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Conserved domains on  [gi|58037203|ref|NP_081658|]
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histone deacetylase 8 isoform 1 [Mus musculus]

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 ...
 16-377 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: 723.36  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  16 PVYIYSPEYVSICDSLVKVPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDEDHP--DS 93
Cdd:cd10000   1 VVYIHSPEYVNLCDRLPKVPNRASMVHSLIEAYGLLKQLRVVKPRVATEEELASFHSDEYIQFLKKASNEGDNDEEpsEQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  94 IEYGLGYDCPATEGIFDYAAAIGGGTITAAQCLIDGKCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFDRIL 173
Cdd:cd10000  81 QEFGLGYDCPIFEGIYDYAAAVAGATLTAAQLLIDGKCKVAINWFGGWHHAQRDEASGFCYVNDIVLGILKLREKFDRVL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 174 YVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDMSDVGLGKGRYYSVNVPIQDGIQDEKYYHICESVLKEVYQ 253
Cdd:cd10000 161 YVDLDLHHGDGVEDAFSFTSKVMTVSLHKYSPGFFPGTGDVSDVGLGKGKYYTVNVPLRDGIQDEQYLQIFTAVVPEIVA 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 254 AFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYVLQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPD 333
Cdd:cd10000 241 AFRPEAVVLQCGADTLAGDPMGAFNLTPVGIGKCLKYVLGWKLPTLILGGGGYNLANTARCWTYLTGLILGEPLSSDIPD 320

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 58037203 334 HEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLKHVV 377
Cdd:cd10000 321 HEFFTSYGPDYELEISPSLRPDLNEDQYIEKILETIKGNLKNVV 364
 
Name Accession Description Interval E-value
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 16-377 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: 723.36  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  16 PVYIYSPEYVSICDSLVKVPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDEDHP--DS 93
Cdd:cd10000   1 VVYIHSPEYVNLCDRLPKVPNRASMVHSLIEAYGLLKQLRVVKPRVATEEELASFHSDEYIQFLKKASNEGDNDEEpsEQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  94 IEYGLGYDCPATEGIFDYAAAIGGGTITAAQCLIDGKCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFDRIL 173
Cdd:cd10000  81 QEFGLGYDCPIFEGIYDYAAAVAGATLTAAQLLIDGKCKVAINWFGGWHHAQRDEASGFCYVNDIVLGILKLREKFDRVL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 174 YVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDMSDVGLGKGRYYSVNVPIQDGIQDEKYYHICESVLKEVYQ 253
Cdd:cd10000 161 YVDLDLHHGDGVEDAFSFTSKVMTVSLHKYSPGFFPGTGDVSDVGLGKGKYYTVNVPLRDGIQDEQYLQIFTAVVPEIVA 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 254 AFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYVLQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPD 333
Cdd:cd10000 241 AFRPEAVVLQCGADTLAGDPMGAFNLTPVGIGKCLKYVLGWKLPTLILGGGGYNLANTARCWTYLTGLILGEPLSSDIPD 320

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 58037203 334 HEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLKHVV 377
Cdd:cd10000 321 HEFFTSYGPDYELEISPSLRPDLNEDQYIEKILETIKGNLKNVV 364
PTZ00063 PTZ00063
histone deacetylase; Provisional
 35-376 1.01e-113

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 338.32  E-value: 1.01e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203   35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDEDHPDSIE---YGLGYDCPATEGIFDY 111
Cdd:PTZ00063  27 PQRIRMAHALILSYDLYKHMEIYRPHKSVEPELVLFHDEEYVDFLSSISPENYRDFTYQLKrfnVGEATDCPVFDGLFEF 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  112 AAAIGGGTITAAQCLIDGKCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFDRILYVDLDLHHGDGVEDAFSF 191
Cdd:PTZ00063 107 QQSCAGASIDGAYKLNNHQADICVNWSGGLHHAKRSEASGFCYINDIVLGILELLKYHARVMYIDIDVHHGDGVEEAFYV 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  192 TSKVMTVSLHKFSpGFFPGTGDMSDVGLGKGRYYSVNVPIQDGIQDEKYYHICESVLKEVYQAFNPKAVVLQLGADTIAG 271
Cdd:PTZ00063 187 THRVMTVSFHKFG-DFFPGTGDVTDIGVAQGKYYSVNVPLNDGIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTG 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  272 DPMCSFNMTPVGIGKCLKYVLQWQLATLILGGGGYNLANTARCWTYLTGVILGKT--LSSEIPDHEFFTAYGPDYVLEIT 349
Cdd:PTZ00063 266 DRLGRFNLTIKGHAACVEFVRSLNIPLLVLGGGGYTIRNVARCWAYETGVILNKHdeMSDQISLNDYYDYYAPDFQLHLQ 345

                        330       340
                 ....*....|....*....|....*..
gi 58037203  350 PSCRPDRNEPHRIQQILNYIKGNLKHV 376
Cdd:PTZ00063 346 PSNIPNYNSPEHLEKIKVKILENLRYL 372
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 35-322 1.54e-102

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: 304.93  E-value: 1.54e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203    35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDEDHPDSIEYGlGYDCPATEGIFDYAAA 114
Cdd:pfam00850   5 PERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAAPEGGALLLLSYLSG-DDDTPVSPGSYEAALL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203   115 IGGGTITAAQCLIDGKCK--VAINWsGGWHHAKKDEASGFCYLNDAVLGILRLRRK--FDRILYVDLDLHHGDGVEDAFS 190
Cdd:pfam00850  84 AAGGTLAAADAVLSGEARnaFALVR-PPGHHAERDRASGFCIFNNVAIAAKYLREKygLKRVAIVDFDVHHGNGTQEIFY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203   191 FTSKVMTVSLHKFSPGFFPGTGDMSDVGLGKGRYYSVNVPIQDGIQDEKYYHICESVLKEVYQAFNPKAVVLQLGADTIA 270
Cdd:pfam00850 163 DDPSVLTLSIHQYPGGFYPGTGFADETGEGKGKGYTLNVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAGFDAHA 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 58037203   271 GDPMCSFNMTPVGIGKCLKYVLQWQLAT----LILGGGGYNLANTARCWTYLTGVI 322
Cdd:pfam00850 243 GDPLGGLNLTTEGFAEITRILLELADPLcirvVSVLEGGYNLDALARSATAVLAAL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 35-324 2.87e-77

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 240.39  E-value: 2.87e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDEdhpdsieYGLGYDCPATEGIFDYAAA 114
Cdd:COG0123  22 PERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAASLDGGY-------GQLDPDTPVSPGTWEAALL 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 115 IGGGTITAAQCLIDGKCKVA-INWSGGWHHAKKDEASGFCYLNDAVLGILRLRRK-FDRILYVDLDLHHGDGVEDAFSFT 192
Cdd:COG0123  95 AAGGALAAADAVLEGEARNAfALVRPPGHHAERDRAMGFCLFNNAAIAARYLLAKgLERVAIVDFDVHHGNGTQDIFYDD 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 193 SKVMTVSLHKFspGFFPGTGDMSDVGLGKGRYYSVNVPIQDGIQDEKYYHICESVLKEVYQAFNPKAVVLQLGADTIAGD 272
Cdd:COG0123 175 PDVLTISIHQD--PLYPGTGAADETGEGAGEGSNLNVPLPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHADD 252

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 58037203 273 PMCSFNMTPVGIGKCLKYVLQW----QLATLILGGGGYNLANTARCWTYLTGVILG 324
Cdd:COG0123 253 PLGRLNLTTEGYAWRTRRVLELadhcGGPVVSVLEGGYNLDALARSVAAHLETLLG 308
 
Name Accession Description Interval E-value
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 16-377 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: 723.36  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  16 PVYIYSPEYVSICDSLVKVPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDEDHP--DS 93
Cdd:cd10000   1 VVYIHSPEYVNLCDRLPKVPNRASMVHSLIEAYGLLKQLRVVKPRVATEEELASFHSDEYIQFLKKASNEGDNDEEpsEQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  94 IEYGLGYDCPATEGIFDYAAAIGGGTITAAQCLIDGKCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFDRIL 173
Cdd:cd10000  81 QEFGLGYDCPIFEGIYDYAAAVAGATLTAAQLLIDGKCKVAINWFGGWHHAQRDEASGFCYVNDIVLGILKLREKFDRVL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 174 YVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDMSDVGLGKGRYYSVNVPIQDGIQDEKYYHICESVLKEVYQ 253
Cdd:cd10000 161 YVDLDLHHGDGVEDAFSFTSKVMTVSLHKYSPGFFPGTGDVSDVGLGKGKYYTVNVPLRDGIQDEQYLQIFTAVVPEIVA 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 254 AFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYVLQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPD 333
Cdd:cd10000 241 AFRPEAVVLQCGADTLAGDPMGAFNLTPVGIGKCLKYVLGWKLPTLILGGGGYNLANTARCWTYLTGLILGEPLSSDIPD 320

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 58037203 334 HEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLKHVV 377
Cdd:cd10000 321 HEFFTSYGPDYELEISPSLRPDLNEDQYIEKILETIKGNLKNVV 364
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
 19-322 3.44e-171

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: 479.39  E-value: 3.44e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  19 IYSPEYVSICDSL--VKVPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDED-HPDSIE 95
Cdd:cd09991   1 FYDPDVGNYYYGQghPMKPHRIRMTHSLILSYGLYKKMEIYRPRPATAEELTKFHSDDYIDFLRSVSPDNMKEfKKQLER 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  96 YGLGYDCPATEGIFDYAAAIGGGTITAAQCLIDGKCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFDRILYV 175
Cdd:cd09991  81 FNVGEDCPVFDGLYEYCQLYAGGSIAAAVKLNRGQADIAINWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 176 DLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDmSDVGLGKGRYYSVNVPIQDGIQDEKYYHICESVLKEVYQAF 255
Cdd:cd09991 161 DIDIHHGDGVEEAFYTTDRVMTVSFHKFGEYFFPGTGL-RDIGAGKGKYYAVNVPLKDGIDDESYLQIFEPVLSKVMEVF 239

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 58037203 256 NPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYVLQWQLATLILGGGGYNLANTARCWTYLTGVI 322
Cdd:cd09991 240 QPSAVVLQCGADSLAGDRLGCFNLSIKGHAKCVKFVKSFNIPLLVLGGGGYTLRNVARCWTYETAVL 306
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
 35-374 5.47e-123

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: 359.79  E-value: 5.47e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDEDHPDSI-EYGLGYDCPATEGIFDYAA 113
Cdd:cd10005  24 PHRLALTHSLVLHYGLYKKMQVYKPYRASAHDMCRFHSEDYIDFLQRVTPQNIQGFTKSLnQFNVGDDCPVFPGLFDFCS 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 114 AIGGGTITAAQCLIDGKCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFDRILYVDLDLHHGDGVEDAFSFTS 193
Cdd:cd10005 104 MYTGASLEGATKLNHKICDIAINWSGGLHHAKKFEASGFCYVNDIVIAILELLKYHPRVLYIDIDIHHGDGVQEAFYLTD 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 194 KVMTVSLHKFSPGFFPGTGDMSDVGLGKGRYYSVNVPIQDGIQDEKYYHICESVLKEVYQAFNPKAVVLQLGADTIAGDP 273
Cdd:cd10005 184 RVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYSVNVPLKDGIDDQSYLQLFKPVIQQVIDFYQPTCIVLQCGADSLGCDR 263

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 274 MCSFNMTPVGIGKCLKYVLQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCR 353
Cdd:cd10005 264 LGCFNLSIKGHGECVEFVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVDEEISNELPYNEYFEYFAPDFTLHPDVSTR 343

                       330       340
                ....*....|....*....|..
gi 58037203 354 PD-RNEPHRIQQILNYIKGNLK 374
Cdd:cd10005 344 IEnQNSKQYLDQIRQTVFENLK 365
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
 35-375 9.19e-122

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: 356.81  E-value: 9.19e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEG-DEDHPDSIEYGLGYDCPATEGIFDYAA 113
Cdd:cd10004  25 PHRIRMAHSLVMNYGLYKKMEIYRAKPATKNEMTQFHTDEYIDFLSRVTPDNmEKFQKEQVKYNVGDDCPVFDGLFEFCS 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 114 AIGGGTITAAQCLIDGKCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFDRILYVDLDLHHGDGVEDAFSFTS 193
Cdd:cd10004 105 ISAGGSMEGAARLNRGKCDIAVNWAGGLHHAKKSEASGFCYVNDIVLGILELLRYHQRVLYIDIDVHHGDGVEEAFYTTD 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 194 KVMTVSLHKFSPgFFPGTGDMSDVGLGKGRYYSVNVPIQDGIQDEKYYHICESVLKEVYQAFNPKAVVLQLGADTIAGDP 273
Cdd:cd10004 185 RVMTCSFHKYGE-YFPGTGELRDIGIGTGKNYAVNVPLRDGIDDESYKSIFEPVIKHVMEWYQPEAVVLQCGGDSLSGDR 263

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 274 MCSFNMTPVGIGKCLKYVLQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCR 353
Cdd:cd10004 264 LGCFNLSMKGHANCVNFVKSFNLPMLVLGGGGYTMRNVARTWAFETGLLAGEELDKDLPYNEYYEYYGPDYELNVRPSNM 343

                       330       340
                ....*....|....*....|..
gi 58037203 354 PDRNEPHRIQQILNYIKGNLKH 375
Cdd:cd10004 344 ENHNTPEYLDKITTAVIENLRN 365
PTZ00063 PTZ00063
histone deacetylase; Provisional
 35-376 1.01e-113

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 338.32  E-value: 1.01e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203   35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDEDHPDSIE---YGLGYDCPATEGIFDY 111
Cdd:PTZ00063  27 PQRIRMAHALILSYDLYKHMEIYRPHKSVEPELVLFHDEEYVDFLSSISPENYRDFTYQLKrfnVGEATDCPVFDGLFEF 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  112 AAAIGGGTITAAQCLIDGKCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFDRILYVDLDLHHGDGVEDAFSF 191
Cdd:PTZ00063 107 QQSCAGASIDGAYKLNNHQADICVNWSGGLHHAKRSEASGFCYINDIVLGILELLKYHARVMYIDIDVHHGDGVEEAFYV 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  192 TSKVMTVSLHKFSpGFFPGTGDMSDVGLGKGRYYSVNVPIQDGIQDEKYYHICESVLKEVYQAFNPKAVVLQLGADTIAG 271
Cdd:PTZ00063 187 THRVMTVSFHKFG-DFFPGTGDVTDIGVAQGKYYSVNVPLNDGIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTG 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  272 DPMCSFNMTPVGIGKCLKYVLQWQLATLILGGGGYNLANTARCWTYLTGVILGKT--LSSEIPDHEFFTAYGPDYVLEIT 349
Cdd:PTZ00063 266 DRLGRFNLTIKGHAACVEFVRSLNIPLLVLGGGGYTIRNVARCWAYETGVILNKHdeMSDQISLNDYYDYYAPDFQLHLQ 345

                        330       340
                 ....*....|....*....|....*..
gi 58037203  350 PSCRPDRNEPHRIQQILNYIKGNLKHV 376
Cdd:PTZ00063 346 PSNIPNYNSPEHLEKIKVKILENLRYL 372
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
 35-374 5.63e-110

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: 326.64  E-value: 5.63e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDEDHPDSIE-YGLGYDCPATEGIFDYAA 113
Cdd:cd10010  29 PHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQrFNVGEDCPVFDGLFEFCQ 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 114 AIGGGTITAAQCLIDGKCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFDRILYVDLDLHHGDGVEDAFSFTS 193
Cdd:cd10010 109 LSAGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTD 188

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 194 KVMTVSLHKFSPgFFPGTGDMSDVGLGKGRYYSVNVPIQDGIQDEKYYHICESVLKEVYQAFNPKAVVLQLGADTIAGDP 273
Cdd:cd10010 189 RVMTVSFHKYGE-YFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGADSLSGDR 267

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 274 MCSFNMTPVGIGKCLKYVLQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCR 353
Cdd:cd10010 268 LGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDSEIPNELPYNDYFEYFGPDFKLHISPSNM 347

                       330       340
                ....*....|....*....|.
gi 58037203 354 PDRNEPHRIQQILNYIKGNLK 374
Cdd:cd10010 348 TNQNTNEYLEKIKQRLFENLR 368
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
 35-321 1.21e-109

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: 323.25  E-value: 1.21e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVS-QEGDEDHPDSIE-YGLGYDCPATEGIFDYA 112
Cdd:cd11598  22 PFRLTLTKHLVMGYGLHKAMDTYEARAATREELRQFHDADYLDFLSKVSpENANQLRFDKAEpFNIGDDCPVFDGMYDYC 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 113 AAIGGGTITAAQCLIDGKCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFDRILYVDLDLHHGDGVEDAFSFT 192
Cdd:cd11598 102 QLYAGASLDAARKLCSGQSDIAINWSGGLHHAKKSEASGFCYVNDIVLAILNLLRYFPRVLYIDIDVHHGDGVEEAFYRT 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 193 SKVMTVSLHKFSPGFFPGTGDMSDVGLGKGRYYSVNVPIQDGIQDEKYYHICESVLKEVYQAFNPKAVVLQLGADTIAGD 272
Cdd:cd11598 182 DRVMTLSFHKYNGEFFPGTGDLDDNGGTPGKHFALNVPLEDGIDDEQYNLLFKSIIGPTIEKFQPSAIVLQCGADSLGGD 261

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 58037203 273 PMCSFNMTPVGIGKCLKYVLQWQLATLILGGGGYNLANTARCWTYLTGV 321
Cdd:cd11598 262 RLGQFNLNIKAHGACVKFVKSFGIPMLVVGGGGYTPRNVARAWCYETAV 310
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
 17-322 1.88e-109

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: 322.29  E-value: 1.88e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  17 VYIYSPEYVSICDSLVKVPKRASMVHSLIEAYALHKQM-RIVKPKVASMEEMATFHTDAYLQHLQKvsqegdedhpdsiE 95
Cdd:cd11680   1 ILSVSEELTKIADLLPSNKGRSSLVHSLIRAYGLLQHFdEIIEPERATRKDLTKYHDKDYVDFLLK-------------K 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  96 YGLGYDCPATEGIFDYAAAIGGGTITAAQCLIDG-KCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRK-FDRIL 173
Cdd:cd11680  68 YGLEDDCPVFPFLSMYVQLVAGSSLALAKHLITQvERDIAINWYGGRHHAQKSRASGFCYVNDIVLAILRLRRArFRRVF 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 174 YVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDMSDvglgKGRYYSVNVPIQDGIQDEKYYHICESVLKEVYQ 253
Cdd:cd11680 148 YLDLDLHHGDGVESAFFFSKNVLTCSIHRYDPGFFPGTGSLKN----SSDKGMLNIPLKRGLSDKTLLRIIDSIVRPLIE 223

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58037203 254 AFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYVLQW--QLATLILGGGGYNLANTARCWTYLTGVI 322
Cdd:cd11680 224 KFEPEVIVIQCGCDGLSGDPHKEWNLTIRGYGSVIELLLKEfkDKPTLLLGGGGYNHTEAARAWTYLTSMV 294
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
 35-374 1.49e-105

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: 315.08  E-value: 1.49e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDEDHPDSIE-YGLGYDCPATEGIFDYAA 113
Cdd:cd10011  25 PHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQrFNVGEDCPVFDGLFEFCQ 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 114 AIGGGTITAAQCLIDGKCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFDRILYVDLDLHHGDGVEDAFSFTS 193
Cdd:cd10011 105 LSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTD 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 194 KVMTVSLHKFSPGFfPGTGDMSDVGLGKGRYYSVNVPIQDGIQDEKYYHICESVLKEVYQAFNPKAVVLQLGADTIAGDP 273
Cdd:cd10011 185 RVMTVSFHKYGEYF-PGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDR 263

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 274 MCSFNMTPVGIGKCLKYVLQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCR 353
Cdd:cd10011 264 LGCFNLTVKGHAKCVEVVKTFNLPLLMLGGGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNM 343

                       330       340
                ....*....|....*....|.
gi 58037203 354 PDRNEPHRIQQILNYIKGNLK 374
Cdd:cd10011 344 TNQNTPEYMEKIKQRLFENLR 364
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 35-322 1.54e-102

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: 304.93  E-value: 1.54e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203    35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDEDHPDSIEYGlGYDCPATEGIFDYAAA 114
Cdd:pfam00850   5 PERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAAPEGGALLLLSYLSG-DDDTPVSPGSYEAALL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203   115 IGGGTITAAQCLIDGKCK--VAINWsGGWHHAKKDEASGFCYLNDAVLGILRLRRK--FDRILYVDLDLHHGDGVEDAFS 190
Cdd:pfam00850  84 AAGGTLAAADAVLSGEARnaFALVR-PPGHHAERDRASGFCIFNNVAIAAKYLREKygLKRVAIVDFDVHHGNGTQEIFY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203   191 FTSKVMTVSLHKFSPGFFPGTGDMSDVGLGKGRYYSVNVPIQDGIQDEKYYHICESVLKEVYQAFNPKAVVLQLGADTIA 270
Cdd:pfam00850 163 DDPSVLTLSIHQYPGGFYPGTGFADETGEGKGKGYTLNVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAGFDAHA 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 58037203   271 GDPMCSFNMTPVGIGKCLKYVLQWQLAT----LILGGGGYNLANTARCWTYLTGVI 322
Cdd:pfam00850 243 GDPLGGLNLTTEGFAEITRILLELADPLcirvVSVLEGGYNLDALARSATAVLAAL 298
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
 35-322 4.18e-100

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: 299.09  E-value: 4.18e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDEDhpDSIEYGLG-YDCPATEGIFDYAA 113
Cdd:cd09994  21 PPRLSLTKDLLRALGLLPPVDLVPPRPATEEELLLFHTPDYIEAVKEASRGQEPE--GRGRLGLGtEDNPVFPGMHEAAA 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 114 AIGGGTITAAQCLIDGKCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRK-FDRILYVDLDLHHGDGVEDAFSFT 192
Cdd:cd09994  99 LVVGGTLLAARLVLEGEARRAFNPAGGLHHAMRGRASGFCVYNDAAVAIERLRDKgGLRVAYVDIDAHHGDGVQAAFYDD 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 193 SKVMTVSLHKFSPGFFPGTGDMSDVGLGKGRYYSVNVPIQDGIQDEKYYHICESVLKEVYQAFNPKAVVLQLGADTIAGD 272
Cdd:cd09994 179 PRVLTISLHESGRYLFPGTGFVDEIGEGEGYGYAVNIPLPPGTGDDEFLRAFEAVVPPLLRAFRPDVIVSQHGADAHAGD 258

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 58037203 273 PMCSFNMTPVGIGKCLKYVLQW-----QLATLILGGGGYNLANTARCWTYLTGVI 322
Cdd:cd09994 259 PLTHLNLSNRAYRAAVRRIRELadeycGGRWLALGGGGYNPDVVARAWALLWAVL 313
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 35-324 2.87e-77

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 240.39  E-value: 2.87e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDEdhpdsieYGLGYDCPATEGIFDYAAA 114
Cdd:COG0123  22 PERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAASLDGGY-------GQLDPDTPVSPGTWEAALL 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 115 IGGGTITAAQCLIDGKCKVA-INWSGGWHHAKKDEASGFCYLNDAVLGILRLRRK-FDRILYVDLDLHHGDGVEDAFSFT 192
Cdd:COG0123  95 AAGGALAAADAVLEGEARNAfALVRPPGHHAERDRAMGFCLFNNAAIAARYLLAKgLERVAIVDFDVHHGNGTQDIFYDD 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 193 SKVMTVSLHKFspGFFPGTGDMSDVGLGKGRYYSVNVPIQDGIQDEKYYHICESVLKEVYQAFNPKAVVLQLGADTIAGD 272
Cdd:COG0123 175 PDVLTISIHQD--PLYPGTGAADETGEGAGEGSNLNVPLPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHADD 252

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 58037203 273 PMCSFNMTPVGIGKCLKYVLQW----QLATLILGGGGYNLANTARCWTYLTGVILG 324
Cdd:COG0123 253 PLGRLNLTTEGYAWRTRRVLELadhcGGPVVSVLEGGYNLDALARSVAAHLETLLG 308
PTZ00346 PTZ00346
histone deacetylase; Provisional
 35-327 3.23e-77

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 244.56  E-value: 3.23e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203   35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDEDHPDSIEYGLGYDCPATEGIFDYAAA 114
Cdd:PTZ00346  47 PYRVLAAMEIVRSLKIDAHCRTVVPPLVKVEELMAYHTDTYLANLGLHSCRSWLWNAETSKVFFSGDCPPVEGLMEHSIA 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  115 IGGGTITAAQCLIDGKCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFDRILYVDLDLHHGDGVEDAFSFTSK 194
Cdd:PTZ00346 127 TASGTLMGAVLLNSGQVDVAVHWGGGMHHSKCGECSGFCYVNDIVLGILELLKCHDRVLYVDIDMHHGDGVDEAFCTSDR 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  195 VMTVSLHKFSPGFFPGTGDMSDVGLGKGRYYSVNVPIQDGIQDEKYYHICESVLKEVYQAFNPKAVVLQLGADTIAGDPM 274
Cdd:PTZ00346 207 VFTLSLHKFGESFFPGTGHPRDVGYGRGRYYSMNLAVWDGITDFYYLGLFEHALHSIVRRYSPDAIVLQCGADSLAGDRL 286

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 58037203  275 CSFNMTPVGIGKCLKYVLQWQLATLILGGGGYNLANTARCWTYLTGVILGKTL 327
Cdd:PTZ00346 287 GLLNLSSFGHGQCVQAVRDLGIPMLALGGGGYTIRNVAKLWAYETSILTGHPL 339
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
 37-322 1.03e-69

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: 220.38  E-value: 1.03e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  37 RASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKvsQEGDEDHPDSIEYGLGYDCPATEGIFDYAAAIG 116
Cdd:cd09301   1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKA--NFAVATITESKPVIFGPNFPVQRHYFRGARLST 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 117 GGTITAAQCLIDGKCKVAINW-SGGWHHAKKDEASGFCYLNDAVLGILRLRRK-FDRILYVDLDLHHGDGVEDAFSFTSK 194
Cdd:cd09301  79 GGVVEAAELVAKGELERAFAVvGAGGHHAGKSRAWGFCYFNDVVLAIKFLRERgISRILIIDTDAHHGDGTREAFYDDDR 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 195 VMTVSLHKFSPGFFpgtgdmsdvGLGKGRYYSVNVPIQDGIQDEKYYHICESVLKEVYQAFNPKAVVLQLGADTIAGDPM 274
Cdd:cd09301 159 VLHMSFHNYDIYPF---------GRGKGKGYKINVPLEDGLGDEEYLDAVERVISKVLEEFEPEVVVLQFGHDTHEGDRL 229

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 58037203 275 CSFNMTPVGIGKCLKYV--LQWQLATLILGGGGYNLANTARCWTYLTGVI 322
Cdd:cd09301 230 GGFNLSEKGFVKLAEIVkeFARGGPILMVLGGGYNPEAAARIWTAIIKEL 279
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
 35-314 6.04e-48

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: 164.21  E-value: 6.04e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGD-EDHPDsieyglgydCPATEGIFD--Y 111
Cdd:cd09992   5 PERLLAILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYIERVEETCEAGGgYLDPD---------TYVSPGSYEaaL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 112 AAAigGGTITAAQCLIDGKCK---VAINWSGgwHHAKKDEASGFCYLNDAVLGI--LRLRRKFDRILYVDLDLHHGDGVE 186
Cdd:cd09992  76 LAA--GAALAAVDAVLSGEAEnafALVRPPG--HHAEPDRAMGFCLFNNVAIAAryAQKRYGLKRVLIVDWDVHHGNGTQ 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 187 DAFSFTSKVMTVSLHKFspGFFPGTGDMSDVGLGKGRYYSVNVPIQDGIQDEKYYHICESVLKEVYQAFNPKAVVLQLGA 266
Cdd:cd09992 152 DIFYDDPSVLYFSIHQY--PFYPGTGAAEETGGGAGEGFTINVPLPPGSGDAEYLAAFEEVLLPIAREFQPDLVLVSAGF 229

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 58037203 267 DTIAGDPMCSFNMTPVGIGKCLKYVLqwQLATLILGG-------GGYNLANTARC 314
Cdd:cd09992 230 DAHRGDPLGGMNLTPEGYARLTRLLK--ELADEHCGGrlvfvleGGYNLEALAES 282
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
 23-329 3.40e-43

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: 153.26  E-value: 3.40e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  23 EYVSICDS-LVKVPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDED-HPDSIEYGLGY 100
Cdd:cd10003   7 NHHNLWDPgHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHLDEMKSLEKMKPRElNRLGKEYDSIY 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 101 DCPATegiFDYAAAIGGGTITAAQCLIDGKCK--VAINWSGGwHHAKKDEASGFCYLNDAVLGILRLRRKFD--RILYVD 176
Cdd:cd10003  87 IHPDS---YQCALLAAGCVLQVVEAVLTGESRngVAIVRPPG-HHAEQDTACGFCFFNNVAIAARYAQKKYGlkRILIVD 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 177 LDLHHGDGVEDAFSFTSKVMTVSLHKFSPG-FFPGT--GDMSDVGLGKGRYYSVNVPI-QDGIQDEKYYHICESVLKEVY 252
Cdd:cd10003 163 WDVHHGNGTQHMFESDPSVLYISLHRYDNGsFFPNSpeGNYDVVGKGKGEGFNVNIPWnKGGMGDAEYIAAFQQVVLPIA 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 253 QAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKclkyvLQWQLATLILGG------GGYNLANTARCWTYLTGVILGKT 326
Cdd:cd10003 243 YEFNPELVLVSAGFDAARGDPLGGCKVTPEGYAH-----MTHMLMSLAGGRvivileGGYNLTSISESMSMCTKTLLGDP 317


                ...
gi 58037203 327 LSS 329
Cdd:cd10003 318 PPV 320
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
 41-314 2.26e-40

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: 146.17  E-value: 2.26e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  41 VHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDEDhpdsieygLGYDCPATEGIFDYAAAIGGGTI 120
Cdd:cd09996  43 IKNLLEVSGLSDHLVLITPRPATDEELLRVHTPEYIDRVKAASAAGGGE--------AGGGTPFGPGSYEIALLAAGGAI 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 121 TAAQCLIDGKCKVA---INWSGgwHHAKKDEASGFCYLNDAVLGILRLRRKFD--RILYVDLDLHHGDGVEDAFSFTSKV 195
Cdd:cd09996 115 AAVDAVLDGEVDNAyalVRPPG--HHAEPDQGMGFCLFNNVAIAARHALAVGGvkRVAVVDWDVHHGNGTQAIFYDDPDV 192

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 196 MTVSLHKFSPgFFPGTGDMSDVGLGKGRYYSVNVPIQDGIQDEKYYHICESVLKEVYQAFNPKAVVLQLGADTIAGDPMC 275
Cdd:cd09996 193 LTISLHQDRC-FPPDSGAVEERGEGAGEGYNLNIPLPPGSGDGAYLHAFERIVLPALRAFRPELIIVASGFDASAFDPLG 271

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 58037203 276 SFNMTPVG---IGKCLKyvlqwQLATLILGG-------GGYNLANTARC 314
Cdd:cd09996 272 RMMLTSDGfraLTRKLR-----DLADELCGGrlvmvheGGYSEAYVPFC 315
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
 34-309 3.87e-39

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: 141.14  E-value: 3.87e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  34 VPKRASMVHSLIEAYALhkqMRIVKPKVASMEEMATFHTDAYLQHLQKVSQegdedhpdsieyglgyDCPATEGIFDYAA 113
Cdd:cd10001  28 NPERAEAILDALKRAGL---GEVLPPRDFGLEPILAVHDPDYVDFLETADT----------------DTPISEGTWEAAL 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 114 AIGGGTITAAQCLIDGkCKVAINWS---GgwHHAKKDEASGFCYLNDAVLGILRLRRKFDRILYVDLDLHHGDGVEDAFS 190
Cdd:cd10001  89 AAADTALTAADLVLEG-ERAAYALCrppG--HHAGRDRAGGFCYFNNAAIAAQYLRDRAGRVAILDVDVHHGNGTQEIFY 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 191 FTSKVMTVSLHKFSPGFFPGT-GDMSDVGLGKGRYYSVNVPIQDGIQDEKYYHICESVLKEVyQAFNPKAVVLQLGADTI 269
Cdd:cd10001 166 ERPDVLYVSIHGDPRTFYPFFlGFADETGEGEGEGYNLNLPLPPGTGDDDYLAALDEALAAI-AAFGPDALVVSLGFDTH 244

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 58037203 270 AGDPMCSFNMTPVG---IGKCLKyvlQWQLATLILGGGGYNLA 309
Cdd:cd10001 245 EGDPLSDFKLTTEDyarIGRRIA---ALGLPTVFVQEGGYNVD 284
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 37-307 5.58e-39

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: 140.33  E-value: 5.58e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  37 RASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLqkVSQEGDEDHPDSIEYglgydcPATEGIFDYAAAIG 116
Cdd:cd09993   7 KYGLLREALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLESL--KSGELSREEIRRIGF------PWSPELVERTRLAV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 117 GGTITAAQ-CLidgKCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRK--FDRILYVDLDLHHGDGVEDAFSFTS 193
Cdd:cd09993  79 GGTILAARlAL---EHGLAINLAGGTHHAFPDRGEGFCVFNDIAIAARVLLAEglVRRVLIVDLDVHQGNGTAAIFADDP 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 194 KVMTVSLHkfSPGFFPGTGDMSDvglgkgryysVNVPIQDGIQDEKYYHICESVLKEVYQAFNPKAVVLQLGADTIAGDP 273
Cdd:cd09993 156 SVFTFSMH--GEKNYPFRKEPSD----------LDVPLPDGTGDDEYLAALEEALPRLLAEFRPDLVFYNAGVDVLAGDR 223

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 58037203 274 MCSFNMTPVGIGKCLKYVLQWQLA----TLILGGGGYN 307
Cdd:cd09993 224 LGRLSLSLEGLRERDRLVLRFARArgipVAMVLGGGYS 261
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 35-324 3.26e-34

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: 128.62  E-value: 3.26e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDEDHPDSIEYGLG---YDCPATegiFDY 111
Cdd:cd11600   7 PSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEHWDRVEATEKMSDEQLKDRTEIFERdslYVNNDT---AFC 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 112 AAAIGGGTITAAQCLIDGKCK--VAINWSGGwHHAKKDEASGFCYLNDAVLG--ILRLRR--KFDRILYVDLDLHHGDGV 185
Cdd:cd11600  84 ARLSCGGAIEACRAVAEGRVKnaFAVVRPPG-HHAEPDESMGFCFFNNVAVAakWLQTEYpdKIKKILILDWDIHHGNGT 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 186 EDAFSFTSKVMTVSLHKFSPG-FFPGT--GDMSDVGLGKGRYYSVNVP-IQDGIQDEKYYHICESVLKEVYQAFNPKAVV 261
Cdd:cd11600 163 QRAFYDDPNVLYISLHRFENGgFYPGTpyGDYESVGEGAGLGFNVNIPwPQGGMGDADYIYAFQRIVMPIAYEFDPDLVI 242

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58037203 262 LQLGADTIAGDPMCSFNMTPVGIGKclkyvLQWQLATLILGG------GGYNLANTARCWTYLTGVILG 324
Cdd:cd11600 243 ISAGFDAADGDELGQCHVTPAGYAH-----MTHMLMSLAGGKlvvaleGGYNLDAISDSALAVAKVLLG 306
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 29-324 5.58e-30

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: 117.41  E-value: 5.58e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  29 DSLVKVPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQ-EGDEDHPDSIEYGLGYDCPATeg 107
Cdd:cd10002   5 SNHIECPERLEAILERLTQDGLLERCVKIPAREAEEDEILLVHSQEYIDLVKSTETmEKEELESLCSGYDSVYLCPST-- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 108 iFDYAAAIGGGTITAAQCLIDGKCK--VAINWSGGwHHAKKDEASGFCYLNDAVLGILRLRRKF--DRILYVDLDLHHGD 183
Cdd:cd10002  83 -YEAARLAAGSTIELVKAVMAGKIQngFALIRPPG-HHAMRNEANGYCIFNNVAIAAKYAIEKLglKRILIVDWDVHHGQ 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 184 GVEDAFSFTSKVMTVSLHKFSPG-FFPG--TGDMSDVGLGKGRYYSVNVPI-QDGIQDEKYYHICESVLKEVYQAFNPKA 259
Cdd:cd10002 161 GTQQGFYEDPRVLYFSIHRYEHGrFWPHlfESDYDYIGVGHGYGFNVNVPLnQTGLGDADYLAIFHHILLPLALEFQPEL 240

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58037203 260 VVLQLGADTIAGDPMCSFNMTPVGIGKCLKYVLQWQLATLILG-GGGYNLANTARCWTYLTGVILG 324
Cdd:cd10002 241 VLVSAGFDASIGDPEGEMAVTPAGYAHLTRLLMGLAGGKLLLVlEGGYLLESLAESVSMTLRGLLG 306
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
 27-324 4.24e-29

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: 116.67  E-value: 4.24e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  27 ICDSLVKVPKRASMVHSL---IEAYALHKQMRIVKPKVASMEEMATFHTDAYLQ-------HLQKVSQEGDEDHPDSIEY 96
Cdd:cd10006  20 TCGNSNSHPEHAGRIQSIwsrLQETGLRGKCECIRGRKATLEELQTVHSEAHTLlygtnplNRQKLDSKKLLGSLASVFV 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  97 -----GLGYDcpaTEGIFDYAAAIGGGTItAAQCLIDGKCKVAI-NWSGGW-------HHAKKDEASGFCYLNDAVLG-- 161
Cdd:cd10006 100 rlpcgGVGVD---SDTIWNEVHSSGAARL-AVGCVVELVFKVATgELKNGFavvrppgHHAEESTPMGFCYFNSVAIAak 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 162 ILRLRRKFDRILYVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPG-FFPGTGDMSDVGLGKGRYYSVNVPIQDGIQ---- 236
Cdd:cd10006 176 LLQQRLNVSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYDDGnFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDppmg 255

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 237 DEKYYHICESVLKEVYQAFNPKAVVLQLGADTIAGDPmcsfnmTPVgigkclkyvlqwqlatlilggGGYNLanTARCWT 316
Cdd:cd10006 256 DAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHP------TPL---------------------GGYNL--SAKCFG 306


                ....*...
gi 58037203 317 YLTGVILG 324
Cdd:cd10006 307 YLTKQLMG 314
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 44-319 1.36e-28

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: 114.75  E-value: 1.36e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  44 LIEAYALHKQMRIvKPKVASMEEMATFHTDAY-------LQHLQKVSQEGDEDHPDSIEY-----GLGYDcpaTEGIFDY 111
Cdd:cd11681  38 LQETGLVNRCERL-RGRKATLEELQLVHSEVHtllygtnPLSRLKLDPTKLAGLPQKSFVrlpcgGIGVD---SDTVWNE 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 112 AAAIGGGTItAAQCLIDGKCKVAIN-WSGGW-------HHAKKDEASGFCYLNDAVLG--ILRLRRKFDRILYVDLDLHH 181
Cdd:cd11681 114 LHTSNAARM-AVGCVIDLAFKVATGeLKNGFavvrppgHHAEPSQAMGFCFFNSVAIAakQLQQKLKLRKILIVDWDVHH 192

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 182 GDGVEDAFSFTSKVMTVSLHKFSPG-FFPGTGDMSDVGLGKGRYYSVNVPIQDGIQ----DEKYYHICESVLKEVYQAFN 256
Cdd:cd11681 193 GNGTQQIFYEDPNVLYISLHRYDDGnFFPGTGAPTEVGSGAGEGFNVNIAWSGGLDppmgDAEYLAAFRTVVMPIAREFS 272

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58037203 257 PKAVVLQLGADTIAGDPmcsfnmtpvgigkclkyvlqwqlATLilggGGYNLanTARCWTYLT 319
Cdd:cd11681 273 PDIVLVSAGFDAAEGHP-----------------------PPL----GGYKV--SPACFGYMT 306
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
 121-314 4.78e-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: 105.45  E-value: 4.78e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 121 TAAQCLIDGKCKVAI-NWSGGW-------HHAKKDEASGFCYLNDAVLGILRLRRKFD--RILYVDLDLHHGDGVEDAFS 190
Cdd:cd10007 125 MAVGCLIELAFKVAAgELKNGFavirppgHHAEESTAMGFCFFNSVAIAAKLLQQKLNvgKILIVDWDIHHGNGTQQAFY 204

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 191 FTSKVMTVSLHKFSPG-FFPGTGDMSDVGLGKGRYYSVNVPIQDGIQ----DEKYYHICESVLKEVYQAFNPKAVVLQLG 265
Cdd:cd10007 205 NDPNVLYISLHRYDDGnFFPGSGAPDEVGAGPGVGFNVNIAWTGGVDppigDVEYLTAFRTVVMPIANEFSPDVVLVSAG 284

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 58037203 266 ADTIAG--DPMCSFNMTpvgiGKCLKYvLQWQLATLIlGG-------GGYNLanTARC 314
Cdd:cd10007 285 FDAVEGhqSPLGGYSVT----AKCFGH-LTKQLMTLA-GGrvvlaleGGHDL--TAIC 334
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
 142-314 9.34e-25

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: 103.94  E-value: 9.34e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 142 HHAKKDEASGFCYLNDAVLGI--LRLRRKFDRILYVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPG-FFPGTGDMSDVG 218
Cdd:cd10008 152 HHADHSTAMGFCFFNSVAIACrqLQQQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGnFFPGSGAVDEVG 231

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 219 LGKGRYYSVNVPIQDGIQ----DEKYYHICESVLKEVYQAFNPKAVVLQLGADTIAGDPmcsfnmTPVG----IGKCLKY 290
Cdd:cd10008 232 AGSGEGFNVNVAWAGGLDppmgDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHP------APLGgyhvSAKCFGY 305

                       170       180       190
                ....*....|....*....|....*....|
gi 58037203 291 VLQwQLATLILGG------GGYNLanTARC 314
Cdd:cd10008 306 MTQ-QLMNLAGGAvvlaleGGHDL--TAIC 332
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
 27-314 1.02e-23

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: 1.02e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  27 ICDSLVKVPKRASMVHS----LIEAYALHKQMRIvKPKVASMEEMATFHTDAYLQHLQKVSQEGDEDHP------DSIEY 96
Cdd:cd10009  17 VCGNSTTHPEHAGRIQSiwsrLQETGLLNKCERI-QGRKASLEEIQLVHSEHHSLLYGTNPLDGQKLDPrillgdDSQKF 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  97 -------GLGYDcpaTEGIFDYAAAIGGGTItAAQCLIDGKCKVAI-NWSGGW-------HHAKKDEASGFCYLNDAVLG 161
Cdd:cd10009  96 fsslpcgGLGVD---SDTIWNELHSSGAARM-AVGCVIELASKVASgELKNGFavvrppgHHAEESTAMGFCFFNSVAIT 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 162 ILRLRRKFD--RILYVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPG-FFPGTGDMSDVGLGKGRYYSVNVPIQDGIQ-- 236
Cdd:cd10009 172 AKYLRDQLNisKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGnFFPGSGAPNEVGTGLGEGYNINIAWTGGLDpp 251

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 237 --DEKYYHICESVLKEVYQAFNPKAVVLQLGADTIAGD--PMCSFNMTPVGIGKCLKYVLQWQLATLILG-GGGYNLanT 311
Cdd:cd10009 252 mgDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLADGRVVLAlEGGHDL--T 329


                ...
gi 58037203 312 ARC 314
Cdd:cd10009 330 AIC 332
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
 29-312 1.60e-23

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: 99.93  E-value: 1.60e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  29 DSLVKVPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQhLQKVSQEGDEDHPDSI--EYGLGYDCPate 106
Cdd:cd11682   5 ESFPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYVA-LMKSTQYMTEEELRTLadTYDSVYLHP--- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 107 GIFDYAAAIGGGTITAAQCLIDGKCK--VAINWSGGwHHAKKDEASGFCYLNDAVLGI--LRLRRKFDRILYVDLDLHHG 182
Cdd:cd11682  81 NSYSCACLAVGSVLQLVDKVLGGEIRngLAIVRPPG-HHAQHDKMDGYCMFNNVAIAAryAQQKHGVQRVLIVDWDVHHG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 183 DGVEDAFSFTSKVMTVSLHKFSPG-FFP--GTGDMSDVGLGKGRYYSVNVPI-QDGIQDEKYYHICESVLKEVYQAFNPK 258
Cdd:cd11682 160 QGTQFIFEQDPSVLYFSIHRYEQGrFWPhlKESDSSAVGFGRGEGYNINVPWnQVGMRDADYIAAFLHVLLPVALEFQPQ 239

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 58037203 259 AVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYVLQWQLATLILG-GGGYNLANTA 312
Cdd:cd11682 240 LVLVAAGFDAVIGDPKGEMAATPACFAHLTHLLMGLAGGKLILSlEGGYNLRSLA 294
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
 55-280 3.64e-22

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: 94.89  E-value: 3.64e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  55 RIVKPKVASMEEMATFHTDAYLQHL-QKVSQEG----DED---HPDSIEYGLgydcpategifdYAAaigGGTITAAQCL 126
Cdd:cd11599  25 RQLEAPPATREQLLRVHDAAYVDRLeAAAPEEGlvqlDPDtamSPGSLEAAL------------RAA---GAVVAAVDAV 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 127 IDGKCK---VAINWSGgwHHAKKDEASGFCYLNDAVLGIL--RLRRKFDRILYVDLDLHHGDGVEDAFSFTSKVMTVSLH 201
Cdd:cd11599  90 MAGEARnafCAVRPPG--HHAERDKAMGFCLFNNVAIAAAhaLAHHGLERVAIVDFDVHHGNGTEDIFRDDPRVLFCSSH 167

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58037203 202 KFspGFFPGTGDMSDVGLGkgryYSVNVPIQDGIQDEKYYHICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMT 280
Cdd:cd11599 168 QH--PLYPGTGAPDETGHG----NIVNVPLPAGTGGAEFREAVEDRWLPALDAFKPDLILISAGFDAHRDDPLAQLNLT 240
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 27-319 4.86e-21

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: 92.62  E-value: 4.86e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  27 ICDslVKVPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDEDHPD-SIEYGLGYDCPAT 105
Cdd:cd11683   5 ECE--IEVPERLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRETQVMNKEELMAiSGKYDAVYFHPNT 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 106 egiFDYAAAIGGGTITAAQCLIDGKCK--VAINWSGGwHHAKKDEASGFCYLNDAVLGILRLRRKF--DRILYVDLDLHH 181
Cdd:cd11683  83 ---FHCARLAAGATLQLVDAVLTGEVQngMALVRPPG-HHSQRNAANGFCVFNNVAIAAEYAKKKYglHRILIVDWDVHH 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 182 GDGVEDAFSFTSKVMTVSLHKFSPG-FFPG--TGDMSDVGLGKGRYYSVNVPI-QDGIQDEKYYHICESVLKEVYQAFNP 257
Cdd:cd11683 159 GQGIQYIFEEDPSVLYFSWHRYEHQrFWPFlrESDYDAVGRGKGLGFNINLPWnKVGMGNADYLAAFFHVLLPLAFEFDP 238

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58037203 258 KAVVLQLGADTIAGDPMCSFNMTPvgigKCLKYVLqwQLATLILGG-------GGYNLANTAR--CWTYLT 319
Cdd:cd11683 239 ELVLVSAGFDSAIGDPEGQMCATP----ECFAHLT--HLLMVLAGGklcavleGGYHLESLAEsvCMTVQT 303
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 121-322 1.00e-12

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: 66.63  E-value: 1.00e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 121 TAAQCL--IDGKCKVAINWSGgwHHAKKdeasgfcylNDAVLGILRLrrkFDRILYVDLDLHHGDGVEDAFSFTSK---- 194
Cdd:cd09987  13 LLAGVVvaVLKDGKVPVVLGG--DHSIA---------NGAIRAVAEL---HPDLGVIDVDAHHDVRTPEAFGKGNHhtpr 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203 195 ----------VMTVSLHKFSPGFFPGTGDmsdvglGKGRYYSVNVPIQDGIqDEKYYHICESVLKevYQAFNPKAVVLQL 264
Cdd:cd09987  79 hllceplisdVHIVSIGIRGVSNGEAGGA------YARKLGVVYFSMTEVD-KLGLGDVFEEIVS--YLGDKGDNVYLSV 149

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58037203 265 GADTIAGDPMCS------FNMTPVGIGKCLKYVLQWQLATLILGGGGYNLA----NTARCWTYLTGVI 322
Cdd:cd09987 150 DVDGLDPSFAPGtgtpgpGGLSYREGLYITERIAKTNLVVGLDIVEVNPLLdetgRTARLAAALTLEL 217
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
 10-187 2.01e-09

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: 58.62  E-value: 2.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  10 SGHSLPPVYIYSPEYVSICDSLVKVPKRASMVHSLIEAyALHKQmrivkpkvASMEEMATFhtdayLQHLQKVSQEGDED 89
Cdd:cd09998   1 QDECYKHRYSRSKTSKSYLSTIVERPERLRASVLGLSA-AVHGS--------KWSAELIEM-----CDMAEAKLAKGESE 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037203  90 HPDSIEYGLGYDCPATEGIFDyaAAIGG-----GTITAAQCLIDGKCKVAINWSGgwHHAKKDEASGFCYLNDAVLGILR 164
Cdd:cd09998  67 IPAHLPQGDLYLCPESLDAIQ--GALGAvceavDSVFKPESPGTKRAFVAIRPPG--HHCSESTPSGFCWVNNVHVGAAH 142

                       170       180
                ....*....|....*....|....*
gi 58037203 165 --LRRKFDRILYVDLDLHHGDGVED 187
Cdd:cd09998 143 ayLTHGITRVVILDIDLHHGNGTQD 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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