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Conserved domains on  [gi|1622899648|ref|XP_028698897|]
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histone deacetylase 11 isoform X5 [Macaca mulatta]

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 ...
7-252 5.59e-123

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: 351.80  E-value: 5.59e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648   7 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELK------------------------------ 56
Cdd:cd09993     1 HRFPMRKYGLLREALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLESLKsgelsreeirrigfpwspelvertrlavgg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  57 ---AGKLAVERGWAINVGGGFHHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNGHERDFMDDKRVYI 133
Cdd:cd09993    81 tilAARLALEHGLAINLAGGTHHAFPDRGEGFCVFNDIAIAARVLLAE-GLVRRVLIVDLDVHQGNGTAAIFADDPSVFT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 134 MDVYNRHIYPGDrfaKQAIRRKVELEWGTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVK 213
Cdd:cd09993   160 FSMHGEKNYPFR---KEPSDLDVPLPDGTGDDEYLAALEEALPRLLAEFRPDLVFYNAGVDVLAGDRLGRLSLSLEGLRE 236
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1622899648 214 RDELVFRMVRGRHVPILMVTSGGYQKRTARIIADSILNL 252
Cdd:cd09993   237 RDRLVLRFARARGIPVAMVLGGGYSRDIARLVARHAQTL 275
 
Name Accession Description Interval E-value
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
7-252 5.59e-123

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: 351.80  E-value: 5.59e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648   7 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELK------------------------------ 56
Cdd:cd09993     1 HRFPMRKYGLLREALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLESLKsgelsreeirrigfpwspelvertrlavgg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  57 ---AGKLAVERGWAINVGGGFHHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNGHERDFMDDKRVYI 133
Cdd:cd09993    81 tilAARLALEHGLAINLAGGTHHAFPDRGEGFCVFNDIAIAARVLLAE-GLVRRVLIVDLDVHQGNGTAAIFADDPSVFT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 134 MDVYNRHIYPGDrfaKQAIRRKVELEWGTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVK 213
Cdd:cd09993   160 FSMHGEKNYPFR---KEPSDLDVPLPDGTGDDEYLAALEEALPRLLAEFRPDLVFYNAGVDVLAGDRLGRLSLSLEGLRE 236
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1622899648 214 RDELVFRMVRGRHVPILMVTSGGYQKRTARIIADSILNL 252
Cdd:cd09993   237 RDRLVLRFARARGIPVAMVLGGGYSRDIARLVARHAQTL 275
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
7-253 8.40e-57

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: 184.36  E-value: 8.40e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648   7 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELK-----------------------------A 57
Cdd:pfam00850   1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEeaapeggallllsylsgdddtpvspgsyeA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  58 GKLAV---------------ERGWAINVGGGfHHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNGHE 122
Cdd:pfam00850  81 ALLAAggtlaaadavlsgeaRNAFALVRPPG-HHAERDRASGFCIFNNVAIAAKYLREK-YGLKRVAIVDFDVHHGNGTQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 123 RDFMDDKRVYIMDV--YNRHIYPGDRFAKQAIRRK-------VELEWGTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGT 193
Cdd:pfam00850 159 EIFYDDPSVLTLSIhqYPGGFYPGTGFADETGEGKgkgytlnVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAGF 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 194 DILEGDRLGGLSISPAGIVKRDELVFRMVRGRHVPILMVTSGGYqkrTARIIADSILNLF 253
Cdd:pfam00850 239 DAHAGDPLGGLNLTTEGFAEITRILLELADPLCIRVVSVLEGGY---NLDALARSATAVL 295
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
7-253 1.99e-54

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 178.38  E-value: 1.99e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648   7 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKAGKLAVERGW-------------------- 66
Cdd:COG0123    18 HPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAASLDGGYGQldpdtpvspgtweaallaag 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  67 -AI----------------NVGGGFHHCSSDRGGGFCAYADITLAIKFLfeRVEGISRATIIDLDAHQGNGHERDFMDDK 129
Cdd:COG0123    98 gALaaadavlegearnafaLVRPPGHHAERDRAMGFCLFNNAAIAARYL--LAKGLERVAIVDFDVHHGNGTQDIFYDDP 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 130 RVYIMDVYNRHIYPGDRFAKQAIRRK-------VELEWGTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLG 202
Cdd:COG0123   176 DVLTISIHQDPLYPGTGAADETGEGAgegsnlnVPLPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHADDPLG 255
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622899648 203 GLSISPAGIVKRDELVFRMVRGRHVPILMVTSGGYQKRTARIIADSILNLF 253
Cdd:COG0123   256 RLNLTTEGYAWRTRRVLELADHCGGPVVSVLEGGYNLDALARSVAAHLETL 306
PTZ00063 PTZ00063
histone deacetylase; Provisional
68-240 4.79e-15

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 74.46  E-value: 4.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  68 INVGGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYN-RHIYPG-- 144
Cdd:PTZ00063  130 VNWSGGLHHAKRSEASGFCYINDIVLGI---LELLKYHARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKfGDFFPGtg 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 145 ---DRFAKQA--IRRKVELEWGTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLGGLSISpagiVKRDELVF 219
Cdd:PTZ00063  207 dvtDIGVAQGkyYSVNVPLNDGIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLT----IKGHAACV 282
                         170       180
                  ....*....|....*....|.
gi 1622899648 220 RMVRGRHVPILMVTSGGYQKR 240
Cdd:PTZ00063  283 EFVRSLNIPLLVLGGGGYTIR 303
 
Name Accession Description Interval E-value
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
7-252 5.59e-123

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: 351.80  E-value: 5.59e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648   7 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELK------------------------------ 56
Cdd:cd09993     1 HRFPMRKYGLLREALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLESLKsgelsreeirrigfpwspelvertrlavgg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  57 ---AGKLAVERGWAINVGGGFHHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNGHERDFMDDKRVYI 133
Cdd:cd09993    81 tilAARLALEHGLAINLAGGTHHAFPDRGEGFCVFNDIAIAARVLLAE-GLVRRVLIVDLDVHQGNGTAAIFADDPSVFT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 134 MDVYNRHIYPGDrfaKQAIRRKVELEWGTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVK 213
Cdd:cd09993   160 FSMHGEKNYPFR---KEPSDLDVPLPDGTGDDEYLAALEEALPRLLAEFRPDLVFYNAGVDVLAGDRLGRLSLSLEGLRE 236
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1622899648 214 RDELVFRMVRGRHVPILMVTSGGYQKRTARIIADSILNL 252
Cdd:cd09993   237 RDRLVLRFARARGIPVAMVLGGGYSRDIARLVARHAQTL 275
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
13-252 2.20e-98

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: 289.72  E-value: 2.20e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  13 KWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELK------------------------------------ 56
Cdd:cd09301     1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKanfavatiteskpvifgpnfpvqrhyfrgarlstgg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  57 ---AGKLAVE----RGWAInVGGGFHHCSSDRGGGFCAYADITLAIKFLFERveGISRATIIDLDAHQGNGHERDFMDDK 129
Cdd:cd09301    81 vveAAELVAKgeleRAFAV-VGAGGHHAGKSRAWGFCYFNDVVLAIKFLRER--GISRILIIDTDAHHGDGTREAFYDDD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 130 RVYIMDVYNRHIYPGDRFAKQAIRRKVELEWGTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPA 209
Cdd:cd09301   158 RVLHMSFHNYDIYPFGRGKGKGYKINVPLEDGLGDEEYLDAVERVISKVLEEFEPEVVVLQFGHDTHEGDRLGGFNLSEK 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1622899648 210 GIVKRDELVFRMVRGrhVPILMVTSGGYQ-KRTARIIADSILNL 252
Cdd:cd09301   238 GFVKLAEIVKEFARG--GPILMVLGGGYNpEAAARIWTAIIKEL 279
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
7-253 8.40e-57

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: 184.36  E-value: 8.40e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648   7 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELK-----------------------------A 57
Cdd:pfam00850   1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEeaapeggallllsylsgdddtpvspgsyeA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  58 GKLAV---------------ERGWAINVGGGfHHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNGHE 122
Cdd:pfam00850  81 ALLAAggtlaaadavlsgeaRNAFALVRPPG-HHAERDRASGFCIFNNVAIAAKYLREK-YGLKRVAIVDFDVHHGNGTQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 123 RDFMDDKRVYIMDV--YNRHIYPGDRFAKQAIRRK-------VELEWGTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGT 193
Cdd:pfam00850 159 EIFYDDPSVLTLSIhqYPGGFYPGTGFADETGEGKgkgytlnVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAGF 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 194 DILEGDRLGGLSISPAGIVKRDELVFRMVRGRHVPILMVTSGGYqkrTARIIADSILNLF 253
Cdd:pfam00850 239 DAHAGDPLGGLNLTTEGFAEITRILLELADPLCIRVVSVLEGGY---NLDALARSATAVL 295
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
7-253 1.99e-54

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 178.38  E-value: 1.99e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648   7 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKAGKLAVERGW-------------------- 66
Cdd:COG0123    18 HPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAASLDGGYGQldpdtpvspgtweaallaag 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  67 -AI----------------NVGGGFHHCSSDRGGGFCAYADITLAIKFLfeRVEGISRATIIDLDAHQGNGHERDFMDDK 129
Cdd:COG0123    98 gALaaadavlegearnafaLVRPPGHHAERDRAMGFCLFNNAAIAARYL--LAKGLERVAIVDFDVHHGNGTQDIFYDDP 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 130 RVYIMDVYNRHIYPGDRFAKQAIRRK-------VELEWGTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLG 202
Cdd:COG0123   176 DVLTISIHQDPLYPGTGAADETGEGAgegsnlnVPLPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHADDPLG 255
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622899648 203 GLSISPAGIVKRDELVFRMVRGRHVPILMVTSGGYQKRTARIIADSILNLF 253
Cdd:COG0123   256 RLNLTTEGYAWRTRRVLELADHCGGPVVSVLEGGYNLDALARSVAAHLETL 306
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
7-244 1.82e-35

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: 129.22  E-value: 1.82e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648   7 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKA---------------GK------------ 59
Cdd:cd09994    17 HPFNPPRLSLTKDLLRALGLLPPVDLVPPRPATEEELLLFHTPDYIEAVKEasrgqepegrgrlglGTednpvfpgmhea 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  60 ---------LAVERGW------AINVGGGFHHCSSDRGGGFCAYADITLAIKFLFERveGISRATIIDLDAHQGNGHERD 124
Cdd:cd09994    97 aalvvggtlLAARLVLegearrAFNPAGGLHHAMRGRASGFCVYNDAAVAIERLRDK--GGLRVAYVDIDAHHGDGVQAA 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 125 FMDDKRVYIMDV--YNRHIYPGDRFAKQAIRRK-------VELEWGTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDI 195
Cdd:cd09994   175 FYDDPRVLTISLheSGRYLFPGTGFVDEIGEGEgygyavnIPLPPGTGDDEFLRAFEAVVPPLLRAFRPDVIVSQHGADA 254
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622899648 196 LEGDRLGGLSISPAGIVKrdelVFRMVR--------GRhvpILMVTSGGYQKR-TARI 244
Cdd:cd09994   255 HAGDPLTHLNLSNRAYRA----AVRRIReladeycgGR---WLALGGGGYNPDvVARA 305
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
26-237 2.70e-23

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: 97.41  E-value: 2.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  26 LLSDSMLVEAREASEEDLLVVHTRRYLNELKAG----------KLAVERGW----------------------------- 66
Cdd:cd10000    35 LLKQLRVVKPRVATEEELASFHSDEYIQFLKKAsnegdndeepSEQQEFGLgydcpifegiydyaaavagatltaaqlli 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  67 ------AINVGGGFHHCSSDRGGGFCAYADITLAIKFLFERVEgisRATIIDLDAHQGNGHERDFMDDKRVYI--MDVYN 138
Cdd:cd10000   115 dgkckvAINWFGGWHHAQRDEASGFCYVNDIVLGILKLREKFD---RVLYVDLDLHHGDGVEDAFSFTSKVMTvsLHKYS 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 139 RHIYPGDRFAKQAIRRK-------VELEWGTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGI 211
Cdd:cd10000   192 PGFFPGTGDVSDVGLGKgkyytvnVPLRDGIQDEQYLQIFTAVVPEIVAAFRPEAVVLQCGADTLAGDPMGAFNLTPVGI 271
                         250       260
                  ....*....|....*....|....*.
gi 1622899648 212 VKrdelVFRMVRGRHVPILMVTSGGY 237
Cdd:cd10000   272 GK----CLKYVLGWKLPTLILGGGGY 293
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
17-237 3.98e-23

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: 95.64  E-value: 3.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  17 VINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKA------GKL--------------------------AVER 64
Cdd:cd09992    11 ILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYIERVEEtceaggGYLdpdtyvspgsyeaallaagaalaavdAVLS 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  65 GWAINvggGF-------HHCSSDRGGGFCAYADITLAIKFLFERVeGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVY 137
Cdd:cd09992    91 GEAEN---AFalvrppgHHAEPDRAMGFCLFNNVAIAARYAQKRY-GLKRVLIVDWDVHHGNGTQDIFYDDPSVLYFSIH 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 138 NRHIYPGDRFAKQAIRRK-------VELEWGTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAG 210
Cdd:cd09992   167 QYPFYPGTGAAEETGGGAgegftinVPLPPGSGDAEYLAAFEEVLLPIAREFQPDLVLVSAGFDAHRGDPLGGMNLTPEG 246
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1622899648 211 ------IVKrdELVFRMVRGRhvpILMVTSGGY 237
Cdd:cd09992   247 yarltrLLK--ELADEHCGGR---LVFVLEGGY 274
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
67-243 6.54e-22

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: 92.65  E-value: 6.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  67 AINVGGGFHHCSSDRGGGFCAYADITLAIKFL---FERVegisraTIIDLDAHQGNGHERDFMDDKRVyiMDVyNRHIYP 143
Cdd:cd09991   119 AINWAGGLHHAKKSEASGFCYVNDIVLAILELlkyHQRV------LYIDIDIHHGDGVEEAFYTTDRV--MTV-SFHKFG 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 144 GDRFAKQAIR----RK-------VELEWGTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIV 212
Cdd:cd09991   190 EYFFPGTGLRdigaGKgkyyavnVPLKDGIDDESYLQIFEPVLSKVMEVFQPSAVVLQCGADSLAGDRLGCFNLSIKGHA 269
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622899648 213 KrdelVFRMVRGRHVPILMVTSGGYQKR-TAR 243
Cdd:cd09991   270 K----CVKFVKSFNIPLLVLGGGGYTLRnVAR 297
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
7-250 1.45e-21

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: 92.02  E-value: 1.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648   7 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRR----------------------------YLNE---- 54
Cdd:cd11600     3 HPEDPSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEhwdrveatekmsdeqlkdrteiferdslYVNNdtaf 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  55 ---LKAGK-----LAVERGwaiNVGGGF-------HHCSSDRGGGFCAYADITLAIKFL-FERVEGISRATIIDLDAHQG 118
Cdd:cd11600    83 carLSCGGaieacRAVAEG---RVKNAFavvrppgHHAEPDESMGFCFFNNVAVAAKWLqTEYPDKIKKILILDWDIHHG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 119 NGHERDFMDDKRV-YI-MDVY-NRHIYPGDRFAK-------QAIRRKVELEW---GTEDDEYLDKVERNIEKSLQEHLPD 185
Cdd:cd11600   160 NGTQRAFYDDPNVlYIsLHRFeNGGFYPGTPYGDyesvgegAGLGFNVNIPWpqgGMGDADYIYAFQRIVMPIAYEFDPD 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622899648 186 VVVYNAGTDILEGDRLGGLSISPAGIVKRDELVFRMVRGRhvpILMVTSGGYQKRTariIADSIL 250
Cdd:cd11600   240 LVIISAGFDAADGDELGQCHVTPAGYAHMTHMLMSLAGGK---LVVALEGGYNLDA---ISDSAL 298
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
19-246 4.14e-20

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: 88.39  E-value: 4.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  19 NFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKAGKLA--VERGWAINVG-GGF--------------------- 74
Cdd:cd09996    45 NLLEVSGLSDHLVLITPRPATDEELLRVHTPEYIDRVKAASAAggGEAGGGTPFGpGSYeiallaaggaiaavdavldge 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  75 ------------HHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYNRHIY 142
Cdd:cd09996   125 vdnayalvrppgHHAEPDQGMGFCLFNNVAIAARHALAV-GGVKRVAVVDWDVHHGNGTQAIFYDDPDVLTISLHQDRCF 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 143 PGDRFAKQAIRR--------KVELEWGTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLGglsispagivkr 214
Cdd:cd09996   204 PPDSGAVEERGEgagegynlNIPLPPGSGDGAYLHAFERIVLPALRAFRPELIIVASGFDASAFDPLG------------ 271
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1622899648 215 delvfRMvrgrhvpilMVTSGGYQKRTARIIA 246
Cdd:cd09996   272 -----RM---------MLTSDGFRALTRKLRD 289
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
32-237 4.78e-20

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: 87.32  E-value: 4.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  32 LVEAREASEEDLLVVHTRRYLNEL-----------------------------KAGKLA--VERGWAINVGGGFHHCSSD 80
Cdd:cd11680    41 IIEPERATRKDLTKYHDKDYVDFLlkkygleddcpvfpflsmyvqlvagsslaLAKHLItqVERDIAINWYGGRHHAQKS 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  81 RGGGFCAYADITLAIKFLfeRVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDV--YNRHIYPG-----DRFAKQAIr 153
Cdd:cd11680   121 RASGFCYVNDIVLAILRL--RRARFRRVFYLDLDLHHGDGVESAFFFSKNVLTCSIhrYDPGFFPGtgslkNSSDKGML- 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 154 rKVELEWGTeDDEYLDKVERNIE-KSLQEHLPDVVVYNAGTDILEGDRLG--GLSISPAGIVkrdeLVFRMVRGRHVPIL 230
Cdd:cd11680   198 -NIPLKRGL-SDKTLLRIIDSIVrPLIEKFEPEVIVIQCGCDGLSGDPHKewNLTIRGYGSV----IELLLKEFKDKPTL 271

                  ....*..
gi 1622899648 231 MVTSGGY 237
Cdd:cd11680   272 LLGGGGY 278
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
17-237 1.22e-19

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: 86.44  E-value: 1.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  17 VINFLKEEKLlsdSMLVEAREASEEDLLVVHTRRYLNELK---AGKLAVERGW-------------AINVGGGF------ 74
Cdd:cd10001    35 ILDALKRAGL---GEVLPPRDFGLEPILAVHDPDYVDFLEtadTDTPISEGTWeaalaaadtaltaADLVLEGEraayal 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  75 -----HHCSSDRGGGFCAYADITLAIKFLFERVEgisRATIIDLDAHQGNGHERDFMDDKRVYIMDV--YNRHIYPG--- 144
Cdd:cd10001   112 crppgHHAGRDRAGGFCYFNNAAIAAQYLRDRAG---RVAILDVDVHHGNGTQEIFYERPDVLYVSIhgDPRTFYPFflg 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 145 ---DRFAKQAIRRKVE--LEWGTEDDEYLDKVERNIEKsLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIvkrdELVF 219
Cdd:cd10001   189 fadETGEGEGEGYNLNlpLPPGTGDDDYLAALDEALAA-IAAFGPDALVVSLGFDTHEGDPLSDFKLTTEDY----ARIG 263
                         250
                  ....*....|....*...
gi 1622899648 220 RMVRGRHVPILMVTSGGY 237
Cdd:cd10001   264 RRIAALGLPTVFVQEGGY 281
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
67-240 3.69e-19

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: 85.20  E-value: 3.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  67 AINVGGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDV--YNRHIYPG 144
Cdd:cd11598   123 AINWSGGLHHAKKSEASGFCYVNDIVLAI---LNLLRYFPRVLYIDIDVHHGDGVEEAFYRTDRVMTLSFhkYNGEFFPG 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 145 ---------DRFAKQAIrrKVELEWGTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLGGLSISpagIVKRD 215
Cdd:cd11598   200 tgdlddnggTPGKHFAL--NVPLEDGIDDEQYNLLFKSIIGPTIEKFQPSAIVLQCGADSLGGDRLGQFNLN---IKAHG 274
                         170       180
                  ....*....|....*....|....*
gi 1622899648 216 ELVfRMVRGRHVPILMVTSGGYQKR 240
Cdd:cd11598   275 ACV-KFVKSFGIPMLVVGGGGYTPR 298
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
4-237 7.70e-18

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: 82.00  E-value: 7.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648   4 EKLHPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELK--------------------------- 56
Cdd:cd10003    13 DPGHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHLDEMKslekmkprelnrlgkeydsiyihpdsy 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  57 ------AGKL-----AVERGWAINvGGGF-----HHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNG 120
Cdd:cd10003    93 qcallaAGCVlqvveAVLTGESRN-GVAIvrppgHHAEQDTACGFCFFNNVAIAARYAQKK-YGLKRILIVDWDVHHGNG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 121 HERDFMDDKRV-YI-MDVY-NRHIYPGDRFAKQAIRRK-------VELEW---GTEDDEYLDKVERNIEKSLQEHLPDVV 187
Cdd:cd10003   171 TQHMFESDPSVlYIsLHRYdNGSFFPNSPEGNYDVVGKgkgegfnVNIPWnkgGMGDAEYIAAFQQVVLPIAYEFNPELV 250
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622899648 188 VYNAGTDILEGDRLGGLSISPAGIVKRDELVFRMVRGRhvpILMVTSGGY 237
Cdd:cd10003   251 LVSAGFDAARGDPLGGCKVTPEGYAHMTHMLMSLAGGR---VIVILEGGY 297
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
7-270 4.97e-17

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: 79.51  E-value: 4.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648   7 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYL-----------NELKA-----------------G 58
Cdd:cd11682     7 FPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYValmkstqymteEELRTladtydsvylhpnsyscA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  59 KLA-------VERGWAINVGGGF-------HHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNGHERD 124
Cdd:cd11682    87 CLAvgsvlqlVDKVLGGEIRNGLaivrppgHHAQHDKMDGYCMFNNVAIAARYAQQK-HGVQRVLIVDWDVHHGQGTQFI 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 125 FMDDKRVYIMDVynrHIYPGDRF-------------AKQAIRRKVELEW---GTEDDEYLDKVERNIEKSLQEHLPDVVV 188
Cdd:cd11682   166 FEQDPSVLYFSI---HRYEQGRFwphlkesdssavgFGRGEGYNINVPWnqvGMRDADYIAAFLHVLLPVALEFQPQLVL 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 189 YNAGTDILEGDRLGGLSISPAGIVKRDELVFRMVRGRhvpILMVTSGGYQKR-TARIIADSILNLFG---LGLIGPESPS 264
Cdd:cd11682   243 VAAGFDAVIGDPKGEMAATPACFAHLTHLLMGLAGGK---LILSLEGGYNLRsLAEGVCASLKALLGdpcPMLESPGAPC 319

                  ....*.
gi 1622899648 265 ISAQNS 270
Cdd:cd11682   320 RSALAS 325
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
32-205 1.20e-16

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: 77.94  E-value: 1.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  32 LVEAREASEEDLLVVHTRRYLNELK------------------------------AGKLAVER---GWAINVgggF---- 74
Cdd:cd11599    26 QLEAPPATREQLLRVHDAAYVDRLEaaapeeglvqldpdtamspgsleaalraagAVVAAVDAvmaGEARNA---Fcavr 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  75 ---HHCSSDRGGGFCAYADITLAIKFLFERVeGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYNRHIYPGDRFAKQA 151
Cdd:cd11599   103 ppgHHAERDKAMGFCLFNNVAIAAAHALAHH-GLERVAIVDFDVHHGNGTEDIFRDDPRVLFCSSHQHPLYPGTGAPDET 181
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622899648 152 IR---RKVELEWGTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLGGLS 205
Cdd:cd11599   182 GHgniVNVPLPAGTGGAEFREAVEDRWLPALDAFKPDLILISAGFDAHRDDPLAQLN 238
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
67-240 1.36e-16

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: 78.57  E-value: 1.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  67 AINVGGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMDDKRVY-IMDVYNRHIYPG- 144
Cdd:cd10011   125 AVNWAGGLHHAKKSEASGFCYVNDIVLAI---LELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMtVSFHKYGEYFPGt 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 145 ----DRFAKQAIRRKVELEW--GTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVKRDELv 218
Cdd:cd10011   202 gdlrDIGAGKGKYYAVNFPMrdGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEV- 280
                         170       180
                  ....*....|....*....|..
gi 1622899648 219 frmVRGRHVPILMVTSGGYQKR 240
Cdd:cd10011   281 ---VKTFNLPLLMLGGGGYTIR 299
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
67-240 2.01e-16

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: 78.21  E-value: 2.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  67 AINVGGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMDDKRVyiMDV----YNRHIY 142
Cdd:cd10005   124 AINWSGGLHHAKKFEASGFCYVNDIVIAI---LELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRV--MTVsfhkYGNYFF 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 143 P--GDRFAKQAIRRK-----VELEWGTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGivkRD 215
Cdd:cd10005   199 PgtGDMYEVGAESGRyysvnVPLKDGIDDQSYLQLFKPVIQQVIDFYQPTCIVLQCGADSLGCDRLGCFNLSIKG---HG 275
                         170       180
                  ....*....|....*....|....*
gi 1622899648 216 ELVfRMVRGRHVPILMVTSGGYQKR 240
Cdd:cd10005   276 ECV-EFVKSFNIPLLVLGGGGYTVR 299
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
67-240 4.57e-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: 74.33  E-value: 4.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  67 AINVGGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYNR-HIYPG- 144
Cdd:cd10010   129 AVNWAGGLHHAKKSEASGFCYVNDIVLAI---LELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYgEYFPGt 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 145 ----DRFAKQAIRRKVE--LEWGTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVKRDELv 218
Cdd:cd10010   206 gdlrDIGAGKGKYYAVNypLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEF- 284
                         170       180
                  ....*....|....*....|..
gi 1622899648 219 frmVRGRHVPILMVTSGGYQKR 240
Cdd:cd10010   285 ---VKSFNLPMLMLGGGGYTIR 303
PTZ00063 PTZ00063
histone deacetylase; Provisional
68-240 4.79e-15

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 74.46  E-value: 4.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  68 INVGGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYN-RHIYPG-- 144
Cdd:PTZ00063  130 VNWSGGLHHAKRSEASGFCYINDIVLGI---LELLKYHARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKfGDFFPGtg 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 145 ---DRFAKQA--IRRKVELEWGTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLGGLSISpagiVKRDELVF 219
Cdd:PTZ00063  207 dvtDIGVAQGkyYSVNVPLNDGIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLT----IKGHAACV 282
                         170       180
                  ....*....|....*....|.
gi 1622899648 220 RMVRGRHVPILMVTSGGYQKR 240
Cdd:PTZ00063  283 EFVRSLNIPLLVLGGGGYTIR 303
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
21-237 2.29e-14

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: 71.96  E-value: 2.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  21 LKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELK----------------------------AGKLAVerGWAIN--- 69
Cdd:cd10002    21 LTQDGLLERCVKIPAREAEEDEILLVHSQEYIDLVKstetmekeeleslcsgydsvylcpstyeAARLAA--GSTIElvk 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  70 ------VGGGF-------HHCSSDRGGGFCAYADITLAIKFLFErVEGISRATIIDLDAHQGNGHERDFMDDKRVyimDV 136
Cdd:cd10002    99 avmagkIQNGFalirppgHHAMRNEANGYCIFNNVAIAAKYAIE-KLGLKRILIVDWDVHHGQGTQQGFYEDPRV---LY 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 137 YNRHIYPGDRF-------------AKQAIRRKVELEWGTE---DDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDR 200
Cdd:cd10002   175 FSIHRYEHGRFwphlfesdydyigVGHGYGFNVNVPLNQTglgDADYLAIFHHILLPLALEFQPELVLVSAGFDASIGDP 254
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1622899648 201 LGGLSISPAGIVKRDELVFRMVRGRhvpILMVTSGGY 237
Cdd:cd10002   255 EGEMAVTPAGYAHLTRLLMGLAGGK---LLLVLEGGY 288
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
67-240 2.59e-14

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: 72.15  E-value: 2.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  67 AINVGGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVynrHIYpGDR 146
Cdd:cd10004   125 AVNWAGGLHHAKKSEASGFCYVNDIVLGI---LELLRYHQRVLYIDIDVHHGDGVEEAFYTTDRVMTCSF---HKY-GEY 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 147 FAKQAIRR------------KVELEWGTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGivkr 214
Cdd:cd10004   198 FPGTGELRdigigtgknyavNVPLRDGIDDESYKSIFEPVIKHVMEWYQPEAVVLQCGGDSLSGDRLGCFNLSMKG---- 273
                         170       180
                  ....*....|....*....|....*.
gi 1622899648 215 DELVFRMVRGRHVPILMVTSGGYQKR 240
Cdd:cd10004   274 HANCVNFVKSFNLPMLVLGGGGYTMR 299
PTZ00346 PTZ00346
histone deacetylase; Provisional
55-240 5.31e-14

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 71.60  E-value: 5.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  55 LKAGKLAVERGWainvGGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMDDKRVYIM 134
Cdd:PTZ00346  138 LNSGQVDVAVHW----GGGMHHSKCGECSGFCYVNDIVLGI---LELLKCHDRVLYVDIDMHHGDGVDEAFCTSDRVFTL 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 135 DV--YNRHIYPGD---RFAKQAIRRKVELE---W-GTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLGGLS 205
Cdd:PTZ00346  211 SLhkFGESFFPGTghpRDVGYGRGRYYSMNlavWdGITDFYYLGLFEHALHSIVRRYSPDAIVLQCGADSLAGDRLGLLN 290
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622899648 206 ISPAGIVKrdelVFRMVRGRHVPILMVTSGGYQKR 240
Cdd:PTZ00346  291 LSSFGHGQ----CVQAVRDLGIPMLALGGGGYTIR 321
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
54-207 2.06e-11

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: 63.85  E-value: 2.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  54 ELKAGKLavERGWAINVGGGfHHCSSDRGGGFCAYADITLAIKFLFERVeGISRATIIDLDAHQGNGHERDFMDDKRVYI 133
Cdd:cd10007   136 KVAAGEL--KNGFAVIRPPG-HHAEESTAMGFCFFNSVAIAAKLLQQKL-NVGKILIVDWDIHHGNGTQQAFYNDPNVLY 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 134 MDVY---NRHIYPGDRFAKQ-----AIRRKVELEW--GTE----DDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGD 199
Cdd:cd10007   212 ISLHrydDGNFFPGSGAPDEvgagpGVGFNVNIAWtgGVDppigDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGH 291
                         170
                  ....*....|
gi 1622899648 200 R--LGGLSIS 207
Cdd:cd10007   292 QspLGGYSVT 301
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
7-207 2.29e-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: 63.49  E-value: 2.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648   7 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRY--------LNELK------AGKLAVERGWAINVGG 72
Cdd:cd10008    24 HPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHvllygtnpLSRLKldngklAGLLAQRMFVMLPCGG 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  73 ---------------------------------------GF-------HHCSSDRGGGFCAYADITLAIKFLFERVEgIS 106
Cdd:cd10008   104 vgvdtdtiwnelhssnaarwaagsvtdlafkvasrelknGFavvrppgHHADHSTAMGFCFFNSVAIACRQLQQQGK-AS 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 107 RATIIDLDAHQGNGHERDFMDDKRVYIMDVYnRH----IYPGDRFAKQAIRR-----KVELEW--GTE----DDEYLDKV 171
Cdd:cd10008   183 KILIVDWDVHHGNGTQQTFYQDPSVLYISLH-RHddgnFFPGSGAVDEVGAGsgegfNVNVAWagGLDppmgDPEYLAAF 261
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1622899648 172 ERNIEKSLQEHLPDVVVYNAGTDILEGD--RLGGLSIS 207
Cdd:cd10008   262 RIVVMPIAREFSPDLVLVSAGFDAAEGHpaPLGGYHVS 299
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
28-207 2.62e-10

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: 60.44  E-value: 2.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  28 SDSMLVEAREASEEDLLVVHTRRYLNELKAGKLavERGWAINVGGGfHHCSSDRGGGFCAYADITLAIKFLFERVEgISR 107
Cdd:cd10006   110 SDTIWNEVHSSGAARLAVGCVVELVFKVATGEL--KNGFAVVRPPG-HHAEESTPMGFCYFNSVAIAAKLLQQRLN-VSK 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 108 ATIIDLDAHQGNGHERDFMDDKRVYIMDVY---NRHIYPGDRFAKQ-----AIRRKVELEW--GTE----DDEYLDKVER 173
Cdd:cd10006   186 ILIVDWDVHHGNGTQQAFYSDPNVLYMSLHrydDGNFFPGSGAPDEvgtgpGVGFNVNMAFtgGLDppmgDAEYLAAFRT 265
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622899648 174 NIEKSLQEHLPDVVVYNAGTDILEGD--RLGGLSIS 207
Cdd:cd10006   266 VVMPIASEFAPDVVLVSSGFDAVEGHptPLGGYNLS 301
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
7-237 2.55e-09

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: 57.33  E-value: 2.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648   7 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHT---------------------------RRYLNELKAGK 59
Cdd:cd10009    24 HPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSehhsllygtnpldgqkldprillgddsQKFFSSLPCGG 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  60 LAVERGWAIN-----------VG---------------GGF-------HHCSSDRGGGFCAYADITLAIKFLFERVEgIS 106
Cdd:cd10009   104 LGVDSDTIWNelhssgaarmaVGcvielaskvasgelkNGFavvrppgHHAEESTAMGFCFFNSVAITAKYLRDQLN-IS 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 107 RATIIDLDAHQGNGHERDFMDDKRVYIMDVYNR---HIYPGDRFAKQAIR-----RKVELEW--GTE----DDEYLDKVE 172
Cdd:cd10009   183 KILIVDLDVHHGNGTQQAFYADPSILYISLHRYdegNFFPGSGAPNEVGTglgegYNINIAWtgGLDppmgDVEYLEAFR 262
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622899648 173 RNIEKSLQEHLPDVVVYNAGTDILEGDR--LGGLSISPAGIVKRDELVFRMVRGRhvpILMVTSGGY 237
Cdd:cd10009   263 TIVKPVAKEFDPDMVLVSAGFDALEGHTppLGGYKVTAKCFGHLTKQLMTLADGR---VVLALEGGH 326
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
7-237 3.93e-09

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: 56.58  E-value: 3.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648   7 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYL---------------------------------- 52
Cdd:cd11681    24 HPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTllygtnplsrlkldptklaglpqksfvrlpcggi 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  53 --------NEL---KAGKLAV---------------ERGWAINVGGGfHHCSSDRGGGFCAYADITLAIKFLFERVeGIS 106
Cdd:cd11681   104 gvdsdtvwNELhtsNAARMAVgcvidlafkvatgelKNGFAVVRPPG-HHAEPSQAMGFCFFNSVAIAAKQLQQKL-KLR 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 107 RATIIDLDAHQGNGHERDFMDDKRVYIMDVYnRH----IYPG----DRFAKQA-IRRKVELEW------GTEDDEYLDKV 171
Cdd:cd11681   182 KILIVDWDVHHGNGTQQIFYEDPNVLYISLH-RYddgnFFPGtgapTEVGSGAgEGFNVNIAWsggldpPMGDAEYLAAF 260
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622899648 172 ERNIEKSLQEHLPDVVVYNAGTDILEG--DRLGGLSISPAGIVKRDELVFRMVRGRhvpILMVTSGGY 237
Cdd:cd11681   261 RTVVMPIAREFSPDIVLVSAGFDAAEGhpPPLGGYKVSPACFGYMTRQLMNLAGGK---VVLALEGGY 325
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
21-270 1.88e-06

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: 48.32  E-value: 1.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  21 LKEEKLLSDSMLVEAREASEEDLLVVHTRRYLN-----------ELKA-----------------GKLA----------- 61
Cdd:cd11683    21 LRQYGLVQRCLRLPAREASEEEILLVHSPEYLSlvretqvmnkeELMAisgkydavyfhpntfhcARLAagatlqlvdav 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648  62 ----VERGWAINVGGGfHHCSSDRGGGFCAYADITLAIKFLfERVEGISRATIIDLDAHQGNGHERDFMDDKRVYimdVY 137
Cdd:cd11683   101 ltgeVQNGMALVRPPG-HHSQRNAANGFCVFNNVAIAAEYA-KKKYGLHRILIVDWDVHHGQGIQYIFEEDPSVL---YF 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899648 138 NRHIYPGDRF-------AKQAIRR------KVELEW---GTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRL 201
Cdd:cd11683   176 SWHRYEHQRFwpflresDYDAVGRgkglgfNINLPWnkvGMGNADYLAAFFHVLLPLAFEFDPELVLVSAGFDSAIGDPE 255
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622899648 202 GGLSISPAGIVKRDELVFRMVRGRhvpILMVTSGGYQKRT-ARIIADSILNLFG---LGLIGPESPSISAQNS 270
Cdd:cd11683   256 GQMCATPECFAHLTHLLMVLAGGK---LCAVLEGGYHLESlAESVCMTVQTLLGdplPRLSGEMTPCQSALES 325
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
75-120 9.45e-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: 43.21  E-value: 9.45e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1622899648  75 HHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNG 120
Cdd:cd09998   120 HHCSESTPSGFCWVNNVHVGAAHAYLT-HGITRVVILDIDLHHGNG 164
 
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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