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Conserved domains on  [gi|8923769|ref|NP_060956|]
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histone deacetylase 8 isoform 1 [Homo sapiens]

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: 727.60  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   16 PVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHP--DS 93
Cdd:cd10000   1 VVYIHSPEYVNLCDRLPKVPNRASMVHSLIEAYGLLKQLRVVKPRVATEEELASFHSDEYIQFLKKASNEGDNDEEpsEQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   94 IEYGLGYDCPATEGIFDYAAAIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERIL 173
Cdd:cd10000  81 QEFGLGYDCPIFEGIYDYAAAVAGATLTAAQLLIDGKCKVAINWFGGWHHAQRDEASGFCYVNDIVLGILKLREKFDRVL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  174 YVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQ 253
Cdd:cd10000 161 YVDLDLHHGDGVEDAFSFTSKVMTVSLHKYSPGFFPGTGDVSDVGLGKGKYYTVNVPLRDGIQDEQYLQIFTAVVPEIVA 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  254 AFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPD 333
Cdd:cd10000 241 AFRPEAVVLQCGADTLAGDPMGAFNLTPVGIGKCLKYVLGWKLPTLILGGGGYNLANTARCWTYLTGLILGEPLSSDIPD 320

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 8923769  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: 727.60  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   16 PVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHP--DS 93
Cdd:cd10000   1 VVYIHSPEYVNLCDRLPKVPNRASMVHSLIEAYGLLKQLRVVKPRVATEEELASFHSDEYIQFLKKASNEGDNDEEpsEQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   94 IEYGLGYDCPATEGIFDYAAAIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERIL 173
Cdd:cd10000  81 QEFGLGYDCPIFEGIYDYAAAVAGATLTAAQLLIDGKCKVAINWFGGWHHAQRDEASGFCYVNDIVLGILKLREKFDRVL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  174 YVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQ 253
Cdd:cd10000 161 YVDLDLHHGDGVEDAFSFTSKVMTVSLHKYSPGFFPGTGDVSDVGLGKGKYYTVNVPLRDGIQDEQYLQIFTAVVPEIVA 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  254 AFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPD 333
Cdd:cd10000 241 AFRPEAVVLQCGADTLAGDPMGAFNLTPVGIGKCLKYVLGWKLPTLILGGGGYNLANTARCWTYLTGLILGEPLSSDIPD 320

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 8923769  334 HEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLKHVV 377
Cdd:cd10000 321 HEFFTSYGPDYELEISPSLRPDLNEDQYIEKILETIKGNLKNVV 364
PTZ00063 PTZ00063
histone deacetylase; Provisional
 35-376 3.35e-114

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 339.48  E-value: 3.35e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769    35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIE---YGLGYDCPATEGIFDY 111
Cdd:PTZ00063  27 PQRIRMAHALILSYDLYKHMEIYRPHKSVEPELVLFHDEEYVDFLSSISPENYRDFTYQLKrfnVGEATDCPVFDGLFEF 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   112 AAAIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDGVEDAFSF 191
Cdd:PTZ00063 107 QQSCAGASIDGAYKLNNHQADICVNWSGGLHHAKRSEASGFCYINDIVLGILELLKYHARVMYIDIDVHHGDGVEEAFYV 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   192 TSKVMTVSLHKFSpGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAG 271
Cdd:PTZ00063 187 THRVMTVSFHKFG-DFFPGTGDVTDIGVAQGKYYSVNVPLNDGIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTG 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   272 DPMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKT--LSSEIPDHEFFTAYGPDYVLEIT 349
Cdd:PTZ00063 266 DRLGRFNLTIKGHAACVEFVRSLNIPLLVLGGGGYTIRNVARCWAYETGVILNKHdeMSDQISLNDYYDYYAPDFQLHLQ 345

                        330       340
                 ....*....|....*....|....*..
gi 8923769   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 5.03e-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: 303.39  E-value: 5.03e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769     35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIEYGlGYDCPATEGIFDYAAA 114
Cdd:pfam00850   5 PERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAAPEGGALLLLSYLSG-DDDTPVSPGSYEAALL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769    115 IGGATITAAQCLIDGMCK--VAINWsGGWHHAKKDEASGFCYLNDAVLGILRLRRK--FERILYVDLDLHHGDGVEDAFS 190
Cdd:pfam00850  84 AAGGTLAAADAVLSGEARnaFALVR-PPGHHAERDRASGFCIFNNVAIAAKYLREKygLKRVAIVDFDVHHGNGTQEIFY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769    191 FTSKVMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIA 270
Cdd:pfam00850 163 DDPSVLTLSIHQYPGGFYPGTGFADETGEGKGKGYTLNVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAGFDAHA 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 8923769    271 GDPMCSFNMTPVGIGKCLKYILQWQLAT----LILGGGGYNLANTARCWTYLTGVI 322
Cdd:pfam00850 243 GDPLGGLNLTTEGFAEITRILLELADPLcirvVSVLEGGYNLDALARSATAVLAAL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 18-324 9.43e-78

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 241.93  E-value: 9.43e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   18 YIYSPEYVS--------MCdslakiPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGddd 89
Cdd:COG0123   3 LIYHPDYLLhdlgpghpEP------PERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAASLDG--- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   90 hpdsiEYG-LGYDCPATEGIFDYAAAIGGATITAAQCLIDGMCKVA-INWSGGWHHAKKDEASGFCYLNDAVLGILRLRR 167
Cdd:COG0123  74 -----GYGqLDPDTPVSPGTWEAALLAAGGALAAADAVLEGEARNAfALVRPPGHHAERDRAMGFCLFNNAAIAARYLLA 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  168 K-FERILYVDLDLHHGDGVEDAFSFTSKVMTVSLHKFspGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICES 246
Cdd:COG0123 149 KgLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD--PLYPGTGAADETGEGAGEGSNLNVPLPPGTGDAEYLAALEE 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  247 VLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQW----QLATLILGGGGYNLANTARCWTYLTGVI 322
Cdd:COG0123 227 ALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELadhcGGPVVSVLEGGYNLDALARSVAAHLETL 306


                ..
gi 8923769  323 LG 324
Cdd:COG0123 307 LG 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: 727.60  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   16 PVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHP--DS 93
Cdd:cd10000   1 VVYIHSPEYVNLCDRLPKVPNRASMVHSLIEAYGLLKQLRVVKPRVATEEELASFHSDEYIQFLKKASNEGDNDEEpsEQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   94 IEYGLGYDCPATEGIFDYAAAIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERIL 173
Cdd:cd10000  81 QEFGLGYDCPIFEGIYDYAAAVAGATLTAAQLLIDGKCKVAINWFGGWHHAQRDEASGFCYVNDIVLGILKLREKFDRVL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  174 YVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQ 253
Cdd:cd10000 161 YVDLDLHHGDGVEDAFSFTSKVMTVSLHKYSPGFFPGTGDVSDVGLGKGKYYTVNVPLRDGIQDEQYLQIFTAVVPEIVA 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  254 AFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPD 333
Cdd:cd10000 241 AFRPEAVVLQCGADTLAGDPMGAFNLTPVGIGKCLKYVLGWKLPTLILGGGGYNLANTARCWTYLTGLILGEPLSSDIPD 320

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 8923769  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 7.21e-173

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: 483.62  E-value: 7.21e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   19 IYSPEYVSMCDSL--AKIPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDD-HPDSIE 95
Cdd:cd09991   1 FYDPDVGNYYYGQghPMKPHRIRMTHSLILSYGLYKKMEIYRPRPATAEELTKFHSDDYIDFLRSVSPDNMKEfKKQLER 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   96 YGLGYDCPATEGIFDYAAAIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYV 175
Cdd:cd09991  81 FNVGEDCPVFDGLYEYCQLYAGGSIAAAVKLNRGQADIAINWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  176 DLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDvSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAF 255
Cdd:cd09991 161 DIDIHHGDGVEEAFYTTDRVMTVSFHKFGEYFFPGTGL-RDIGAGKGKYYAVNVPLKDGIDDESYLQIFEPVLSKVMEVF 239

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8923769  256 NPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVI 322
Cdd:cd09991 240 QPSAVVLQCGADSLAGDRLGCFNLSIKGHAKCVKFVKSFNIPLLVLGGGGYTLRNVARCWTYETAVL 306
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
 35-374 5.74e-124

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: 362.48  E-value: 5.74e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSI-EYGLGYDCPATEGIFDYAA 113
Cdd:cd10005  24 PHRLALTHSLVLHYGLYKKMQVYKPYRASAHDMCRFHSEDYIDFLQRVTPQNIQGFTKSLnQFNVGDDCPVFPGLFDFCS 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  114 AIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDGVEDAFSFTS 193
Cdd:cd10005 104 MYTGASLEGATKLNHKICDIAINWSGGLHHAKKFEASGFCYVNDIVIAILELLKYHPRVLYIDIDIHHGDGVQEAFYLTD 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  194 KVMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDP 273
Cdd:cd10005 184 RVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYSVNVPLKDGIDDQSYLQLFKPVIQQVIDFYQPTCIVLQCGADSLGCDR 263

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  274 MCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCR 353
Cdd:cd10005 264 LGCFNLSIKGHGECVEFVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVDEEISNELPYNEYFEYFAPDFTLHPDVSTR 343

                       330       340
                ....*....|....*....|..
gi 8923769  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 3.30e-120

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: 352.57  E-value: 3.30e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDH-PDSIEYGLGYDCPATEGIFDYAA 113
Cdd:cd10004  25 PHRIRMAHSLVMNYGLYKKMEIYRAKPATKNEMTQFHTDEYIDFLSRVTPDNMEKFqKEQVKYNVGDDCPVFDGLFEFCS 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  114 AIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDGVEDAFSFTS 193
Cdd:cd10004 105 ISAGGSMEGAARLNRGKCDIAVNWAGGLHHAKKSEASGFCYVNDIVLGILELLRYHQRVLYIDIDVHHGDGVEEAFYTTD 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  194 KVMTVSLHKFSPgFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDP 273
Cdd:cd10004 185 RVMTCSFHKYGE-YFPGTGELRDIGIGTGKNYAVNVPLRDGIDDESYKSIFEPVIKHVMEWYQPEAVVLQCGGDSLSGDR 263

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  274 MCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCR 353
Cdd:cd10004 264 LGCFNLSMKGHANCVNFVKSFNLPMLVLGGGGYTMRNVARTWAFETGLLAGEELDKDLPYNEYYEYYGPDYELNVRPSNM 343

                       330       340
                ....*....|....*....|..
gi 8923769  354 PDRNEPHRIQQILNYIKGNLKH 375
Cdd:cd10004 344 ENHNTPEYLDKITTAVIENLRN 365
PTZ00063 PTZ00063
histone deacetylase; Provisional
 35-376 3.35e-114

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 339.48  E-value: 3.35e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769    35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIE---YGLGYDCPATEGIFDY 111
Cdd:PTZ00063  27 PQRIRMAHALILSYDLYKHMEIYRPHKSVEPELVLFHDEEYVDFLSSISPENYRDFTYQLKrfnVGEATDCPVFDGLFEF 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   112 AAAIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDGVEDAFSF 191
Cdd:PTZ00063 107 QQSCAGASIDGAYKLNNHQADICVNWSGGLHHAKRSEASGFCYINDIVLGILELLKYHARVMYIDIDVHHGDGVEEAFYV 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   192 TSKVMTVSLHKFSpGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAG 271
Cdd:PTZ00063 187 THRVMTVSFHKFG-DFFPGTGDVTDIGVAQGKYYSVNVPLNDGIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTG 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   272 DPMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKT--LSSEIPDHEFFTAYGPDYVLEIT 349
Cdd:PTZ00063 266 DRLGRFNLTIKGHAACVEFVRSLNIPLLVLGGGGYTIRNVARCWAYETGVILNKHdeMSDQISLNDYYDYYAPDFQLHLQ 345

                        330       340
                 ....*....|....*....|....*..
gi 8923769   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 1.08e-109

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: 325.87  E-value: 1.08e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIE-YGLGYDCPATEGIFDYAA 113
Cdd:cd10010  29 PHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQrFNVGEDCPVFDGLFEFCQ 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  114 AIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDGVEDAFSFTS 193
Cdd:cd10010 109 LSAGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTD 188

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  194 KVMTVSLHKFSPgFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDP 273
Cdd:cd10010 189 RVMTVSFHKYGE-YFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGADSLSGDR 267

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  274 MCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCR 353
Cdd:cd10010 268 LGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDSEIPNELPYNDYFEYFGPDFKLHISPSNM 347

                       330       340
                ....*....|....*....|.
gi 8923769  354 PDRNEPHRIQQILNYIKGNLK 374
Cdd:cd10010 348 TNQNTNEYLEKIKQRLFENLR 368
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
 17-322 3.54e-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: 321.52  E-value: 3.54e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   17 VYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQM-RIVKPKVASMEEMATFHTDAYLQHLQKvsqegdddhpdsiE 95
Cdd:cd11680   1 ILSVSEELTKIADLLPSNKGRSSLVHSLIRAYGLLQHFdEIIEPERATRKDLTKYHDKDYVDFLLK-------------K 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   96 YGLGYDCPATEGIFDYAAAIGGATITAAQCLIDGMCK-VAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRK-FERIL 173
Cdd:cd11680  68 YGLEDDCPVFPFLSMYVQLVAGSSLALAKHLITQVERdIAINWYGGRHHAQKSRASGFCYVNDIVLAILRLRRArFRRVF 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  174 YVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSDvglgKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQ 253
Cdd:cd11680 148 YLDLDLHHGDGVESAFFFSKNVLTCSIHRYDPGFFPGTGSLKN----SSDKGMLNIPLKRGLSDKTLLRIIDSIVRPLIE 223

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8923769  254 AFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQW--QLATLILGGGGYNLANTARCWTYLTGVI 322
Cdd:cd11680 224 KFEPEVIVIQCGCDGLSGDPHKEWNLTIRGYGSVIELLLKEfkDKPTLLLGGGGYNHTEAARAWTYLTSMV 294
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
 35-321 2.90e-108

Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I histone deacetylase (HDAC) Hos2 from Saccharomyces cerevisiae as well as a histone deacetylase Phd1 from Schizosaccharomyces pombe. Hos2 binds to the coding regions of genes during gene activation, specifically it deacetylates the lysines in H3 and H4 histone tails. It is preferentially associated with genes of high activity genome-wide and is shown to be necessary for efficient transcription. Thus, Hos2 is directly required for gene activation in contrast to other class I histone deacetylases. Protein encoded by phd1 is inhibited by trichostatin A (TSA), a specific inhibitor of histone deacetylase, and is involved in the meiotic cell cycle in S. pombe. Class 1 HDACs are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues in histone amino termini to yield a deacetylated histone (EC 3.5.1.98).


Pssm-ID: 212540 [Multi-domain]  Cd Length: 311  Bit Score: 319.79  E-value: 2.90e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVS-QEGDDDHPDSIE-YGLGYDCPATEGIFDYA 112
Cdd:cd11598  22 PFRLTLTKHLVMGYGLHKAMDTYEARAATREELRQFHDADYLDFLSKVSpENANQLRFDKAEpFNIGDDCPVFDGMYDYC 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  113 AAIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDGVEDAFSFT 192
Cdd:cd11598 102 QLYAGASLDAARKLCSGQSDIAINWSGGLHHAKKSEASGFCYVNDIVLAILNLLRYFPRVLYIDIDVHHGDGVEEAFYRT 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  193 SKVMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGD 272
Cdd:cd11598 182 DRVMTLSFHKYNGEFFPGTGDLDDNGGTPGKHFALNVPLEDGIDDEQYNLLFKSIIGPTIEKFQPSAIVLQCGADSLGGD 261

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 8923769  273 PMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGV 321
Cdd:cd11598 262 RLGQFNLNIKAHGACVKFVKSFGIPMLVVGGGGYTPRNVARAWCYETAV 310
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
 35-374 2.09e-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: 314.69  E-value: 2.09e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIE-YGLGYDCPATEGIFDYAA 113
Cdd:cd10011  25 PHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQrFNVGEDCPVFDGLFEFCQ 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  114 AIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDGVEDAFSFTS 193
Cdd:cd10011 105 LSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTD 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  194 KVMTVSLHKFSPGFfPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDP 273
Cdd:cd10011 185 RVMTVSFHKYGEYF-PGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDR 263

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  274 MCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCR 353
Cdd:cd10011 264 LGCFNLTVKGHAKCVEVVKTFNLPLLMLGGGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNM 343

                       330       340
                ....*....|....*....|.
gi 8923769  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 5.03e-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: 303.39  E-value: 5.03e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769     35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIEYGlGYDCPATEGIFDYAAA 114
Cdd:pfam00850   5 PERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAAPEGGALLLLSYLSG-DDDTPVSPGSYEAALL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769    115 IGGATITAAQCLIDGMCK--VAINWsGGWHHAKKDEASGFCYLNDAVLGILRLRRK--FERILYVDLDLHHGDGVEDAFS 190
Cdd:pfam00850  84 AAGGTLAAADAVLSGEARnaFALVR-PPGHHAERDRASGFCIFNNVAIAAKYLREKygLKRVAIVDFDVHHGNGTQEIFY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769    191 FTSKVMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIA 270
Cdd:pfam00850 163 DDPSVLTLSIHQYPGGFYPGTGFADETGEGKGKGYTLNVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAGFDAHA 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 8923769    271 GDPMCSFNMTPVGIGKCLKYILQWQLAT----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 3.83e-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: 3.83e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDhpDSIEYGLG-YDCPATEGIFDYAA 113
Cdd:cd09994  21 PPRLSLTKDLLRALGLLPPVDLVPPRPATEEELLLFHTPDYIEAVKEASRGQEPE--GRGRLGLGtEDNPVFPGMHEAAA 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  114 AIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRK-FERILYVDLDLHHGDGVEDAFSFT 192
Cdd:cd09994  99 LVVGGTLLAARLVLEGEARRAFNPAGGLHHAMRGRASGFCVYNDAAVAIERLRDKgGLRVAYVDIDAHHGDGVQAAFYDD 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  193 SKVMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGD 272
Cdd:cd09994 179 PRVLTISLHESGRYLFPGTGFVDEIGEGEGYGYAVNIPLPPGTGDDEFLRAFEAVVPPLLRAFRPDVIVSQHGADAHAGD 258

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 8923769  273 PMCSFNMTPVGIGKCLKYILQW-----QLATLILGGGGYNLANTARCWTYLTGVI 322
Cdd:cd09994 259 PLTHLNLSNRAYRAAVRRIRELadeycGGRWLALGGGGYNPDVVARAWALLWAVL 313
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 18-324 9.43e-78

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 241.93  E-value: 9.43e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   18 YIYSPEYVS--------MCdslakiPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGddd 89
Cdd:COG0123   3 LIYHPDYLLhdlgpghpEP------PERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAASLDG--- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   90 hpdsiEYG-LGYDCPATEGIFDYAAAIGGATITAAQCLIDGMCKVA-INWSGGWHHAKKDEASGFCYLNDAVLGILRLRR 167
Cdd:COG0123  74 -----GYGqLDPDTPVSPGTWEAALLAAGGALAAADAVLEGEARNAfALVRPPGHHAERDRAMGFCLFNNAAIAARYLLA 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  168 K-FERILYVDLDLHHGDGVEDAFSFTSKVMTVSLHKFspGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICES 246
Cdd:COG0123 149 KgLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD--PLYPGTGAADETGEGAGEGSNLNVPLPPGTGDAEYLAALEE 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  247 VLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQW----QLATLILGGGGYNLANTARCWTYLTGVI 322
Cdd:COG0123 227 ALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELadhcGGPVVSVLEGGYNLDALARSVAAHLETL 306


                ..
gi 8923769  323 LG 324
Cdd:COG0123 307 LG 308
PTZ00346 PTZ00346
histone deacetylase; Provisional
 35-327 1.99e-75

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 239.93  E-value: 1.99e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769    35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIEYGLGYDCPATEGIFDYAAA 114
Cdd:PTZ00346  47 PYRVLAAMEIVRSLKIDAHCRTVVPPLVKVEELMAYHTDTYLANLGLHSCRSWLWNAETSKVFFSGDCPPVEGLMEHSIA 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   115 IGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDGVEDAFSFTSK 194
Cdd:PTZ00346 127 TASGTLMGAVLLNSGQVDVAVHWGGGMHHSKCGECSGFCYVNDIVLGILELLKCHDRVLYVDIDMHHGDGVDEAFCTSDR 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   195 VMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPM 274
Cdd:PTZ00346 207 VFTLSLHKFGESFFPGTGHPRDVGYGRGRYYSMNLAVWDGITDFYYLGLFEHALHSIVRRYSPDAIVLQCGADSLAGDRL 286

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 8923769   275 CSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTL 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 2.38e-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: 219.23  E-value: 2.38e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   37 RASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKvsQEGDDDHPDSIEYGLGYDCPATEGIFDYAAAIG 116
Cdd:cd09301   1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKA--NFAVATITESKPVIFGPNFPVQRHYFRGARLST 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  117 GATITAAQCLIDGMCKVAINW-SGGWHHAKKDEASGFCYLNDAVLGILRLRRK-FERILYVDLDLHHGDGVEDAFSFTSK 194
Cdd:cd09301  79 GGVVEAAELVAKGELERAFAVvGAGGHHAGKSRAWGFCYFNDVVLAIKFLRERgISRILIIDTDAHHGDGTREAFYDDDR 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  195 VMTVSLHKFSPGFFpgtgdvsdvGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPM 274
Cdd:cd09301 159 VLHMSFHNYDIYPF---------GRGKGKGYKINVPLEDGLGDEEYLDAVERVISKVLEEFEPEVVVLQFGHDTHEGDRL 229

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 8923769  275 CSFNMTPVGIGKCLKYI--LQWQLATLILGGGGYNLANTARCWTYLTGVI 322
Cdd:cd09301 230 GGFNLSEKGFVKLAEIVkeFARGGPILMVLGGGYNPEAAARIWTAIIKEL 279
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
 35-314 1.17e-47

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: 163.44  E-value: 1.17e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDD-DHPDsieyglgydCPATEGIFD--Y 111
Cdd:cd09992   5 PERLLAILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYIERVEETCEAGGGyLDPD---------TYVSPGSYEaaL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  112 AAAigGATITAAQCLIDGMCK---VAINWSGgwHHAKKDEASGFCYLNDAVLGI--LRLRRKFERILYVDLDLHHGDGVE 186
Cdd:cd09992  76 LAA--GAALAAVDAVLSGEAEnafALVRPPG--HHAEPDRAMGFCLFNNVAIAAryAQKRYGLKRVLIVDWDVHHGNGTQ 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  187 DAFSFTSKVMTVSLHKFspGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGA 266
Cdd:cd09992 152 DIFYDDPSVLYFSIHQY--PFYPGTGAAEETGGGAGEGFTINVPLPPGSGDAEYLAAFEEVLLPIAREFQPDLVLVSAGF 229

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 8923769  267 DTIAGDPMCSFNMTPVGIGKCLKYILqwQLATLILGG-------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 6.10e-42

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: 150.18  E-value: 6.10e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   23 EYVSMCDS-LAKIPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDD-HPDSIEYGLGY 100
Cdd:cd10003   7 NHHNLWDPgHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHLDEMKSLEKMKPRElNRLGKEYDSIY 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  101 DCPATegiFDYAAAIGGATITAAQCLIDGMCK--VAINWSGGwHHAKKDEASGFCYLNDAVLGILRLRRKF--ERILYVD 176
Cdd:cd10003  87 IHPDS---YQCALLAAGCVLQVVEAVLTGESRngVAIVRPPG-HHAEQDTACGFCFFNNVAIAARYAQKKYglKRILIVD 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  177 LDLHHGDGVEDAFSFTSKVMTVSLHKFSPG-FFPGT--GDVSDVGLGKGRYYSVNVPI-QDGIQDEKYYQICESVLKEVY 252
Cdd:cd10003 163 WDVHHGNGTQHMFESDPSVLYISLHRYDNGsFFPNSpeGNYDVVGKGKGEGFNVNIPWnKGGMGDAEYIAAFQQVVLPIA 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  253 QAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKclkyiLQWQLATLILGG------GGYNLANTARCWTYLTGVILGKT 326
Cdd:cd10003 243 YEFNPELVLVSAGFDAARGDPLGGCKVTPEGYAH-----MTHMLMSLAGGRvivileGGYNLTSISESMSMCTKTLLGDP 317


                ...
gi 8923769  327 LSS 329
Cdd:cd10003 318 PPV 320
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
 34-309 5.27e-41

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: 146.14  E-value: 5.27e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   34 IPKRASMVHSLIEAYALhkqMRIVKPKVASMEEMATFHTDAYLQHLQKVSQegdddhpdsieyglgyDCPATEGIFDYAA 113
Cdd:cd10001  28 NPERAEAILDALKRAGL---GEVLPPRDFGLEPILAVHDPDYVDFLETADT----------------DTPISEGTWEAAL 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  114 AIGGATITAAQCLIDGmCKVAINWS---GgwHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDGVEDAFS 190
Cdd:cd10001  89 AAADTALTAADLVLEG-ERAAYALCrppG--HHAGRDRAGGFCYFNNAAIAAQYLRDRAGRVAILDVDVHHGNGTQEIFY 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  191 FTSKVMTVSLHKFSPGFFPGT-GDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVyQAFNPKAVVLQLGADTI 269
Cdd:cd10001 166 ERPDVLYVSIHGDPRTFYPFFlGFADETGEGEGEGYNLNLPLPPGTGDDDYLAALDEALAAI-AAFGPDALVVSLGFDTH 244

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 8923769  270 AGDPMCSFNMTPVG---IGKClkyILQWQLATLILGGGGYNLA 309
Cdd:cd10001 245 EGDPLSDFKLTTEDyarIGRR---IAALGLPTVFVQEGGYNVD 284
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
 41-314 2.68e-39

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: 143.08  E-value: 2.68e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   41 VHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDhpdsieygLGYDCPATEGIFDYAAAIGGATI 120
Cdd:cd09996  43 IKNLLEVSGLSDHLVLITPRPATDEELLRVHTPEYIDRVKAASAAGGGE--------AGGGTPFGPGSYEIALLAAGGAI 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  121 TAAQCLIDGMCKVA---INWSGgwHHAKKDEASGFCYLNDAVLGILRLRRKF--ERILYVDLDLHHGDGVEDAFSFTSKV 195
Cdd:cd09996 115 AAVDAVLDGEVDNAyalVRPPG--HHAEPDQGMGFCLFNNVAIAARHALAVGgvKRVAVVDWDVHHGNGTQAIFYDDPDV 192

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  196 MTVSLHKFSPgFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMC 275
Cdd:cd09996 193 LTISLHQDRC-FPPDSGAVEERGEGAGEGYNLNIPLPPGSGDGAYLHAFERIVLPALRAFRPELIIVASGFDASAFDPLG 271

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 8923769  276 SFNMTPVG---IGKCLKyilqwQLATLILGG-------GGYNLANTARC 314
Cdd:cd09996 272 RMMLTSDGfraLTRKLR-----DLADELCGGrlvmvheGGYSEAYVPFC 315
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 37-307 7.49e-38

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: 137.24  E-value: 7.49e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   37 RASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLqkVSQEGDDDHPDSIEYglgydcPATEGIFDYAAAIG 116
Cdd:cd09993   7 KYGLLREALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLESL--KSGELSREEIRRIGF------PWSPELVERTRLAV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  117 GATITAAQ-CLIDGmckVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRK--FERILYVDLDLHHGDGVEDAFSFTS 193
Cdd:cd09993  79 GGTILAARlALEHG---LAINLAGGTHHAFPDRGEGFCVFNDIAIAARVLLAEglVRRVLIVDLDVHQGNGTAAIFADDP 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  194 KVMTVSLHkfSPGFFPGTGDVSDvglgkgryysVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDP 273
Cdd:cd09993 156 SVFTFSMH--GEKNYPFRKEPSD----------LDVPLPDGTGDDEYLAALEEALPRLLAEFRPDLVFYNAGVDVLAGDR 223

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 8923769  274 MCSFNMTPVGIGKCLKYILQWQLA----TLILGGGGYN 307
Cdd:cd09993 224 LGRLSLSLEGLRERDRLVLRFARArgipVAMVLGGGYS 261
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
 27-324 5.22e-31

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: 122.07  E-value: 5.22e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   27 MCDSLAKIPKRASMVHSL---IEAYALHKQMRIVKPKVASMEEMATFHTDAYLQ-------HLQKVSQEGDDDHPDSIEY 96
Cdd:cd10006  20 TCGNSNSHPEHAGRIQSIwsrLQETGLRGKCECIRGRKATLEELQTVHSEAHTLlygtnplNRQKLDSKKLLGSLASVFV 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   97 -----GLGYDcpaTEGIFDYAAAIGGATItAAQCLIDGMCKVAI-NWSGGW-------HHAKKDEASGFCYLNDAVLG-- 161
Cdd:cd10006 100 rlpcgGVGVD---SDTIWNEVHSSGAARL-AVGCVVELVFKVATgELKNGFavvrppgHHAEESTPMGFCYFNSVAIAak 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  162 ILRLRRKFERILYVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPG-FFPGTGDVSDVGLGKGRYYSVNVPIQDGIQ---- 236
Cdd:cd10006 176 LLQQRLNVSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYDDGnFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDppmg 255

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  237 DEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPmcsfnmTPVgigkclkyilqwqlatlilggGGYNLanTARCWT 316
Cdd:cd10006 256 DAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHP------TPL---------------------GGYNL--SAKCFG 306


                ....*...
gi 8923769  317 YLTGVILG 324
Cdd:cd10006 307 YLTKQLMG 314
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 44-314 8.73e-31

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: 120.53  E-value: 8.73e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   44 LIEAYALHKQMRIvKPKVASMEEMATFHTDAY-------LQHLQKVSQEGDDDHPDSIEY-----GLGYDcpaTEGIFDY 111
Cdd:cd11681  38 LQETGLVNRCERL-RGRKATLEELQLVHSEVHtllygtnPLSRLKLDPTKLAGLPQKSFVrlpcgGIGVD---SDTVWNE 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  112 AAAIGGATItAAQCLIDGMCKVAIN-WSGGW-------HHAKKDEASGFCYLNDAVLG--ILRLRRKFERILYVDLDLHH 181
Cdd:cd11681 114 LHTSNAARM-AVGCVIDLAFKVATGeLKNGFavvrppgHHAEPSQAMGFCFFNSVAIAakQLQQKLKLRKILIVDWDVHH 192

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  182 GDGVEDAFSFTSKVMTVSLHKFSPG-FFPGTGDVSDVGLGKGRYYSVNVPIQDGIQ----DEKYYQICESVLKEVYQAFN 256
Cdd:cd11681 193 GNGTQQIFYEDPNVLYISLHRYDDGnFFPGTGAPTEVGSGAGEGFNVNIAWSGGLDppmgDAEYLAAFRTVVMPIAREFS 272

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8923769  257 PKAVVLQLGADTIAGDP--MCSFNMTPvgigKCLKYILQwQLATLILGG------GGYNLanTARC 314
Cdd:cd11681 273 PDIVLVSAGFDAAEGHPppLGGYKVSP----ACFGYMTR-QLMNLAGGKvvlaleGGYDL--TAIC 331
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 35-324 8.91e-31

Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone deacetylase Zn-dependent enzyme that catalyzes hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Clr3 is the homolog of the class-II HDAC HdaI in S. cerevisiae, and is essential for silencing in heterochromatin regions, such as centromeric regions, ribosomal DNA, the mating-type region and telomeric loci. Clr3 has also been implicated in the regulation of stress-related genes; the histone acetyltransferase, Gcn5, in S. cerevisiae, preferentially acetylates global histone H3K14 while Clr3 preferentially deacetylates H3K14ac, and therefore, interplay between Gcn5 and Clr3 is crucial for the regulation of many stress-response genes.


Pssm-ID: 212542 [Multi-domain]  Cd Length: 313  Bit Score: 119.37  E-value: 8.91e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIEYGLG---YDCPATegiFDY 111
Cdd:cd11600   7 PSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEHWDRVEATEKMSDEQLKDRTEIFERdslYVNNDT---AFC 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  112 AAAIGGATITAAQCLIDGMCK--VAINWSGGwHHAKKDEASGFCYLNDAVLG--ILRLRR--KFERILYVDLDLHHGDGV 185
Cdd:cd11600  84 ARLSCGGAIEACRAVAEGRVKnaFAVVRPPG-HHAEPDESMGFCFFNNVAVAakWLQTEYpdKIKKILILDWDIHHGNGT 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  186 EDAFSFTSKVMTVSLHKFSPG-FFPGT--GDVSDVGLGKGRYYSVNVP-IQDGIQDEKYYQICESVLKEVYQAFNPKAVV 261
Cdd:cd11600 163 QRAFYDDPNVLYISLHRFENGgFYPGTpyGDYESVGEGAGLGFNVNIPwPQGGMGDADYIYAFQRIVMPIAYEFDPDLVI 242

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8923769  262 LQLGADTIAGDPMCSFNMTPVGIGKclkyiLQWQLATLILGG------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 ...
 35-324 7.17e-28

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: 111.63  E-value: 7.17e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPD-SIEYGLGYDCPATegiFDYAA 113
Cdd:cd10002  11 PERLEAILERLTQDGLLERCVKIPAREAEEDEILLVHSQEYIDLVKSTETMEKEELESlCSGYDSVYLCPST---YEAAR 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  114 AIGGATITAAQCLIDGMCK--VAINWSGGwHHAKKDEASGFCYLNDAVLGILRLRRKF--ERILYVDLDLHHGDGVEDAF 189
Cdd:cd10002  88 LAAGSTIELVKAVMAGKIQngFALIRPPG-HHAMRNEANGYCIFNNVAIAAKYAIEKLglKRILIVDWDVHHGQGTQQGF 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  190 SFTSKVMTVSLHKFSPG-FFPG--TGDVSDVGLGKGRYYSVNVPI-QDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLG 265
Cdd:cd10002 167 YEDPRVLYFSIHRYEHGrFWPHlfESDYDYIGVGHGYGFNVNVPLnQTGLGDADYLAIFHHILLPLALEFQPELVLVSAG 246

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8923769  266 ADTIAGDPMCSFNMTPVGIGKcLKYIL--QWQLATLILGGGGYNLANTARCWTYLTGVILG 324
Cdd:cd10002 247 FDASIGDPEGEMAVTPAGYAH-LTRLLmgLAGGKLLLVLEGGYLLESLAESVSMTLRGLLG 306
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
 117-314 9.39e-26

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: 107.38  E-value: 9.39e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  117 GATITAAQCLIDGMCKVAI-NWSGGW-------HHAKKDEASGFCYLNDAVLGILRLRRKFE--RILYVDLDLHHGDGVE 186
Cdd:cd10007 121 SAVRMAVGCLIELAFKVAAgELKNGFavirppgHHAEESTAMGFCFFNSVAIAAKLLQQKLNvgKILIVDWDIHHGNGTQ 200

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  187 DAFSFTSKVMTVSLHKFSPG-FFPGTGDVSDVGLGKGRYYSVNVPIQDGIQ----DEKYYQICESVLKEVYQAFNPKAVV 261
Cdd:cd10007 201 QAFYNDPNVLYISLHRYDDGnFFPGSGAPDEVGAGPGVGFNVNIAWTGGVDppigDVEYLTAFRTVVMPIANEFSPDVVL 280

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8923769  262 LQLGADTIAG--DPMCSFNMTpvgiGKCLKYILQwQLATLIlGG-------GGYNLanTARC 314
Cdd:cd10007 281 VSAGFDAVEGhqSPLGGYSVT----AKCFGHLTK-QLMTLA-GGrvvlaleGGHDL--TAIC 334
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
 27-314 1.82e-25

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: 105.87  E-value: 1.82e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   27 MCDSLAKIPKRASMVHS----LIEAYALHKQMRIvKPKVASMEEMATFHTDAYL----------QHLQKVSQEGDDDHP- 91
Cdd:cd10009  17 VCGNSTTHPEHAGRIQSiwsrLQETGLLNKCERI-QGRKASLEEIQLVHSEHHSllygtnpldgQKLDPRILLGDDSQKf 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   92 -DSIEYG-LGYDcpaTEGIFDYAAAIGGATItAAQCLIDGMCKVAI-NWSGGW-------HHAKKDEASGFCYLNDAVLG 161
Cdd:cd10009  96 fSSLPCGgLGVD---SDTIWNELHSSGAARM-AVGCVIELASKVASgELKNGFavvrppgHHAEESTAMGFCFFNSVAIT 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  162 ILRLRRKFE--RILYVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPG-FFPGTGDVSDVGLGKGRYYSVNVPIQDGIQ-- 236
Cdd:cd10009 172 AKYLRDQLNisKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGnFFPGSGAPNEVGTGLGEGYNINIAWTGGLDpp 251

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  237 --DEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGD--PMCSFNMTPVGIGKCLKYILQWQLATLILG-GGGYNLanT 311
Cdd:cd10009 252 mgDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLADGRVVLAlEGGHDL--T 329


                ...
gi 8923769  312 ARC 314
Cdd:cd10009 330 AIC 332
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
 142-314 2.01e-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: 105.86  E-value: 2.01e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  142 HHAKKDEASGFCYLNDAVLGI--LRLRRKFERILYVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPG-FFPGTGDVSDVG 218
Cdd:cd10008 152 HHADHSTAMGFCFFNSVAIACrqLQQQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGnFFPGSGAVDEVG 231

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  219 LGKGRYYSVNVPIQDGIQ----DEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPmcsfnmTPVG----IGKCLKY 290
Cdd:cd10008 232 AGSGEGFNVNVAWAGGLDppmgDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHP------APLGgyhvSAKCFGY 305

                       170       180       190
                ....*....|....*....|....*....|
gi 8923769  291 ILQwQLATLILGG------GGYNLanTARC 314
Cdd:cd10008 306 MTQ-QLMNLAGGAvvlaleGGHDL--TAIC 332
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
 55-280 2.19e-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: 95.66  E-value: 2.19e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   55 RIVKPKVASMEEMATFHTDAYLQHL-QKVSQEG----DDD---HPDSIEYGLgydcpategifdYAAaigGATITAAQCL 126
Cdd:cd11599  25 RQLEAPPATREQLLRVHDAAYVDRLeAAAPEEGlvqlDPDtamSPGSLEAAL------------RAA---GAVVAAVDAV 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  127 IDGMCK---VAINWSGgwHHAKKDEASGFCYLNDAVLGIL--RLRRKFERILYVDLDLHHGDGVEDAFSFTSKVMTVSLH 201
Cdd:cd11599  90 MAGEARnafCAVRPPG--HHAERDKAMGFCLFNNVAIAAAhaLAHHGLERVAIVDFDVHHGNGTEDIFRDDPRVLFCSSH 167

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8923769  202 KFspGFFPGTGDVSDVGLGkgryYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMT 280
Cdd:cd11599 168 QH--PLYPGTGAPDETGHG----NIVNVPLPAGTGGAEFREAVEDRWLPALDAFKPDLILISAGFDAHRDDPLAQLNLT 240
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
 29-312 4.81e-22

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: 95.69  E-value: 4.81e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   29 DSLAKIPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQhLQKVSQEGDDDHPDSI--EYGLGYDCPate 106
Cdd:cd11682   5 ESFPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYVA-LMKSTQYMTEEELRTLadTYDSVYLHP--- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  107 GIFDYAAAIGGATITAAQCLIDGMCK--VAINWSGGwHHAKKDEASGFCYLNDAVLGI--LRLRRKFERILYVDLDLHHG 182
Cdd:cd11682  81 NSYSCACLAVGSVLQLVDKVLGGEIRngLAIVRPPG-HHAQHDKMDGYCMFNNVAIAAryAQQKHGVQRVLIVDWDVHHG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  183 DGVEDAFSFTSKVMTVSLHKFSPG-FFP--GTGDVSDVGLGKGRYYSVNVPI-QDGIQDEKYYQICESVLKEVYQAFNPK 258
Cdd:cd11682 160 QGTQFIFEQDPSVLYFSIHRYEQGrFWPhlKESDSSAVGFGRGEGYNINVPWnQVGMRDADYIAAFLHVLLPVALEFQPQ 239

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 8923769  259 AVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLILG-GGGYNLANTA 312
Cdd:cd11682 240 LVLVAAGFDAVIGDPKGEMAATPACFAHLTHLLMGLAGGKLILSlEGGYNLRSLA 294
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 33-319 2.53e-20

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: 90.69  E-value: 2.53e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   33 KIPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQ-----------HLQKVSQEGDDD--HPDSieyglg 99
Cdd:cd11683   9 EVPERLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSlvretqvmnkeELMAISGKYDAVyfHPNT------ 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  100 YDCpategifdyAAAIGGATITAAQCLIDGMCK--VAINWSGGwHHAKKDEASGFCYLNDAVLGILRLRRKF--ERILYV 175
Cdd:cd11683  83 FHC---------ARLAAGATLQLVDAVLTGEVQngMALVRPPG-HHSQRNAANGFCVFNNVAIAAEYAKKKYglHRILIV 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  176 DLDLHHGDGVEDAFSFTSKVMTVSLHKFSPG-FFPG--TGDVSDVGLGKGRYYSVNVPI-QDGIQDEKYYQICESVLKEV 251
Cdd:cd11683 153 DWDVHHGQGIQYIFEEDPSVLYFSWHRYEHQrFWPFlrESDYDAVGRGKGLGFNINLPWnKVGMGNADYLAAFFHVLLPL 232

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8923769  252 YQAFNPKAVVLQLGADTIAGDPMCSFNMTPvgigKCLKYILqwQLATLILGG-------GGYNLANTAR--CWTYLT 319
Cdd:cd11683 233 AFEFDPELVLVSAGFDSAIGDPEGQMCATP----ECFAHLT--HLLMVLAGGklcavleGGYHLESLAEsvCMTVQT 303
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 131-322 1.12e-13

Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily includes metal-dependent enzymes that belong to Arginase-like amidino hydrolase family and histone/histone-like deacetylase class I, II, IV family, respectively. These enzymes catalyze hydrolysis of amide bond. Arginases are known to be involved in control of cellular levels of arginine and ornithine, in histidine and arginine degradation and in clavulanic acid biosynthesis. Deacetylases play a role in signal transduction through histone and/or other protein modification and can repress/activate transcription of a number of different genes. They participate in different cellular processes including cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and post-translational control of the acetyl coenzyme A synthetase. Mammalian histone deacetyases are known to be involved in progression of different tumors. Specific inhibitors of mammalian histone deacetylases are an emerging class of promising novel anticancer drugs.


Pssm-ID: 212513  Cd Length: 217  Bit Score: 69.33  E-value: 1.12e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  131 CKVAINWSGgwHHAKKdeasgfcylNDAVLGILRLrrkFERILYVDLDLHHGDGVEDAFSFTSK--------------VM 196
Cdd:cd09987  25 GKVPVVLGG--DHSIA---------NGAIRAVAEL---HPDLGVIDVDAHHDVRTPEAFGKGNHhtprhllceplisdVH 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769  197 TVSLHKFSPGFFPGTGDvsdvglGKGRYYSVNVPIQDGIqDEKYYQICESVLKevYQAFNPKAVVLQLGADTIAGDPMCS 276
Cdd:cd09987  91 IVSIGIRGVSNGEAGGA------YARKLGVVYFSMTEVD-KLGLGDVFEEIVS--YLGDKGDNVYLSVDVDGLDPSFAPG 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 8923769  277 ------FNMTPVGIGKCLKYILQWQLATLILGGGGYNLA----NTARCWTYLTGVI 322
Cdd:cd09987 162 tgtpgpGGLSYREGLYITERIAKTNLVVGLDIVEVNPLLdetgRTARLAAALTLEL 217
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
 86-187 1.17e-08

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: 56.31  E-value: 1.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923769   86 GDDDHPDSIEYGLGYDCPATEGIFDYAAaigGATITAAQCLIDGMCK------VAINWSGgwHHAKKDEASGFCYLNDAV 159
Cdd:cd09998  63 GESEIPAHLPQGDLYLCPESLDAIQGAL---GAVCEAVDSVFKPESPgtkrafVAIRPPG--HHCSESTPSGFCWVNNVH 137

                        90       100       110
                ....*....|....*....|....*....|
gi 8923769  160 LGILR--LRRKFERILYVDLDLHHGDGVED 187
Cdd:cd09998 138 VGAAHayLTHGITRVVILDIDLHHGNGTQD 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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