 366  Bit Score: 342.81  E-value: 6.13e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   1 MTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGC 80
Cdd:cd10011  187 MTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGC 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932  81 FNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQ 160
Cdd:cd10011  267 FNLTVKGHAKCVEVVKTFNLPLLMLGGGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQ 346
                        170       180
                 ....*....|....*....|
gi 767903932 161 NTNEYLEKIKQRLFENLRML 180
Cdd:cd10011  347 NTPEYMEKIKQRLFENLRML 366
PTZ00063 PTZ00063
histone deacetylase; Provisional
1-194 2.24e-111

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 328.69  E-value: 2.24e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   1 MTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGC 80
Cdd:PTZ00063 191 MTVSFHKFGDFFPGTGDVTDIGVAQGKYYSVNVPLNDGIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGR 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932  81 FNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALD--TEIPNELPYNDYFEYFGPDFKLHISPSNMT 158
Cdd:PTZ00063 271 FNLTIKGHAACVEFVRSLNIPLLVLGGGGYTIRNVARCWAYETGVILNkhDEMSDQISLNDYYDYYAPDFQLHLQPSNIP 350
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767903932 159 NQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPED 194
Cdd:PTZ00063 351 NYNSPEHLEKIKVKILENLRYLEHAPGVQFAYVPPD 386
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
1-189 7.36e-111

reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I Zn-dependent Histone deacetylases that catalyze hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). RPD3 is the yeast homolog of class I HDACs. The main function of RPD3-like group members is regulation of a number of different processes through protein (mostly different histones) modification (deacetylation). This group includes fungal RPD3 and acts via the formation of large multiprotein complexes. Members of this group are involved in cell cycle regulation, DNA damage response, embryonic development and cytokine signaling important for immune response. Histone deacetylation by yeast RPD3 represses genes regulated by the Ash1 and Ume6 DNA-binding proteins. In mammals, they are known to be involved in progression of various tumors. Specific inhibitors of mammalian histone deacetylases could be a therapeutic drug option.


Pssm-ID: 212528  Cd Length: 375  Bit Score: 325.22  E-value: 7.36e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   1 MTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGC 80
Cdd:cd10004  187 MTCSFHKYGEYFPGTGELRDIGIGTGKNYAVNVPLRDGIDDESYKSIFEPVIKHVMEWYQPEAVVLQCGGDSLSGDRLGC 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932  81 FNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQ 160
Cdd:cd10004  267 FNLSMKGHANCVNFVKSFNLPMLVLGGGGYTMRNVARTWAFETGLLAGEELDKDLPYNEYYEYYGPDYELNVRPSNMENH 346
                        170       180
                 ....*....|....*....|....*....
gi 767903932 161 NTNEYLEKIKQRLFENLRMLPHAPGVQMQ 189
Cdd:cd10004  347 NTPEYLDKITTAVIENLRNTSFAPSVQMQ 375
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
1-126 1.10e-97

Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues in histone amino termini to yield a deacetylated histone (EC 3.5.1.98). Enzymes belonging to this group participate in regulation of a number of processes through protein (mostly different histones) modification (deacetylation). Class I histone deacetylases in general act via the formation of large multiprotein complexes. This group includes animal HDAC1, HDAC2, HDAC3, HDAC8, fungal RPD3, HOS1 and HOS2, plant HDA9, protist, archaeal and bacterial (AcuC) deacetylases. Members of this class are involved in cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and in posttranslational control of the acetyl coenzyme A synthetase. In mammals, they are known to be involved in progression of various tumors. Specific inhibitors of mammalian histone deacetylases are an emerging class of promising novel anticancer drugs.


Pssm-ID: 212517  Cd Length: 306  Bit Score: 289.10  E-value: 1.10e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   1 MTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGC 80
Cdd:cd09991  181 MTVSFHKFGEYFFPGTGLRDIGAGKGKYYAVNVPLKDGIDDESYLQIFEPVLSKVMEVFQPSAVVLQCGADSLAGDRLGC 260
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767903932  81 FNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVA 126
Cdd:cd09991  261 FNLSIKGHAKCVKFVKSFNIPLLVLGGGGYTLRNVARCWTYETAVL 306
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
1-177 5.32e-83

Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that catalyzes hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. HDAC8 is found in human cytoskeleton-bound protein fraction and insoluble cell pellets. It plays a crucial role in intramembraneous bone formation; germline deletion of HDAC8 is detrimental to skull bone formation. HDAC8 is possibly associated with the smooth muscle actin cytockeleton and may regulate the contractive capacity of smooth muscle cells. HDAC8 is also involved in the metabolic control of the estrogen receptor related receptor (ERR)-alpha/peroxisome proliferator activated receptor (PPAR) gamma coactivator 1 alpha (PGC1-alpha) transcriptional complex as well as in the development of neuroblastoma and T-cell lymphoma. HDAC8-selective small-molecule inhibitors could be a therapeutic drug option for these diseases.


Pssm-ID: 212524  Cd Length: 364  Bit Score: 253.80  E-value: 5.32e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   1 MTVSFHKYGE-YFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLG 79
Cdd:cd10000  183 MTVSLHKYSPgFFPGTGDVSDVGLGKGKYYTVNVPLRDGIQDEQYLQIFTAVVPEIVAAFRPEAVVLQCGADTLAGDPMG 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932  80 CFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTN 159
Cdd:cd10000  263 AFNLTPVGIGKCLKYVLGWKLPTLILGGGGYNLANTARCWTYLTGLILGEPLSSDIPDHEFFTSYGPDYELEISPSLRPD 342
                        170
                 ....*....|....*...
gi 767903932 160 QNTNEYLEKIKQRLFENL 177
Cdd:cd10000  343 LNEDQYIEKILETIKGNL 360
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
1-126 1.22e-71

Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I histone deacetylase (HDAC) Hos2 from Saccharomyces cerevisiae as well as a histone deacetylase Phd1 from Schizosaccharomyces pombe. Hos2 binds to the coding regions of genes during gene activation, specifically it deacetylates the lysines in H3 and H4 histone tails. It is preferentially associated with genes of high activity genome-wide and is shown to be necessary for efficient transcription. Thus, Hos2 is directly required for gene activation in contrast to other class I histone deacetylases. Protein encoded by phd1 is inhibited by trichostatin A (TSA), a specific inhibitor of histone deacetylase, and is involved in the meiotic cell cycle in S. pombe. Class 1 HDACs are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues in histone amino termini to yield a deacetylated histone (EC 3.5.1.98).


Pssm-ID: 212540  Cd Length: 311  Bit Score: 222.72  E-value: 1.22e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   1 MTVSFHKY-GEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLG 79
Cdd:cd11598  185 MTLSFHKYnGEFFPGTGDLDDNGGTPGKHFALNVPLEDGIDDEQYNLLFKSIIGPTIEKFQPSAIVLQCGADSLGGDRLG 264
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767903932  80 CFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVA 126
Cdd:cd11598  265 QFNLNIKAHGACVKFVKSFGIPMLVVGGGGYTPRNVARAWCYETAVA 311
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
1-125 1.60e-46

Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. Regulation of transcription is caused in part by this mechanism. Histone deacetylases catalyze the removal of the acetyl group. Histone deacetylases are related to other proteins.


Pssm-ID: 334285  Cd Length: 300  Bit Score: 157.77  E-value: 1.60e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932    1 MTVSFHKYGEY-FPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLG 79
Cdd:pfam00850 170 LTLSIHQYPGGfYPGTGAADETGEGAGKGFTLNVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAGFDAHAGDPLG 249
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 767903932   80 CFNLTIKGHAKCVEFVKSFNL----PMLMLGGGGYTIRNVARCWTYETAV 125
Cdd:pfam00850 250 GLNLTTEGYGELTRLLLELADehcgRVVSVLEGGYNLDALARSATAVLAA 299
PTZ00346 PTZ00346
histone deacetylase; Provisional
2-132 3.51e-44

histone deacetylase; Provisional


Pssm-ID: 240374  Cd Length: 429  Bit Score: 155.19  E-value: 3.51e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   2 TVSFHKYGE-YFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGC 80
Cdd:PTZ00346 209 TLSLHKFGEsFFPGTGHPRDVGYGRGRYYSMNLAVWDGITDFYYLGLFEHALHSIVRRYSPDAIVLQCGADSLAGDRLGL 288
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767903932  81 FNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIP 132
Cdd:PTZ00346 289 LNLSSFGHGQCVQAVRDLGIPMLALGGGGYTIRNVAKLWAYETSILTGHPLP 340
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
1-126 4.34e-44

Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family includes Zn-dependent histone deacetylase classes I, II and IV (class III HDACs, also called sirtuins, are NAD-dependent and structurally unrelated, and therefore not part of this family). Histone deacetylases catalyze hydrolysis of N(6)-acetyl-lysine residues in histone amino termini to yield a deacetylated histone (EC 3.5.1.98), as opposed to the acetylation reaction by some histone acetyltransferases (EC 2.3.1.48). Deacetylases of this family are involved in signal transduction through histone and other protein modification, and can repress/activate transcription of a number of different genes. They usually act via the formation of large multiprotein complexes. They are involved in various cellular processes, including cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and post-translational control of the acetyl coenzyme A synthetase. In mammals, they are known to be involved in progression of different tumors. Specific inhibitors of mammalian histone deacetylases are an emerging class of promising novel anticancer drugs.


Pssm-ID: 212512 [Multi-domain]  Cd Length: 279  Bit Score: 151.05  E-value: 4.34e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   1 MTVSFHKYGEYFPGTGdlrdigagKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGC 80
Cdd:cd09301  160 LHMSFHNYDIYPFGRG--------KGKGYKINVPLEDGLGDEEYLDAVERVISKVLEEFEPEVVVLQFGHDTHEGDRLGG 231
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767903932  81 FNLTIKGHAKCVEFVKSFN--LPMLMLGGGGYTIRNVARCWTYETAVA 126
Cdd:cd09301  232 FNLSEKGFVKLAEIVKEFArgGPILMVLGGGYNPEAAARIWTAIIKEL 279
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Chromatin structure and ...
1-147 6.97e-44

Acetoin utilization deacetylase AcuC or a related deacetylase [Chromatin structure and dynamics, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 223201  Cd Length: 340  Bit Score: 152.14  E-value: 6.97e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   1 MTVSFHKYGEY-FPGTGDLRDIGAGKgKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLG 79
Cdd:COG0123  180 LTVSLHQDGRPfYPGTGGADEIGEGK-EGNNVNIPLPPGTGDDSYLEALEEIVLPLLEEFKPDLVIVSAGFDAHRGDPLG 258
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767903932  80 CFNLTIKGHAKCVEFVKSFNL----PMLMLGGGGYTIRNVARCWTYETAVALD---TEIPNELPYN-DYFEYFGPD 147
Cdd:COG0123  259 RLNLTEEGYAKIGRAVRKLAEgyggPVVAVLEGGYNLDALARSLVAFLAGLAGlveEELEEPLPEDlELRRAFRAD 334
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
2-126 1.80e-36

Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is responsible for Smc3 deacetylation. Smc3 is an important player during the establishment of sister chromatid cohesion. Hos1 belongs to the class I histone deacetylases (HDACs). HDACs are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues in histone amino termini to yield a deacetylated histone (EC 3.5.1.98). Enzymes belonging to this group participate in regulation of a number of processes through protein (mostly different histones) modification (deacetylation). Class I histone deacetylases in general act via the formation of large multiprotein complexes. Other class I HDACs are animal HDAC1, HDAC2, HDAC3, HDAC8, fungal RPD3 and HOS2, plant HDA9, protist, archaeal and bacterial (AcuC) deacetylases. Members of this class are involved in cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and in posttranslational control of the acetyl coenzyme A synthetase.


Pssm-ID: 212543  Cd Length: 294  Bit Score: 131.62  E-value: 1.80e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   2 TVSFHKYGE-YFPGTGDLRDigagKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGC 80
Cdd:cd11680  171 TCSIHRYDPgFFPGTGSLKN----SSDKGMLNIPLKRGLSDKTLLRIIDSIVRPLIEKFEPEVIVIQCGCDGLSGDPHKE 246
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767903932  81 FNLTIKGHAKCVEFVKSF--NLPMLMLGGGGYTIRNVARCWTYETAVA 126
Cdd:cd11680  247 WNLTIRGYGSVIELLLKEfkDKPTLLLGGGGYNHTEAARAWTYLTSMV 294
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
1-120 2.18e-36

Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin utilization protein) is a class I deacetylase found only in bacteria and is involved in post-translational control of the acetyl-coenzyme A synthetase (AcsA). Deacetylase AcuC works in coordination with deacetylase SrtN (class III), possibly to maintain AcsA in active (deacetylated) form and let the cell grow under low concentration of acetate. B. subtilis AcuC is a member of operon acuABC; this operon is repressed by the presence of glucose and does not show induction by acetoin; acetoin is a bacterial fermentation product that can be converted to acetate via the butanediol cycle in absence of other carbon sources. Inactivation of AcuC leads to slower growth and lower cell yield under low-acetate conditions in Bacillus subtilis. In general, Class I histone deacetylases (HDACs) are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues in histone amino termini to yield a deacetylated histone (EC 3.5.1.98). Enzymes belonging to this group participate in regulation of a number of processes through protein (mostly different histones) modification (deacetylation). Class I histone deacetylases in general act via the formation of large multiprotein complexes. Members of this class are involved in cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and in posttranslational control of the acetyl coenzyme A synthetase.


Pssm-ID: 212520  Cd Length: 313  Bit Score: 131.53  E-value: 2.18e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   1 MTVSFHKYGEY-FPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLG 79
Cdd:cd09994  182 LTISLHESGRYlFPGTGFVDEIGEGEGYGYAVNIPLPPGTGDDEFLRAFEAVVPPLLRAFRPDVIVSQHGADAHAGDPLT 261
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767903932  80 CFNLTIKGHAKCVEFVK-----SFNLPMLMLGGGGYTIRNVARCWT 120
Cdd:cd09994  262 HLNLSNRAYRAAVRRIReladeYCGGRWLALGGGGYNPDVVARAWA 307
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
1-126 1.43e-24

Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily includes metal-dependent enzymes that belong to Arginase-like amidino hydrolase family and histone/histone-like deacetylase class I, II, IV family, respectively. These enzymes catalyze hydrolysis of amide bond. Arginases are known to be involved in control of cellular levels of arginine and ornithine, in histidine and arginine degradation and in clavulanic acid biosynthesis. Deacetylases play a role in signal transduction through histone and/or other protein modification and can repress/activate transcription of a number of different genes. They participate in different cellular processes including cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and post-translational control of the acetyl coenzyme A synthetase. Mammalian histone deacetyases are known to be involved in progression of different tumors. Specific inhibitors of mammalian histone deacetylases are an emerging class of promising novel anticancer drugs.


Pssm-ID: 212513  Cd Length: 217  Bit Score: 98.22  E-value: 1.43e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   1 MTVSFHKYGEYFPGTGdlrdiGAGKGKYYAVNYPLRDGiDDESYEAIFKPVMSKVMemFQPSAVVLQCGSDSLSGD---- 76
Cdd:cd09987   90 HIVSIGIRGVSNGEAG-----GAYARKLGVVYFSMTEV-DKLGLGDVFEEIVSYLG--DKGDNVYLSVDVDGLDPSfapg 161
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767903932  77 --RLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTI----RNVARCWTYETAVA 126
Cdd:cd09987  162 tgTPGPGGLSYREGLYITERIAKTNLVVGLDIVEVNPLldetGRTARLAAALTLEL 217
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
3-118 4.15e-17

Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues of histones (EC 3.5.1.98) and possibly other proteins to yield deacetylated histones/other proteins. This group includes animal HDAC4,5,6,7,8,9,10, fungal HOS3 and HDA1, plant HDA5 and HDA15 as well as other eukaryotes, archaeal and bacterial histone-like deacetylases. Eukaryotic deacetylases mostly use histones (H2, H3, H4) as substrates for deacetylation; however, non-histone substrates are known (for example, tubulin). Substrates for prokaryotic histone-like deacetylases are not known. Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. Interaction partners of class II deacetylases include 14-3-3 proteins, MEF2 family of transcriptional factors, CtBP, calmodulin (CaM), SMRT, N-CoR, BCL6, HP1alpha and SUMO. Histone deacetylases play a role in the regulation of cell cycle, cell differentiation and survival. Class II mammalian HDACs are differentially inhibited by structurally diverse compounds with known antitumor activities, thus presenting them as potential drug targets for human diseases resulting from aberrant acetylation.


Pssm-ID: 212518  Cd Length: 291  Bit Score: 79.08  E-value: 4.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   3 VSFHKYGeYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFN 82
Cdd:cd09992  163 FSIHQYP-FYPGTGAAEETGGGAGEGFTINVPLPPGSGDAEYLAAFEEVLLPIAREFQPDLVLVSAGFDAHRGDPLGGMN 241
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767903932  83 LTIKGHAKCVEFVKSF-----NLPMLMLGGGGYTIRNVARC 118
Cdd:cd09992  242 LTPEGYARLTRLLKELadehcGGRLVFVLEGGYNLEALAES 282
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
1-118 7.57e-14

Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine amidohydrolase (APAH) as well as other Class II histone deacetylase (HDAC) and related proteins. Deacetylases of class II are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues of histones (EC 3.5.1.98) and possibly other proteins to yield deacetylated histones/other proteins. Mycoplana ramosa APAH exhibits broad substrate specificity and catalyzes the deacetylation of polyamines such as putrescine, spermidine, and spermine by cleavage of a non-peptide amide bond.


Pssm-ID: 212525  Cd Length: 298  Bit Score: 69.87  E-value: 7.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   1 MTVSFHKYGE-YFPGT-GDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEmFQPSAVVLQCGSDSLSGDRL 78
Cdd:cd10001  171 LYVSIHGDPRtFYPFFlGFADETGEGEGEGYNLNLPLPPGTGDDDYLAALDEALAAIAA-FGPDALVVSLGFDTHEGDPL 249
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767903932  79 GCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARC 118
Cdd:cd10001  250 SDFKLTTEDYARIGRRIAALGLPTVFVQEGGYNVDALGRN 289
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
1-118 1.39e-11

Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are class IIb Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. HDACs usually act via association with DNA binding proteins to target specific chromatin regions. HDAC6 is the only histone deacetylase with internal duplication of two catalytic domains which appear to function independently of each other, and also has a C-terminal ubiquitin-binding domain. It is located in the cytoplasm and associates with microtubule motor complex, functioning as the tubulin deacetylase and regulating microtubule-dependent cell motility. HDAC10 has an N-terminal deacetylase domain and a C-terminal pseudo-repeat that shares significant similarity with its catalytic domain. It is located in the nucleus and cytoplasm, and is involved in regulation of melanogenesis. It transcriptionally down-regulates thioredoxin-interacting protein (TXNIP), leading to altered reactive oxygen species (ROS) signaling in human gastric cancer cells. Known interaction partners of HDAC6 are alpha tubulin (substrate) and ubiquitin-like modifier FAT10 (also known as Ubiquitin D or UBD) while interaction partners of HDAC10 are Pax3, KAP1, hsc70 and HDAC3 proteins.


Pssm-ID: 212526  Cd Length: 336  Bit Score: 63.87  E-value: 1.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   1 MTVSFHKY--GEYFPG--TGDLRDIGAGKGKYYAVNYPLRD-GIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSG 75
Cdd:cd10002  173 LYFSIHRYehGRFWPHlfESDYDYIGVGHGYGFNVNVPLNQtGLGDADYLAIFHHILLPLALEFQPELVLVSAGFDASIG 252
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 767903932  76 DRLGCFNLTIKGHAKCVEFVKSFNLPMLMLG-GGGYTIRNVARC 118
Cdd:cd10002  253 DPEGEMAVTPAGYAHLTRLLMGLAGGKLLLVlEGGYLLESLAES 296
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
32-117 2.27e-11

Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone deacetylases (HDAC11; EC 3.5.1.98) are predicted Zn-dependent enzymes. This class includes animal HDAC11, plant HDA2 and related bacterial deacetylases. Enzymes in this subfamily participate in regulation of a number of different processes through protein modification (deacetylation). They catalyze hydrolysis of N(6)-acetyl-lysine of histones (or other proteins) to yield a deacetylated proteins. Histone deacetylases often act as members of large multi-protein complexes such as mSin3A or SMRT/N-CoR. Human HDAC11 does not associate with them but can interact with HDAC6 in vivo. It has been suggested that HDAC11 and HDAC6 may use non-histone proteins as their substrates and play a role other than to directly modulate chromatin structure. In normal tissues, expression of HDAC11 is limited to kidney, heart, brain, skeletal muscle and testis, suggesting that its function might be tissue-specific. In mammals, HDAC11 proteins are known to be involved in progression of various tumors. HDAC11 plays an essential role in regulating OX40 ligand (OX40L) expression in Hodgkin lymphoma (HL); selective inhibition of HDAC11 expression significantly up-regulates OX40L and induces apoptosis in HL cell lines. Thus, inhibition of HDAC11 could be a therapeutic drug option for antitumor immune response in HL patients.


Pssm-ID: 212519  Cd Length: 275  Bit Score: 62.52  E-value: 2.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932  32 NYPLR-----------DGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAK----CVEFVK 96
Cdd:cd09993  167 NYPFRkepsdldvplpDGTGDDEYLAALEEALPRLLAEFRPDLVFYNAGVDVLAGDRLGRLSLSLEGLRErdrlVLRFAR 246
                         90       100
                 ....*....|....*....|.
gi 767903932  97 SFNLPMLMLGGGGYTiRNVAR 117
Cdd:cd09993  247 ARGIPVAMVLGGGYS-RDIAR 266
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
2-147 8.74e-11

Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial as well as eukaryotic Class II histone deacetylase (HDAC) and related proteins. Deacetylases of class II are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues of histones (EC 3.5.1.98) and possibly other proteins to yield deacetylated histones/other proteins. Included in this family is a bacterial HDAC-like amidohydrolase (Bordetella/Alcaligenes species FB18817, denoted as FB188 HDAH) shown to be most similar in sequence and function to class II HDAC6 domain 3 or b (HDAC6b). FB188 HDAH is able to remove the acetyl moiety from acetylated histones, and can be inhibited by common HDAC inhibitors such as SAHA (suberoylanilide hydroxamic acid) as well as class II-specific but not class I specific inhibitors.


Pssm-ID: 212521  Cd Length: 359  Bit Score: 61.42  E-value: 8.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   2 TVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCF 81
Cdd:cd09996  194 TISLHQDRCFPPDSGAVEERGEGAGEGYNLNIPLPPGSGDGAYLHAFERIVLPALRAFRPELIIVASGFDASAFDPLGRM 273
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767903932  82 NLTIKGHAKCVEFVKSF-------NLpmLMLGGGGYTIRNVARCW--TYETAVALDTEIPNelPYNDYFEYFGPD 147
Cdd:cd09996  274 MLTSDGFRALTRKLRDLadelcggRL--VMVHEGGYSEAYVPFCGlaVLEELSGVRTGIAD--PLLYYPEAQGGQ 344
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
3-136 9.78e-11

Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone deacetylase Zn-dependent enzyme that catalyzes hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Clr3 is the homolog of the class-II HDAC HdaI in S. cerevisiae, and is essential for silencing in heterochromatin regions, such as centromeric regions, ribosomal DNA, the mating-type region and telomeric loci. Clr3 has also been implicated in the regulation of stress-related genes; the histone acetyltransferase, Gcn5, in S. cerevisiae, preferentially acetylates global histone H3K14 while Clr3 preferentially deacetylates H3K14ac, and therefore, interplay between Gcn5 and Clr3 is crucial for the regulation of many stress-response genes.


Pssm-ID: 212542  Cd Length: 313  Bit Score: 61.21  E-value: 9.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   3 VSFHKY--GEYFPGT--GDLRDIGAGKGKYYAVNYPLRD-GIDDESYEAIF-KPVMSKVMEmFQPSAVVLQCGSDSLSGD 76
Cdd:cd11600  175 ISLHRFenGGFYPGTpyGDYESVGEGAGLGFNVNIPWPQgGMGDADYIYAFqRIVMPIAYE-FDPDLVIISAGFDAADGD 253
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767903932  77 RLGCFNLTIKGHAKCVEFVKSfnlpmlMLGG-------GGYTIRNVARCwTYETAVALDTEIPNELP 136
Cdd:cd11600  254 ELGQCHVTPAGYAHMTHMLMS------LAGGklvvaleGGYNLDAISDS-ALAVAKVLLGEAPPKLP 313
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
1-91 3.40e-10

Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues of histones (EC 3.5.1.98) to yield deacetylated histones. This subclass includes animal HDAC4, HDAC5, HDAC7, and HDCA9. Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. Class IIa histone deacetylases are signal-dependent co-repressors, they have N-terminal regulatory domain with two or three conserved serine residues, phosphorylation of these residues is important for ability to shuttle between the nucleus and cytoplasm and act as transcriptional co-repressors. HDAC9 is involved in regulation of gene expression and dendritic growth in developing cortical neurons. It also plays a role in hematopoiesis. HDAC7 is involved in regulation of myocyte migration and differentiation. HDAC5 is involved in integration of chronic drug (cocaine) addiction and depression with changes in chromatin structure and gene expression. HDAC4 participates in regulation of chondrocyte hypertrophy and skeletogenesis.


Pssm-ID: 212544  Cd Length: 377  Bit Score: 59.67  E-value: 3.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   1 MTVSFHKY--GEYFPGTGDLRDIGAGKGKYYAVNYPLRDGID----DESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLS 74
Cdd:cd11681  207 LYISLHRYddGNFFPGTGAPTEVGSGAGEGFNVNIAWSGGLDppmgDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAE 286
                         90
                 ....*....|....*....
gi 767903932  75 G--DRLGCFNLTikghAKC 91
Cdd:cd11681  287 GhpPPLGGYKVS----PAC 301
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
3-132 5.27e-10

Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that catalyzes hydrolysis of N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. HDACs usually act via association with DNA binding proteins to target specific chromatin regions. HDAC6 is the only histone deacetylase with internal duplication of two catalytic domains which appear to function independently of each other, and also has a C-terminal ubiquitin-binding domain. It is located in the cytoplasm and associates with microtubule motor complex, functioning as the tubulin deacetylase and regulating microtubule-dependent cell motility. Known interaction partners of HDAC6 are alpha tubulin and ubiquitin-like modifier FAT10 (also known as Ubiquitin D or UBD).


Pssm-ID: 212527  Cd Length: 350  Bit Score: 59.27  E-value: 5.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   3 VSFHKY--GEYFPGT--GDLRDIGAGKGKYYAVNYPL-RDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDR 77
Cdd:cd10003  184 ISLHRYdnGSFFPNSpeGNYDVVGKGKGEGFNVNIPWnKGGMGDAEYIAAFQQVVLPIAYEFNPELVLVSAGFDAARGDP 263
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767903932  78 LGCFNLTIKGHAKCVEFVKSfnlpmlMLGG-------GGYTIRNVARCWTYETAVALDTEIP 132
Cdd:cd10003  264 LGGCKVTPEGYAHMTHMLMS------LAGGrvivileGGYNLTSISESMSMCTKTLLGDPPP 319
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
3-88 1.14e-09

Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. Class IIa histone deacetylases are signal-dependent co-repressors, having N-terminal regulatory domain with two or three conserved serine residues; phosphorylation of these residues is important for ability to shuttle between the nucleus and cytoplasm and act as transcriptional co-repressors. HDAC5 is involved in integration of chronic drug (cocaine) addiction and depression with changes in chromatin structure and gene expression; cocaine regulates HDAC5 function to antagonize the rewarding impact of cocaine, possibly by blocking drug-stimulated gene expression that supports drug-induced behavioral change. It is also involved in regulation of angiogenesis and cell cycle as well as immune system development. HDAC5 and HDAC9 have been found to be significantly up-regulated in high-risk medulloblastoma compared with low-risk and may potentially be novel drug targets.


Pssm-ID: 212531  Cd Length: 420  Bit Score: 58.46  E-value: 1.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   3 VSFHKY--GEYFPGTGDLRDIGAGKGKYYAVNYPLRDGID----DESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGD 76
Cdd:cd10007  212 ISLHRYddGNFFPGSGAPDEVGAGPGVGFNVNIAWTGGVDppigDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGH 291
                         90
                 ....*....|....*.
gi 767903932  77 R--LGCFNLTIK--GH 88
Cdd:cd10007  292 QspLGGYSVTAKcfGH 307
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
1-108 1.50e-09

Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. Class IIa histone deacetylases are signal-dependent co-repressors, having N-terminal regulatory domain with two or three conserved serine residues; phosphorylation of these residues is important for ability to shuttle between the nucleus and cytoplasm and act as transcriptional co-repressors. HDAC4 participates in regulation of chondrocyte hypertrophy and skeletogenesis. However, biological substrates for HDAC4 have not been identified; only low lysine deacetylation activity has been demonstrated and active site mutant has enhanced activity toward acetylated lysines. HDAC4 does not bind DNA directly, but through transcription factors MEF2C (myocyte enhancer factor-2C) and MEF2D. Other known interaction partners of the protein are 14-3-3 proteins, SMRT and N-CoR co-repressors, BCL6, HP1, SUMO-1 ubiquitin-like protein, and ANKRA2. It appears to interact in a multiprotein complex with RbAp48 and HDAC3. Furthermore, HDAC4 is required for TGFbeta1-induced myofibroblastic differentiation.


Pssm-ID: 212530  Cd Length: 409  Bit Score: 58.12  E-value: 1.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   1 MTVSFHKY--GEYFPGTGDLRDIGAGKGKYYAVNYPLRDGID----DESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLS 74
Cdd:cd10006  210 LYMSLHRYddGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDppmgDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVE 289
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767903932  75 GD--RLGCFNLTikghAKCVEFVKSfnlPMLMLGGG 108
Cdd:cd10006  290 GHptPLGGYNLS----AKCFGYLTK---QLMGLAGG 318
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
1-108 7.27e-09

Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. Class IIa histone deacetylases are signal-dependent co-repressors, having N-terminal regulatory domain with two or three conserved serine residues; phosphorylation of these residues is important for ability to shuttle between the nucleus and cytoplasm and act as transcriptional co-repressors. HDAC7 is involved in regulation of myocyte migration and differentiation. Known interaction partners of class IIa HDAC7 are myocyte enhancer factors - MEF2A, -2C, and -2D, 14-3-3 proteins, SMRT and N-CoR co-repressors, HDAC3, ETA (endothelin receptor). This enzyme is also involved in the development of the immune system as well as brain and heart development. Multiple alternatively spliced transcript variants encoding several isoforms have been found for this gene.


Pssm-ID: 212532  Cd Length: 378  Bit Score: 55.79  E-value: 7.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   1 MTVSFHKY--GEYFPGTGDLRDIGAGKGKYYAVNYPLRDGID----DESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLS 74
Cdd:cd10008  208 LYISLHRHddGNFFPGSGAVDEVGAGSGEGFNVNVAWAGGLDppmgDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAE 287
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767903932  75 GD--RLGCFNLTikghAKCVEFVKSfnlPMLMLGGG 108
Cdd:cd10008  288 GHpaPLGGYHVS----AKCFGYMTQ---QLMNLAGG 316
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
1-88 3.84e-08

Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. Class IIa histone deacetylases are signal-dependent co-repressors, they have N-terminal regulatory domain with two or three conserved serine residues, phosphorylation of these residues is important for ability to shuttle between the nucleus and cytoplasm and act as transcriptional co-repressors. HDAC9 is involved in regulation of gene expression and dendritic growth in developing cortical neurons. It also plays a role in hematopoiesis. Its deregulated expression may be associated with some human cancers. HDAC5 and HDAC9 have been found to be significantly up-regulated in high-risk medulloblastoma compared with low-risk and may potentially be novel drug targets.


Pssm-ID: 212533  Cd Length: 379  Bit Score: 53.48  E-value: 3.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   1 MTVSFHKY--GEYFPGTGDLRDIGAGKGKYYAVNYPLRDGID----DESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLS 74
Cdd:cd10009  208 LYISLHRYdeGNFFPGSGAPNEVGTGLGEGYNINIAWTGGLDppmgDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALE 287
                         90
                 ....*....|....*...
gi 767903932  75 GDR--LGCFNLTIK--GH 88
Cdd:cd10009  288 GHTppLGGYKVTAKcfGH 305
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
4-116 1.64e-06

Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. HDACs usually act via association with DNA binding proteins to target specific chromatin regions. HDAC6 is the only histone deacetylase with internal duplication of two catalytic domains which appear to function independently of each other, and also has a C-terminal ubiquitin-binding domain. It is located in the cytoplasm and associates with microtubule motor complex, functioning as the tubulin deacetylase and regulating microtubule-dependent cell motility. Known interaction partners of HDAC6 are alpha tubulin (substrate) and ubiquitin-like modifier FAT10 (also known as Ubiquitin D or UBD).


Pssm-ID: 212545  Cd Length: 337  Bit Score: 48.31  E-value: 1.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   4 SFHKY--GEYFP--GTGDLRDIGAGKGKYYAVNYPL-RDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRL 78
Cdd:cd11682  176 SIHRYeqGRFWPhlKESDSSAVGFGRGEGYNINVPWnQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDAVIGDPK 255
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 767903932  79 GCFNLTIKGHAKCVEFVKSFNLPMLMLG-GGGYTIRNVA 116
Cdd:cd11682  256 GEMAATPACFAHLTHLLMGLAGGKLILSlEGGYNLRSLA 294
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
4-123 7.17e-05

Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. HDACs usually act via association with DNA binding proteins to target specific chromatin regions. HDAC10 has an N-terminal deacetylase domain and a C-terminal pseudo-repeat that shares significant similarity with its catalytic domain. It is located in the nucleus and cytoplasm, and is involved in regulation of melanogenesis. It transcriptionally down-regulates thioredoxin-interacting protein (TXNIP), leading to altered reactive oxygen species (ROS) signaling in human gastric cancer cells. Known interaction partners of HDAC10 are Pax3, KAP1, hsc70 and HDAC3 proteins.


Pssm-ID: 212546  Cd Length: 337  Bit Score: 43.31  E-value: 7.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903932   4 SFHKY--GEYFPG--TGDLRDIGAGKGKYYAVNYPLRD-GIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRL 78
Cdd:cd11683  176 SWHRYehQRFWPFlrESDYDAVGRGKGLGFNINLPWNKvGMGNADYLAAFFHVLLPLAFEFDPELVLVSAGFDSAIGDPE 255
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767903932  79 GCFNLTikghAKCveFVKSFNLPMLMLGG-------GGYTIRNVAR--CWTYET 123
Cdd:cd11683  256 GQMCAT----PEC--FAHLTHLLMVLAGGklcavleGGYHLESLAEsvCMTVQT 303
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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