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Conserved domains on  [gi|217272877|ref|NP_079103|]
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histone deacetylase 11 isoform 1 [Homo sapiens]

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 ...
 35-319 5.28e-143

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: 405.34  E-value: 5.28e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  35 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKWSfavATITEIPPVIFLPNFLvqrKVLRPL 114
Cdd:cd09993    1 HRFPMRKYGLLREALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLESLKSG---ELSREEIRRIGFPWSP---ELVERT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 115 RTQTGGTIMAGKLAVERGWAINVGGGFHHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNGHERDFMD 194
Cdd:cd09993   75 RLAVGGTILAARLALEHGLAINLAGGTHHAFPDRGEGFCVFNDIAIAARVLLAE-GLVRRVLIVDLDVHQGNGTAAIFAD 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 195 DKRVYIMDVYNRHIYPGDrfaKQAIRRKVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSIS 274
Cdd:cd09993  154 DPSVFTFSMHGEKNYPFR---KEPSDLDVPLPDGTGDDEYLAALEEALPRLLAEFRPDLVFYNAGVDVLAGDRLGRLSLS 230

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 217272877 275 PAGIVKRDELVFRMVRGRRVPILMVTSGGYQKRTARIIADSILNL 319
Cdd:cd09993  231 LEGLRERDRLVLRFARARGIPVAMVLGGGYSRDIARLVARHAQTL 275
 
Name Accession Description Interval E-value
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 35-319 5.28e-143

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: 405.34  E-value: 5.28e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  35 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKWSfavATITEIPPVIFLPNFLvqrKVLRPL 114
Cdd:cd09993    1 HRFPMRKYGLLREALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLESLKSG---ELSREEIRRIGFPWSP---ELVERT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 115 RTQTGGTIMAGKLAVERGWAINVGGGFHHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNGHERDFMD 194
Cdd:cd09993   75 RLAVGGTILAARLALEHGLAINLAGGTHHAFPDRGEGFCVFNDIAIAARVLLAE-GLVRRVLIVDLDVHQGNGTAAIFAD 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 195 DKRVYIMDVYNRHIYPGDrfaKQAIRRKVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSIS 274
Cdd:cd09993  154 DPSVFTFSMHGEKNYPFR---KEPSDLDVPLPDGTGDDEYLAALEEALPRLLAEFRPDLVFYNAGVDVLAGDRLGRLSLS 230

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 217272877 275 PAGIVKRDELVFRMVRGRRVPILMVTSGGYQKRTARIIADSILNL 319
Cdd:cd09993  231 LEGLRERDRLVLRFARARGIPVAMVLGGGYSRDIARLVARHAQTL 275
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 35-320 4.83e-64

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: 205.16  E-value: 4.83e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877   35 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKWSFAVATITEIPPVIFLPNFL-VQRKVLRP 113
Cdd:pfam00850   1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAAPEGGALLLLSYLSGDDDTpVSPGSYEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  114 LRTQTGGTIMAGKLAVE----RGWAINVGGGfHHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNGHE 189
Cdd:pfam00850  81 ALLAAGGTLAAADAVLSgearNAFALVRPPG-HHAERDRASGFCIFNNVAIAAKYLREK-YGLKRVAIVDFDVHHGNGTQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  190 RDFMDDKRVYIMDV--YNRHIYPGDRFAKQAIRRK-------VELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGT 260
Cdd:pfam00850 159 EIFYDDPSVLTLSIhqYPGGFYPGTGFADETGEGKgkgytlnVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAGF 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  261 DILEGDRLGGLSISPAGIVKRDELVFRMVRGRRVPILMVTSGGYqkrTARIIADSILNLF 320
Cdd:pfam00850 239 DAHAGDPLGGLNLTTEGFAEITRILLELADPLCIRVVSVLEGGY---NLDALARSATAVL 295
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 17-320 4.39e-61

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 198.02  E-value: 4.39e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  17 PIVYSPRYNITFMGleKLHPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKwsfavaTITEIP 96
Cdd:COG0123    2 ALIYHPDYLLHDLG--PGHPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALR------AASLDG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  97 PVIFL-PNFLVQRKVLRPLRTQTGGTIMAGKLAVERGWAI---NVGGGFHHCSSDRGGGFCAYADITLAIKFLfeRVEGI 172
Cdd:COG0123   74 GYGQLdPDTPVSPGTWEAALLAAGGALAAADAVLEGEARNafaLVRPPGHHAERDRAMGFCLFNNAAIAARYL--LAKGL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 173 SRATIIDLDAHQGNGHERDFMDDKRVYIMDVYNRHIYPGDRFAKQAIRRK-------VELEWGTEDDEYLDKVERNIKKS 245
Cdd:COG0123  152 ERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQDPLYPGTGAADETGEGAgegsnlnVPLPPGTGDAEYLAALEEALLPA 231

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 217272877 246 LQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVKRDELVFRMVRGRRVPILMVTSGGYQKRTARIIADSILNLF 320
Cdd:COG0123  232 LEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELADHCGGPVVSVLEGGYNLDALARSVAAHLETL 306
PTZ00063 PTZ00063
histone deacetylase; Provisional
 135-307 8.23e-15

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 74.85  E-value: 8.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 135 INVGGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYN-RHIYPG-- 211
Cdd:PTZ00063 130 VNWSGGLHHAKRSEASGFCYINDIVLGI---LELLKYHARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKfGDFFPGtg 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 212 ---DRFAKQA--IRRKVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSISpagiVKRDELVF 286
Cdd:PTZ00063 207 dvtDIGVAQGkyYSVNVPLNDGIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLT----IKGHAACV 282

                        170       180
                 ....*....|....*....|.
gi 217272877 287 RMVRGRRVPILMVTSGGYQKR 307
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 ...
 35-319 5.28e-143

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: 405.34  E-value: 5.28e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  35 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKWSfavATITEIPPVIFLPNFLvqrKVLRPL 114
Cdd:cd09993    1 HRFPMRKYGLLREALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLESLKSG---ELSREEIRRIGFPWSP---ELVERT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 115 RTQTGGTIMAGKLAVERGWAINVGGGFHHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNGHERDFMD 194
Cdd:cd09993   75 RLAVGGTILAARLALEHGLAINLAGGTHHAFPDRGEGFCVFNDIAIAARVLLAE-GLVRRVLIVDLDVHQGNGTAAIFAD 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 195 DKRVYIMDVYNRHIYPGDrfaKQAIRRKVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSIS 274
Cdd:cd09993  154 DPSVFTFSMHGEKNYPFR---KEPSDLDVPLPDGTGDDEYLAALEEALPRLLAEFRPDLVFYNAGVDVLAGDRLGRLSLS 230

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 217272877 275 PAGIVKRDELVFRMVRGRRVPILMVTSGGYQKRTARIIADSILNL 319
Cdd:cd09993  231 LEGLRERDRLVLRFARARGIPVAMVLGGGYSRDIARLVARHAQTL 275
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
 41-319 1.72e-124

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: 358.67  E-value: 1.72e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  41 KWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKWSFAVATITEIPPVIFLPNFLVQRKVLRPLRTQTGG 120
Cdd:cd09301    1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKANFAVATITESKPVIFGPNFPVQRHYFRGARLSTGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 121 TIMAGKLAV----ERGWAInVGGGFHHCSSDRGGGFCAYADITLAIKFLFERveGISRATIIDLDAHQGNGHERDFMDDK 196
Cdd:cd09301   81 VVEAAELVAkgelERAFAV-VGAGGHHAGKSRAWGFCYFNDVVLAIKFLRER--GISRILIIDTDAHHGDGTREAFYDDD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 197 RVYIMDVYNRHIYPGDRFAKQAIRRKVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPA 276
Cdd:cd09301  158 RVLHMSFHNYDIYPFGRGKGKGYKINVPLEDGLGDEEYLDAVERVISKVLEEFEPEVVVLQFGHDTHEGDRLGGFNLSEK 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 217272877 277 GIVKRDELVFRMVRGrrVPILMVTSGGYQ-KRTARIIADSILNL 319
Cdd:cd09301  238 GFVKLAEIVKEFARG--GPILMVLGGGYNpEAAARIWTAIIKEL 279
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 35-320 4.83e-64

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: 205.16  E-value: 4.83e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877   35 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKWSFAVATITEIPPVIFLPNFL-VQRKVLRP 113
Cdd:pfam00850   1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAAPEGGALLLLSYLSGDDDTpVSPGSYEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  114 LRTQTGGTIMAGKLAVE----RGWAINVGGGfHHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNGHE 189
Cdd:pfam00850  81 ALLAAGGTLAAADAVLSgearNAFALVRPPG-HHAERDRASGFCIFNNVAIAAKYLREK-YGLKRVAIVDFDVHHGNGTQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  190 RDFMDDKRVYIMDV--YNRHIYPGDRFAKQAIRRK-------VELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGT 260
Cdd:pfam00850 159 EIFYDDPSVLTLSIhqYPGGFYPGTGFADETGEGKgkgytlnVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAGF 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  261 DILEGDRLGGLSISPAGIVKRDELVFRMVRGRRVPILMVTSGGYqkrTARIIADSILNLF 320
Cdd:pfam00850 239 DAHAGDPLGGLNLTTEGFAEITRILLELADPLCIRVVSVLEGGY---NLDALARSATAVL 295
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 17-320 4.39e-61

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 198.02  E-value: 4.39e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  17 PIVYSPRYNITFMGleKLHPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKwsfavaTITEIP 96
Cdd:COG0123    2 ALIYHPDYLLHDLG--PGHPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALR------AASLDG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  97 PVIFL-PNFLVQRKVLRPLRTQTGGTIMAGKLAVERGWAI---NVGGGFHHCSSDRGGGFCAYADITLAIKFLfeRVEGI 172
Cdd:COG0123   74 GYGQLdPDTPVSPGTWEAALLAAGGALAAADAVLEGEARNafaLVRPPGHHAERDRAMGFCLFNNAAIAARYL--LAKGL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 173 SRATIIDLDAHQGNGHERDFMDDKRVYIMDVYNRHIYPGDRFAKQAIRRK-------VELEWGTEDDEYLDKVERNIKKS 245
Cdd:COG0123  152 ERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQDPLYPGTGAADETGEGAgegsnlnVPLPPGTGDAEYLAALEEALLPA 231

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 217272877 246 LQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVKRDELVFRMVRGRRVPILMVTSGGYQKRTARIIADSILNLF 320
Cdd:COG0123  232 LEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELADHCGGPVVSVLEGGYNLDALARSVAAHLETL 306
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
 18-311 2.37e-38

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: 138.85  E-value: 2.37e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  18 IVYSPRYNITFMGleKLHPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKwsfaVATITEIPP 97
Cdd:cd09994    2 FIYSEEYLRYSFG--PNHPFNPPRLSLTKDLLRALGLLPPVDLVPPRPATEEELLLFHTPDYIEAVK----EASRGQEPE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  98 VIFL--------PNFlvqRKVLRPLRTQTGGTIMAGKLAVERGW--AINVGGGFHHCSSDRGGGFCAYADITLAIKFLFE 167
Cdd:cd09994   76 GRGRlglgtednPVF---PGMHEAAALVVGGTLLAARLVLEGEArrAFNPAGGLHHAMRGRASGFCVYNDAAVAIERLRD 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 168 RveGISRATIIDLDAHQGNGHERDFMDDKRVYIMDV--YNRHIYPGDRFAKQAIRRK-------VELEWGTEDDEYLDKV 238
Cdd:cd09994  153 K--GGLRVAYVDIDAHHGDGVQAAFYDDPRVLTISLheSGRYLFPGTGFVDEIGEGEgygyavnIPLPPGTGDDEFLRAF 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 239 ERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVKrdelVFRMVR--------GRrvpILMVTSGGYQKR-TA 309
Cdd:cd09994  231 EAVVPPLLRAFRPDVIVSQHGADAHAGDPLTHLNLSNRAYRA----AVRRIReladeycgGR---WLALGGGGYNPDvVA 303


                 ..
gi 217272877 310 RI 311
Cdd:cd09994  304 RA 305
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 54-304 2.65e-25

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: 104.73  E-value: 2.65e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  54 LLSDSMLVEAREASEEDLLVVHTRRYLNELKWSFAVATITEIPPVI----------FLPNflvqrkVLRPLRTQTGGTIM 123
Cdd:cd10000   35 LLKQLRVVKPRVATEEELASFHSDEYIQFLKKASNEGDNDEEPSEQqefglgydcpIFEG------IYDYAAAVAGATLT 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 124 AGKLAV--ERGWAINVGGGFHHCSSDRGGGFCAYADITLAIKFLFERVEgisRATIIDLDAHQGNGHERDFMDDKRVYI- 200
Cdd:cd10000  109 AAQLLIdgKCKVAINWFGGWHHAQRDEASGFCYVNDIVLGILKLREKFD---RVLYVDLDLHHGDGVEDAFSFTSKVMTv 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 201 -MDVYNRHIYPGDRFAKQAIRRK-------VELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLS 272
Cdd:cd10000  186 sLHKYSPGFFPGTGDVSDVGLGKgkyytvnVPLRDGIQDEQYLQIFTAVVPEIVAAFRPEAVVLQCGADTLAGDPMGAFN 265

                        250       260       270
                 ....*....|....*....|....*....|..
gi 217272877 273 ISPAGIVKrdelVFRMVRGRRVPILMVTSGGY 304
Cdd:cd10000  266 LTPVGIGK----CLKYVLGWKLPTLILGGGGY 293
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
 60-310 3.05e-25

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: 103.43  E-value: 3.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  60 LVEAREASEEDLLVVHTRRYLNELKwsfavatitEIPPviflPNFLVQRKVLR--------PL--------RTQTGGTIM 123
Cdd:cd09991   40 IYRPRPATAEELTKFHSDDYIDFLR---------SVSP----DNMKEFKKQLErfnvgedcPVfdglyeycQLYAGGSIA 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 124 AG-KLA-VERGWAINVGGGFHHCSSDRGGGFCAYADITLAIKFL---FERVegisraTIIDLDAHQGNGHERDFMDDKRV 198
Cdd:cd09991  107 AAvKLNrGQADIAINWAGGLHHAKKSEASGFCYVNDIVLAILELlkyHQRV------LYIDIDIHHGDGVEEAFYTTDRV 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 199 yiMDVyNRHIYPGDRFAKQAIR----RK-------VELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDR 267
Cdd:cd09991  181 --MTV-SFHKFGEYFFPGTGLRdigaGKgkyyavnVPLKDGIDDESYLQIFEPVLSKVMEVFQPSAVVLQCGADSLAGDR 257

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 217272877 268 LGGLSISPAGIVKrdelVFRMVRGRRVPILMVTSGGYQKR-TAR 310
Cdd:cd09991  258 LGCFNLSIKGHAK----CVKFVKSFNIPLLVLGGGGYTLRnVAR 297
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 35-317 2.79e-24

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: 100.88  E-value: 2.79e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  35 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKwSFAVATITEIPPVIFLPNFL---VQRKVL 111
Cdd:cd11600    3 HPEDPSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEHWDRVE-ATEKMSDEQLKDRTEIFERDslyVNNDTA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 112 RPLRTQTGGTIMAGKlAVERGwaiNVGGGF-------HHCSSDRGGGFCAYADITLAIKFL-FERVEGISRATIIDLDAH 183
Cdd:cd11600   82 FCARLSCGGAIEACR-AVAEG---RVKNAFavvrppgHHAEPDESMGFCFFNNVAVAAKWLqTEYPDKIKKILILDWDIH 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 184 QGNGHERDFMDDKRV-YI-MDVY-NRHIYPGDRFAK-------QAIRRKVELEW---GTEDDEYLDKVERNIKKSLQEHL 250
Cdd:cd11600  158 HGNGTQRAFYDDPNVlYIsLHRFeNGGFYPGTPYGDyesvgegAGLGFNVNIPWpqgGMGDADYIYAFQRIVMPIAYEFD 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 217272877 251 PDVVVYNAGTDILEGDRLGGLSISPAGIVKRDELVFRMVRGRRVPILmvtSGGYQKRTariIADSIL 317
Cdd:cd11600  238 PDLVIISAGFDAADGDELGQCHVTPAGYAHMTHMLMSLAGGKLVVAL---EGGYNLDA---ISDSAL 298
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
 45-304 2.94e-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: 97.57  E-value: 2.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  45 VINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKwSFAVATITEIPPVIFlpnflVQRKVLRPLRTQTGGTIMA 124
Cdd:cd09992   11 ILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYIERVE-ETCEAGGGYLDPDTY-----VSPGSYEAALLAAGAALAA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 125 GKlAVERGWAINvggGF-------HHCSSDRGGGFCAYADITLAIKFLFERVeGISRATIIDLDAHQGNGHERDFMDDKR 197
Cdd:cd09992   85 VD-AVLSGEAEN---AFalvrppgHHAEPDRAMGFCLFNNVAIAARYAQKRY-GLKRVLIVDWDVHHGNGTQDIFYDDPS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 198 VYIMDVYNRHIYPGDRFAKQAIRRK-------VELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGG 270
Cdd:cd09992  160 VLYFSIHQYPFYPGTGAAEETGGGAgegftinVPLPPGSGDAEYLAAFEEVLLPIAREFQPDLVLVSAGFDAHRGDPLGG 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 217272877 271 LSISPAG------IVKrdELVFRMVRGRrvpILMVTSGGY 304
Cdd:cd09992  240 MNLTPEGyarltrLLK--ELADEHCGGR---LVFVLEGGY 274
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
 60-304 2.96e-23

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: 97.72  E-value: 2.96e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  60 LVEAREASEEDLLVVHTRRYLNELKWSFAVatITEIPPVIFLPNFLvqrkvlrplRTQTGGTIMAGKL---AVERGWAIN 136
Cdd:cd11680   41 IIEPERATRKDLTKYHDKDYVDFLLKKYGL--EDDCPVFPFLSMYV---------QLVAGSSLALAKHlitQVERDIAIN 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 137 VGGGFHHCSSDRGGGFCAYADITLAIKFLfeRVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDV--YNRHIYPG--- 211
Cdd:cd11680  110 WYGGRHHAQKSRASGFCYVNDIVLAILRL--RRARFRRVFYLDLDLHHGDGVESAFFFSKNVLTCSIhrYDPGFFPGtgs 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 212 --DRFAKQAIrrKVELEWGTeDDEYLDKVERNI-KKSLQEHLPDVVVYNAGTDILEGDRLG--GLSISPAGIVkrdeLVF 286
Cdd:cd11680  188 lkNSSDKGML--NIPLKRGL-SDKTLLRIIDSIvRPLIEKFEPEVIVIQCGCDGLSGDPHKewNLTIRGYGSV----IEL 260

                        250
                 ....*....|....*...
gi 217272877 287 RMVRGRRVPILMVTSGGY 304
Cdd:cd11680  261 LLKEFKDKPTLLLGGGGY 278
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
 18-304 1.24e-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: 87.59  E-value: 1.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  18 IVYSPRYnitfmgleKLH----PFDAGKWGK----------VINFLKEEKLlsdSMLVEAREASEEDLLVVHTRRYLNEL 83
Cdd:cd10001    2 IVYSEDH--------LLHhpktELSRGKLVPhpenperaeaILDALKRAGL---GEVLPPRDFGLEPILAVHDPDYVDFL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  84 KwSFAVAT-ITEippviflpnflvqrKVLRPLRTQTGGTIMAGKLAVE-RGWAINVG---GgfHHCSSDRGGGFCAYADI 158
Cdd:cd10001   71 E-TADTDTpISE--------------GTWEAALAAADTALTAADLVLEgERAAYALCrppG--HHAGRDRAGGFCYFNNA 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 159 TLAIKFLFERVEgisRATIIDLDAHQGNGHERDFMDDKRVYIMDV--YNRHIYPG------DRFAKQAIRRKVE--LEWG 228
Cdd:cd10001  134 AIAAQYLRDRAG---RVAILDVDVHHGNGTQEIFYERPDVLYVSIhgDPRTFYPFflgfadETGEGEGEGYNLNlpLPPG 210

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 217272877 229 TEDDEYLDKVERNIKKsLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIvkrdELVFRMVRGRRVPILMVTSGGY 304
Cdd:cd10001  211 TGDDDYLAALDEALAA-IAAFGPDALVVSLGFDTHEGDPLSDFKLTTEDY----ARIGRRIAALGLPTVFVQEGGY 281
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
 62-307 3.11e-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: 86.74  E-value: 3.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  62 EAREASEEDLLVVHTRRYLNELKwSFAVATITEIPPVIFLPNFL-----VQRKVLRPLRTQTGGTIMAGKLAV--ERGWA 134
Cdd:cd11598   45 EARAATREELRQFHDADYLDFLS-KVSPENANQLRFDKAEPFNIgddcpVFDGMYDYCQLYAGASLDAARKLCsgQSDIA 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 135 INVGGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDV--YNRHIYPG- 211
Cdd:cd11598  124 INWSGGLHHAKKSEASGFCYVNDIVLAI---LNLLRYFPRVLYIDIDVHHGDGVEEAFYRTDRVMTLSFhkYNGEFFPGt 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 212 --------DRFAKQAIrrKVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSISpagIVKRDE 283
Cdd:cd11598  201 gdlddnggTPGKHFAL--NVPLEDGIDDEQYNLLFKSIIGPTIEKFQPSAIVLQCGADSLGGDRLGQFNLN---IKAHGA 275

                        250       260
                 ....*....|....*....|....
gi 217272877 284 LVfRMVRGRRVPILMVTSGGYQKR 307
Cdd:cd11598  276 CV-KFVKSFGIPMLVVGGGGYTPR 298
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
 47-313 9.27e-19

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: 86.08  E-value: 9.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  47 NFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKwSFAVATITEIPPVIFLPN--FLVQRKvlrplrtQTGGTIMA 124
Cdd:cd09996   45 NLLEVSGLSDHLVLITPRPATDEELLRVHTPEYIDRVK-AASAAGGGEAGGGTPFGPgsYEIALL-------AAGGAIAA 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 125 GKlAVERGWAINV-------GggfHHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNGHERDFMDDKR 197
Cdd:cd09996  117 VD-AVLDGEVDNAyalvrppG---HHAEPDQGMGFCLFNNVAIAARHALAV-GGVKRVAVVDWDVHHGNGTQAIFYDDPD 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 198 VYIMDVYNRHIYPGDRFAKQAIRR--------KVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLG 269
Cdd:cd09996  192 VLTISLHQDRCFPPDSGAVEERGEgagegynlNIPLPPGSGDGAYLHAFERIVLPALRAFRPELIIVASGFDASAFDPLG 271

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 217272877 270 glsispagivkrdelvfRMvrgrrvpilMVTSGGYQKRTARIIA 313
Cdd:cd09996  272 -----------------RM---------MLTSDGFRALTRKLRD 289
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
 35-337 1.72e-18

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: 84.90  E-value: 1.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  35 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLnELKWSFAVATITEI-------PPVIFLPNF--- 104
Cdd:cd11682    7 FPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYV-ALMKSTQYMTEEELrtladtyDSVYLHPNSysc 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 105 --LVQRKVLRPLRTQTGGTImagklavERGWAINVGGGfHHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDA 182
Cdd:cd11682   86 acLAVGSVLQLVDKVLGGEI-------RNGLAIVRPPG-HHAQHDKMDGYCMFNNVAIAARYAQQK-HGVQRVLIVDWDV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 183 HQGNGHERDFMDDKRVYIMDVynrHIYPGDRF-------------AKQAIRRKVELEW---GTEDDEYLDKVERNIKKSL 246
Cdd:cd11682  157 HHGQGTQFIFEQDPSVLYFSI---HRYEQGRFwphlkesdssavgFGRGEGYNINVPWnqvGMRDADYIAAFLHVLLPVA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 247 QEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVKRDELVFRMVRGRrvpILMVTSGGYQKR-TARIIADSILNLFG---L 322
Cdd:cd11682  234 LEFQPQLVLVAAGFDAVIGDPKGEMAATPACFAHLTHLLMGLAGGK---LILSLEGGYNLRsLAEGVCASLKALLGdpcP 310

                        330
                 ....*....|....*
gi 217272877 323 GLIGPESPSVSAQNS 337
Cdd:cd11682  311 MLESPGAPCRSALAS 325
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
 32-304 1.35e-17

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: 82.39  E-value: 1.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  32 EKLHPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKwsfAVATIT--------EIPPVIFLPN 103
Cdd:cd10003   13 DPGHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHLDEMK---SLEKMKprelnrlgKEYDSIYIHP 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 104 flvqrKVLRPLRTQTGGTIMAGKlAVERGWAINvGGGF-----HHCSSDRGGGFCAYADITLAIKFLFERvEGISRATII 178
Cdd:cd10003   90 -----DSYQCALLAAGCVLQVVE-AVLTGESRN-GVAIvrppgHHAEQDTACGFCFFNNVAIAARYAQKK-YGLKRILIV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 179 DLDAHQGNGHERDFMDDKRV-YI-MDVY-NRHIYPGDRFAKQAIRRK-------VELEW---GTEDDEYLDKVERNIKKS 245
Cdd:cd10003  162 DWDVHHGNGTQHMFESDPSVlYIsLHRYdNGSFFPNSPEGNYDVVGKgkgegfnVNIPWnkgGMGDAEYIAAFQQVVLPI 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 217272877 246 LQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVKRDELVFRMVRGRrvpILMVTSGGY 304
Cdd:cd10003  242 AYEFNPELVLVSAGFDAARGDPLGGCKVTPEGYAHMTHMLMSLAGGR---VIVILEGGY 297
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
 118-307 2.78e-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: 82.03  E-value: 2.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 118 TGGTImAGKLAVER---GWAINVGGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMD 194
Cdd:cd10011  107 TGGSV-AGAVKLNRqqtDMAVNWAGGLHHAKKSEASGFCYVNDIVLAI---LELLKYHQRVLYIDIDIHHGDGVEEAFYT 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 195 DKRVY-IMDVYNRHIYPG-----DRFAKQAIRRKVELEW--GTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGD 266
Cdd:cd10011  183 TDRVMtVSFHKYGEYFPGtgdlrDIGAGKGKYYAVNFPMrdGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGD 262

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 217272877 267 RLGGLSISPAGIVKRDELvfrmVRGRRVPILMVTSGGYQKR 307
Cdd:cd10011  263 RLGCFNLTVKGHAKCVEV----VKTFNLPLLMLGGGGYTIR 299
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
 60-272 1.17e-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: 79.09  E-value: 1.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  60 LVEAREASEEDLLVVHTRRYLNELKwsfavatiTEIP--PVIFL-PNFLVQRKVLRPLRTQTGGTIMAGKlAVERGWAIN 136
Cdd:cd11599   26 QLEAPPATREQLLRVHDAAYVDRLE--------AAAPeeGLVQLdPDTAMSPGSLEAALRAAGAVVAAVD-AVMAGEARN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 137 VgggF-------HHCSSDRGGGFCAYADITLAIKFLFERVeGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYNRHIY 209
Cdd:cd11599   97 A---FcavrppgHHAERDKAMGFCLFNNVAIAAAHALAHH-GLERVAIVDFDVHHGNGTEDIFRDDPRVLFCSSHQHPLY 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 217272877 210 PGDRFAKQAIR---RKVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLS 272
Cdd:cd11599  173 PGTGAPDETGHgniVNVPLPAGTGGAEFREAVEDRWLPALDAFKPDLILISAGFDAHRDDPLAQLN 238
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
 134-307 4.46e-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: 78.59  E-value: 4.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 134 AINVGGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMDDKRVyiMDV----YNRHIY 209
Cdd:cd10005  124 AINWSGGLHHAKKFEASGFCYVNDIVIAI---LELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRV--MTVsfhkYGNYFF 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 210 P--GDRFAKQAIRRK-----VELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGivkRD 282
Cdd:cd10005  199 PgtGDMYEVGAESGRyysvnVPLKDGIDDQSYLQLFKPVIQQVIDFYQPTCIVLQCGADSLGCDRLGCFNLSIKG---HG 275

                        170       180
                 ....*....|....*....|....*
gi 217272877 283 ELVfRMVRGRRVPILMVTSGGYQKR 307
Cdd:cd10005  276 ECV-EFVKSFNIPLLVLGGGGYTVR 299
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
 118-307 5.26e-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: 75.10  E-value: 5.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 118 TGGTIMAG-KLAVER-GWAINVGGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMDD 195
Cdd:cd10010  111 AGGSVASAvKLNKQQtDIAVNWAGGLHHAKKSEASGFCYVNDIVLAI---LELLKYHQRVLYIDIDIHHGDGVEEAFYTT 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 196 KRVYIMDVYNR-HIYPG-----DRFAKQAIRRKVE--LEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDR 267
Cdd:cd10010  188 DRVMTVSFHKYgEYFPGtgdlrDIGAGKGKYYAVNypLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGADSLSGDR 267

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 217272877 268 LGGLSISPAGIVKRDELvfrmVRGRRVPILMVTSGGYQKR 307
Cdd:cd10010  268 LGCFNLTIKGHAKCVEF----VKSFNLPMLMLGGGGYTIR 303
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 49-304 5.87e-15

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: 74.65  E-value: 5.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  49 LKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKwSFAVATITEIPP-------VIFLPN-FLVQRKVLrplrtqtGG 120
Cdd:cd10002   21 LTQDGLLERCVKIPAREAEEDEILLVHSQEYIDLVK-STETMEKEELESlcsgydsVYLCPStYEAARLAA-------GS 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 121 TIMAGKLAVERGwainVGGGF-------HHCSSDRGGGFCAYADITLAIKFLFErVEGISRATIIDLDAHQGNGHERDFM 193
Cdd:cd10002   93 TIELVKAVMAGK----IQNGFalirppgHHAMRNEANGYCIFNNVAIAAKYAIE-KLGLKRILIVDWDVHHGQGTQQGFY 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 194 DDKRVyimDVYNRHIYPGDRF-------------AKQAIRRKVELEWGTE---DDEYLDKVERNIKKSLQEHLPDVVVYN 257
Cdd:cd10002  168 EDPRV---LYFSIHRYEHGRFwphlfesdydyigVGHGYGFNVNVPLNQTglgDADYLAIFHHILLPLALEFQPELVLVS 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 217272877 258 AGTDILEGDRLGGLSISPAGIVKRDELVFRMVRGRrvpILMVTSGGY 304
Cdd:cd10002  245 AGFDASIGDPEGEMAVTPAGYAHLTRLLMGLAGGK---LLLVLEGGY 288
PTZ00063 PTZ00063
histone deacetylase; Provisional
 135-307 8.23e-15

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 74.85  E-value: 8.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 135 INVGGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYN-RHIYPG-- 211
Cdd:PTZ00063 130 VNWSGGLHHAKRSEASGFCYINDIVLGI---LELLKYHARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKfGDFFPGtg 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 212 ---DRFAKQA--IRRKVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSISpagiVKRDELVF 286
Cdd:PTZ00063 207 dvtDIGVAQGkyYSVNVPLNDGIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLT----IKGHAACV 282

                        170       180
                 ....*....|....*....|.
gi 217272877 287 RMVRGRRVPILMVTSGGYQKR 307
Cdd:PTZ00063 283 EFVRSLNIPLLVLGGGGYTIR 303
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
 118-307 1.06e-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: 74.46  E-value: 1.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 118 TGGTIMAGKLAVERG---WAINVGGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMD 194
Cdd:cd10004  106 SAGGSMEGAARLNRGkcdIAVNWAGGLHHAKKSEASGFCYVNDIVLGI---LELLRYHQRVLYIDIDVHHGDGVEEAFYT 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 195 DKRVyiMDVyNRHIYpGDRFAKQAIRR------------KVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDI 262
Cdd:cd10004  183 TDRV--MTC-SFHKY-GEYFPGTGELRdigigtgknyavNVPLRDGIDDESYKSIFEPVIKHVMEWYQPEAVVLQCGGDS 258

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 217272877 263 LEGDRLGGLSISPAGivkrDELVFRMVRGRRVPILMVTSGGYQKR 307
Cdd:cd10004  259 LSGDRLGCFNLSMKG----HANCVNFVKSFNLPMLVLGGGGYTMR 299
PTZ00346 PTZ00346
histone deacetylase; Provisional
 69-307 1.99e-14

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 73.91  E-value: 1.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  69 EDLLVVHTRRYLNELK--------WSFAVATI---TEIPPViflpNFLVQRKVLRPLRTQTGGTIM-AGKLAVERGWain 136
Cdd:PTZ00346  77 EELMAYHTDTYLANLGlhscrswlWNAETSKVffsGDCPPV----EGLMEHSIATASGTLMGAVLLnSGQVDVAVHW--- 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 137 vGGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDV--YNRHIYPGD-- 212
Cdd:PTZ00346 150 -GGGMHHSKCGECSGFCYVNDIVLGI---LELLKCHDRVLYVDIDMHHGDGVDEAFCTSDRVFTLSLhkFGESFFPGTgh 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 213 -RFAKQAIRRKVELE---W-GTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVKrdelVFR 287
Cdd:PTZ00346 226 pRDVGYGRGRYYSMNlavWdGITDFYYLGLFEHALHSIVRRYSPDAIVLQCGADSLAGDRLGLLNLSSFGHGQ----CVQ 301

                        250       260
                 ....*....|....*....|
gi 217272877 288 MVRGRRVPILMVTSGGYQKR 307
Cdd:PTZ00346 302 AVRDLGIPMLALGGGGYTIR 321
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
 27-274 5.20e-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: 69.63  E-value: 5.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  27 TFM-------GLEKLHPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRY--------LNELKWSFA--V 89
Cdd:cd10007   11 TFMlkhqctcGNTNVHPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHSEHHtllygtspLNRQKLDSKklL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  90 ATITE----IPPV--IFLPNFLVQRKVLRP--LRTQTGGTI-MAGKLA---VERGWAINVGGGfHHCSSDRGGGFCAYAD 157
Cdd:cd10007   91 GPLSQkmyaVLPCggIGVDSDTVWNEMHSSsaVRMAVGCLIeLAFKVAageLKNGFAVIRPPG-HHAEESTAMGFCFFNS 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 158 ITLAIKFLFERVeGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVY---NRHIYPGDRFAKQ-----AIRRKVELEW-- 227
Cdd:cd10007  170 VAIAAKLLQQKL-NVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHrydDGNFFPGSGAPDEvgagpGVGFNVNIAWtg 248

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 217272877 228 GTE----DDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDR--LGGLSIS 274
Cdd:cd10007  249 GVDppigDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGHQspLGGYSVT 301
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
 35-274 6.90e-13

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: 68.88  E-value: 6.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  35 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRY--------LNELKW-SFAVATITEIPPVIFLP--- 102
Cdd:cd10008   24 HPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHvllygtnpLSRLKLdNGKLAGLLAQRMFVMLPcgg 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 103 ---------NFLVQRKVLRplrtQTGGTI--MAGKLA---VERGWAINVGGGfHHCSSDRGGGFCAYADITLAIKFLFER 168
Cdd:cd10008  104 vgvdtdtiwNELHSSNAAR----WAAGSVtdLAFKVAsreLKNGFAVVRPPG-HHADHSTAMGFCFFNSVAIACRQLQQQ 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 169 VEgISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYnRH----IYPGDRFAKQAIRR-----KVELEW--GTE----DDE 233
Cdd:cd10008  179 GK-ASKILIVDWDVHHGNGTQQTFYQDPSVLYISLH-RHddgnFFPGSGAVDEVGAGsgegfNVNVAWagGLDppmgDPE 256

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 217272877 234 YLDKVERNIKKSLQEHLPDVVVYNAGTDILEGD--RLGGLSIS 274
Cdd:cd10008  257 YLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHpaPLGGYHVS 299
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
 35-304 1.26e-12

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: 68.12  E-value: 1.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  35 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYlnELKWSFAVATITEIPPVIFLPNflVQRKVLRPL 114
Cdd:cd10009   24 HPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHH--SLLYGTNPLDGQKLDPRILLGD--DSQKFFSSL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 115 ----------------------RTQTGGTI-MAGKLA---VERGWAINVGGGfHHCSSDRGGGFCAYADITLAIKFLFER 168
Cdd:cd10009  100 pcgglgvdsdtiwnelhssgaaRMAVGCVIeLASKVAsgeLKNGFAVVRPPG-HHAEESTAMGFCFFNSVAITAKYLRDQ 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 169 VEgISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYNR---HIYPGDRFAKQAIR-----RKVELEW--GTE----DDEY 234
Cdd:cd10009  179 LN-ISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdegNFFPGSGAPNEVGTglgegYNINIAWtgGLDppmgDVEY 257

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 217272877 235 LDKVERNIKKSLQEHLPDVVVYNAGTDILEGDR--LGGLSISPAGIVKRDELVFRMVRGRrvpILMVTSGGY 304
Cdd:cd10009  258 LEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTppLGGYKVTAKCFGHLTKQLMTLADGR---VVLALEGGH 326
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
 30-274 1.40e-11

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: 65.06  E-value: 1.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  30 GLEKLHPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRY--------LNELKWSFAVATITEIPPVIFL 101
Cdd:cd10006   22 GNSNSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHtllygtnpLNRQKLDSKKLLGSLASVFVRL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 102 P--NFLVQRKVLRPLRTQTGGTIMAGKLAVERGWAINVG---GGF-------HHCSSDRGGGFCAYADITLAIKFLFERV 169
Cdd:cd10006  102 PcgGVGVDSDTIWNEVHSSGAARLAVGCVVELVFKVATGelkNGFavvrppgHHAEESTPMGFCYFNSVAIAAKLLQQRL 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 170 EgISRATIIDLDAHQGNGHERDFMDDKRVYIMDVY---NRHIYPGDRFAKQ-----AIRRKVELEW--GTE----DDEYL 235
Cdd:cd10006  182 N-VSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHrydDGNFFPGSGAPDEvgtgpGVGFNVNMAFtgGLDppmgDAEYL 260

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 217272877 236 DKVERNIKKSLQEHLPDVVVYNAGTDILEGD--RLGGLSIS 274
Cdd:cd10006  261 AAFRTVVMPIASEFAPDVVLVSSGFDAVEGHptPLGGYNLS 301
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 35-304 1.35e-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: 61.98  E-value: 1.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  35 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRY--------LNELKWSfavATITEIPPvifLPNFLV 106
Cdd:cd11681   24 HPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHtllygtnpLSRLKLD---PTKLAGLP---QKSFVR 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 107 ---------QRKVLRPLRTQTGGTIMAG-----KLAVERGWAINvggGF-------HHCSSDRGGGFCAYADITLAIKFL 165
Cdd:cd11681   98 lpcggigvdSDTVWNELHTSNAARMAVGcvidlAFKVATGELKN---GFavvrppgHHAEPSQAMGFCFFNSVAIAAKQL 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 166 FERVeGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYnRH----IYPG----DRFAKQA-IRRKVELEW------GTE 230
Cdd:cd11681  175 QQKL-KLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLH-RYddgnFFPGtgapTEVGSGAgEGFNVNIAWsggldpPMG 252

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 217272877 231 DDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEG--DRLGGLSISPAGIVKRDELVFRMVRGRrvpILMVTSGGY 304
Cdd:cd11681  253 DAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGhpPPLGGYKVSPACFGYMTRQLMNLAGGK---VVLALEGGY 325
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 49-337 2.86e-09

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: 57.56  E-value: 2.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877  49 LKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKwSFAVATITEI-------PPVIFLPNFLVQRKVLRPLRTQTGGT 121
Cdd:cd11683   21 LRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVR-ETQVMNKEELmaisgkyDAVYFHPNTFHCARLAAGATLQLVDA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 122 IMAGKlaVERGWAINVGGGfHHCSSDRGGGFCAYADITLAIKFLfERVEGISRATIIDLDAHQGNGHERDFMDDKRVYim 201
Cdd:cd11683  100 VLTGE--VQNGMALVRPPG-HHSQRNAANGFCVFNNVAIAAEYA-KKKYGLHRILIVDWDVHHGQGIQYIFEEDPSVL-- 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272877 202 dVYNRHIYPGDRF-------AKQAIRR------KVELEW---GTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEG 265
Cdd:cd11683  174 -YFSWHRYEHQRFwpflresDYDAVGRgkglgfNINLPWnkvGMGNADYLAAFFHVLLPLAFEFDPELVLVSAGFDSAIG 252

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 217272877 266 DRLGGLSISPAGIVKRDELVFRMVRGRRVPILmvtSGGYQKRT-ARIIADSILNLFG---LGLIGPESPSVSAQNS 337
Cdd:cd11683  253 DPEGQMCATPECFAHLTHLLMVLAGGKLCAVL---EGGYHLESlAESVCMTVQTLLGdplPRLSGEMTPCQSALES 325
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
 142-187 1.41e-04

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: 1.41e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 217272877 142 HHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNG 187
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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