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Conserved domains on  [gi|847153304|ref|XP_012823482|]
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histone deacetylase 8 isoform X2 [Xenopus tropicalis]

Protein Classification

histone deacetylase 8( domain architecture ID 10177994)

histone deacetylase 8 (HD8) 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)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 3-325 0e+00

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: 656.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304   3 RVVKPKVASMEEMAAFHTDSYLQHLHKVSEEGDNDDP--ETLEYGLGYDCPITEGIYDYAAAVGGATLTAAEQLMAGKTR 80
Cdd:cd10000   40 RVVKPRVATEEELASFHSDEYIQFLKKASNEGDNDEEpsEQQEFGLGYDCPIFEGIYDYAAAVAGATLTAAQLLIDGKCK 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  81 IAINWPGGWHHAKKDEASGFCYLNDAVLGILKLREKFDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTG 160
Cdd:cd10000  120 VAINWFGGWHHAQRDEASGFCYVNDIVLGILKLREKFDRVLYVDLDLHHGDGVEDAFSFTSKVMTVSLHKYSPGFFPGTG 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 161 DVSDIGLGKGRYYSVNVPLQDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMTPQGIGKCLKYVL 240
Cdd:cd10000  200 DVSDVGLGKGKYYTVNVPLRDGIQDEQYLQIFTAVVPEIVAAFRPEAVVLQCGADTLAGDPMGAFNLTPVGIGKCLKYVL 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 241 QWQLPTLILGGGGYHLPNTARCWTYLTALIVGRTLSSEIPDHEFFTEYGPDYVLEVTPSCRPDRNDSQKVQEILQSIKGH 320
Cdd:cd10000  280 GWKLPTLILGGGGYNLANTARCWTYLTGLILGEPLSSDIPDHEFFTSYGPDYELEISPSLRPDLNEDQYIEKILETIKGN 359


                 ....*
gi 847153304 321 LKQVV 325
Cdd:cd10000  360 LKNVV 364
 
Name Accession Description Interval E-value
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 3-325 0e+00

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: 656.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304   3 RVVKPKVASMEEMAAFHTDSYLQHLHKVSEEGDNDDP--ETLEYGLGYDCPITEGIYDYAAAVGGATLTAAEQLMAGKTR 80
Cdd:cd10000   40 RVVKPRVATEEELASFHSDEYIQFLKKASNEGDNDEEpsEQQEFGLGYDCPIFEGIYDYAAAVAGATLTAAQLLIDGKCK 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  81 IAINWPGGWHHAKKDEASGFCYLNDAVLGILKLREKFDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTG 160
Cdd:cd10000  120 VAINWFGGWHHAQRDEASGFCYVNDIVLGILKLREKFDRVLYVDLDLHHGDGVEDAFSFTSKVMTVSLHKYSPGFFPGTG 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 161 DVSDIGLGKGRYYSVNVPLQDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMTPQGIGKCLKYVL 240
Cdd:cd10000  200 DVSDVGLGKGKYYTVNVPLRDGIQDEQYLQIFTAVVPEIVAAFRPEAVVLQCGADTLAGDPMGAFNLTPVGIGKCLKYVL 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 241 QWQLPTLILGGGGYHLPNTARCWTYLTALIVGRTLSSEIPDHEFFTEYGPDYVLEVTPSCRPDRNDSQKVQEILQSIKGH 320
Cdd:cd10000  280 GWKLPTLILGGGGYNLANTARCWTYLTGLILGEPLSSDIPDHEFFTSYGPDYELEISPSLRPDLNEDQYIEKILETIKGN 359


                 ....*
gi 847153304 321 LKQVV 325
Cdd:cd10000  360 LKNVV 364
PTZ00063 PTZ00063
histone deacetylase; Provisional
 4-324 1.46e-104

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 312.90  E-value: 1.46e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304   4 VVKPKVASMEEMAAFHTDSYLQHLHKVSEEGDNDDPETLE---YGLGYDCPITEGIYDYAAAVGGATLTAAEQLMAGKTR 80
Cdd:PTZ00063  48 IYRPHKSVEPELVLFHDEEYVDFLSSISPENYRDFTYQLKrfnVGEATDCPVFDGLFEFQQSCAGASIDGAYKLNNHQAD 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  81 IAINWPGGWHHAKKDEASGFCYLNDAVLGILKLREKFDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFSpGFFPGTG 160
Cdd:PTZ00063 128 ICVNWSGGLHHAKRSEASGFCYINDIVLGILELLKYHARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKFG-DFFPGTG 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 161 DVSDIGLGKGRYYSVNVPLQDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMTPQGIGKCLKYVL 240
Cdd:PTZ00063 207 DVTDIGVAQGKYYSVNVPLNDGIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAACVEFVR 286

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 241 QWQLPTLILGGGGYHLPNTARCWTYLTALIVGRT--LSSEIPDHEFFTEYGPDYVLEVTPSCRPDRNDSQKVQEILQSIK 318
Cdd:PTZ00063 287 SLNIPLLVLGGGGYTIRNVARCWAYETGVILNKHdeMSDQISLNDYYDYYAPDFQLHLQPSNIPNYNSPEHLEKIKVKIL 366


                 ....*.
gi 847153304 319 GHLKQV 324
Cdd:PTZ00063 367 ENLRYL 372
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 2-270 8.81e-104

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: 306.09  E-value: 8.81e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304    2 PRVVKPKVASMEEMAAFHTDSYLQHLHKVSEEGDNDdPETLEYGLGYDCPITEGIYDYAAAVGGATLTAAEQLMAGKTR- 80
Cdd:pfam00850  24 LEIIAPRPATEEELLLVHSPEYLEFLEEAAPEGGAL-LLLSYLSGDDDTPVSPGSYEAALLAAGGTLAAADAVLSGEARn 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304   81 -IAINWPGGwHHAKKDEASGFCYLNDAVLGILKLREK--FDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFP 157
Cdd:pfam00850 103 aFALVRPPG-HHAERDRASGFCIFNNVAIAAKYLREKygLKRVAIVDFDVHHGNGTQEIFYDDPSVLTLSIHQYPGGFYP 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  158 GTGDVSDIGLGKGRYYSVNVPLQDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMTPQGIGKCLK 237
Cdd:pfam00850 182 GTGFADETGEGKGKGYTLNVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAGFDAHAGDPLGGLNLTTEGFAEITR 261

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 847153304  238 YVLQWQLPT----LILGGGGYHLPNTARCWTYLTALI 270
Cdd:pfam00850 262 ILLELADPLcirvVSVLEGGYNLDALARSATAVLAAL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 3-264 1.96e-79

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 244.25  E-value: 1.96e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304   3 RVVKPKVASMEEMAAFHTDSYLQHLHKVSEEGdnddpetlEYG-LGYDCPITEGIYDYAAAVGGATLTAAEQLMAGKTRI 81
Cdd:COG0123   42 ELVEPPPATEEDLLRVHTPDYVDALRAASLDG--------GYGqLDPDTPVSPGTWEAALLAAGGALAAADAVLEGEARN 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  82 A-INWPGGWHHAKKDEASGFCYLNDAVLGILKLREK-FDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFspGFFPGT 159
Cdd:COG0123  114 AfALVRPPGHHAERDRAMGFCLFNNAAIAARYLLAKgLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD--PLYPGT 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 160 GDVSDIGLGKGRYYSVNVPLQDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMTPQGIGKCLKYV 239
Cdd:COG0123  192 GAADETGEGAGEGSNLNVPLPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRV 271

                        250       260
                 ....*....|....*....|....*....
gi 847153304 240 LQW----QLPTLILGGGGYHLPNTARCWT 264
Cdd:COG0123  272 LELadhcGGPVVSVLEGGYNLDALARSVA 300
 
Name Accession Description Interval E-value
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 3-325 0e+00

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: 656.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304   3 RVVKPKVASMEEMAAFHTDSYLQHLHKVSEEGDNDDP--ETLEYGLGYDCPITEGIYDYAAAVGGATLTAAEQLMAGKTR 80
Cdd:cd10000   40 RVVKPRVATEEELASFHSDEYIQFLKKASNEGDNDEEpsEQQEFGLGYDCPIFEGIYDYAAAVAGATLTAAQLLIDGKCK 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  81 IAINWPGGWHHAKKDEASGFCYLNDAVLGILKLREKFDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTG 160
Cdd:cd10000  120 VAINWFGGWHHAQRDEASGFCYVNDIVLGILKLREKFDRVLYVDLDLHHGDGVEDAFSFTSKVMTVSLHKYSPGFFPGTG 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 161 DVSDIGLGKGRYYSVNVPLQDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMTPQGIGKCLKYVL 240
Cdd:cd10000  200 DVSDVGLGKGKYYTVNVPLRDGIQDEQYLQIFTAVVPEIVAAFRPEAVVLQCGADTLAGDPMGAFNLTPVGIGKCLKYVL 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 241 QWQLPTLILGGGGYHLPNTARCWTYLTALIVGRTLSSEIPDHEFFTEYGPDYVLEVTPSCRPDRNDSQKVQEILQSIKGH 320
Cdd:cd10000  280 GWKLPTLILGGGGYNLANTARCWTYLTGLILGEPLSSDIPDHEFFTSYGPDYELEISPSLRPDLNEDQYIEKILETIKGN 359


                 ....*
gi 847153304 321 LKQVV 325
Cdd:cd10000  360 LKNVV 364
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
 3-270 1.35e-153

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: 432.78  E-value: 1.35e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304   3 RVVKPKVASMEEMAAFHTDSYLQHLHKVSEEGDNDDPETLE-YGLGYDCPITEGIYDYAAAVGGATLTAAEQLMAGKTRI 81
Cdd:cd09991   39 EIYRPRPATAEELTKFHSDDYIDFLRSVSPDNMKEFKKQLErFNVGEDCPVFDGLYEYCQLYAGGSIAAAVKLNRGQADI 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  82 AINWPGGWHHAKKDEASGFCYLNDAVLGILKLREKFDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGD 161
Cdd:cd09991  119 AINWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKFGEYFFPGTGL 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 162 vSDIGLGKGRYYSVNVPLQDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMTPQGIGKCLKYVLQ 241
Cdd:cd09991  199 -RDIGAGKGKYYAVNVPLKDGIDDESYLQIFEPVLSKVMEVFQPSAVVLQCGADSLAGDRLGCFNLSIKGHAKCVKFVKS 277

                        250       260
                 ....*....|....*....|....*....
gi 847153304 242 WQLPTLILGGGGYHLPNTARCWTYLTALI 270
Cdd:cd09991  278 FNIPLLVLGGGGYTLRNVARCWTYETAVL 306
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
 4-324 4.98e-118

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: 345.15  E-value: 4.98e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304   4 VVKPKVASMEEMAAFHTDSYLQHLHKVSEEGDNDDPETL-EYGLGYDCPITEGIYDYAAAVGGATLTAAEQLMAGKTRIA 82
Cdd:cd10005   45 VYKPYRASAHDMCRFHSEDYIDFLQRVTPQNIQGFTKSLnQFNVGDDCPVFPGLFDFCSMYTGASLEGATKLNHKICDIA 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  83 INWPGGWHHAKKDEASGFCYLNDAVLGILKLREKFDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDV 162
Cdd:cd10005  125 INWSGGLHHAKKFEASGFCYVNDIVIAILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDM 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 163 SDIGLGKGRYYSVNVPLQDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMTPQGIGKCLKYVLQW 242
Cdd:cd10005  205 YEVGAESGRYYSVNVPLKDGIDDQSYLQLFKPVIQQVIDFYQPTCIVLQCGADSLGCDRLGCFNLSIKGHGECVEFVKSF 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 243 QLPTLILGGGGYHLPNTARCWTYLTALIVGRTLSSEIPDHEFFTEYGPDYVLEVTPSCRPD-RNDSQKVQEILQSIKGHL 321
Cdd:cd10005  285 NIPLLVLGGGGYTVRNVARCWTYETSLLVDEEISNELPYNEYFEYFAPDFTLHPDVSTRIEnQNSKQYLDQIRQTVFENL 364


                 ...
gi 847153304 322 KQV 324
Cdd:cd10005  365 KML 367
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
 4-322 1.59e-112

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: 331.00  E-value: 1.59e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304   4 VVKPKVASMEEMAAFHTDSYLQHLHKVSEegDNDD---PETLEYGLGYDCPITEGIYDYAAAVGGATLTAAEQLMAGKTR 80
Cdd:cd10004   46 IYRAKPATKNEMTQFHTDEYIDFLSRVTP--DNMEkfqKEQVKYNVGDDCPVFDGLFEFCSISAGGSMEGAARLNRGKCD 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  81 IAINWPGGWHHAKKDEASGFCYLNDAVLGILKLREKFDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFSPgFFPGTG 160
Cdd:cd10004  124 IAVNWAGGLHHAKKSEASGFCYVNDIVLGILELLRYHQRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYGE-YFPGTG 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 161 DVSDIGLGKGRYYSVNVPLQDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMTPQGIGKCLKYVL 240
Cdd:cd10004  203 ELRDIGIGTGKNYAVNVPLRDGIDDESYKSIFEPVIKHVMEWYQPEAVVLQCGGDSLSGDRLGCFNLSMKGHANCVNFVK 282

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 241 QWQLPTLILGGGGYHLPNTARCWTYLTALIVGRTLSSEIPDHEFFTEYGPDYVLEVTPSCRPDRNDSQKVQEILQSIKGH 320
Cdd:cd10004  283 SFNLPMLVLGGGGYTMRNVARTWAFETGLLAGEELDKDLPYNEYYEYYGPDYELNVRPSNMENHNTPEYLDKITTAVIEN 362


                 ..
gi 847153304 321 LK 322
Cdd:cd10004  363 LR 364
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
 7-269 3.64e-108

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: 317.48  E-value: 3.64e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304   7 PKVASMEEMAAFHTDSYLQHLHKVS-EEGDNDDPETLE-YGLGYDCPITEGIYDYAAAVGGATLTAAEQLMAGKTRIAIN 84
Cdd:cd11598   46 ARAATREELRQFHDADYLDFLSKVSpENANQLRFDKAEpFNIGDDCPVFDGMYDYCQLYAGASLDAARKLCSGQSDIAIN 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  85 WPGGWHHAKKDEASGFCYLNDAVLGILKLREKFDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSD 164
Cdd:cd11598  126 WSGGLHHAKKSEASGFCYVNDIVLAILNLLRYFPRVLYIDIDVHHGDGVEEAFYRTDRVMTLSFHKYNGEFFPGTGDLDD 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 165 IGLGKGRYYSVNVPLQDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMTPQGIGKCLKYVLQWQL 244
Cdd:cd11598  206 NGGTPGKHFALNVPLEDGIDDEQYNLLFKSIIGPTIEKFQPSAIVLQCGADSLGGDRLGQFNLNIKAHGACVKFVKSFGI 285

                        250       260
                 ....*....|....*....|....*
gi 847153304 245 PTLILGGGGYHLPNTARCWTYLTAL 269
Cdd:cd11598  286 PMLVVGGGGYTPRNVARAWCYETAV 310
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
 4-324 8.46e-105

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: 311.23  E-value: 8.46e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304   4 VVKPKVASMEEMAAFHTDSYLQHLHKVSEEGDNDDPETLE-YGLGYDCPITEGIYDYAAAVGGATLTAAEQLMAGKTRIA 82
Cdd:cd10010   50 IYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQrFNVGEDCPVFDGLFEFCQLSAGGSVASAVKLNKQQTDIA 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  83 INWPGGWHHAKKDEASGFCYLNDAVLGILKLREKFDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFSPgFFPGTGDV 162
Cdd:cd10010  130 VNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGE-YFPGTGDL 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 163 SDIGLGKGRYYSVNVPLQDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMTPQGIGKCLKYVLQW 242
Cdd:cd10010  209 RDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEFVKSF 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 243 QLPTLILGGGGYHLPNTARCWTYLTALIVGRTLSSEIPDHEFFTEYGPDYVLEVTPSCRPDRNDSQKVQEILQSIKGHLK 322
Cdd:cd10010  289 NLPMLMLGGGGYTIRNVARCWTYETAVALDSEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLR 368


                 ..
gi 847153304 323 QV 324
Cdd:cd10010  369 ML 370
PTZ00063 PTZ00063
histone deacetylase; Provisional
 4-324 1.46e-104

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 312.90  E-value: 1.46e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304   4 VVKPKVASMEEMAAFHTDSYLQHLHKVSEEGDNDDPETLE---YGLGYDCPITEGIYDYAAAVGGATLTAAEQLMAGKTR 80
Cdd:PTZ00063  48 IYRPHKSVEPELVLFHDEEYVDFLSSISPENYRDFTYQLKrfnVGEATDCPVFDGLFEFQQSCAGASIDGAYKLNNHQAD 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  81 IAINWPGGWHHAKKDEASGFCYLNDAVLGILKLREKFDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFSpGFFPGTG 160
Cdd:PTZ00063 128 ICVNWSGGLHHAKRSEASGFCYINDIVLGILELLKYHARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKFG-DFFPGTG 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 161 DVSDIGLGKGRYYSVNVPLQDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMTPQGIGKCLKYVL 240
Cdd:PTZ00063 207 DVTDIGVAQGKYYSVNVPLNDGIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAACVEFVR 286

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 241 QWQLPTLILGGGGYHLPNTARCWTYLTALIVGRT--LSSEIPDHEFFTEYGPDYVLEVTPSCRPDRNDSQKVQEILQSIK 318
Cdd:PTZ00063 287 SLNIPLLVLGGGGYTIRNVARCWAYETGVILNKHdeMSDQISLNDYYDYYAPDFQLHLQPSNIPNYNSPEHLEKIKVKIL 366


                 ....*.
gi 847153304 319 GHLKQV 324
Cdd:PTZ00063 367 ENLRYL 372
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 2-270 8.81e-104

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: 306.09  E-value: 8.81e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304    2 PRVVKPKVASMEEMAAFHTDSYLQHLHKVSEEGDNDdPETLEYGLGYDCPITEGIYDYAAAVGGATLTAAEQLMAGKTR- 80
Cdd:pfam00850  24 LEIIAPRPATEEELLLVHSPEYLEFLEEAAPEGGAL-LLLSYLSGDDDTPVSPGSYEAALLAAGGTLAAADAVLSGEARn 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304   81 -IAINWPGGwHHAKKDEASGFCYLNDAVLGILKLREK--FDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFP 157
Cdd:pfam00850 103 aFALVRPPG-HHAERDRASGFCIFNNVAIAAKYLREKygLKRVAIVDFDVHHGNGTQEIFYDDPSVLTLSIHQYPGGFYP 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  158 GTGDVSDIGLGKGRYYSVNVPLQDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMTPQGIGKCLK 237
Cdd:pfam00850 182 GTGFADETGEGKGKGYTLNVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAGFDAHAGDPLGGLNLTTEGFAEITR 261

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 847153304  238 YVLQWQLPT----LILGGGGYHLPNTARCWTYLTALI 270
Cdd:pfam00850 262 ILLELADPLcirvVSVLEGGYNLDALARSATAVLAAL 298
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
 4-324 2.53e-99

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: 296.97  E-value: 2.53e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304   4 VVKPKVASMEEMAAFHTDSYLQHLHKVSEEGDNDDPETLE-YGLGYDCPITEGIYDYAAAVGGATLTAAEQLMAGKTRIA 82
Cdd:cd10011   46 IYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQrFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMA 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  83 INWPGGWHHAKKDEASGFCYLNDAVLGILKLREKFDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFfPGTGDV 162
Cdd:cd10011  126 VNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYF-PGTGDL 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 163 SDIGLGKGRYYSVNVPLQDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMTPQGIGKCLKYVLQW 242
Cdd:cd10011  205 RDIGAGKGKYYAVNFPMRDGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTF 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 243 QLPTLILGGGGYHLPNTARCWTYLTALIVGRTLSSEIPDHEFFTEYGPDYVLEVTPSCRPDRNDSQKVQEILQSIKGHLK 322
Cdd:cd10011  285 NLPLLMLGGGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYMEKIKQRLFENLR 364


                 ..
gi 847153304 323 QV 324
Cdd:cd10011  365 ML 366
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
 3-270 4.08e-99

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: 293.79  E-value: 4.08e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304   3 RVVKPKVASMEEMAAFHTDSYLQHLHKvseegdnddpetlEYGLGYDCPITEGIYDYAAAVGGATLTAAEQLMAGKTR-I 81
Cdd:cd11680   40 EIIEPERATRKDLTKYHDKDYVDFLLK-------------KYGLEDDCPVFPFLSMYVQLVAGSSLALAKHLITQVERdI 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  82 AINWPGGWHHAKKDEASGFCYLNDAVLGILKLREK-FDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTG 160
Cdd:cd11680  107 AINWYGGRHHAQKSRASGFCYVNDIVLAILRLRRArFRRVFYLDLDLHHGDGVESAFFFSKNVLTCSIHRYDPGFFPGTG 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 161 DVSDiglgKGRYYSVNVPLQDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMTPQGIGKCLKYVL 240
Cdd:cd11680  187 SLKN----SSDKGMLNIPLKRGLSDKTLLRIIDSIVRPLIEKFEPEVIVIQCGCDGLSGDPHKEWNLTIRGYGSVIELLL 262

                        250       260       270
                 ....*....|....*....|....*....|..
gi 847153304 241 QW--QLPTLILGGGGYHLPNTARCWTYLTALI 270
Cdd:cd11680  263 KEfkDKPTLLLGGGGYNHTEAARAWTYLTSMV 294
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
 3-270 3.51e-94

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: 282.14  E-value: 3.51e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304   3 RVVKPKVASMEEMAAFHTDSYLQHLHKVSEEGDNDDpeTLEYGLG-YDCPITEGIYDYAAAVGGATLTAAEQLMAGKTRI 81
Cdd:cd09994   41 DLVPPRPATEEELLLFHTPDYIEAVKEASRGQEPEG--RGRLGLGtEDNPVFPGMHEAAALVVGGTLLAARLVLEGEARR 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  82 AINWPGGWHHAKKDEASGFCYLNDAVLGILKLREK-FDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTG 160
Cdd:cd09994  119 AFNPAGGLHHAMRGRASGFCVYNDAAVAIERLRDKgGLRVAYVDIDAHHGDGVQAAFYDDPRVLTISLHESGRYLFPGTG 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 161 DVSDIGLGKGRYYSVNVPLQDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMTPQGIGKCLKYVL 240
Cdd:cd09994  199 FVDEIGEGEGYGYAVNIPLPPGTGDDEFLRAFEAVVPPLLRAFRPDVIVSQHGADAHAGDPLTHLNLSNRAYRAAVRRIR 278

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 847153304 241 QW-----QLPTLILGGGGYHLPNTARCWTYLTALI 270
Cdd:cd09994  279 ELadeycGGRWLALGGGGYNPDVVARAWALLWAVL 313
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 3-264 1.96e-79

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 244.25  E-value: 1.96e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304   3 RVVKPKVASMEEMAAFHTDSYLQHLHKVSEEGdnddpetlEYG-LGYDCPITEGIYDYAAAVGGATLTAAEQLMAGKTRI 81
Cdd:COG0123   42 ELVEPPPATEEDLLRVHTPDYVDALRAASLDG--------GYGqLDPDTPVSPGTWEAALLAAGGALAAADAVLEGEARN 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  82 A-INWPGGWHHAKKDEASGFCYLNDAVLGILKLREK-FDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFspGFFPGT 159
Cdd:COG0123  114 AfALVRPPGHHAERDRAMGFCLFNNAAIAARYLLAKgLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD--PLYPGT 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 160 GDVSDIGLGKGRYYSVNVPLQDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMTPQGIGKCLKYV 239
Cdd:COG0123  192 GAADETGEGAGEGSNLNVPLPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRV 271

                        250       260
                 ....*....|....*....|....*....
gi 847153304 240 LQW----QLPTLILGGGGYHLPNTARCWT 264
Cdd:COG0123  272 LELadhcGGPVVSVLEGGYNLDALARSVA 300
PTZ00346 PTZ00346
histone deacetylase; Provisional
 3-275 1.77e-78

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 245.71  E-value: 1.77e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304   3 RVVKPKVASMEEMAAFHTDSYLQHLHKVSEEGDNDDPETLEYGLGYDCPITEGIYDYAAAVGGATLTAAEQLMAGKTRIA 82
Cdd:PTZ00346  67 RTVVPPLVKVEELMAYHTDTYLANLGLHSCRSWLWNAETSKVFFSGDCPPVEGLMEHSIATASGTLMGAVLLNSGQVDVA 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  83 INWPGGWHHAKKDEASGFCYLNDAVLGILKLREKFDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDV 162
Cdd:PTZ00346 147 VHWGGGMHHSKCGECSGFCYVNDIVLGILELLKCHDRVLYVDIDMHHGDGVDEAFCTSDRVFTLSLHKFGESFFPGTGHP 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 163 SDIGLGKGRYYSVNVPLQDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMTPQGIGKCLKYVLQW 242
Cdd:PTZ00346 227 RDVGYGRGRYYSMNLAVWDGITDFYYLGLFEHALHSIVRRYSPDAIVLQCGADSLAGDRLGLLNLSSFGHGQCVQAVRDL 306

                        250       260       270
                 ....*....|....*....|....*....|...
gi 847153304 243 QLPTLILGGGGYHLPNTARCWTYLTALIVGRTL 275
Cdd:PTZ00346 307 GIPMLALGGGGYTIRNVAKLWAYETSILTGHPL 339
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
 5-268 2.38e-67

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: 212.30  E-value: 2.38e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304   5 VKPKVASMEEMAAFHTDSYLQHLHKvsEEGDNDDPETLEYGLGYDCPITEGIYDYAAAVGGATLTAAEQLMAGKTRIAIN 84
Cdd:cd09301   21 IECREATEELLLKVHTEEYLNELKA--NFAVATITESKPVIFGPNFPVQRHYFRGARLSTGGVVEAAELVAKGELERAFA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  85 W-PGGWHHAKKDEASGFCYLNDAVLGILKLREK-FDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFpgtgdv 162
Cdd:cd09301   99 VvGAGGHHAGKSRAWGFCYFNDVVLAIKFLRERgISRILIIDTDAHHGDGTREAFYDDDRVLHMSFHNYDIYPF------ 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 163 sdiGLGKGRYYSVNVPLQDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMTPQGIGKCLKYV--L 240
Cdd:cd09301  173 ---GRGKGKGYKINVPLEDGLGDEEYLDAVERVISKVLEEFEPEVVVLQFGHDTHEGDRLGGFNLSEKGFVKLAEIVkeF 249

                        250       260
                 ....*....|....*....|....*...
gi 847153304 241 QWQLPTLILGGGGYHLPNTARCWTYLTA 268
Cdd:cd09301  250 ARGGPILMVLGGGYNPEAAARIWTAIIK 277
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
 2-262 4.30e-54

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: 178.46  E-value: 4.30e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304   2 PRVVKPKVASMEEMAAFHTDSYLQHLHKVSEEGDN-DDPetleyglgyDCPITEGIYDYA-AAVGGAtLTAAEQLMAGKT 79
Cdd:cd09992   24 LVFVEPRPATEEELLRVHTPEYIERVEETCEAGGGyLDP---------DTYVSPGSYEAAlLAAGAA-LAAVDAVLSGEA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  80 RIA---INWPGgwHHAKKDEASGFCYLNDAVLGILKLREK--FDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFspG 154
Cdd:cd09992   94 ENAfalVRPPG--HHAEPDRAMGFCLFNNVAIAARYAQKRygLKRVLIVDWDVHHGNGTQDIFYDDPSVLYFSIHQY--P 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 155 FFPGTGDVSDIGLGKGRYYSVNVPLQDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMTPQGIGK 234
Cdd:cd09992  170 FYPGTGAAEETGGGAGEGFTINVPLPPGSGDAEYLAAFEEVLLPIAREFQPDLVLVSAGFDAHRGDPLGGMNLTPEGYAR 249

                        250       260       270
                 ....*....|....*....|....*....|...
gi 847153304 235 CLKYVLQW-----QLPTLILGGGGYHLPNTARC 262
Cdd:cd09992  250 LTRLLKELadehcGGRLVFVLEGGYNLEALAES 282
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
 4-257 9.93e-46

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: 156.93  E-value: 9.93e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304   4 VVKPKVASMEEMAAFHTDSYLQHLhkvsEEGDnddpetleyglgYDCPITEGIYDYAAAVGGATLTAAEQLMAGKTR-IA 82
Cdd:cd10001   47 VLPPRDFGLEPILAVHDPDYVDFL----ETAD------------TDTPISEGTWEAALAAADTALTAADLVLEGERAaYA 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  83 INWPGGwHHAKKDEASGFCYLNDAVLGILKLREKFDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGT-GD 161
Cdd:cd10001  111 LCRPPG-HHAGRDRAGGFCYFNNAAIAAQYLRDRAGRVAILDVDVHHGNGTQEIFYERPDVLYVSIHGDPRTFYPFFlGF 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 162 VSDIGLGKGRYYSVNVPLQDGIQDEKYYQICEGVLKEVfTTFNPEAVVLQLGADTIAGDPMCSFNMTPQG---IGKCLKy 238
Cdd:cd10001  190 ADETGEGEGEGYNLNLPLPPGTGDDDYLAALDEALAAI-AAFGPDALVVSLGFDTHEGDPLSDFKLTTEDyarIGRRIA- 267

                        250
                 ....*....|....*....
gi 847153304 239 vlQWQLPTLILGGGGYHLP 257
Cdd:cd10001  268 --ALGLPTVFVQEGGYNVD 284
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 3-255 7.54e-42

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: 146.10  E-value: 7.54e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304   3 RVVKPKVASMEEMAAFHTDSYLQHLHkvseEGDNDDPETLEYGLgydcPITEGIYDYA-AAVGGaTLTAAEqlMAGKTRI 81
Cdd:cd09993   25 DIVEPEPATREDLLRVHDPEYLESLK----SGELSREEIRRIGF----PWSPELVERTrLAVGG-TILAAR--LALEHGL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  82 AINWPGGWHHAKKDEASGFCYLNDAVLGILKLREK--FDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHkfSPGFFPGT 159
Cdd:cd09993   94 AINLAGGTHHAFPDRGEGFCVFNDIAIAARVLLAEglVRRVLIVDLDVHQGNGTAAIFADDPSVFTFSMH--GEKNYPFR 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 160 GDVSDIglgkgryysvNVPLQDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMTPQGIGKCLKYV 239
Cdd:cd09993  172 KEPSDL----------DVPLPDGTGDDEYLAALEEALPRLLAEFRPDLVFYNAGVDVLAGDRLGRLSLSLEGLRERDRLV 241

                        250       260
                 ....*....|....*....|
gi 847153304 240 LQW----QLPTLILGGGGYH 255
Cdd:cd09993  242 LRFararGIPVAMVLGGGYS 261
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
 3-280 4.56e-38

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: 138.24  E-value: 4.56e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304   3 RVVKPKVASMEEMAAFHTDSYLQHLHKVSEEGDND-DPETLEYGLGYDCPITegiYDYAAAVGGATLTAAEQLMAGKTR- 80
Cdd:cd10003   40 LRLPSRLATEDELLLCHSEEHLDEMKSLEKMKPRElNRLGKEYDSIYIHPDS---YQCALLAAGCVLQVVEAVLTGESRn 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  81 -IAINWPGGwHHAKKDEASGFCYLNDAVLGILKLREKFD--RVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFSPG-FF 156
Cdd:cd10003  117 gVAIVRPPG-HHAEQDTACGFCFFNNVAIAARYAQKKYGlkRILIVDWDVHHGNGTQHMFESDPSVLYISLHRYDNGsFF 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 157 PGT--GDVSDIGLGKGRYYSVNVPL-QDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMTPQGIG 233
Cdd:cd10003  196 PNSpeGNYDVVGKGKGEGFNVNIPWnKGGMGDAEYIAAFQQVVLPIAYEFNPELVLVSAGFDAARGDPLGGCKVTPEGYA 275

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 847153304 234 KclkyvLQWQLPTLILGG------GGYHLPNTARCWTYLTALIVG---RTLSSEIP 280
Cdd:cd10003  276 H-----MTHMLMSLAGGRvivileGGYNLTSISESMSMCTKTLLGdppPVLDLPRP 326
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
 4-222 5.64e-38

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: 138.46  E-value: 5.64e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304   4 VVKPKVASMEEMAAFHTDSYLQHLHKVSEEGDNDdpetleygLGYDCPITEGIYDYAAAVGGATLTAAEQLMAGKTRIA- 82
Cdd:cd09996   58 LITPRPATDEELLRVHTPEYIDRVKAASAAGGGE--------AGGGTPFGPGSYEIALLAAGGAIAAVDAVLDGEVDNAy 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  83 --INWPGgwHHAKKDEASGFCYLNDAVLGILKLREKFD--RVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFSPgFFPG 158
Cdd:cd09996  130 alVRPPG--HHAEPDQGMGFCLFNNVAIAARHALAVGGvkRVAVVDWDVHHGNGTQAIFYDDPDVLTISLHQDRC-FPPD 206

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 847153304 159 TGDVSDIGLGKGRYYSVNVPLQDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPM 222
Cdd:cd09996  207 SGAVEERGEGAGEGYNLNIPLPPGSGDGAYLHAFERIVLPALRAFRPELIIVASGFDASAFDPL 270
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 2-262 3.32e-35

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: 130.51  E-value: 3.32e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304   2 PRVVKPKVASMEEMAAFHTDSYLQHLhkVSEEGDNDDpETLEYGLGYD----CPITegiYDYAAAVGGATLTAAEQLMAG 77
Cdd:cd10002   30 CVKIPAREAEEDEILLVHSQEYIDLV--KSTETMEKE-ELESLCSGYDsvylCPST---YEAARLAAGSTIELVKAVMAG 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  78 KTR--IAINWPGGwHHAKKDEASGFCYLNDAVLGILKLREKF--DRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFSP 153
Cdd:cd10002  104 KIQngFALIRPPG-HHAMRNEANGYCIFNNVAIAAKYAIEKLglKRILIVDWDVHHGQGTQQGFYEDPRVLYFSIHRYEH 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 154 G-FFPG--TGDVSDIGLGKGRYYSVNVPL-QDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMTP 229
Cdd:cd10002  183 GrFWPHlfESDYDYIGVGHGYGFNVNVPLnQTGLGDADYLAIFHHILLPLALEFQPELVLVSAGFDASIGDPEGEMAVTP 262

                        250       260       270
                 ....*....|....*....|....*....|....
gi 847153304 230 QGIGKCLKYVLQWQLPTLILG-GGGYHLPNTARC 262
Cdd:cd10002  263 AGYAHLTRLLMGLAGGKLLLVlEGGYLLESLAES 296
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 64-281 6.55e-31

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: 118.22  E-value: 6.55e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  64 GGAtLTAAEQLMAGKTR--IAINWPGGwHHAKKDEASGFCYLNDAVLGILKLR----EKFDRVLYVDMDLHHGDGVEDAF 137
Cdd:cd11600   89 GGA-IEACRAVAEGRVKnaFAVVRPPG-HHAEPDESMGFCFFNNVAVAAKWLQteypDKIKKILILDWDIHHGNGTQRAF 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 138 SFTSKVMTVSLHKFSPG-FFPGT--GDVSDIGLGKGRYYSVNVPL-QDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLG 213
Cdd:cd11600  167 YDDPNVLYISLHRFENGgFYPGTpyGDYESVGEGAGLGFNVNIPWpQGGMGDADYIYAFQRIVMPIAYEFDPDLVIISAG 246

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 847153304 214 ADTIAGDPMCSFNMTPQGigkclkYVLQWQLPTLILGG-------GGYHLPNTARcwtylTALIVGRTLSSEIPD 281
Cdd:cd11600  247 FDAADGDELGQCHVTPAG------YAHMTHMLMSLAGGklvvaleGGYNLDAISD-----SALAVAKVLLGEAPP 310
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
 3-228 2.94e-29

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: 113.38  E-value: 2.94e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304   3 RVVKPKVASMEEMAAFHTDSYLQHL-HKVSEEGDN-DDPETLeyglgydcpITEGIYDYAAAVGGATLTAAEQLMAGKTR 80
Cdd:cd11599   25 RQLEAPPATREQLLRVHDAAYVDRLeAAAPEEGLVqLDPDTA---------MSPGSLEAALRAAGAVVAAVDAVMAGEAR 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  81 ---IAINWPGgwHHAKKDEASGFCYLNDAVLGILKLREK--FDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFspGF 155
Cdd:cd11599   96 nafCAVRPPG--HHAERDKAMGFCLFNNVAIAAAHALAHhgLERVAIVDFDVHHGNGTEDIFRDDPRVLFCSSHQH--PL 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 847153304 156 FPGTGDVSDIGLGkgryYSVNVPLQDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMT 228
Cdd:cd11599  172 YPGTGAPDETGHG----NIVNVPLPAGTGGAEFREAVEDRWLPALDAFKPDLILISAGFDAHRDDPLAQLNLT 240
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 65-267 4.42e-26

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: 106.66  E-value: 4.42e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  65 GATLTAAEQLMAGKTR--IAINWPGGwHHAKKDEASGFCYLNDAVLG--ILKLREKFDRVLYVDMDLHHGDGVEDAFSFT 140
Cdd:cd11681  125 GCVIDLAFKVATGELKngFAVVRPPG-HHAEPSQAMGFCFFNSVAIAakQLQQKLKLRKILIVDWDVHHGNGTQQIFYED 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 141 SKVMTVSLHKFSPG-FFPGTGDVSDIGLGKGRYYSVNVPLQDGIQ----DEKYYQICEGVLKEVFTTFNPEAVVLQLGAD 215
Cdd:cd11681  204 PNVLYISLHRYDDGnFFPGTGAPTEVGSGAGEGFNVNIAWSGGLDppmgDAEYLAAFRTVVMPIAREFSPDIVLVSAGFD 283

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 847153304 216 TIAGDPmcsfnmtpqgigkclkyvlqwqlPTLilggGGYHLpnTARCWTYLT 267
Cdd:cd11681  284 AAEGHP-----------------------PPL----GGYKV--SPACFGYMT 306
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
 45-272 1.27e-25

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: 105.89  E-value: 1.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  45 GLGYDcpiTEGIYDYAAAVGGATLTA------AEQLMAGKTR--IAINWPGGwHHAKKDEASGFCYLNDAVLG--ILKLR 114
Cdd:cd10006  105 GVGVD---SDTIWNEVHSSGAARLAVgcvvelVFKVATGELKngFAVVRPPG-HHAEESTPMGFCYFNSVAIAakLLQQR 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 115 EKFDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFSPG-FFPGTGDVSDIGLGKGRYYSVNVPLQDGIQ----DEKYY 189
Cdd:cd10006  181 LNVSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYDDGnFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDppmgDAEYL 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 190 QICEGVLKEVFTTFNPEAVVLQLGADTIAGDPmcsfnmTPQgigkclkyvlqwqlptlilggGGYHLpnTARCWTYLTAL 269
Cdd:cd10006  261 AAFRTVVMPIASEFAPDVVLVSSGFDAVEGHP------TPL---------------------GGYNL--SAKCFGYLTKQ 311


                 ...
gi 847153304 270 IVG 272
Cdd:cd10006  312 LMG 314
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
 65-262 3.01e-25

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: 104.68  E-value: 3.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  65 GATLTAAEQLMAG--KTRIAINWPGGwHHAKKDEASGFCYLNDAVLGILKLREKFD--RVLYVDMDLHHGDGVEDAFSFT 140
Cdd:cd10007  128 GCLIELAFKVAAGelKNGFAVIRPPG-HHAEESTAMGFCFFNSVAIAAKLLQQKLNvgKILIVDWDIHHGNGTQQAFYND 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 141 SKVMTVSLHKFSPG-FFPGTGDVSDIGLGKGRYYSVNVPLQDGIQ----DEKYYQICEGVLKEVFTTFNPEAVVLQLGAD 215
Cdd:cd10007  207 PNVLYISLHRYDDGnFFPGSGAPDEVGAGPGVGFNVNIAWTGGVDppigDVEYLTAFRTVVMPIANEFSPDVVLVSAGFD 286

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 847153304 216 TIAG--DPMCSFNMTPQGIGKCLKYVLQWQLPTLILG-GGGYHLpnTARC 262
Cdd:cd10007  287 AVEGhqSPLGGYSVTAKCFGHLTKQLMTLAGGRVVLAlEGGHDL--TAIC 334
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 10-269 1.38e-24

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: 101.86  E-value: 1.38e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  10 ASMEEMAAFHTDSYLQhlhKVSEEGDNDDPETLEYGLGYDCP-ITEGIYDYAAAVGGATLTAAEQLMAGKTR--IAINWP 86
Cdd:cd11683   38 ASEEEILLVHSPEYLS---LVRETQVMNKEELMAISGKYDAVyFHPNTFHCARLAAGATLQLVDAVLTGEVQngMALVRP 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  87 GGwHHAKKDEASGFCYLNDAVLGIL--KLREKFDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFSPG-FFPG--TGD 161
Cdd:cd11683  115 PG-HHSQRNAANGFCVFNNVAIAAEyaKKKYGLHRILIVDWDVHHGQGIQYIFEEDPSVLYFSWHRYEHQrFWPFlrESD 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 162 VSDIGLGKGRYYSVNVPL-QDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMTPQgigkCLKYVL 240
Cdd:cd11683  194 YDAVGRGKGLGFNINLPWnKVGMGNADYLAAFFHVLLPLAFEFDPELVLVSAGFDSAIGDPEGQMCATPE----CFAHLT 269

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 847153304 241 QWQLPtlILGG-------GGYHLPNTAR--CWTYLTAL 269
Cdd:cd11683  270 HLLMV--LAGGklcavleGGYHLESLAEsvCMTVQTLL 305
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
 5-262 4.74e-24

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: 100.86  E-value: 4.74e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304   5 VKPKVASMEEMAAFHTDSYLQHLHKVSEEGDNDDPETLEY-------------GLGYDcpiTEGIYDYAAAVGGATLTA- 70
Cdd:cd10009   50 IQGRKASLEEIQLVHSEHHSLLYGTNPLDGQKLDPRILLGddsqkffsslpcgGLGVD---SDTIWNELHSSGAARMAVg 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  71 -----AEQLMAG--KTRIAINWPGGwHHAKKDEASGFCYLNDAVLGILKLREKFD--RVLYVDMDLHHGDGVEDAFSFTS 141
Cdd:cd10009  127 cvielASKVASGelKNGFAVVRPPG-HHAEESTAMGFCFFNSVAITAKYLRDQLNisKILIVDLDVHHGNGTQQAFYADP 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 142 KVMTVSLHKFSPG-FFPGTGDVSDIGLGKGRYYSVNVPLQDGIQ----DEKYYQICEGVLKEVFTTFNPEAVVLQLGADT 216
Cdd:cd10009  206 SILYISLHRYDEGnFFPGSGAPNEVGTGLGEGYNINIAWTGGLDppmgDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDA 285

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 847153304 217 IAGD--PMCSFNMTPQGIGKCLKYVLQWQLPTLILG-GGGYHLpnTARC 262
Cdd:cd10009  286 LEGHtpPLGGYKVTAKCFGHLTKQLMTLADGRVVLAlEGGHDL--TAIC 332
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
 5-260 4.81e-24

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: 100.31  E-value: 4.81e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304   5 VKPKVASMEEMAAFHTDSYLQhLHKVSEEGDNDDPETL--EYGLGYDCPiteGIYDYAAAVGGATLTAAEQLMAGKTR-- 80
Cdd:cd11682   33 VQAREASEEELLLVHSPEYVA-LMKSTQYMTEEELRTLadTYDSVYLHP---NSYSCACLAVGSVLQLVDKVLGGEIRng 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  81 IAINWPGGwHHAKKDEASGFCYLNDAVLGI--LKLREKFDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFSPG-FFP 157
Cdd:cd11682  109 LAIVRPPG-HHAQHDKMDGYCMFNNVAIAAryAQQKHGVQRVLIVDWDVHHGQGTQFIFEQDPSVLYFSIHRYEQGrFWP 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 158 --GTGDVSDIGLGKGRYYSVNVPL-QDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMTPQGIGK 234
Cdd:cd11682  188 hlKESDSSAVGFGRGEGYNINVPWnQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDAVIGDPKGEMAATPACFAH 267

                        250       260
                 ....*....|....*....|....*..
gi 847153304 235 CLKYVLQWQLPTLILG-GGGYHLPNTA 260
Cdd:cd11682  268 LTHLLMGLAGGKLILSlEGGYNLRSLA 294
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
 78-267 1.21e-23

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: 99.70  E-value: 1.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  78 KTRIAINWPGGwHHAKKDEASGFCYLNDAVLGI--LKLREKFDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFSPG- 154
Cdd:cd10008  141 KNGFAVVRPPG-HHADHSTAMGFCFFNSVAIACrqLQQQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGn 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 155 FFPGTGDVSDIGLGKGRYYSVNVPLQDGIQ----DEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPmcsfnmtpq 230
Cdd:cd10008  220 FFPGSGAVDEVGAGSGEGFNVNVAWAGGLDppmgDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHP--------- 290

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 847153304 231 gigkclkyvlqwqlPTLilggGGYHLpnTARCWTYLT 267
Cdd:cd10008  291 --------------APL----GGYHV--SAKCFGYMT 307
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 67-268 4.22e-13

Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily includes metal-dependent enzymes that belong to Arginase-like amidino hydrolase family and histone/histone-like deacetylase class I, II, IV family, respectively. These enzymes catalyze hydrolysis of amide bond. Arginases are known to be involved in control of cellular levels of arginine and ornithine, in histidine and arginine degradation and in clavulanic acid biosynthesis. Deacetylases play a role in signal transduction through histone and/or other protein modification and can repress/activate transcription of a number of different genes. They participate in different 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. Mammalian histone deacetyases 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: 212513  Cd Length: 217  Bit Score: 67.40  E-value: 4.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  67 TLTAAEQLMAGKTRIAINWPGgwHHAKKdeasgfcylNDAVLGILKLREkfdRVLYVDMDLHHGDGVEDAFSFTSK---- 142
Cdd:cd09987   13 LLAGVVVAVLKDGKVPVVLGG--DHSIA---------NGAIRAVAELHP---DLGVIDVDAHHDVRTPEAFGKGNHhtpr 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304 143 ----------VMTVSLHKFSPGFFPGTGDvsdiglGKGRYYSVNVPLQDGIqDEKYYQicegVLKEVF--TTFNPEAVVL 210
Cdd:cd09987   79 hllceplisdVHIVSIGIRGVSNGEAGGA------YARKLGVVYFSMTEVD-KLGLGD----VFEEIVsyLGDKGDNVYL 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 847153304 211 QLGADTIAGDPMCS------FNMTPQGIGKCLKYVLQWQLPTLILGGGGY----HLPNTARCWTYLTA 268
Cdd:cd09987  148 SVDVDGLDPSFAPGtgtpgpGGLSYREGLYITERIAKTNLVVGLDIVEVNplldETGRTARLAAALTL 215
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
 16-135 1.52e-12

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: 67.48  E-value: 1.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847153304  16 AAFHTDSYLQHLHKVSE-------EGDNDDPETLEYGLGYDCPiteGIYDYAAAVGGATLTAAEQLMAG---KTR---IA 82
Cdd:cd09998   38 AAVHGSKWSAELIEMCDmaeaklaKGESEIPAHLPQGDLYLCP---ESLDAIQGALGAVCEAVDSVFKPespGTKrafVA 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 847153304  83 INWPGgwHHAKKDEASGFCYLNDAVLGILK--LREKFDRVLYVDMDLHHGDGVED 135
Cdd:cd09998  115 IRPPG--HHCSESTPSGFCWVNNVHVGAAHayLTHGITRVVILDIDLHHGNGTQD 167
 
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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