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Conserved domains on  [gi|1907172212|ref|XP_036021947|]
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histone deacetylase 11 isoform X1 [Mus musculus]

Protein Classification

histone deacetylase( domain architecture ID 10177964)

class IV histone deacetylase catalyzes the hydrolysis of N(6)-acetyl-lysine residues of histones (or other proteins) to yield deacetylated proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 16-197 9.57e-93

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 [Multi-domain]  Cd Length: 275  Bit Score: 272.83  E-value: 9.57e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  16 GGGFHHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNGHERDFMGDKRVYIMDVYNRHIYPGDrfaKE 95
Cdd:cd09993    98 AGGTHHAFPDRGEGFCVFNDIAIAARVLLAE-GLVRRVLIVDLDVHQGNGTAAIFADDPSVFTFSMHGEKNYPFR---KE 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  96 AIRRKVELEWGTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLSISPAGIVKRDEVVFRVVRAHDIPIL 175
Cdd:cd09993   174 PSDLDVPLPDGTGDDEYLAALEEALPRLLAEFRPDLVFYNAGVDVLAGDRLGRLSLSLEGLRERDRLVLRFARARGIPVA 253

                         170       180
                  ....*....|....*....|..
gi 1907172212 176 MVTSGGYQKRTARIIADSILNL 197
Cdd:cd09993   254 MVLGGGYSRDIARLVARHAQTL 275
 
Name Accession Description Interval E-value
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 16-197 9.57e-93

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 [Multi-domain]  Cd Length: 275  Bit Score: 272.83  E-value: 9.57e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  16 GGGFHHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNGHERDFMGDKRVYIMDVYNRHIYPGDrfaKE 95
Cdd:cd09993    98 AGGTHHAFPDRGEGFCVFNDIAIAARVLLAE-GLVRRVLIVDLDVHQGNGTAAIFADDPSVFTFSMHGEKNYPFR---KE 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  96 AIRRKVELEWGTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLSISPAGIVKRDEVVFRVVRAHDIPIL 175
Cdd:cd09993   174 PSDLDVPLPDGTGDDEYLAALEEALPRLLAEFRPDLVFYNAGVDVLAGDRLGRLSLSLEGLRERDRLVLRFARARGIPVA 253

                         170       180
                  ....*....|....*....|..
gi 1907172212 176 MVTSGGYQKRTARIIADSILNL 197
Cdd:cd09993   254 MVLGGGYSRDIARLVARHAQTL 275
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 11-196 5.65e-44

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: 425906 [Multi-domain]  Cd Length: 298  Bit Score: 149.31  E-value: 5.65e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  11 LCRPsggGFHHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNGHERDFMGDKRVYIMDV--YNRHIYP 88
Cdd:pfam00850 106 LVRP---PGHHAERDRASGFCIFNNVAIAAKYLREK-YGLKRVAIVDFDVHHGNGTQEIFYDDPSVLTLSIhqYPGGFYP 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  89 GDRFAKEAIRRK-------VELEWGTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLSISPAGIVKRDE 161
Cdd:pfam00850 182 GTGFADETGEGKgkgytlnVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAGFDAHAGDPLGGLNLTTEGFAEITR 261

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1907172212 162 VVFRVVRAHDIPILMVTSGGYQKRTARIIADSILN 196
Cdd:pfam00850 262 ILLELADPLCIRVVSVLEGGYNLDALARSATAVLA 296
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 11-182 1.29e-42

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 146.02  E-value: 1.29e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  11 LCRPsggGFHHCSSDRGGGFCAYADITLAIKFLfeRVEGISRATIIDLDAHQGNGHERDFMGDKRVYIMDVYNRHIYPGD 90
Cdd:COG0123   117 LVRP---PGHHAERDRAMGFCLFNNAAIAARYL--LAKGLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQDPLYPGT 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  91 RFAKEAIRRK-------VELEWGTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLSISPAGIVKRDEVV 163
Cdd:COG0123   192 GAADETGEGAgegsnlnVPLPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRV 271

                         170
                  ....*....|....*....
gi 1907172212 164 FRVVRAHDIPILMVTSGGY 182
Cdd:COG0123   272 LELADHCGGPVVSVLEGGY 290
PTZ00063 PTZ00063
histone deacetylase; Provisional
 7-200 3.89e-14

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 70.61  E-value: 3.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212   7 HPESLCRPSGGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMGDKRVYIMDVYN-RH 85
Cdd:PTZ00063  124 HQADICVNWSGGLHHAKRSEASGFCYINDIVLGI---LELLKYHARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKfGD 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  86 IYP--GDRFAKEAIRRK-----VELEWGTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLSISpagiVK 158
Cdd:PTZ00063  201 FFPgtGDVTDIGVAQGKyysvnVPLNDGIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLT----IK 276

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907172212 159 RDEVVFRVVRAHDIPILMVTSGGYQKR-TARIIA---DSILNLHDL 200
Cdd:PTZ00063  277 GHAACVEFVRSLNIPLLVLGGGGYTIRnVARCWAyetGVILNKHDE 322
 
Name Accession Description Interval E-value
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 16-197 9.57e-93

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 [Multi-domain]  Cd Length: 275  Bit Score: 272.83  E-value: 9.57e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  16 GGGFHHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNGHERDFMGDKRVYIMDVYNRHIYPGDrfaKE 95
Cdd:cd09993    98 AGGTHHAFPDRGEGFCVFNDIAIAARVLLAE-GLVRRVLIVDLDVHQGNGTAAIFADDPSVFTFSMHGEKNYPFR---KE 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  96 AIRRKVELEWGTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLSISPAGIVKRDEVVFRVVRAHDIPIL 175
Cdd:cd09993   174 PSDLDVPLPDGTGDDEYLAALEEALPRLLAEFRPDLVFYNAGVDVLAGDRLGRLSLSLEGLRERDRLVLRFARARGIPVA 253

                         170       180
                  ....*....|....*....|..
gi 1907172212 176 MVTSGGYQKRTARIIADSILNL 197
Cdd:cd09993   254 MVLGGGYSRDIARLVARHAQTL 275
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
 14-197 5.58e-77

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: 233.10  E-value: 5.58e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  14 PSGGGFHHCSSDRGGGFCAYADITLAIKFLFERveGISRATIIDLDAHQGNGHERDFMGDKRVYIMDVYNRHIYPGDRFA 93
Cdd:cd09301    99 VVGAGGHHAGKSRAWGFCYFNDVVLAIKFLRER--GISRILIIDTDAHHGDGTREAFYDDDRVLHMSFHNYDIYPFGRGK 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  94 KEAIRRKVELEWGTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLSISPAGIVKRDEVVFRVVRahDIP 173
Cdd:cd09301   177 GKGYKINVPLEDGLGDEEYLDAVERVISKVLEEFEPEVVVLQFGHDTHEGDRLGGFNLSEKGFVKLAEIVKEFAR--GGP 254

                         170       180
                  ....*....|....*....|....*
gi 1907172212 174 ILMVTSGGYQ-KRTARIIADSILNL 197
Cdd:cd09301   255 ILMVLGGGYNpEAAARIWTAIIKEL 279
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 11-196 5.65e-44

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: 425906 [Multi-domain]  Cd Length: 298  Bit Score: 149.31  E-value: 5.65e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  11 LCRPsggGFHHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNGHERDFMGDKRVYIMDV--YNRHIYP 88
Cdd:pfam00850 106 LVRP---PGHHAERDRASGFCIFNNVAIAAKYLREK-YGLKRVAIVDFDVHHGNGTQEIFYDDPSVLTLSIhqYPGGFYP 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  89 GDRFAKEAIRRK-------VELEWGTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLSISPAGIVKRDE 161
Cdd:pfam00850 182 GTGFADETGEGKgkgytlnVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAGFDAHAGDPLGGLNLTTEGFAEITR 261

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1907172212 162 VVFRVVRAHDIPILMVTSGGYQKRTARIIADSILN 196
Cdd:pfam00850 262 ILLELADPLCIRVVSVLEGGYNLDALARSATAVLA 296
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 11-182 1.29e-42

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 146.02  E-value: 1.29e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  11 LCRPsggGFHHCSSDRGGGFCAYADITLAIKFLfeRVEGISRATIIDLDAHQGNGHERDFMGDKRVYIMDVYNRHIYPGD 90
Cdd:COG0123   117 LVRP---PGHHAERDRAMGFCLFNNAAIAARYL--LAKGLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQDPLYPGT 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  91 RFAKEAIRRK-------VELEWGTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLSISPAGIVKRDEVV 163
Cdd:COG0123   192 GAADETGEGAgegsnlnVPLPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRV 271

                         170
                  ....*....|....*....
gi 1907172212 164 FRVVRAHDIPILMVTSGGY 182
Cdd:COG0123   272 LELADHCGGPVVSVLEGGY 290
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
 16-189 8.62e-28

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 [Multi-domain]  Cd Length: 313  Bit Score: 107.26  E-value: 8.62e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  16 GGGFHHCSSDRGGGFCAYADITLAIKFLFERveGISRATIIDLDAHQGNGHERDFMGDKRVYIMDV--YNRHIYPGDRFA 93
Cdd:cd09994   123 AGGLHHAMRGRASGFCVYNDAAVAIERLRDK--GGLRVAYVDIDAHHGDGVQAAFYDDPRVLTISLheSGRYLFPGTGFV 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  94 KEAIRRK-------VELEWGTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLSISPAGIVKrdevVFRV 166
Cdd:cd09994   201 DEIGEGEgygyavnIPLPPGTGDDEFLRAFEAVVPPLLRAFRPDVIVSQHGADAHAGDPLTHLNLSNRAYRA----AVRR 276

                         170       180
                  ....*....|....*....|....*....
gi 1907172212 167 VR--AHDI---PILMVTSGGYQKR-TARI 189
Cdd:cd09994   277 IRelADEYcggRWLALGGGGYNPDvVARA 305
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
 10-182 5.76e-21

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 [Multi-domain]  Cd Length: 298  Bit Score: 88.75  E-value: 5.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  10 SLCRPSGggfHHCSSDRGGGFCAYADITLAIKFLFERVEgisRATIIDLDAHQGNGHERDFMGDKRVYIMDV--YNRHIY 87
Cdd:cd10001   110 ALCRPPG---HHAGRDRAGGFCYFNNAAIAAQYLRDRAG---RVAILDVDVHHGNGTQEIFYERPDVLYVSIhgDPRTFY 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  88 PG------DRFAKEAIRRKVE--LEWGTEDEEYLEKVERNVRRsLQEHLPDVVVYNAGTDVLEGDRLGGLSISPAGIVKr 159
Cdd:cd10001   184 PFflgfadETGEGEGEGYNLNlpLPPGTGDDDYLAALDEALAA-IAAFGPDALVVSLGFDTHEGDPLSDFKLTTEDYAR- 261

                         170       180
                  ....*....|....*....|...
gi 1907172212 160 devVFRVVRAHDIPILMVTSGGY 182
Cdd:cd10001   262 ---IGRRIAALGLPTVFVQEGGY 281
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
 11-182 2.75e-20

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 [Multi-domain]  Cd Length: 291  Bit Score: 86.78  E-value: 2.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  11 LCRPSGggfHHCSSDRGGGFCAYADITLAIKFLFERVeGISRATIIDLDAHQGNGHERDFMGDKRVYIMDVYNRHIYPGD 90
Cdd:cd09992    99 LVRPPG---HHAEPDRAMGFCLFNNVAIAARYAQKRY-GLKRVLIVDWDVHHGNGTQDIFYDDPSVLYFSIHQYPFYPGT 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  91 RFAKEAIRRK-------VELEWGTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLSISPAG---IVKRd 160
Cdd:cd09992   175 GAAEETGGGAgegftinVPLPPGSGDAEYLAAFEEVLLPIAREFQPDLVLVSAGFDAHRGDPLGGMNLTPEGyarLTRL- 253

                         170       180
                  ....*....|....*....|..
gi 1907172212 161 eVVFRVVRAHDIPILMVTSGGY 182
Cdd:cd09992   254 -LKELADEHCGGRLVFVLEGGY 274
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
 16-188 3.67e-20

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 [Multi-domain]  Cd Length: 306  Bit Score: 86.48  E-value: 3.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  16 GGGFHHCSSDRGGGFCAYADITLAIKFL---FERVegisraTIIDLDAHQGNGHERDFMGDKRVyiMDVyNRHIYPGDRF 92
Cdd:cd09991   123 AGGLHHAKKSEASGFCYVNDIVLAILELlkyHQRV------LYIDIDIHHGDGVEEAFYTTDRV--MTV-SFHKFGEYFF 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  93 AKEAIR----RK-------VELEWGTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLSISPAGIVKrde 161
Cdd:cd09991   194 PGTGLRdigaGKgkyyavnVPLKDGIDDESYLQIFEPVLSKVMEVFQPSAVVLQCGADSLAGDRLGCFNLSIKGHAK--- 270

                         170       180
                  ....*....|....*....|....*...
gi 1907172212 162 vVFRVVRAHDIPILMVTSGGYQKR-TAR 188
Cdd:cd09991   271 -CVKFVKSFNIPLLVLGGGGYTLRnVAR 297
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 17-182 5.32e-20

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 [Multi-domain]  Cd Length: 364  Bit Score: 87.01  E-value: 5.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  17 GGFHHCSSDRGGGFCAYADITLAIKFLFERVEgisRATIIDLDAHQGNGHERDFMGDKRVYI--MDVYNRHIYPGDRFAK 94
Cdd:cd10000   126 GGWHHAQRDEASGFCYVNDIVLGILKLREKFD---RVLYVDLDLHHGDGVEDAFSFTSKVMTvsLHKYSPGFFPGTGDVS 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  95 EAIRRK-------VELEWGTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLSISPAGIVKrdevVFRVV 167
Cdd:cd10000   203 DVGLGKgkyytvnVPLRDGIQDEQYLQIFTAVVPEIVAAFRPEAVVLQCGADTLAGDPMGAFNLTPVGIGK----CLKYV 278

                         170
                  ....*....|....*
gi 1907172212 168 RAHDIPILMVTSGGY 182
Cdd:cd10000   279 LGWKLPTLILGGGGY 293
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
 17-182 4.03e-18

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 [Multi-domain]  Cd Length: 294  Bit Score: 80.77  E-value: 4.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  17 GGFHHCSSDRGGGFCAYADITLAIKFLfeRVEGISRATIIDLDAHQGNGHERDFMGDKRVYIMDV--YNRHIYPGDRFAK 94
Cdd:cd11680   112 GGRHHAQKSRASGFCYVNDIVLAILRL--RRARFRRVFYLDLDLHHGDGVESAFFFSKNVLTCSIhrYDPGFFPGTGSLK 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  95 EAIRRK---VELEWGTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLG--GLSISPAGIVkrdeVVFRVVRA 169
Cdd:cd11680   190 NSSDKGmlnIPLKRGLSDKTLLRIIDSIVRPLIEKFEPEVIVIQCGCDGLSGDPHKewNLTIRGYGSV----IELLLKEF 265

                         170
                  ....*....|...
gi 1907172212 170 HDIPILMVTSGGY 182
Cdd:cd11680   266 KDKPTLLLGGGGY 278
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
 16-185 2.74e-17

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 [Multi-domain]  Cd Length: 311  Bit Score: 78.65  E-value: 2.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  16 GGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMGDKRVYIMDV--YNRHIYPG---- 89
Cdd:cd11598   127 SGGLHHAKKSEASGFCYVNDIVLAI---LNLLRYFPRVLYIDIDVHHGDGVEEAFYRTDRVMTLSFhkYNGEFFPGtgdl 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  90 -----DRFAKEAIrrKVELEWGTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLSISpagiVKRDEVVF 164
Cdd:cd11598   204 ddnggTPGKHFAL--NVPLEDGIDDEQYNLLFKSIIGPTIEKFQPSAIVLQCGADSLGGDRLGQFNLN----IKAHGACV 277

                         170       180
                  ....*....|....*....|.
gi 1907172212 165 RVVRAHDIPILMVTSGGYQKR 185
Cdd:cd11598   278 KFVKSFGIPMLVVGGGGYTPR 298
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
 16-185 8.73e-17

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 [Multi-domain]  Cd Length: 366  Bit Score: 77.80  E-value: 8.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  16 GGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMGDKRVY-IMDVYNRHIYPG----- 89
Cdd:cd10011   129 AGGLHHAKKSEASGFCYVNDIVLAI---LELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMtVSFHKYGEYFPGtgdlr 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  90 DRFAKEAIRRKVELEW--GTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLSISPAGIVKRDEvvfrVV 167
Cdd:cd10011   206 DIGAGKGKYYAVNFPMrdGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVE----VV 281

                         170
                  ....*....|....*...
gi 1907172212 168 RAHDIPILMVTSGGYQKR 185
Cdd:cd10011   282 KTFNLPLLMLGGGGYTIR 299
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 13-155 9.17e-16

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 [Multi-domain]  Cd Length: 313  Bit Score: 74.30  E-value: 9.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  13 RPSGggfHHCSSDRGGGFCAYADITLAIKFL-FERVEGISRATIIDLDAHQGNGHERDFMGDKRVYIMDVY---NRHIYP 88
Cdd:cd11600   111 RPPG---HHAEPDESMGFCFFNNVAVAAKWLqTEYPDKIKKILILDWDIHHGNGTQRAFYDDPNVLYISLHrfeNGGFYP 187

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907172212  89 GDRFAK-------EAIRRKVELEW---GTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLSISPAG 155
Cdd:cd11600   188 GTPYGDyesvgegAGLGFNVNIPWpqgGMGDADYIYAFQRIVMPIAYEFDPDLVIISAGFDAADGDELGQCHVTPAG 264
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
 10-139 9.75e-16

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 [Multi-domain]  Cd Length: 359  Bit Score: 74.90  E-value: 9.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  10 SLCRPSGggfHHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNGHERDFMGDKRVYIMDVYNRHIYPG 89
Cdd:cd09996   130 ALVRPPG---HHAEPDQGMGFCLFNNVAIAARHALAV-GGVKRVAVVDWDVHHGNGTQAIFYDDPDVLTISLHQDRCFPP 205

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907172212  90 DRFAKEAIRR--------KVELEWGTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTD 139
Cdd:cd09996   206 DSGAVEERGEgagegynlNIPLPPGSGDGAYLHAFERIVLPALRAFRPELIIVASGFD 263
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
 17-185 4.42e-15

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 [Multi-domain]  Cd Length: 371  Bit Score: 73.18  E-value: 4.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  17 GGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMGDKRVYIMDVYNR-HIYPG-----D 90
Cdd:cd10010   134 GGLHHAKKSEASGFCYVNDIVLAI---LELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYgEYFPGtgdlrD 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  91 RFAKEAIRRKVE--LEWGTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLSISPAGIVKRDEvvfrVVR 168
Cdd:cd10010   211 IGAGKGKYYAVNypLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVE----FVK 286

                         170
                  ....*....|....*..
gi 1907172212 169 AHDIPILMVTSGGYQKR 185
Cdd:cd10010   287 SFNLPMLMLGGGGYTIR 303
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
 17-185 8.79e-15

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: 72.04  E-value: 8.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  17 GGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMGDKRVyiMDV----YNRHIYP--GD 90
Cdd:cd10005   129 GGLHHAKKFEASGFCYVNDIVIAI---LELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRV--MTVsfhkYGNYFFPgtGD 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  91 RFAKEAIRRK-----VELEWGTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLSISPAGivkRDEVVfR 165
Cdd:cd10005   204 MYEVGAESGRyysvnVPLKDGIDDQSYLQLFKPVIQQVIDFYQPTCIVLQCGADSLGCDRLGCFNLSIKG---HGECV-E 279

                         170       180
                  ....*....|....*....|
gi 1907172212 166 VVRAHDIPILMVTSGGYQKR 185
Cdd:cd10005   280 FVKSFNIPLLVLGGGGYTVR 299
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
 12-150 2.86e-14

Histone deacetylases and histone-like deacetylases, classII; This subfamily includes eukaryotic as well as bacterial 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. In D. discoideum, where four homologs (HdaA, HdaB, HdaC, HdaD) have been identified, HDAC activity is important for regulating the timing of gene expression during development. Also, inhibition of HDAC activity by trichostatin A is shown to cause hyperacetylation of the histone and a delay in cell aggregation and differentiation.


Pssm-ID: 212541 [Multi-domain]  Cd Length: 288  Bit Score: 69.85  E-value: 2.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  12 CRPSGggfHHCSSDRGGGFCAYADITLAIKFLFERVeGISRATIIDLDAHQGNGHERDFMGDKRVYIMDVYNRHIYPGDR 91
Cdd:cd11599   101 VRPPG---HHAERDKAMGFCLFNNVAIAAAHALAHH-GLERVAIVDFDVHHGNGTEDIFRDDPRVLFCSSHQHPLYPGTG 176

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907172212  92 FAKEAIR---RKVELEWGTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLS 150
Cdd:cd11599   177 APDETGHgniVNVPLPAGTGGAEFREAVEDRWLPALDAFKPDLILISAGFDAHRDDPLAQLN 238
PTZ00063 PTZ00063
histone deacetylase; Provisional
 7-200 3.89e-14

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 70.61  E-value: 3.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212   7 HPESLCRPSGGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMGDKRVYIMDVYN-RH 85
Cdd:PTZ00063  124 HQADICVNWSGGLHHAKRSEASGFCYINDIVLGI---LELLKYHARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKfGD 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  86 IYP--GDRFAKEAIRRK-----VELEWGTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLSISpagiVK 158
Cdd:PTZ00063  201 FFPgtGDVTDIGVAQGKyysvnVPLNDGIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLT----IK 276

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907172212 159 RDEVVFRVVRAHDIPILMVTSGGYQKR-TARIIA---DSILNLHDL 200
Cdd:PTZ00063  277 GHAACVEFVRSLNIPLLVLGGGGYTIRnVARCWAyetGVILNKHDE 322
PTZ00346 PTZ00346
histone deacetylase; Provisional
 16-200 6.41e-14

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 70.06  E-value: 6.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  16 GGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMGDKRVYIMDV--YNRHIYPGDRFA 93
Cdd:PTZ00346  150 GGGMHHSKCGECSGFCYVNDIVLGI---LELLKCHDRVLYVDIDMHHGDGVDEAFCTSDRVFTLSLhkFGESFFPGTGHP 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  94 KEA-------IRRKVELEWGTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLSISPAGIVKrdevVFRV 166
Cdd:PTZ00346  227 RDVgygrgryYSMNLAVWDGITDFYYLGLFEHALHSIVRRYSPDAIVLQCGADSLAGDRLGLLNLSSFGHGQ----CVQA 302

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907172212 167 VRAHDIPILMVTSGGYQKR-TARIIA--DSILNLHDL 200
Cdd:PTZ00346  303 VRDLGIPMLALGGGGYTIRnVAKLWAyeTSILTGHPL 339
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
 10-152 2.09e-13

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 [Multi-domain]  Cd Length: 420  Bit Score: 68.48  E-value: 2.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  10 SLCRPSGggfHHCSSDRGGGFCAYADITLAIKFLFERVeGISRATIIDLDAHQGNGHERDFMGDKRVYIMDVY---NRHI 86
Cdd:cd10007   147 AVIRPPG---HHAEESTAMGFCFFNSVAIAAKLLQQKL-NVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHrydDGNF 222

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907172212  87 YPGDRFAKE-----AIRRKVELEW--GTE----DEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDR--LGGLSIS 152
Cdd:cd10007   223 FPGSGAPDEvgagpGVGFNVNIAWtgGVDppigDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGHQspLGGYSVT 301
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
 17-185 3.25e-13

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 [Multi-domain]  Cd Length: 375  Bit Score: 67.53  E-value: 3.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  17 GGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMGDKRVYIMDVYNR-HIYPGDRFAKE 95
Cdd:cd10004   130 GGLHHAKKSEASGFCYVNDIVLGI---LELLRYHQRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYgEYFPGTGELRD 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  96 ---------AIrrKVELEWGTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLSISPAGivkrDEVVFRV 166
Cdd:cd10004   207 igigtgknyAV--NVPLRDGIDDESYKSIFEPVIKHVMEWYQPEAVVLQCGGDSLSGDRLGCFNLSMKG----HANCVNF 280

                         170
                  ....*....|....*....
gi 1907172212 167 VRAHDIPILMVTSGGYQKR 185
Cdd:cd10004   281 VKSFNLPMLVLGGGGYTMR 299
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
 13-155 3.19e-12

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 [Multi-domain]  Cd Length: 350  Bit Score: 64.67  E-value: 3.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  13 RPSGggfHHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNGHERDFMGDKRV-YI-MDVY-NRHIYPG 89
Cdd:cd10003   122 RPPG---HHAEQDTACGFCFFNNVAIAARYAQKK-YGLKRILIVDWDVHHGNGTQHMFESDPSVlYIsLHRYdNGSFFPN 197

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907172212  90 DRFAKEAIRRK-------VELEW---GTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLSISPAG 155
Cdd:cd10003   198 SPEGNYDVVGKgkgegfnVNIPWnkgGMGDAEYIAAFQQVVLPIAYEFNPELVLVSAGFDAARGDPLGGCKVTPEG 273
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
 10-152 5.35e-12

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 [Multi-domain]  Cd Length: 409  Bit Score: 64.29  E-value: 5.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  10 SLCRPSGggfHHCSSDRGGGFCAYADITLAIKFLFERVEgISRATIIDLDAHQGNGHERDFMGDKRVYIMDVY---NRHI 86
Cdd:cd10006   147 AVVRPPG---HHAEESTPMGFCYFNSVAIAAKLLQQRLN-VSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHrydDGNF 222

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907172212  87 YPGDRFAKE-----AIRRKVELEW--GTE----DEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGD--RLGGLSIS 152
Cdd:cd10006   223 FPGSGAPDEvgtgpGVGFNVNMAFtgGLDppmgDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHptPLGGYNLS 301
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
 10-152 1.49e-11

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 [Multi-domain]  Cd Length: 378  Bit Score: 62.72  E-value: 1.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  10 SLCRPSGggfHHCSSDRGGGFCAYADITLAIKFLFERVEgISRATIIDLDAHQGNGHERDFMGDKRVYIMDVYnRH---- 85
Cdd:cd10008   145 AVVRPPG---HHADHSTAMGFCFFNSVAIACRQLQQQGK-ASKILIVDWDVHHGNGTQQTFYQDPSVLYISLH-RHddgn 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  86 IYPGDRFAKEAIRR-----KVELEW--GTE----DEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGD--RLGGLSIS 152
Cdd:cd10008   220 FFPGSGAVDEVGAGsgegfNVNVAWagGLDppmgDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHpaPLGGYHVS 299
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
 10-152 4.75e-11

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 [Multi-domain]  Cd Length: 379  Bit Score: 61.57  E-value: 4.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  10 SLCRPSGggfHHCSSDRGGGFCAYADITLAIKFLFERVEgISRATIIDLDAHQGNGHERDFMGDKRVYIMDVYNR---HI 86
Cdd:cd10009   145 AVVRPPG---HHAEESTAMGFCFFNSVAITAKYLRDQLN-ISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdegNF 220

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907172212  87 YPGDRFAKEAIR-----RKVELEW--GTE----DEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDR--LGGLSIS 152
Cdd:cd10009   221 FPGSGAPNEVGTglgegYNINIAWtgGLDppmgDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTppLGGYKVT 299
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 11-154 3.69e-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 [Multi-domain]  Cd Length: 377  Bit Score: 58.90  E-value: 3.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  11 LCRPSGggfHHCSSDRGGGFCAYADITLAIKFLFERVeGISRATIIDLDAHQGNGHERDFMGDKRVYIMDVYnRH----I 86
Cdd:cd11681   145 VVRPPG---HHAEPSQAMGFCFFNSVAIAAKQLQQKL-KLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLH-RYddgnF 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  87 YPGDRFAKE-----AIRRKVELEW------GTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEG--DRLGGLSISP 153
Cdd:cd11681   220 FPGTGAPTEvgsgaGEGFNVNIAWsggldpPMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGhpPPLGGYKVSP 299


                  .
gi 1907172212 154 A 154
Cdd:cd11681   300 A 300
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
 10-224 4.76e-10

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 [Multi-domain]  Cd Length: 337  Bit Score: 58.32  E-value: 4.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  10 SLCRPSGggfHHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNGHERDFMGDKRVYIMDVynrHIYPG 89
Cdd:cd11682   110 AIVRPPG---HHAQHDKMDGYCMFNNVAIAARYAQQK-HGVQRVLIVDWDVHHGQGTQFIFEQDPSVLYFSI---HRYEQ 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  90 DRF---AKEAI----------RRKVELEW---GTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLSISP 153
Cdd:cd11682   183 GRFwphLKESDssavgfgrgeGYNINVPWnqvGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDAVIGDPKGEMAATP 262

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907172212 154 AGIVKRDEVVFRVVRAHdipILMVTSGGYQKR-TARIIADSILNLhdLG-----LIGPEFPCVSAQNSgiplLSCAV 224
Cdd:cd11682   263 ACFAHLTHLLMGLAGGK---LILSLEGGYNLRsLAEGVCASLKAL--LGdpcpmLESPGAPCRSALAS----VSCTI 330
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 11-181 8.50e-08

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 [Multi-domain]  Cd Length: 336  Bit Score: 51.54  E-value: 8.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  11 LCRPSGggfHHCSSDRGGGFCAYADITLAIKFLFErVEGISRATIIDLDAHQGNGHERDFMGDKRVyimDVYNRHIYPGD 90
Cdd:cd10002   111 LIRPPG---HHAMRNEANGYCIFNNVAIAAKYAIE-KLGLKRILIVDWDVHHGQGTQQGFYEDPRV---LYFSIHRYEHG 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  91 RF-------------AKEAIRRKVELEWGTE---DEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLSISPA 154
Cdd:cd10002   184 RFwphlfesdydyigVGHGYGFNVNVPLNQTglgDADYLAIFHHILLPLALEFQPELVLVSAGFDASIGDPEGEMAVTPA 263

                         170       180
                  ....*....|....*....|....*..
gi 1907172212 155 GIvkrdevvfrvvrAHDIPILMVTSGG 181
Cdd:cd10002   264 GY------------AHLTRLLMGLAGG 278
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
 13-65 1.28e-05

Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from Saccharomyces cerevisiae is a Zn-dependent enzyme belonging to HDAC class II. It 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. Hos3 deacetylase is homodimer, in vitro it shows specificity to H4, H3 and H2A.


Pssm-ID: 212522 [Multi-domain]  Cd Length: 353  Bit Score: 45.14  E-value: 1.28e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907172212  13 RPSGggfHHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNG 65
Cdd:cd09998   116 RPPG---HHCSESTPSGFCWVNNVHVGAAHAYLT-HGITRVVILDIDLHHGNG 164
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 10-215 4.19e-04

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 [Multi-domain]  Cd Length: 337  Bit Score: 40.62  E-value: 4.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  10 SLCRPSGggfHHCSSDRGGGFCAYADITLAIKFLfERVEGISRATIIDLDAHQGNGHERDFMGDKRVYimdVYNRHIYPG 89
Cdd:cd11683   110 ALVRPPG---HHSQRNAANGFCVFNNVAIAAEYA-KKKYGLHRILIVDWDVHHGQGIQYIFEEDPSVL---YFSWHRYEH 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172212  90 DRF-------AKEAIRR------KVELEW---GTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLSISP 153
Cdd:cd11683   183 QRFwpflresDYDAVGRgkglgfNINLPWnkvGMGNADYLAAFFHVLLPLAFEFDPELVLVSAGFDSAIGDPEGQMCATP 262

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907172212 154 AgivkrdevvfrvVRAHDIPILM---------VTSGGYQKRTariIADSI-LNLHDL------GLIGPEFPCVSAQNS 215
Cdd:cd11683   263 E------------CFAHLTHLLMvlaggklcaVLEGGYHLES---LAESVcMTVQTLlgdplpRLSGEMTPCQSALES 325
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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