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Conserved domains on  [gi|209862883|ref|NP_001129513|]
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histone deacetylase 11 isoform 2 [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 ...
 7-268 7.96e-135

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: 382.62  E-value: 7.96e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883   7 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKR-----------------KVLRPLRTQTGG 69
Cdd:cd09993    1 HRFPMRKYGLLREALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLESLKSgelsreeirrigfpwspELVERTRLAVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  70 TIMAGKLAVERGWAINVGGGFHHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNGHERDFMDDKRVYI 149
Cdd:cd09993   81 TILAARLALEHGLAINLAGGTHHAFPDRGEGFCVFNDIAIAARVLLAE-GLVRRVLIVDLDVHQGNGTAAIFADDPSVFT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 150 MDVYNRHIYPGDrfaKQAIRRKVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVK 229
Cdd:cd09993  160 FSMHGEKNYPFR---KEPSDLDVPLPDGTGDDEYLAALEEALPRLLAEFRPDLVFYNAGVDVLAGDRLGRLSLSLEGLRE 236

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 209862883 230 RDELVFRMVRGRRVPILMVTSGGYQKRTARIIADSILNL 268
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 ...
 7-268 7.96e-135

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: 382.62  E-value: 7.96e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883   7 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKR-----------------KVLRPLRTQTGG 69
Cdd:cd09993    1 HRFPMRKYGLLREALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLESLKSgelsreeirrigfpwspELVERTRLAVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  70 TIMAGKLAVERGWAINVGGGFHHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNGHERDFMDDKRVYI 149
Cdd:cd09993   81 TILAARLALEHGLAINLAGGTHHAFPDRGEGFCVFNDIAIAARVLLAE-GLVRRVLIVDLDVHQGNGTAAIFADDPSVFT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 150 MDVYNRHIYPGDrfaKQAIRRKVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVK 229
Cdd:cd09993  160 FSMHGEKNYPFR---KEPSDLDVPLPDGTGDDEYLAALEEALPRLLAEFRPDLVFYNAGVDVLAGDRLGRLSLSLEGLRE 236

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 209862883 230 RDELVFRMVRGRRVPILMVTSGGYQKRTARIIADSILNL 268
Cdd:cd09993  237 RDRLVLRFARARGIPVAMVLGGGYSRDIARLVARHAQTL 275
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 7-269 1.21e-61

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: 197.07  E-value: 1.21e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883    7 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKRKVLR----------------PL------- 63
Cdd:pfam00850   1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAAPEggallllsylsgdddtPVspgsyea 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883   64 -RTQTGGTIMAGKLAVE----RGWAINVGGGfHHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNGHE 138
Cdd:pfam00850  81 aLLAAGGTLAAADAVLSgearNAFALVRPPG-HHAERDRASGFCIFNNVAIAAKYLREK-YGLKRVAIVDFDVHHGNGTQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  139 RDFMDDKRVYIMDV--YNRHIYPGDRFAKQAIRRK-------VELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGT 209
Cdd:pfam00850 159 EIFYDDPSVLTLSIhqYPGGFYPGTGFADETGEGKgkgytlnVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAGF 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  210 DILEGDRLGGLSISPAGIVKRDELVFRMVRGRRVPILMVTSGGYqkrTARIIADSILNLF 269
Cdd:pfam00850 239 DAHAGDPLGGLNLTTEGFAEITRILLELADPLCIRVVSVLEGGY---NLDALARSATAVL 295
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 7-269 2.30e-59

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 191.47  E-value: 2.30e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883   7 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKRKVLR----------PL--------RTQTG 68
Cdd:COG0123   18 HPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAASLDggygqldpdtPVspgtweaaLLAAG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  69 GTIMAGKLAVERGWAI---NVGGGFHHCSSDRGGGFCAYADITLAIKFLfeRVEGISRATIIDLDAHQGNGHERDFMDDK 145
Cdd:COG0123   98 GALAAADAVLEGEARNafaLVRPPGHHAERDRAMGFCLFNNAAIAARYL--LAKGLERVAIVDFDVHHGNGTQDIFYDDP 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 146 RVYIMDVYNRHIYPGDRFAKQAIRRK-------VELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLG 218
Cdd:COG0123  176 DVLTISIHQDPLYPGTGAADETGEGAgegsnlnVPLPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHADDPLG 255

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 209862883 219 GLSISPAGIVKRDELVFRMVRGRRVPILMVTSGGYQKRTARIIADSILNLF 269
Cdd:COG0123  256 RLNLTTEGYAWRTRRVLELADHCGGPVVSVLEGGYNLDALARSVAAHLETL 306
PTZ00063 PTZ00063
histone deacetylase; Provisional
 84-256 4.85e-15

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 74.85  E-value: 4.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  84 INVGGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYN-RHIYPG-- 160
Cdd:PTZ00063 130 VNWSGGLHHAKRSEASGFCYINDIVLGI---LELLKYHARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKfGDFFPGtg 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 161 ---DRFAKQA--IRRKVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSISpagiVKRDELVF 235
Cdd:PTZ00063 207 dvtDIGVAQGkyYSVNVPLNDGIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLT----IKGHAACV 282

                        170       180
                 ....*....|....*....|.
gi 209862883 236 RMVRGRRVPILMVTSGGYQKR 256
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 ...
 7-268 7.96e-135

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: 382.62  E-value: 7.96e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883   7 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKR-----------------KVLRPLRTQTGG 69
Cdd:cd09993    1 HRFPMRKYGLLREALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLESLKSgelsreeirrigfpwspELVERTRLAVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  70 TIMAGKLAVERGWAINVGGGFHHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNGHERDFMDDKRVYI 149
Cdd:cd09993   81 TILAARLALEHGLAINLAGGTHHAFPDRGEGFCVFNDIAIAARVLLAE-GLVRRVLIVDLDVHQGNGTAAIFADDPSVFT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 150 MDVYNRHIYPGDrfaKQAIRRKVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVK 229
Cdd:cd09993  160 FSMHGEKNYPFR---KEPSDLDVPLPDGTGDDEYLAALEEALPRLLAEFRPDLVFYNAGVDVLAGDRLGRLSLSLEGLRE 236

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 209862883 230 RDELVFRMVRGRRVPILMVTSGGYQKRTARIIADSILNL 268
Cdd:cd09993  237 RDRLVLRFARARGIPVAMVLGGGYSRDIARLVARHAQTL 275
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
 13-268 4.34e-109

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: 317.45  E-value: 4.34e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  13 KWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELK-----------------------RKVLRPLRTQTGG 69
Cdd:cd09301    1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKanfavatiteskpvifgpnfpvqRHYFRGARLSTGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  70 TIMAGKLAVE----RGWAInVGGGFHHCSSDRGGGFCAYADITLAIKFLFERveGISRATIIDLDAHQGNGHERDFMDDK 145
Cdd:cd09301   81 VVEAAELVAKgeleRAFAV-VGAGGHHAGKSRAWGFCYFNDVVLAIKFLRER--GISRILIIDTDAHHGDGTREAFYDDD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 146 RVYIMDVYNRHIYPGDRFAKQAIRRKVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPA 225
Cdd:cd09301  158 RVLHMSFHNYDIYPFGRGKGKGYKINVPLEDGLGDEEYLDAVERVISKVLEEFEPEVVVLQFGHDTHEGDRLGGFNLSEK 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 209862883 226 GIVKRDELVFRMVRGrrVPILMVTSGGYQ-KRTARIIADSILNL 268
Cdd:cd09301  238 GFVKLAEIVKEFARG--GPILMVLGGGYNpEAAARIWTAIIKEL 279
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 7-269 1.21e-61

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: 197.07  E-value: 1.21e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883    7 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKRKVLR----------------PL------- 63
Cdd:pfam00850   1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAAPEggallllsylsgdddtPVspgsyea 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883   64 -RTQTGGTIMAGKLAVE----RGWAINVGGGfHHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNGHE 138
Cdd:pfam00850  81 aLLAAGGTLAAADAVLSgearNAFALVRPPG-HHAERDRASGFCIFNNVAIAAKYLREK-YGLKRVAIVDFDVHHGNGTQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  139 RDFMDDKRVYIMDV--YNRHIYPGDRFAKQAIRRK-------VELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGT 209
Cdd:pfam00850 159 EIFYDDPSVLTLSIhqYPGGFYPGTGFADETGEGKgkgytlnVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAGF 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  210 DILEGDRLGGLSISPAGIVKRDELVFRMVRGRRVPILMVTSGGYqkrTARIIADSILNLF 269
Cdd:pfam00850 239 DAHAGDPLGGLNLTTEGFAEITRILLELADPLCIRVVSVLEGGY---NLDALARSATAVL 295
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 7-269 2.30e-59

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 191.47  E-value: 2.30e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883   7 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKRKVLR----------PL--------RTQTG 68
Cdd:COG0123   18 HPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAASLDggygqldpdtPVspgtweaaLLAAG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  69 GTIMAGKLAVERGWAI---NVGGGFHHCSSDRGGGFCAYADITLAIKFLfeRVEGISRATIIDLDAHQGNGHERDFMDDK 145
Cdd:COG0123   98 GALAAADAVLEGEARNafaLVRPPGHHAERDRAMGFCLFNNAAIAARYL--LAKGLERVAIVDFDVHHGNGTQDIFYDDP 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 146 RVYIMDVYNRHIYPGDRFAKQAIRRK-------VELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLG 218
Cdd:COG0123  176 DVLTISIHQDPLYPGTGAADETGEGAgegsnlnVPLPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHADDPLG 255

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 209862883 219 GLSISPAGIVKRDELVFRMVRGRRVPILMVTSGGYQKRTARIIADSILNLF 269
Cdd:COG0123  256 RLNLTTEGYAWRTRRVLELADHCGGPVVSVLEGGYNLDALARSVAAHLETL 306
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
 7-260 3.58e-39

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: 139.62  E-value: 3.58e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883   7 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKRKVLRPL----------------------- 63
Cdd:cd09994   17 HPFNPPRLSLTKDLLRALGLLPPVDLVPPRPATEEELLLFHTPDYIEAVKEASRGQEpegrgrlglgtednpvfpgmhea 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  64 -RTQTGGTIMAGKLAVERGW--AINVGGGFHHCSSDRGGGFCAYADITLAIKFLFERveGISRATIIDLDAHQGNGHERD 140
Cdd:cd09994   97 aALVVGGTLLAARLVLEGEArrAFNPAGGLHHAMRGRASGFCVYNDAAVAIERLRDK--GGLRVAYVDIDAHHGDGVQAA 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 141 FMDDKRVYIMDV--YNRHIYPGDRFAKQAIRRK-------VELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDI 211
Cdd:cd09994  175 FYDDPRVLTISLheSGRYLFPGTGFVDEIGEGEgygyavnIPLPPGTGDDEFLRAFEAVVPPLLRAFRPDVIVSQHGADA 254

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 209862883 212 LEGDRLGGLSISPAGIVKrdelVFRMVR--------GRrvpILMVTSGGYQKR-TARI 260
Cdd:cd09994  255 HAGDPLTHLNLSNRAYRA----AVRRIReladeycgGR---WLALGGGGYNPDvVARA 305
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 26-253 5.30e-27

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: 108.19  E-value: 5.30e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  26 LLSDSMLVEAREASEEDLLVVHTRRYLNELKR---------------------------KVLRPLRTQTGGTIMAGKLAV 78
Cdd:cd10000   35 LLKQLRVVKPRVATEEELASFHSDEYIQFLKKasnegdndeepseqqefglgydcpifeGIYDYAAAVAGATLTAAQLLI 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  79 --ERGWAINVGGGFHHCSSDRGGGFCAYADITLAIKFLFERVEgisRATIIDLDAHQGNGHERDFMDDKRVYI--MDVYN 154
Cdd:cd10000  115 dgKCKVAINWFGGWHHAQRDEASGFCYVNDIVLGILKLREKFD---RVLYVDLDLHHGDGVEDAFSFTSKVMTvsLHKYS 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 155 RHIYPGDRFAKQAIRRK-------VELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGI 227
Cdd:cd10000  192 PGFFPGTGDVSDVGLGKgkyytvnVPLRDGIQDEQYLQIFTAVVPEIVAAFRPEAVVLQCGADTLAGDPMGAFNLTPVGI 271

                        250       260
                 ....*....|....*....|....*.
gi 209862883 228 VKrdelVFRMVRGRRVPILMVTSGGY 253
Cdd:cd10000  272 GK----CLKYVLGWKLPTLILGGGGY 293
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
 32-259 4.33e-26

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: 104.59  E-value: 4.33e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  32 LVEAREASEEDLLVVHTRRYLNELKR-------KVLRPL-------------------RTQTGGTIMAG-KLA-VERGWA 83
Cdd:cd09991   40 IYRPRPATAEELTKFHSDDYIDFLRSvspdnmkEFKKQLerfnvgedcpvfdglyeycQLYAGGSIAAAvKLNrGQADIA 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  84 INVGGGFHHCSSDRGGGFCAYADITLAIKFL---FERVegisraTIIDLDAHQGNGHERDFMDDKRVyiMDVyNRHIYPG 160
Cdd:cd09991  120 INWAGGLHHAKKSEASGFCYVNDIVLAILELlkyHQRV------LYIDIDIHHGDGVEEAFYTTDRV--MTV-SFHKFGE 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 161 DRFAKQAIR----RK-------VELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVK 229
Cdd:cd09991  191 YFFPGTGLRdigaGKgkyyavnVPLKDGIDDESYLQIFEPVLSKVMEVFQPSAVVLQCGADSLAGDRLGCFNLSIKGHAK 270

                        250       260       270
                 ....*....|....*....|....*....|.
gi 209862883 230 rdelVFRMVRGRRVPILMVTSGGYQKR-TAR 259
Cdd:cd09991  271 ----CVKFVKSFNIPLLVLGGGGYTLRnVAR 297
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
 17-253 2.08e-25

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: 102.19  E-value: 2.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  17 VINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKRKVLRPLRTQTG----------------GTIMAGKLAVER 80
Cdd:cd09992   11 ILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYIERVEETCEAGGGYLDPdtyvspgsyeaallaaGAALAAVDAVLS 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  81 GWAINvggGF-------HHCSSDRGGGFCAYADITLAIKFLFERVeGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVY 153
Cdd:cd09992   91 GEAEN---AFalvrppgHHAEPDRAMGFCLFNNVAIAARYAQKRY-GLKRVLIVDWDVHHGNGTQDIFYDDPSVLYFSIH 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 154 NRHIYPGDRFAKQAIRRK-------VELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAG 226
Cdd:cd09992  167 QYPFYPGTGAAEETGGGAgegftinVPLPPGSGDAEYLAAFEEVLLPIAREFQPDLVLVSAGFDAHRGDPLGGMNLTPEG 246

                        250       260       270
                 ....*....|....*....|....*....|...
gi 209862883 227 ------IVKrdELVFRMVRGRrvpILMVTSGGY 253
Cdd:cd09992  247 yarltrLLK--ELADEHCGGR---LVFVLEGGY 274
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 7-266 6.15e-25

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: 101.65  E-value: 6.15e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883   7 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKRKVLRP---LRTQT---------------- 67
Cdd:cd11600    3 HPEDPSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEHWDRVEATEKMSdeqLKDRTeiferdslyvnndtaf 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  68 ------GGTIMAGKlAVERGwaiNVGGGF-------HHCSSDRGGGFCAYADITLAIKFL-FERVEGISRATIIDLDAHQ 133
Cdd:cd11600   83 carlscGGAIEACR-AVAEG---RVKNAFavvrppgHHAEPDESMGFCFFNNVAVAAKWLqTEYPDKIKKILILDWDIHH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 134 GNGHERDFMDDKRV-YI-MDVY-NRHIYPGDRFAK-------QAIRRKVELEW---GTEDDEYLDKVERNIKKSLQEHLP 200
Cdd:cd11600  159 GNGTQRAFYDDPNVlYIsLHRFeNGGFYPGTPYGDyesvgegAGLGFNVNIPWpqgGMGDADYIYAFQRIVMPIAYEFDP 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 209862883 201 DVVVYNAGTDILEGDRLGGLSISPAGIVKRDELVFRMVRGRRVPILmvtSGGYQKRTariIADSIL 266
Cdd:cd11600  239 DLVIISAGFDAADGDELGQCHVTPAGYAHMTHMLMSLAGGKLVVAL---EGGYNLDA---ISDSAL 298
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
 32-253 1.72e-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: 97.34  E-value: 1.72e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  32 LVEAREASEEDLLVVHTRRYLNELKRKV-----------LRP-LRTQTGGTIMAGKL---AVERGWAINVGGGFHHCSSD 96
Cdd:cd11680   41 IIEPERATRKDLTKYHDKDYVDFLLKKYgleddcpvfpfLSMyVQLVAGSSLALAKHlitQVERDIAINWYGGRHHAQKS 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  97 RGGGFCAYADITLAIKFLfeRVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDV--YNRHIYPG-----DRFAKQAIr 169
Cdd:cd11680  121 RASGFCYVNDIVLAILRL--RRARFRRVFYLDLDLHHGDGVESAFFFSKNVLTCSIhrYDPGFFPGtgslkNSSDKGML- 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 170 rKVELEWGTeDDEYLDKVERNI-KKSLQEHLPDVVVYNAGTDILEGDRLG--GLSISPAGIVkrdeLVFRMVRGRRVPIL 246
Cdd:cd11680  198 -NIPLKRGL-SDKTLLRIIDSIvRPLIEKFEPEVIVIQCGCDGLSGDPHKewNLTIRGYGSV----IELLLKEFKDKPTL 271


                 ....*..
gi 209862883 247 MVTSGGY 253
Cdd:cd11680  272 LLGGGGY 278
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
 34-256 2.09e-21

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: 91.75  E-value: 2.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  34 EAREASEEDLLVVHTRRYLNELKR------KVLRPLRTQ---------------------TGGTIMAGKLAV--ERGWAI 84
Cdd:cd11598   45 EARAATREELRQFHDADYLDFLSKvspenaNQLRFDKAEpfnigddcpvfdgmydycqlyAGASLDAARKLCsgQSDIAI 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  85 NVGGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDV--YNRHIYPG-- 160
Cdd:cd11598  125 NWSGGLHHAKKSEASGFCYVNDIVLAI---LNLLRYFPRVLYIDIDVHHGDGVEEAFYRTDRVMTLSFhkYNGEFFPGtg 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 161 -------DRFAKQAIrrKVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSISpagIVKRDEL 233
Cdd:cd11598  202 dlddnggTPGKHFAL--NVPLEDGIDDEQYNLLFKSIIGPTIEKFQPSAIVLQCGADSLGGDRLGQFNLN---IKAHGAC 276

                        250       260
                 ....*....|....*....|...
gi 209862883 234 VfRMVRGRRVPILMVTSGGYQKR 256
Cdd:cd11598  277 V-KFVKSFGIPMLVVGGGGYTPR 298
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
 19-262 3.32e-21

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: 91.85  E-value: 3.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  19 NFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKRKVLRPLRTQTGGTIM------AGKLA--------------- 77
Cdd:cd09996   45 NLLEVSGLSDHLVLITPRPATDEELLRVHTPEYIDRVKAASAAGGGEAGGGTPFgpgsyeIALLAaggaiaavdavldge 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  78 VERGWAINVGGGfHHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYNRHI 157
Cdd:cd09996  125 VDNAYALVRPPG-HHAEPDQGMGFCLFNNVAIAARHALAV-GGVKRVAVVDWDVHHGNGTQAIFYDDPDVLTISLHQDRC 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 158 YPGDRFAKQAIRR--------KVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGglsispagivk 229
Cdd:cd09996  203 FPPDSGAVEERGEgagegynlNIPLPPGSGDGAYLHAFERIVLPALRAFRPELIIVASGFDASAFDPLG----------- 271

                        250       260       270
                 ....*....|....*....|....*....|...
gi 209862883 230 rdelvfRMvrgrrvpilMVTSGGYQKRTARIIA 262
Cdd:cd09996  272 ------RM---------MLTSDGFRALTRKLRD 289
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
 17-253 7.97e-21

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


Pssm-ID: 212525 [Multi-domain]  Cd Length: 298  Bit Score: 89.90  E-value: 7.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  17 VINFLKEEKLlsdSMLVEAREASEEDLLVVHTRRYLNELKRK---------VLRPLRTQTGGTIMAGKLAVE-RGWAINV 86
Cdd:cd10001   35 ILDALKRAGL---GEVLPPRDFGLEPILAVHDPDYVDFLETAdtdtpisegTWEAALAAADTALTAADLVLEgERAAYAL 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  87 G---GgfHHCSSDRGGGFCAYADITLAIKFLFERVEgisRATIIDLDAHQGNGHERDFMDDKRVYIMDV--YNRHIYPG- 160
Cdd:cd10001  112 CrppG--HHAGRDRAGGFCYFNNAAIAAQYLRDRAG---RVAILDVDVHHGNGTQEIFYERPDVLYVSIhgDPRTFYPFf 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 161 -----DRFAKQAIRRKVE--LEWGTEDDEYLDKVERNIKKsLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIvkrdEL 233
Cdd:cd10001  187 lgfadETGEGEGEGYNLNlpLPPGTGDDDYLAALDEALAA-IAAFGPDALVVSLGFDTHEGDPLSDFKLTTEDY----AR 261

                        250       260
                 ....*....|....*....|
gi 209862883 234 VFRMVRGRRVPILMVTSGGY 253
Cdd:cd10001  262 IGRRIAALGLPTVFVQEGGY 281
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
 4-253 7.09e-20

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: 88.16  E-value: 7.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883   4 EKLHPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKR---KVLRPL--------------RTQ 66
Cdd:cd10003   13 DPGHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHLDEMKSlekMKPRELnrlgkeydsiyihpDSY 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  67 TGGTIMAGKL-----AVERGWAINvGGGF-----HHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNG 136
Cdd:cd10003   93 QCALLAAGCVlqvveAVLTGESRN-GVAIvrppgHHAEQDTACGFCFFNNVAIAARYAQKK-YGLKRILIVDWDVHHGNG 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 137 HERDFMDDKRV-YI-MDVY-NRHIYPGDRFAKQAIRRK-------VELEW---GTEDDEYLDKVERNIKKSLQEHLPDVV 203
Cdd:cd10003  171 TQHMFESDPSVlYIsLHRYdNGSFFPNSPEGNYDVVGKgkgegfnVNIPWnkgGMGDAEYIAAFQQVVLPIAYEFNPELV 250

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 209862883 204 VYNAGTDILEGDRLGGLSISPAGIVKRDELVFRMVRGRrvpILMVTSGGY 253
Cdd:cd10003  251 LVSAGFDAARGDPLGGCKVTPEGYAHMTHMLMSLAGGR---VIVILEGGY 297
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
 32-221 1.35e-18

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: 83.72  E-value: 1.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  32 LVEAREASEEDLLVVHTRRYLNELKRKVLRPLRTQTGG-TIM-------------AGKLAVER---GWAINVgggF---- 90
Cdd:cd11599   26 QLEAPPATREQLLRVHDAAYVDRLEAAAPEEGLVQLDPdTAMspgsleaalraagAVVAAVDAvmaGEARNA---Fcavr 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  91 ---HHCSSDRGGGFCAYADITLAIKFLFERVeGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYNRHIYPGDRFAKQA 167
Cdd:cd11599  103 ppgHHAERDKAMGFCLFNNVAIAAAHALAHH-GLERVAIVDFDVHHGNGTEDIFRDDPRVLFCSSHQHPLYPGTGAPDET 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 209862883 168 IR---RKVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLS 221
Cdd:cd11599  182 GHgniVNVPLPAGTGGAEFREAVEDRWLPALDAFKPDLILISAGFDAHRDDPLAQLN 238
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
 7-286 4.13e-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: 82.98  E-value: 4.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883   7 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELK------RKVLRPLRTQ-----------TGG 69
Cdd:cd11682    7 FPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYVALMKstqymtEEELRTLADTydsvylhpnsySCA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  70 TIMAGKL--AVERGWAINVGGGF-------HHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNGHERD 140
Cdd:cd11682   87 CLAVGSVlqLVDKVLGGEIRNGLaivrppgHHAQHDKMDGYCMFNNVAIAARYAQQK-HGVQRVLIVDWDVHHGQGTQFI 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 141 FMDDKRVYIMDVynrHIYPGDRF-------------AKQAIRRKVELEW---GTEDDEYLDKVERNIKKSLQEHLPDVVV 204
Cdd:cd11682  166 FEQDPSVLYFSI---HRYEQGRFwphlkesdssavgFGRGEGYNINVPWnqvGMRDADYIAAFLHVLLPVALEFQPQLVL 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 205 YNAGTDILEGDRLGGLSISPAGIVKRDELVFRMVRGRrvpILMVTSGGYQKR-TARIIADSILNLFG---LGLIGPESPS 280
Cdd:cd11682  243 VAAGFDAVIGDPKGEMAATPACFAHLTHLLMGLAGGK---LILSLEGGYNLRsLAEGVCASLKALLGdpcPMLESPGAPC 319


                 ....*.
gi 209862883 281 VSAQNS 286
Cdd:cd11682  320 RSALAS 325
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
 67-256 1.43e-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: 81.65  E-value: 1.43e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  67 TGGTImAGKLAVER---GWAINVGGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMD 143
Cdd:cd10011  107 TGGSV-AGAVKLNRqqtDMAVNWAGGLHHAKKSEASGFCYVNDIVLAI---LELLKYHQRVLYIDIDIHHGDGVEEAFYT 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 144 DKRVY-IMDVYNRHIYPG-----DRFAKQAIRRKVELEW--GTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGD 215
Cdd:cd10011  183 TDRVMtVSFHKYGEYFPGtgdlrDIGAGKGKYYAVNFPMrdGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGD 262

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 209862883 216 RLGGLSISPAGIVKRDELvfrmVRGRRVPILMVTSGGYQKR 256
Cdd:cd10011  263 RLGCFNLTVKGHAKCVEV----VKTFNLPLLMLGGGGYTIR 299
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 21-253 2.53e-17

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: 80.82  E-value: 2.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  21 LKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKR------KVLRPLRTQ------TGGTIMAGKLAVerGWAIN--- 85
Cdd:cd10002   21 LTQDGLLERCVKIPAREAEEDEILLVHSQEYIDLVKStetmekEELESLCSGydsvylCPSTYEAARLAA--GSTIElvk 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  86 ------VGGGF-------HHCSSDRGGGFCAYADITLAIKFLFErVEGISRATIIDLDAHQGNGHERDFMDDKRVyimDV 152
Cdd:cd10002   99 avmagkIQNGFalirppgHHAMRNEANGYCIFNNVAIAAKYAIE-KLGLKRILIVDWDVHHGQGTQQGFYEDPRV---LY 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 153 YNRHIYPGDRF-------------AKQAIRRKVELEWGTE---DDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDR 216
Cdd:cd10002  175 FSIHRYEHGRFwphlfesdydyigVGHGYGFNVNVPLNQTglgDADYLAIFHHILLPLALEFQPELVLVSAGFDASIGDP 254

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 209862883 217 LGGLSISPAGIVKRDELVFRMVRGRrvpILMVTSGGY 253
Cdd:cd10002  255 EGEMAVTPAGYAHLTRLLMGLAGGK---LLLVLEGGY 288
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
 83-256 1.61e-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: 78.98  E-value: 1.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  83 AINVGGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMDDKRVyiMDV----YNRHIY 158
Cdd:cd10005  124 AINWSGGLHHAKKFEASGFCYVNDIVIAI---LELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRV--MTVsfhkYGNYFF 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 159 P--GDRFAKQAIRRK-----VELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGivkRD 231
Cdd:cd10005  199 PgtGDMYEVGAESGRyysvnVPLKDGIDDQSYLQLFKPVIQQVIDFYQPTCIVLQCGADSLGCDRLGCFNLSIKG---HG 275

                        170       180
                 ....*....|....*....|....*
gi 209862883 232 ELVfRMVRGRRVPILMVTSGGYQKR 256
Cdd:cd10005  276 ECV-EFVKSFNIPLLVLGGGGYTVR 299
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
 67-256 2.93e-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: 2.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  67 TGGTIMAG-KLAVER-GWAINVGGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMDD 144
Cdd:cd10010  111 AGGSVASAvKLNKQQtDIAVNWAGGLHHAKKSEASGFCYVNDIVLAI---LELLKYHQRVLYIDIDIHHGDGVEEAFYTT 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 145 KRVYIMDVYNR-HIYPG-----DRFAKQAIRRKVE--LEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDR 216
Cdd:cd10010  188 DRVMTVSFHKYgEYFPGtgdlrDIGAGKGKYYAVNypLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGADSLSGDR 267

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 209862883 217 LGGLSISPAGIVKRDELvfrmVRGRRVPILMVTSGGYQKR 256
Cdd:cd10010  268 LGCFNLTIKGHAKCVEF----VKSFNLPMLMLGGGGYTIR 303
PTZ00063 PTZ00063
histone deacetylase; Provisional
 84-256 4.85e-15

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 74.85  E-value: 4.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  84 INVGGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYN-RHIYPG-- 160
Cdd:PTZ00063 130 VNWSGGLHHAKRSEASGFCYINDIVLGI---LELLKYHARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKfGDFFPGtg 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 161 ---DRFAKQA--IRRKVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSISpagiVKRDELVF 235
Cdd:PTZ00063 207 dvtDIGVAQGkyYSVNVPLNDGIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLT----IKGHAACV 282

                        170       180
                 ....*....|....*....|.
gi 209862883 236 RMVRGRRVPILMVTSGGYQKR 256
Cdd:PTZ00063 283 EFVRSLNIPLLVLGGGGYTIR 303
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
 67-256 7.07e-15

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: 74.07  E-value: 7.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  67 TGGTIMAGKLAVERG---WAINVGGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMD 143
Cdd:cd10004  106 SAGGSMEGAARLNRGkcdIAVNWAGGLHHAKKSEASGFCYVNDIVLGI---LELLRYHQRVLYIDIDVHHGDGVEEAFYT 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 144 DKRVyiMDVyNRHIYpGDRFAKQAIRR------------KVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDI 211
Cdd:cd10004  183 TDRV--MTC-SFHKY-GEYFPGTGELRdigigtgknyavNVPLRDGIDDESYKSIFEPVIKHVMEWYQPEAVVLQCGGDS 258

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 209862883 212 LEGDRLGGLSISPAGivkrDELVFRMVRGRRVPILMVTSGGYQKR 256
Cdd:cd10004  259 LSGDRLGCFNLSMKG----HANCVNFVKSFNLPMLVLGGGGYTMR 299
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
 2-223 2.09e-14

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: 72.71  E-value: 2.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883   2 GLEKLHPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRY--------LNELK---RKVLRPL------- 63
Cdd:cd10007   21 GNTNVHPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHSEHHtllygtspLNRQKldsKKLLGPLsqkmyav 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  64 -----------------------RTQTGGTI-MAGKLA---VERGWAINVGGGfHHCSSDRGGGFCAYADITLAIKFLFE 116
Cdd:cd10007  101 lpcggigvdsdtvwnemhsssavRMAVGCLIeLAFKVAageLKNGFAVIRPPG-HHAEESTAMGFCFFNSVAIAAKLLQQ 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 117 RVeGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVY---NRHIYPGDRFAKQ-----AIRRKVELEW--GTE----DDE 182
Cdd:cd10007  180 KL-NVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHrydDGNFFPGSGAPDEvgagpGVGFNVNIAWtgGVDppigDVE 258

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 209862883 183 YLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDR--LGGLSIS 223
Cdd:cd10007  259 YLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGHQspLGGYSVT 301
PTZ00346 PTZ00346
histone deacetylase; Provisional
 83-256 8.46e-14

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 71.22  E-value: 8.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  83 AINVGGGFHHCSSDRGGGFCAYADITLAIkflFERVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDV--YNRHIYPG 160
Cdd:PTZ00346 146 AVHWGGGMHHSKCGECSGFCYVNDIVLGI---LELLKCHDRVLYVDIDMHHGDGVDEAFCTSDRVFTLSLhkFGESFFPG 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 161 D---RFAKQAIRRKVELE---W-GTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVKrdel 233
Cdd:PTZ00346 223 TghpRDVGYGRGRYYSMNlavWdGITDFYYLGLFEHALHSIVRRYSPDAIVLQCGADSLAGDRLGLLNLSSFGHGQ---- 298

                        170       180
                 ....*....|....*....|...
gi 209862883 234 VFRMVRGRRVPILMVTSGGYQKR 256
Cdd:PTZ00346 299 CVQAVRDLGIPMLALGGGGYTIR 321
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
 7-223 1.61e-12

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: 66.96  E-value: 1.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883   7 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRY--------LNELK---RKVLRPLRTQTGGTIMAGK 75
Cdd:cd10008   24 HPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHvllygtnpLSRLKldnGKLAGLLAQRMFVMLPCGG 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  76 LAVERG-------------WAI-------------NVGGGF-------HHCSSDRGGGFCAYADITLAIKFLFERVEgIS 122
Cdd:cd10008  104 VGVDTDtiwnelhssnaarWAAgsvtdlafkvasrELKNGFavvrppgHHADHSTAMGFCFFNSVAIACRQLQQQGK-AS 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 123 RATIIDLDAHQGNGHERDFMDDKRVYIMDVYnRH----IYPGDRFAKQAIRR-----KVELEW--GTE----DDEYLDKV 187
Cdd:cd10008  183 KILIVDWDVHHGNGTQQTFYQDPSVLYISLH-RHddgnFFPGSGAVDEVGAGsgegfNVNVAWagGLDppmgDPEYLAAF 261

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 209862883 188 ERNIKKSLQEHLPDVVVYNAGTDILEGD--RLGGLSIS 223
Cdd:cd10008  262 RIVVMPIAREFSPDLVLVSAGFDAAEGHpaPLGGYHVS 299
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
 2-223 1.86e-12

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


Pssm-ID: 212530 [Multi-domain]  Cd Length: 409  Bit Score: 66.98  E-value: 1.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883   2 GLEKLHPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYL-----NELKRKVLRP-----------LRT 65
Cdd:cd10006   22 GNSNSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTllygtNPLNRQKLDSkkllgslasvfVRL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  66 QTGG------TIM-------AGKLAV---------------ERGWAINVGGGfHHCSSDRGGGFCAYADITLAIKFLFER 117
Cdd:cd10006  102 PCGGvgvdsdTIWnevhssgAARLAVgcvvelvfkvatgelKNGFAVVRPPG-HHAEESTPMGFCYFNSVAIAAKLLQQR 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 118 VEgISRATIIDLDAHQGNGHERDFMDDKRVYIMDVY---NRHIYPGDRFAKQ-----AIRRKVELEW--GTE----DDEY 183
Cdd:cd10006  181 LN-VSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHrydDGNFFPGSGAPDEvgtgpGVGFNVNMAFtgGLDppmgDAEY 259

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 209862883 184 LDKVERNIKKSLQEHLPDVVVYNAGTDILEGD--RLGGLSIS 223
Cdd:cd10006  260 LAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHptPLGGYNLS 301
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
 7-253 3.86e-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: 65.81  E-value: 3.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883   7 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRY-----LNELKRKVLRP------------------- 62
Cdd:cd10009   24 HPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHsllygTNPLDGQKLDPrillgddsqkffsslpcgg 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  63 -----------------LRTQTGGTI-MAGKLA---VERGWAINVGGGfHHCSSDRGGGFCAYADITLAIKFLFERVEgI 121
Cdd:cd10009  104 lgvdsdtiwnelhssgaARMAVGCVIeLASKVAsgeLKNGFAVVRPPG-HHAEESTAMGFCFFNSVAITAKYLRDQLN-I 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 122 SRATIIDLDAHQGNGHERDFMDDKRVYIMDVYNR---HIYPGDRFAKQAIR-----RKVELEW--GTE----DDEYLDKV 187
Cdd:cd10009  182 SKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdegNFFPGSGAPNEVGTglgegYNINIAWtgGLDppmgDVEYLEAF 261

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 209862883 188 ERNIKKSLQEHLPDVVVYNAGTDILEGDR--LGGLSISPAGIVKRDELVFRMVRGRrvpILMVTSGGY 253
Cdd:cd10009  262 RTIVKPVAKEFDPDMVLVSAGFDALEGHTppLGGYKVTAKCFGHLTKQLMTLADGR---VVLALEGGH 326
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 7-253 3.85e-11

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: 62.75  E-value: 3.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883   7 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYL-----NELKRKVLRP-----------LRTQTGG- 69
Cdd:cd11681   24 HPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTllygtNPLSRLKLDPtklaglpqksfVRLPCGGi 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  70 ------------TIMAGKLAV---------------ERGWAINVGGGfHHCSSDRGGGFCAYADITLAIKFLFERVeGIS 122
Cdd:cd11681  104 gvdsdtvwnelhTSNAARMAVgcvidlafkvatgelKNGFAVVRPPG-HHAEPSQAMGFCFFNSVAIAAKQLQQKL-KLR 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 123 RATIIDLDAHQGNGHERDFMDDKRVYIMDVYnRH----IYPG----DRFAKQA-IRRKVELEW------GTEDDEYLDKV 187
Cdd:cd11681  182 KILIVDWDVHHGNGTQQIFYEDPNVLYISLH-RYddgnFFPGtgapTEVGSGAgEGFNVNIAWsggldpPMGDAEYLAAF 260

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 209862883 188 ERNIKKSLQEHLPDVVVYNAGTDILEG--DRLGGLSISPAGIVKRDELVFRMVRGRrvpILMVTSGGY 253
Cdd:cd11681  261 RTVVMPIAREFSPDIVLVSAGFDAAEGhpPPLGGYKVSPACFGYMTRQLMNLAGGK---VVLALEGGY 325
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 21-286 1.48e-08

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: 54.87  E-value: 1.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  21 LKEEKLLSDSMLVEAREASEEDLLVVHTRRYLN-----------ELKR------------KVLRPLRTQTGGT------I 71
Cdd:cd11683   21 LRQYGLVQRCLRLPAREASEEEILLVHSPEYLSlvretqvmnkeELMAisgkydavyfhpNTFHCARLAAGATlqlvdaV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883  72 MAGKlaVERGWAINVGGGfHHCSSDRGGGFCAYADITLAIKFLfERVEGISRATIIDLDAHQGNGHERDFMDDKRVYimd 151
Cdd:cd11683  101 LTGE--VQNGMALVRPPG-HHSQRNAANGFCVFNNVAIAAEYA-KKKYGLHRILIVDWDVHHGQGIQYIFEEDPSVL--- 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862883 152 VYNRHIYPGDRF-------AKQAIRR------KVELEW---GTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGD 215
Cdd:cd11683  174 YFSWHRYEHQRFwpflresDYDAVGRgkglgfNINLPWnkvGMGNADYLAAFFHVLLPLAFEFDPELVLVSAGFDSAIGD 253

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 209862883 216 RLGGLSISPAGIVKRDELVFRMVRGRRVPILmvtSGGYQKRT-ARIIADSILNLFG---LGLIGPESPSVSAQNS 286
Cdd:cd11683  254 PEGQMCATPECFAHLTHLLMVLAGGKLCAVL---EGGYHLESlAESVCMTVQTLLGdplPRLSGEMTPCQSALES 325
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
 91-136 1.05e-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: 1.05e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 209862883  91 HHCSSDRGGGFCAYADITLAIKFLFERvEGISRATIIDLDAHQGNG 136
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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