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Conserved domains on  [gi|966925567|ref|XP_014985599|]
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histone deacetylase 11 isoform X7 [Macaca mulatta]

Protein Classification

histone deacetylase( domain architecture ID 10177964)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 35-240 8.66e-88

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: 262.05  E-value: 8.66e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  35 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKF------------------LFERV------ 90
Cdd:cd09993    1 HRFPMRKYGLLREALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLESLKSgelsreeirrigfpwspeLVERTrlavgg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  91 -----------------------------EG-------------------ISRATIIDLDAHQGNGHERDFMDDKRVYIM 122
Cdd:cd09993   81 tilaarlalehglainlaggthhafpdrgEGfcvfndiaiaarvllaeglVRRVLIVDLDVHQGNGTAAIFADDPSVFTF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567 123 DVYNRHIYPGDrfaKQAIRRKVELEWGTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVKR 202
Cdd:cd09993  161 SMHGEKNYPFR---KEPSDLDVPLPDGTGDDEYLAALEEALPRLLAEFRPDLVFYNAGVDVLAGDRLGRLSLSLEGLRER 237

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 966925567 203 DELVFRMVRGRHVPILMVTSGGYQKRTARIIADSILNL 240
Cdd:cd09993  238 DRLVLRFARARGIPVAMVLGGGYSRDIARLVARHAQTL 275
 
Name Accession Description Interval E-value
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 35-240 8.66e-88

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: 262.05  E-value: 8.66e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  35 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKF------------------LFERV------ 90
Cdd:cd09993    1 HRFPMRKYGLLREALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLESLKSgelsreeirrigfpwspeLVERTrlavgg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  91 -----------------------------EG-------------------ISRATIIDLDAHQGNGHERDFMDDKRVYIM 122
Cdd:cd09993   81 tilaarlalehglainlaggthhafpdrgEGfcvfndiaiaarvllaeglVRRVLIVDLDVHQGNGTAAIFADDPSVFTF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567 123 DVYNRHIYPGDrfaKQAIRRKVELEWGTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVKR 202
Cdd:cd09993  161 SMHGEKNYPFR---KEPSDLDVPLPDGTGDDEYLAALEEALPRLLAEFRPDLVFYNAGVDVLAGDRLGRLSLSLEGLRER 237

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 966925567 203 DELVFRMVRGRHVPILMVTSGGYQKRTARIIADSILNL 240
Cdd:cd09993  238 DRLVLRFARARGIPVAMVLGGGYSRDIARLVARHAQTL 275
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 17-241 8.14e-39

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 137.55  E-value: 8.14e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  17 PIVYSPRYNITFMGleKLHPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELK------------ 84
Cdd:COG0123    2 ALIYHPDYLLHDLG--PGHPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRaasldggygqld 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  85 -------FLFERV--------------------------------------------------------EGISRATIIDL 101
Cdd:COG0123   80 pdtpvspGTWEAAllaaggalaaadavlegearnafalvrppghhaerdramgfclfnnaaiaaryllaKGLERVAIVDF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567 102 DAHQGNGHERDFMDDKRVYIMDVYNRHIYPGDRFAKQAIRRK-------VELEWGTEDDEYLDKVERNIEKSLQEHLPDV 174
Cdd:COG0123  160 DVHHGNGTQDIFYDDPDVLTISIHQDPLYPGTGAADETGEGAgegsnlnVPLPPGTGDAEYLAALEEALLPALEAFKPDL 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966925567 175 VVYNAGTDILEGDRLGGLSISPAGIVKRDELVFRMVRGRHVPILMVTSGGYQKRTARIIADSILNLF 241
Cdd:COG0123  240 IVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELADHCGGPVVSVLEGGYNLDALARSVAAHLETL 306
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 35-241 5.93e-37

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: 132.36  E-value: 5.93e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567   35 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELK---------------------FLFE----- 88
Cdd:pfam00850   1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEeaapeggallllsylsgdddtPVSPgsyea 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567   89 --------------------------------------------------------RVEGISRATIIDLDAHQGNGHERD 112
Cdd:pfam00850  81 allaaggtlaaadavlsgearnafalvrppghhaerdrasgfcifnnvaiaakylrEKYGLKRVAIVDFDVHHGNGTQEI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  113 FMDDKRVYIMDV--YNRHIYPGDRFAKQAIRRK-------VELEWGTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDI 183
Cdd:pfam00850 161 FYDDPSVLTLSIhqYPGGFYPGTGFADETGEGKgkgytlnVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAGFDA 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 966925567  184 LEGDRLGGLSISPAGIVKRDELVFRMVRGRHVPILMVTSGGYqkrTARIIADSILNLF 241
Cdd:pfam00850 241 HAGDPLGGLNLTTEGFAEITRILLELADPLCIRVVSVLEGGY---NLDALARSATAVL 295
PTZ00063 PTZ00063
histone deacetylase; Provisional
 79-228 4.94e-08

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 53.28  E-value: 4.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  79 YLNELKF-LFERVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYN-RHIYPG-----DRFAKQA--IRRKVELEWG 149
Cdd:PTZ00063 149 YINDIVLgILELLKYHARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKfGDFFPGtgdvtDIGVAQGkyYSVNVPLNDG 228

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966925567 150 TEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLGGLSISpagiVKRDELVFRMVRGRHVPILMVTSGGYQKR 228
Cdd:PTZ00063 229 IDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLT----IKGHAACVEFVRSLNIPLLVLGGGGYTIR 303
 
Name Accession Description Interval E-value
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 35-240 8.66e-88

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: 262.05  E-value: 8.66e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  35 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKF------------------LFERV------ 90
Cdd:cd09993    1 HRFPMRKYGLLREALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLESLKSgelsreeirrigfpwspeLVERTrlavgg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  91 -----------------------------EG-------------------ISRATIIDLDAHQGNGHERDFMDDKRVYIM 122
Cdd:cd09993   81 tilaarlalehglainlaggthhafpdrgEGfcvfndiaiaarvllaeglVRRVLIVDLDVHQGNGTAAIFADDPSVFTF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567 123 DVYNRHIYPGDrfaKQAIRRKVELEWGTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVKR 202
Cdd:cd09993  161 SMHGEKNYPFR---KEPSDLDVPLPDGTGDDEYLAALEEALPRLLAEFRPDLVFYNAGVDVLAGDRLGRLSLSLEGLRER 237

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 966925567 203 DELVFRMVRGRHVPILMVTSGGYQKRTARIIADSILNL 240
Cdd:cd09993  238 DRLVLRFARARGIPVAMVLGGGYSRDIARLVARHAQTL 275
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
 41-240 2.21e-74

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: 228.09  E-value: 2.21e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  41 KWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNEL------------------------------------- 83
Cdd:cd09301    1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELkanfavatiteskpvifgpnfpvqrhyfrgarlstgg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  84 ---------------------------------------------KFLFERveGISRATIIDLDAHQGNGHERDFMDDKR 118
Cdd:cd09301   81 vveaaelvakgelerafavvgagghhagksrawgfcyfndvvlaiKFLRER--GISRILIIDTDAHHGDGTREAFYDDDR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567 119 VYIMDVYNRHIYPGDRFAKQAIRRKVELEWGTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAG 198
Cdd:cd09301  159 VLHMSFHNYDIYPFGRGKGKGYKINVPLEDGLGDEEYLDAVERVISKVLEEFEPEVVVLQFGHDTHEGDRLGGFNLSEKG 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 966925567 199 IVKRDELVFRMVRGrhVPILMVTSGGYQ-KRTARIIADSILNL 240
Cdd:cd09301  239 FVKLAEIVKEFARG--GPILMVLGGGYNpEAAARIWTAIIKEL 279
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 17-241 8.14e-39

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 137.55  E-value: 8.14e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  17 PIVYSPRYNITFMGleKLHPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELK------------ 84
Cdd:COG0123    2 ALIYHPDYLLHDLG--PGHPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRaasldggygqld 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  85 -------FLFERV--------------------------------------------------------EGISRATIIDL 101
Cdd:COG0123   80 pdtpvspGTWEAAllaaggalaaadavlegearnafalvrppghhaerdramgfclfnnaaiaaryllaKGLERVAIVDF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567 102 DAHQGNGHERDFMDDKRVYIMDVYNRHIYPGDRFAKQAIRRK-------VELEWGTEDDEYLDKVERNIEKSLQEHLPDV 174
Cdd:COG0123  160 DVHHGNGTQDIFYDDPDVLTISIHQDPLYPGTGAADETGEGAgegsnlnVPLPPGTGDAEYLAALEEALLPALEAFKPDL 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966925567 175 VVYNAGTDILEGDRLGGLSISPAGIVKRDELVFRMVRGRHVPILMVTSGGYQKRTARIIADSILNLF 241
Cdd:COG0123  240 IVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELADHCGGPVVSVLEGGYNLDALARSVAAHLETL 306
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 35-241 5.93e-37

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: 132.36  E-value: 5.93e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567   35 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELK---------------------FLFE----- 88
Cdd:pfam00850   1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEeaapeggallllsylsgdddtPVSPgsyea 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567   89 --------------------------------------------------------RVEGISRATIIDLDAHQGNGHERD 112
Cdd:pfam00850  81 allaaggtlaaadavlsgearnafalvrppghhaerdrasgfcifnnvaiaakylrEKYGLKRVAIVDFDVHHGNGTQEI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  113 FMDDKRVYIMDV--YNRHIYPGDRFAKQAIRRK-------VELEWGTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDI 183
Cdd:pfam00850 161 FYDDPSVLTLSIhqYPGGFYPGTGFADETGEGKgkgytlnVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAGFDA 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 966925567  184 LEGDRLGGLSISPAGIVKRDELVFRMVRGRHVPILMVTSGGYqkrTARIIADSILNLF 241
Cdd:pfam00850 241 HAGDPLGGLNLTTEGFAEITRILLELADPLCIRVVSVLEGGY---NLDALARSATAVL 295
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
 18-232 5.13e-18

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: 81.84  E-value: 5.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  18 IVYSPRYNITFMGleKLHPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELK------------- 84
Cdd:cd09994    2 FIYSEEYLRYSFG--PNHPFNPPRLSLTKDLLRALGLLPPVDLVPPRPATEEELLLFHTPDYIEAVKeasrgqepegrgr 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  85 ----------F--LFERV-------------------------------------------------------EGISRAT 97
Cdd:cd09994   80 lglgtednpvFpgMHEAAalvvggtllaarlvlegearrafnpagglhhamrgrasgfcvyndaavaierlrdKGGLRVA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  98 IIDLDAHQGNGHERDFMDDKRVYIMDV--YNRHIYPGDRFAKQAIRRK-------VELEWGTEDDEYLDKVERNIEKSLQ 168
Cdd:cd09994  160 YVDIDAHHGDGVQAAFYDDPRVLTISLheSGRYLFPGTGFVDEIGEGEgygyavnIPLPPGTGDDEFLRAFEAVVPPLLR 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966925567 169 EHLPDVVVYNAGTDILEGDRLGGLSISPAGIVKrdelVFRMVR--------GRhvpILMVTSGGYQKR-TARI 232
Cdd:cd09994  240 AFRPDVIVSQHGADAHAGDPLTHLNLSNRAYRA----AVRRIReladeycgGR---WLALGGGGYNPDvVARA 305
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
 45-225 5.11e-13

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: 67.52  E-value: 5.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  45 VINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKFLFER-----------------------------VE---- 91
Cdd:cd09992   11 ILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYIERVEETCEAgggyldpdtyvspgsyeaallaagaalaaVDavls 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  92 ------------------------------------------GISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYNRHI 129
Cdd:cd09992   91 geaenafalvrppghhaepdramgfclfnnvaiaaryaqkryGLKRVLIVDWDVHHGNGTQDIFYDDPSVLYFSIHQYPF 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567 130 YPGDRFAKQAIRRK-------VELEWGTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAG---- 198
Cdd:cd09992  171 YPGTGAAEETGGGAgegftinVPLPPGSGDAEYLAAFEEVLLPIAREFQPDLVLVSAGFDAHRGDPLGGMNLTPEGyarl 250

                        250       260
                 ....*....|....*....|....*....
gi 966925567 199 --IVKrdELVFRMVRGRhvpILMVTSGGY 225
Cdd:cd09992  251 trLLK--ELADEHCGGR---LVFVLEGGY 274
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
 81-231 5.05e-12

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: 64.53  E-value: 5.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  81 NELKFLFERVegisraTIIDLDAHQGNGHERDFMDDKRVyiMDVyNRHIYPGDRFAKQAIR----RK-------VELEWG 149
Cdd:cd09991  148 LELLKYHQRV------LYIDIDIHHGDGVEEAFYTTDRV--MTV-SFHKFGEYFFPGTGLRdigaGKgkyyavnVPLKDG 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567 150 TEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVKrdelVFRMVRGRHVPILMVTSGGYQKR- 228
Cdd:cd09991  219 IDDESYLQIFEPVLSKVMEVFQPSAVVLQCGADSLAGDRLGCFNLSIKGHAK----CVKFVKSFNIPLLVLGGGGYTLRn 294


                 ...
gi 966925567 229 TAR 231
Cdd:cd09991  295 VAR 297
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 35-238 6.00e-12

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: 64.67  E-value: 6.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  35 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVH--------------TRRYLNELKFLFER----------- 89
Cdd:cd11600    3 HPEDPSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHseehwdrveatekmSDEQLKDRTEIFERdslyvnndtaf 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  90 ----------------VEG--------------------------------------------ISRATIIDLDAHQGNGH 109
Cdd:cd11600   83 carlscggaieacravAEGrvknafavvrppghhaepdesmgfcffnnvavaakwlqteypdkIKKILILDWDIHHGNGT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567 110 ERDFMDDKRV-YI-MDVY-NRHIYPGDRFAK-------QAIRRKVELEW---GTEDDEYLDKVERNIEKSLQEHLPDVVV 176
Cdd:cd11600  163 QRAFYDDPNVlYIsLHRFeNGGFYPGTPYGDyesvgegAGLGFNVNIPWpqgGMGDADYIYAFQRIVMPIAYEFDPDLVI 242

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966925567 177 YNAGTDILEGDRLGGLSISPAGIVKRDELVFRMVRGRhvpILMVTSGGYQKRTariIADSIL 238
Cdd:cd11600  243 ISAGFDAADGDELGQCHVTPAGYAHMTHMLMSLAGGK---LVVALEGGYNLDA---ISDSAL 298
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
 92-193 1.56e-09

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: 57.14  E-value: 1.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  92 GISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYNRHIYPGDRFAKQAIR---RKVELEWGTEDDEYLDKVERNIEKSLQ 168
Cdd:cd11599  134 GLERVAIVDFDVHHGNGTEDIFRDDPRVLFCSSHQHPLYPGTGAPDETGHgniVNVPLPAGTGGAEFREAVEDRWLPALD 213

                         90       100
                 ....*....|....*....|....*
gi 966925567 169 EHLPDVVVYNAGTDILEGDRLGGLS 193
Cdd:cd11599  214 AFKPDLILISAGFDAHRDDPLAQLN 238
PTZ00063 PTZ00063
histone deacetylase; Provisional
 79-228 4.94e-08

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 53.28  E-value: 4.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  79 YLNELKF-LFERVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYN-RHIYPG-----DRFAKQA--IRRKVELEWG 149
Cdd:PTZ00063 149 YINDIVLgILELLKYHARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKfGDFFPGtgdvtDIGVAQGkyYSVNVPLNDG 228

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966925567 150 TEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLGGLSISpagiVKRDELVFRMVRGRHVPILMVTSGGYQKR 228
Cdd:PTZ00063 229 IDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLT----IKGHAACVEFVRSLNIPLLVLGGGGYTIR 303
PTZ00346 PTZ00346
histone deacetylase; Provisional
 79-228 6.94e-08

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 52.73  E-value: 6.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  79 YLNELKF-LFERVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDV--YNRHIYPGD---RFAKQAIRRKVELE---W- 148
Cdd:PTZ00346 166 YVNDIVLgILELLKCHDRVLYVDIDMHHGDGVDEAFCTSDRVFTLSLhkFGESFFPGTghpRDVGYGRGRYYSMNlavWd 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567 149 GTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVKrdelVFRMVRGRHVPILMVTSGGYQKR 228
Cdd:PTZ00346 246 GITDFYYLGLFEHALHSIVRRYSPDAIVLQCGADSLAGDRLGLLNLSSFGHGQ----CVQAVRDLGIPMLALGGGGYTIR 321
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
 35-258 7.18e-08

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: 52.55  E-value: 7.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  35 HPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYL-----------NELKFLFERVE------------ 91
Cdd:cd11682    7 FPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYValmkstqymteEELRTLADTYDsvylhpnsysca 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  92 ----------------------------------------------------------GISRATIIDLDAHQGNGHERDF 113
Cdd:cd11682   87 clavgsvlqlvdkvlggeirnglaivrppghhaqhdkmdgycmfnnvaiaaryaqqkhGVQRVLIVDWDVHHGQGTQFIF 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567 114 MDDKRVYIMDVynrHIYPGDRF-------------AKQAIRRKVELEW---GTEDDEYLDKVERNIEKSLQEHLPDVVVY 177
Cdd:cd11682  167 EQDPSVLYFSI---HRYEQGRFwphlkesdssavgFGRGEGYNINVPWnqvGMRDADYIAAFLHVLLPVALEFQPQLVLV 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567 178 NAGTDILEGDRLGGLSISPAGIVKRDELVFRMVRGRhvpILMVTSGGYQKR-TARIIADSILNLFG---LGLIGPESPSI 253
Cdd:cd11682  244 AAGFDAVIGDPKGEMAATPACFAHLTHLLMGLAGGK---LILSLEGGYNLRsLAEGVCASLKALLGdpcPMLESPGAPCR 320


                 ....*
gi 966925567 254 SAQNS 258
Cdd:cd11682  321 SALAS 325
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
 47-234 2.96e-07

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: 50.64  E-value: 2.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  47 NFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKFL------------------FE-------------------- 88
Cdd:cd09996   45 NLLEVSGLSDHLVLITPRPATDEELLRVHTPEYIDRVKAAsaagggeagggtpfgpgsYEiallaaggaiaavdavldge 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  89 -------------------------------------RVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYNRHIYP 131
Cdd:cd09996  125 vdnayalvrppghhaepdqgmgfclfnnvaiaarhalAVGGVKRVAVVDWDVHHGNGTQAIFYDDPDVLTISLHQDRCFP 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567 132 GDRFAKQAIRR--------KVELEWGTEDDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLGglsispagivkrd 203
Cdd:cd09996  205 PDSGAVEERGEgagegynlNIPLPPGSGDGAYLHAFERIVLPALRAFRPELIIVASGFDASAFDPLG------------- 271

                        250       260       270
                 ....*....|....*....|....*....|.
gi 966925567 204 elvfRMvrgrhvpilMVTSGGYQKRTARIIA 234
Cdd:cd09996  272 ----RM---------MLTSDGFRALTRKLRD 289
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
 86-195 9.06e-07

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: 49.60  E-value: 9.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  86 LFERVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVY---NRHIYPGDRFAKQ-----AIRRKVELEW--GTE---- 151
Cdd:cd10007  176 LLQQKLNVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHrydDGNFFPGSGAPDEvgagpGVGFNVNIAWtgGVDppig 255

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 966925567 152 DDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDR--LGGLSIS 195
Cdd:cd10007  256 DVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGHQspLGGYSVT 301
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
 93-195 3.96e-05

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: 44.23  E-value: 3.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  93 ISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYnRH----IYPGDRFAKQAIRR-----KVELEW--GTE----DDEYLD 157
Cdd:cd10008  181 ASKILIVDWDVHHGNGTQQTFYQDPSVLYISLH-RHddgnFFPGSGAVDEVGAGsgegfNVNVAWagGLDppmgDPEYLA 259

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 966925567 158 KVERNIEKSLQEHLPDVVVYNAGTDILEGD--RLGGLSIS 195
Cdd:cd10008  260 AFRIVVMPIAREFSPDLVLVSAGFDAAEGHpaPLGGYHVS 299
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
 84-225 8.35e-05

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: 43.47  E-value: 8.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  84 KFLFERVEgISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYNR---HIYPGDRFAKQAIR-----RKVELEW--GTE-- 151
Cdd:cd10009  173 KYLRDQLN-ISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdegNFFPGSGAPNEVGTglgegYNINIAWtgGLDpp 251

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966925567 152 --DDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDR--LGGLSISPAGIVKRDELVFRMVRGRhvpILMVTSGGY 225
Cdd:cd10009  252 mgDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTppLGGYKVTAKCFGHLTKQLMTLADGR---VVLALEGGH 326
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 49-225 2.16e-03

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: 38.83  E-value: 2.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  49 LKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKFL--------------FERV------------------------ 90
Cdd:cd10002   21 LTQDGLLERCVKIPAREAEEDEILLVHSQEYIDLVKSTetmekeeleslcsgYDSVylcpstyeaarlaagstielvkav 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567  91 -------------------------------------------EGISRATIIDLDAHQGNGHERDFMDDKRVyimDVYNR 127
Cdd:cd10002  101 magkiqngfalirppghhamrneangycifnnvaiaakyaiekLGLKRILIVDWDVHHGQGTQQGFYEDPRV---LYFSI 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966925567 128 HIYPGDRF-------------AKQAIRRKVELEWGTE---DDEYLDKVERNIEKSLQEHLPDVVVYNAGTDILEGDRLGG 191
Cdd:cd10002  178 HRYEHGRFwphlfesdydyigVGHGYGFNVNVPLNQTglgDADYLAIFHHILLPLALEFQPELVLVSAGFDASIGDPEGE 257

                        250       260       270
                 ....*....|....*....|....*....|....
gi 966925567 192 LSISPAGIVKRDELVFRMVRGRhvpILMVTSGGY 225
Cdd:cd10002  258 MAVTPAGYAHLTRLLMGLAGGK---LLLVLEGGY 288
 
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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