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Conserved domains on  [gi|528510099|ref|XP_005159649|]
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histone deacetylase 1 isoform X1 [Danio rerio]

Protein Classification

histone deacetylase 1( domain architecture ID 10178057)

histone deacetylase 1 (HD1) 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)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
 5-375 0e+00

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: 762.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099   5 SQGTKKKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDN 84
Cdd:cd10010    1 SQGTKKKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  85 MSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNKQQTDIAINWAGGLHHAKKSEASGFCYVNDIVLAILEL 164
Cdd:cd10010   81 MSEYSKQMQRFNVGEDCPVFDGLFEFCQLSAGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 165 LKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKP 244
Cdd:cd10010  161 LKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 245 IMSKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEYMKSFNLPLLMLGGGGYTIRNVARCWTFETAVALDST 324
Cdd:cd10010  241 VMSKVMEMFQPSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDSE 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 528510099 325 IPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNDYLEKIKQRLFENLRMLP 375
Cdd:cd10010  321 IPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLP 371
 
Name Accession Description Interval E-value
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
 5-375 0e+00

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: 762.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099   5 SQGTKKKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDN 84
Cdd:cd10010    1 SQGTKKKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  85 MSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNKQQTDIAINWAGGLHHAKKSEASGFCYVNDIVLAILEL 164
Cdd:cd10010   81 MSEYSKQMQRFNVGEDCPVFDGLFEFCQLSAGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 165 LKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKP 244
Cdd:cd10010  161 LKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 245 IMSKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEYMKSFNLPLLMLGGGGYTIRNVARCWTFETAVALDST 324
Cdd:cd10010  241 VMSKVMEMFQPSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDSE 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 528510099 325 IPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNDYLEKIKQRLFENLRMLP 375
Cdd:cd10010  321 IPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLP 371
PTZ00063 PTZ00063
histone deacetylase; Provisional
 8-406 0e+00

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 617.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099   8 TKKKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSE 87
Cdd:PTZ00063   2 MRKRVSYFYDPDIGSYYYGPGHPMKPQRIRMAHALILSYDLYKHMEIYRPHKSVEPELVLFHDEEYVDFLSSISPENYRD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  88 YSKQMQRFNVGE--DCPVFDGLFEFCQLSTGGSVAGAVKLNKQQTDIAINWAGGLHHAKKSEASGFCYVNDIVLAILELL 165
Cdd:PTZ00063  82 FTYQLKRFNVGEatDCPVFDGLFEFQQSCAGASIDGAYKLNNHQADICVNWSGGLHHAKRSEASGFCYINDIVLGILELL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 166 KYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPI 245
Cdd:PTZ00063 162 KYHARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKFGDFFPGTGDVTDIGVAQGKYYSVNVPLNDGIDDDSFVDLFKPV 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 246 MSKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEYMKSFNLPLLMLGGGGYTIRNVARCWTFETAVALDST- 324
Cdd:PTZ00063 242 ISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAACVEFVRSLNIPLLVLGGGGYTIRNVARCWAYETGVILNKHd 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 325 -IPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNDYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAVQEDSGDEEDDPDK 403
Cdd:PTZ00063 322 eMSDQISLNDYYDYYAPDFQLHLQPSNIPNYNSPEHLEKIKVKILENLRYLEHAPGVQFAYVPPDFFDRDIDDEDEKNQY 401


                 ...
gi 528510099 404 RIS 406
Cdd:PTZ00063 402 ELS 404
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 29-319 1.00e-106

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: 319.18  E-value: 1.00e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099   29 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPdnMSEYSKQMQRFNVGEDCPVFDGLF 108
Cdd:pfam00850   1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAAP--EGGALLLLSYLSGDDDTPVSPGSY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  109 EFCQLSTGGSVAGAVKLNKQQTD--IAINWaGGLHHAKKSEASGFCYVNDIVLAILELLKYH--QRVLYIDIDIHHGDGV 184
Cdd:pfam00850  79 EAALLAAGGTLAAADAVLSGEARnaFALVR-PPGHHAERDRASGFCIFNNVAIAAKYLREKYglKRVAIVDFDVHHGNGT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  185 EEAFYTTDRVMTVSFHKYGEY-FPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPIMSKVMEMYQPSAVVLQCG 263
Cdd:pfam00850 158 QEIFYDDPSVLTLSIHQYPGGfYPGTGFADETGEGKGKGYTLNVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAG 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  264 ADSLSGDRLGCFNLTIKGHAKCVEYMKSFNLPLLMLGGGG----YTIRNVARCWTFETAV 319
Cdd:pfam00850 238 FDAHAGDPLGGLNLTTEGFAEITRILLELADPLCIRVVSVleggYNLDALARSATAVLAA 297
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 12-292 2.28e-75

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 239.24  E-value: 2.28e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  12 VCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYskq 91
Cdd:COG0123    1 TALIYHPDYLLHDLGPGHPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAASLDGGYGQ--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  92 mqrfnVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNKQQTDIA-INWAGGLHHAKKSEASGFCYVNDIVLAILELL-KYHQ 169
Cdd:COG0123   78 -----LDPDTPVSPGTWEAALLAAGGALAAADAVLEGEARNAfALVRPPGHHAERDRAMGFCLFNNAAIAARYLLaKGLE 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 170 RVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGeYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPIMSKV 249
Cdd:COG0123  153 RVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQDP-LYPGTGAADETGEGAGEGSNLNVPLPPGTGDAEYLAALEEALLPA 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 528510099 250 MEMYQPSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEYMKSF 292
Cdd:COG0123  232 LEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLEL 274
 
Name Accession Description Interval E-value
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
 5-375 0e+00

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: 762.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099   5 SQGTKKKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDN 84
Cdd:cd10010    1 SQGTKKKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  85 MSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNKQQTDIAINWAGGLHHAKKSEASGFCYVNDIVLAILEL 164
Cdd:cd10010   81 MSEYSKQMQRFNVGEDCPVFDGLFEFCQLSAGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 165 LKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKP 244
Cdd:cd10010  161 LKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 245 IMSKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEYMKSFNLPLLMLGGGGYTIRNVARCWTFETAVALDST 324
Cdd:cd10010  241 VMSKVMEMFQPSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDSE 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 528510099 325 IPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNDYLEKIKQRLFENLRMLP 375
Cdd:cd10010  321 IPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLP 371
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
 9-374 0e+00

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: 693.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099   9 KKKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEY 88
Cdd:cd10011    1 KKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  89 SKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNKQQTDIAINWAGGLHHAKKSEASGFCYVNDIVLAILELLKYH 168
Cdd:cd10011   81 SKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 169 QRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPIMSK 248
Cdd:cd10011  161 QRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQIFKPIISK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 249 VMEMYQPSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEYMKSFNLPLLMLGGGGYTIRNVARCWTFETAVALDSTIPNE 328
Cdd:cd10011  241 VMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLGGGGYTIRNVARCWTYETAVALDCEIPNE 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 528510099 329 LPYNDYFEYFGPDFKLHISPSNMTNQNTNDYLEKIKQRLFENLRML 374
Cdd:cd10011  321 LPYNDYFEYFGPDFKLHISPSNMTNQNTPEYMEKIKQRLFENLRML 366
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
 10-388 0e+00

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: 655.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  10 KKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYS 89
Cdd:cd10005    1 KRVAYFYDPDVGNFHYGPGHPMKPHRLALTHSLVLHYGLYKKMQVYKPYRASAHDMCRFHSEDYIDFLQRVTPQNIQGFT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  90 KQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNKQQTDIAINWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQ 169
Cdd:cd10005   81 KSLNQFNVGDDCPVFPGLFDFCSMYTGASLEGATKLNHKICDIAINWSGGLHHAKKFEASGFCYVNDIVIAILELLKYHP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 170 RVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEY-FPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPIMSK 248
Cdd:cd10005  161 RVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYfFPGTGDMYEVGAESGRYYSVNVPLKDGIDDQSYLQLFKPVIQQ 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 249 VMEMYQPSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEYMKSFNLPLLMLGGGGYTIRNVARCWTFETAVALDSTIPNE 328
Cdd:cd10005  241 VIDFYQPTCIVLQCGADSLGCDRLGCFNLSIKGHGECVEFVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVDEEISNE 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528510099 329 LPYNDYFEYFGPDFKLHIS-PSNMTNQNTNDYLEKIKQRLFENLRMLPHAPGVQMQAIPED 388
Cdd:cd10005  321 LPYNEYFEYFAPDFTLHPDvSTRIENQNSKQYLDQIRQTVFENLKMLNHAPSVQMQDVPPD 381
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
 15-320 0e+00

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: 651.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  15 YYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQR 94
Cdd:cd09991    1 FYDPDVGNYYYGQGHPMKPHRIRMTHSLILSYGLYKKMEIYRPRPATAEELTKFHSDDYIDFLRSVSPDNMKEFKKQLER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  95 FNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNKQQTDIAINWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYI 174
Cdd:cd09991   81 FNVGEDCPVFDGLYEYCQLYAGGSIAAAVKLNRGQADIAINWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 175 DIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPIMSKVMEMYQ 254
Cdd:cd09991  161 DIDIHHGDGVEEAFYTTDRVMTVSFHKFGEYFFPGTGLRDIGAGKGKYYAVNVPLKDGIDDESYLQIFEPVLSKVMEVFQ 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528510099 255 PSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEYMKSFNLPLLMLGGGGYTIRNVARCWTFETAVA 320
Cdd:cd09991  241 PSAVVLQCGADSLAGDRLGCFNLSIKGHAKCVKFVKSFNIPLLVLGGGGYTLRNVARCWTYETAVL 306
PTZ00063 PTZ00063
histone deacetylase; Provisional
 8-406 0e+00

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 617.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099   8 TKKKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSE 87
Cdd:PTZ00063   2 MRKRVSYFYDPDIGSYYYGPGHPMKPQRIRMAHALILSYDLYKHMEIYRPHKSVEPELVLFHDEEYVDFLSSISPENYRD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  88 YSKQMQRFNVGE--DCPVFDGLFEFCQLSTGGSVAGAVKLNKQQTDIAINWAGGLHHAKKSEASGFCYVNDIVLAILELL 165
Cdd:PTZ00063  82 FTYQLKRFNVGEatDCPVFDGLFEFQQSCAGASIDGAYKLNNHQADICVNWSGGLHHAKRSEASGFCYINDIVLGILELL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 166 KYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPI 245
Cdd:PTZ00063 162 KYHARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKFGDFFPGTGDVTDIGVAQGKYYSVNVPLNDGIDDDSFVDLFKPV 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 246 MSKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEYMKSFNLPLLMLGGGGYTIRNVARCWTFETAVALDST- 324
Cdd:PTZ00063 242 ISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAACVEFVRSLNIPLLVLGGGGYTIRNVARCWAYETGVILNKHd 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 325 -IPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNDYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAVQEDSGDEEDDPDK 403
Cdd:PTZ00063 322 eMSDQISLNDYYDYYAPDFQLHLQPSNIPNYNSPEHLEKIKVKILENLRYLEHAPGVQFAYVPPDFFDRDIDDEDEKNQY 401


                 ...
gi 528510099 404 RIS 406
Cdd:PTZ00063 402 ELS 404
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
 9-383 0e+00

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: 614.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099   9 KKKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEY 88
Cdd:cd10004    1 KKKVAYFYDSDVGNYAYGPGHPMKPHRIRMAHSLVMNYGLYKKMEIYRAKPATKNEMTQFHTDEYIDFLSRVTPDNMEKF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  89 SKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNKQQTDIAINWAGGLHHAKKSEASGFCYVNDIVLAILELLKYH 168
Cdd:cd10004   81 QKEQVKYNVGDDCPVFDGLFEFCSISAGGSMEGAARLNRGKCDIAVNWAGGLHHAKKSEASGFCYVNDIVLGILELLRYH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 169 QRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPIMSK 248
Cdd:cd10004  161 QRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYGEYFPGTGELRDIGIGTGKNYAVNVPLRDGIDDESYKSIFEPVIKH 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 249 VMEMYQPSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEYMKSFNLPLLMLGGGGYTIRNVARCWTFETAVALDSTIPNE 328
Cdd:cd10004  241 VMEWYQPEAVVLQCGGDSLSGDRLGCFNLSMKGHANCVNFVKSFNLPMLVLGGGGYTMRNVARTWAFETGLLAGEELDKD 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 528510099 329 LPYNDYFEYFGPDFKLHISPSNMTNQNTNDYLEKIKQRLFENLRMLPHAPGVQMQ 383
Cdd:cd10004  321 LPYNEYYEYYGPDYELNVRPSNMENHNTPEYLDKITTAVIENLRNTSFAPSVQMQ 375
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
 12-320 1.67e-163

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: 464.62  E-value: 1.67e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  12 VCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSK- 90
Cdd:cd11598    1 VSYHFNSRVEDYHFGRTHPMKPFRLTLTKHLVMGYGLHKAMDTYEARAATREELRQFHDADYLDFLSKVSPENANQLRFd 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  91 QMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNKQQTDIAINWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQR 170
Cdd:cd11598   81 KAEPFNIGDDCPVFDGMYDYCQLYAGASLDAARKLCSGQSDIAINWSGGLHHAKKSEASGFCYVNDIVLAILNLLRYFPR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 171 VLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKY-GEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPIMSKV 249
Cdd:cd11598  161 VLYIDIDVHHGDGVEEAFYRTDRVMTLSFHKYnGEFFPGTGDLDDNGGTPGKHFALNVPLEDGIDDEQYNLLFKSIIGPT 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528510099 250 MEMYQPSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEYMKSFNLPLLMLGGGGYTIRNVARCWTFETAVA 320
Cdd:cd11598  241 IEKFQPSAIVLQCGADSLGGDRLGQFNLNIKAHGACVKFVKSFGIPMLVVGGGGYTPRNVARAWCYETAVA 311
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 30-371 1.85e-149

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: 430.99  E-value: 1.85e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  30 PMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRP--DNMSEYSKQmQRFNVGEDCPVFDGL 107
Cdd:cd10000   17 PKVPNRASMVHSLIEAYGLLKQLRVVKPRVATEEELASFHSDEYIQFLKKASNegDNDEEPSEQ-QEFGLGYDCPIFEGI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 108 FEFCQLSTGGSVAGAVKLNKQQTDIAINWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEA 187
Cdd:cd10000   96 YDYAAAVAGATLTAAQLLIDGKCKVAINWFGGWHHAQRDEASGFCYVNDIVLGILKLREKFDRVLYVDLDLHHGDGVEDA 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 188 FYTTDRVMTVSFHKYGE-YFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPIMSKVMEMYQPSAVVLQCGADS 266
Cdd:cd10000  176 FSFTSKVMTVSLHKYSPgFFPGTGDVSDVGLGKGKYYTVNVPLRDGIQDEQYLQIFTAVVPEIVAAFRPEAVVLQCGADT 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 267 LSGDRLGCFNLTIKGHAKCVEYMKSFNLPLLMLGGGGYTIRNVARCWTFETAVALDSTIPNELPYNDYFEYFGPDFKLHI 346
Cdd:cd10000  256 LAGDPMGAFNLTPVGIGKCLKYVLGWKLPTLILGGGGYNLANTARCWTYLTGLILGEPLSSDIPDHEFFTSYGPDYELEI 335

                        330       340
                 ....*....|....*....|....*
gi 528510099 347 SPSNMTNQNTNDYLEKIKQRLFENL 371
Cdd:cd10000  336 SPSLRPDLNEDQYIEKILETIKGNL 360
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
 35-320 5.46e-114

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: 337.10  E-value: 5.46e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  35 RIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQmqrFNVGEDCPVFDGLFEFCQLS 114
Cdd:cd09301    1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKANFAVATITESKP---VIFGPNFPVQRHYFRGARLS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 115 TGGSVAGAVKLNKQQTDIAINWA-GGLHHAKKSEASGFCYVNDIVLAILELLKY-HQRVLYIDIDIHHGDGVEEAFYTTD 192
Cdd:cd09301   78 TGGVVEAAELVAKGELERAFAVVgAGGHHAGKSRAWGFCYFNDVVLAIKFLRERgISRILIIDTDAHHGDGTREAFYDDD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 193 RVMTVSFHKYGEYFPGTgdlrdigaGKGKYYAVNYPLRDGIDDESYEAIFKPIMSKVMEMYQPSAVVLQCGADSLSGDRL 272
Cdd:cd09301  158 RVLHMSFHNYDIYPFGR--------GKGKGYKINVPLEDGLGDEEYLDAVERVISKVLEEFEPEVVVLQFGHDTHEGDRL 229

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 528510099 273 GCFNLTIKGHAKCVEYMKSFNLPLLMLGGGG--YTIRNVARCWTFETAVA 320
Cdd:cd09301  230 GGFNLSEKGFVKLAEIVKEFARGGPILMVLGggYNPEAAARIWTAIIKEL 279
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 29-319 1.00e-106

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: 319.18  E-value: 1.00e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099   29 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPdnMSEYSKQMQRFNVGEDCPVFDGLF 108
Cdd:pfam00850   1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAAP--EGGALLLLSYLSGDDDTPVSPGSY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  109 EFCQLSTGGSVAGAVKLNKQQTD--IAINWaGGLHHAKKSEASGFCYVNDIVLAILELLKYH--QRVLYIDIDIHHGDGV 184
Cdd:pfam00850  79 EAALLAAGGTLAAADAVLSGEARnaFALVR-PPGHHAERDRASGFCIFNNVAIAAKYLREKYglKRVAIVDFDVHHGNGT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  185 EEAFYTTDRVMTVSFHKYGEY-FPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPIMSKVMEMYQPSAVVLQCG 263
Cdd:pfam00850 158 QEIFYDDPSVLTLSIHQYPGGfYPGTGFADETGEGKGKGYTLNVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAG 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  264 ADSLSGDRLGCFNLTIKGHAKCVEYMKSFNLPLLMLGGGG----YTIRNVARCWTFETAV 319
Cdd:pfam00850 238 FDAHAGDPLGGLNLTTEGFAEITRILLELADPLCIRVVSVleggYNLDALARSATAVLAA 297
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
 13-314 9.61e-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: 302.17  E-value: 9.61e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  13 CYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYskqM 92
Cdd:cd09994    1 AFIYSEEYLRYSFGPNHPFNPPRLSLTKDLLRALGLLPPVDLVPPRPATEEELLLFHTPDYIEAVKEASRGQEPEG---R 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  93 QRFNVG-EDCPVFDGLFEFCQLSTGGSVAGAVKLNKQQTDIAINWAGGLHHAKKSEASGFCYVNDIVLAILELL-KYHQR 170
Cdd:cd09994   78 GRLGLGtEDNPVFPGMHEAAALVVGGTLLAARLVLEGEARRAFNPAGGLHHAMRGRASGFCVYNDAAVAIERLRdKGGLR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 171 VLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEY-FPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPIMSKV 249
Cdd:cd09994  158 VAYVDIDAHHGDGVQAAFYDDPRVLTISLHESGRYlFPGTGFVDEIGEGEGYGYAVNIPLPPGTGDDEFLRAFEAVVPPL 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 250 MEMYQPSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEYMKSFNLPLLMLGGGG-----YTIRNVARCWT 314
Cdd:cd09994  238 LRAFRPDVIVSQHGADAHAGDPLTHLNLSNRAYRAAVRRIRELADEYCGGRWLAlggggYNPDVVARAWA 307
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
 35-320 1.13e-89

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: 275.68  E-value: 1.13e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  35 RIRMTHNLLLNYGL-YRKMEIYRPHKANAEEMTKYHSDDYIKFLrsirpdnmseyskqMQRFNVGEDCPVFDGLFEFCQL 113
Cdd:cd11680   21 RSSLVHSLIRAYGLlQHFDEIIEPERATRKDLTKYHDKDYVDFL--------------LKKYGLEDDCPVFPFLSMYVQL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 114 STGGSVAGAVKLNKQQT-DIAINWAGGLHHAKKSEASGFCYVNDIVLAILELLKYH-QRVLYIDIDIHHGDGVEEAFYTT 191
Cdd:cd11680   87 VAGSSLALAKHLITQVErDIAINWYGGRHHAQKSRASGFCYVNDIVLAILRLRRARfRRVFYLDLDLHHGDGVESAFFFS 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 192 DRVMTVSFHKYGE-YFPGTGDLRDigagKGKYYAVNYPLRDGIDDESYEAIFKPIMSKVMEMYQPSAVVLQCGADSLSGD 270
Cdd:cd11680  167 KNVLTCSIHRYDPgFFPGTGSLKN----SSDKGMLNIPLKRGLSDKTLLRIIDSIVRPLIEKFEPEVIVIQCGCDGLSGD 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 528510099 271 RLGCFNLTIKGHAKCVEYMKSFNLPLLMLGG--GGYTIRNVARCWTFETAVA 320
Cdd:cd11680  243 PHKEWNLTIRGYGSVIELLLKEFKDKPTLLLggGGYNHTEAARAWTYLTSMV 294
PTZ00346 PTZ00346
histone deacetylase; Provisional
 16-326 1.12e-86

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 272.67  E-value: 1.12e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  16 YDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLrSIRPDNMSEYSKQMQRF 95
Cdd:PTZ00346  30 YASDMNISAFVPQHAMKPYRVLAAMEIVRSLKIDAHCRTVVPPLVKVEELMAYHTDTYLANL-GLHSCRSWLWNAETSKV 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  96 NVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNKQQTDIAINWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYID 175
Cdd:PTZ00346 109 FFSGDCPPVEGLMEHSIATASGTLMGAVLLNSGQVDVAVHWGGGMHHSKCGECSGFCYVNDIVLGILELLKCHDRVLYVD 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 176 IDIHHGDGVEEAFYTTDRVMTVSFHKYGE-YFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPIMSKVMEMYQ 254
Cdd:PTZ00346 189 IDMHHGDGVDEAFCTSDRVFTLSLHKFGEsFFPGTGHPRDVGYGRGRYYSMNLAVWDGITDFYYLGLFEHALHSIVRRYS 268

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528510099 255 PSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEYMKSFNLPLLMLGGGGYTIRNVARCWTFETAVALDSTIP 326
Cdd:PTZ00346 269 PDAIVLQCGADSLAGDRLGLLNLSSFGHGQCVQAVRDLGIPMLALGGGGYTIRNVAKLWAYETSILTGHPLP 340
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 12-292 2.28e-75

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 239.24  E-value: 2.28e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  12 VCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYskq 91
Cdd:COG0123    1 TALIYHPDYLLHDLGPGHPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAASLDGGYGQ--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  92 mqrfnVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNKQQTDIA-INWAGGLHHAKKSEASGFCYVNDIVLAILELL-KYHQ 169
Cdd:COG0123   78 -----LDPDTPVSPGTWEAALLAAGGALAAADAVLEGEARNAfALVRPPGHHAERDRAMGFCLFNNAAIAARYLLaKGLE 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 170 RVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGeYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPIMSKV 249
Cdd:COG0123  153 RVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQDP-LYPGTGAADETGEGAGEGSNLNVPLPPGTGDAEYLAALEEALLPA 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 528510099 250 MEMYQPSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEYMKSF 292
Cdd:COG0123  232 LEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLEL 274
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
 29-284 5.17e-44

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: 156.50  E-value: 5.17e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  29 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSkqmqrfnvgEDCPVFDGLF 108
Cdd:cd09992    1 HPERPERLLAILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYIERVEETCEAGGGYLD---------PDTYVSPGSY 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 109 EFCQLSTGGSVAGAVKLNKQQTDIAinWA-----GglHHAKKSEASGFCYVNDIVLAILELLKYH--QRVLYIDIDIHHG 181
Cdd:cd09992   72 EAALLAAGAALAAVDAVLSGEAENA--FAlvrppG--HHAEPDRAMGFCLFNNVAIAARYAQKRYglKRVLIVDWDVHHG 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 182 DGVEEAFYTTDRVMTVSFHKYGeYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPIMSKVMEMYQPSAVVLQ 261
Cdd:cd09992  148 NGTQDIFYDDPSVLYFSIHQYP-FYPGTGAAEETGGGAGEGFTINVPLPPGSGDAEYLAAFEEVLLPIAREFQPDLVLVS 226

                        250       260
                 ....*....|....*....|...
gi 528510099 262 CGADSLSGDRLGCFNLTIKGHAK 284
Cdd:cd09992  227 AGFDAHRGDPLGGMNLTPEGYAR 249
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 29-281 4.34e-41

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: 148.03  E-value: 4.34e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  29 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSirpdnmSEYSKQMQR---FnvgedcPVFD 105
Cdd:cd09993    1 HRFPMRKYGLLREALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLESLKS------GELSREEIRrigF------PWSP 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 106 GLFEFCQLSTGGSVAgAVKLnKQQTDIAINWAGGLHHAKKSEASGFCYVNDIVLAILELLKYH--QRVLYIDIDIHHGDG 183
Cdd:cd09993   69 ELVERTRLAVGGTIL-AARL-ALEHGLAINLAGGTHHAFPDRGEGFCVFNDIAIAARVLLAEGlvRRVLIVDLDVHQGNG 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 184 VEEAFYTTDRVMTVSFHkyGEY-FPG---TGDLrDIgagkgkyyavnyPLRDGIDDESYEAIFKPIMSKVMEMYQPSAVV 259
Cdd:cd09993  147 TAAIFADDPSVFTFSMH--GEKnYPFrkePSDL-DV------------PLPDGTGDDEYLAALEEALPRLLAEFRPDLVF 211

                        250       260
                 ....*....|....*....|..
gi 528510099 260 LQCGADSLSGDRLGCFNLTIKG 281
Cdd:cd09993  212 YNAGVDVLAGDRLGRLSLSLEG 233
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
 27-273 3.15e-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: 145.40  E-value: 3.15e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  27 QGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEyskqmqrfnVGEDCPVFDG 106
Cdd:cd09996   31 GRHPENPETKRRIKNLLEVSGLSDHLVLITPRPATDEELLRVHTPEYIDRVKAASAAGGGE---------AGGGTPFGPG 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 107 LFEFCQLSTGGSVAgAVK--LNKQqtdiaINWAGGL-----HHAKKSEASGFCYVNDIVLAILELLKYH--QRVLYIDID 177
Cdd:cd09996  102 SYEIALLAAGGAIA-AVDavLDGE-----VDNAYALvrppgHHAEPDQGMGFCLFNNVAIAARHALAVGgvKRVAVVDWD 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 178 IHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPIMSKVMEMYQPSA 257
Cdd:cd09996  176 VHHGNGTQAIFYDDPDVLTISLHQDRCFPPDSGAVEERGEGAGEGYNLNIPLPPGSGDGAYLHAFERIVLPALRAFRPEL 255

                        250
                 ....*....|....*.
gi 528510099 258 VVLQCGADSLSGDRLG 273
Cdd:cd09996  256 IIVASGFDASAFDPLG 271
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
 28-284 2.32e-37

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: 138.82  E-value: 2.32e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  28 GHPMKPHRIRMTHNLLLNYGLYRKMEiyrPHKANAEEMTKYHSDDYIKFLRSIRPDnmseyskqmqrfnvgedCPVFDGL 107
Cdd:cd10001   24 PHPENPERAEAILDALKRAGLGEVLP---PRDFGLEPILAVHDPDYVDFLETADTD-----------------TPISEGT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 108 FEFCQLSTGGSVAGAVKLNKQQtdiaiNWAGGL-----HHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGD 182
Cdd:cd10001   84 WEAALAAADTALTAADLVLEGE-----RAAYALcrppgHHAGRDRAGGFCYFNNAAIAAQYLRDRAGRVAILDVDVHHGN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 183 GVEEAFYTTDRVMTVSFHKYGE-YFPGT-GDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPIMSKVMEmYQPSAVVL 260
Cdd:cd10001  159 GTQEIFYERPDVLYVSIHGDPRtFYPFFlGFADETGEGEGEGYNLNLPLPPGTGDDDYLAALDEALAAIAA-FGPDALVV 237

                        250       260
                 ....*....|....*....|....
gi 528510099 261 QCGADSLSGDRLGCFNLTIKGHAK 284
Cdd:cd10001  238 SLGFDTHEGDPLSDFKLTTEDYAR 261
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 25-283 5.91e-37

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: 138.60  E-value: 5.91e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  25 YGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRpdNMSEysKQMQRFNVGED---- 100
Cdd:cd10002    3 WDSNHIECPERLEAILERLTQDGLLERCVKIPAREAEEDEILLVHSQEYIDLVKSTE--TMEK--EELESLCSGYDsvyl 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 101 CPvfdGLFEFCQLSTGGSV--AGAVKLNKQQTDIAINWAGGlHHAKKSEASGFCYVNDIVLAILELLKYH--QRVLYIDI 176
Cdd:cd10002   79 CP---STYEAARLAAGSTIelVKAVMAGKIQNGFALIRPPG-HHAMRNEANGYCIFNNVAIAAKYAIEKLglKRILIVDW 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 177 DIHHGDGVEEAFYTTDRVMTVSFHKY--GEYFPG--TGDLRDIGAGKGKYYAVNYPLRD-GIDDESYEAIFKPIMSKVME 251
Cdd:cd10002  155 DVHHGQGTQQGFYEDPRVLYFSIHRYehGRFWPHlfESDYDYIGVGHGYGFNVNVPLNQtGLGDADYLAIFHHILLPLAL 234

                        250       260       270
                 ....*....|....*....|....*....|..
gi 528510099 252 MYQPSAVVLQCGADSLSGDRLGCFNLTIKGHA 283
Cdd:cd10002  235 EFQPELVLVSAGFDASIGDPEGEMAVTPAGYA 266
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 108-320 7.44e-35

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: 129.80  E-value: 7.44e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 108 FEFCQLSTGGSVAGAVKLnkqqtDIAINWAGglHHAKkseasgfcyVNDIVLAILELlkyHQRVLYIDIDIHHGDGVEEA 187
Cdd:cd09987    8 AEAHELLAGVVVAVLKDG-----KVPVVLGG--DHSI---------ANGAIRAVAEL---HPDLGVIDVDAHHDVRTPEA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 188 FY--------------TTDRVMTVSFHKYGEYFPGTGdlrdiGAGKGKYYAVNYPLRDGiDDESYEAIFKPIMSKVmeMY 253
Cdd:cd09987   69 FGkgnhhtprhllcepLISDVHIVSIGIRGVSNGEAG-----GAYARKLGVVYFSMTEV-DKLGLGDVFEEIVSYL--GD 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528510099 254 QPSAVVLQCGADSLSGD------RLGCFNLTIKGHAKCVEYMKSFNLPLLMLGGGGYTI----RNVARCWTFETAVA 320
Cdd:cd09987  141 KGDNVYLSVDVDGLDPSfapgtgTPGPGGLSYREGLYITERIAKTNLVVGLDIVEVNPLldetGRTARLAAALTLEL 217
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
 28-283 3.98e-34

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: 131.31  E-value: 3.98e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  28 GHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPvfdGL 107
Cdd:cd10003   15 GHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHLDEMKSLEKMKPRELNRLGKEYDSIYIHP---DS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 108 FEFCQLSTGGS--VAGAVKLNKQQTDIAINWAGGlHHAKKSEASGFCYVNDIVLAI-LELLKYH-QRVLYIDIDIHHGDG 183
Cdd:cd10003   92 YQCALLAAGCVlqVVEAVLTGESRNGVAIVRPPG-HHAEQDTACGFCFFNNVAIAArYAQKKYGlKRILIVDWDVHHGNG 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 184 VEEAFYTTDRVMTVSFHKY--GEYFPGT--GDLRDIGAGKGKYYAVNYPL-RDGIDDESYEAIFKPIMSKVMEMYQPSAV 258
Cdd:cd10003  171 TQHMFESDPSVLYISLHRYdnGSFFPNSpeGNYDVVGKGKGEGFNVNIPWnKGGMGDAEYIAAFQQVVLPIAYEFNPELV 250

                        250       260
                 ....*....|....*....|....*
gi 528510099 259 VLQCGADSLSGDRLGCFNLTIKGHA 283
Cdd:cd10003  251 LVSAGFDAARGDPLGGCKVTPEGYA 275
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 28-283 4.14e-33

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: 127.46  E-value: 4.14e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  28 GHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIrpDNMSEYSKQMQRFNVGEDCPVFDGL 107
Cdd:cd11600    2 PHPEDPSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEHWDRVEAT--EKMSDEQLKDRTEIFERDSLYVNND 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 108 FEFC-QLSTGGSV--AGAVKLNKQQTDIAINWAGGlHHAKKSEASGFCYVNDIVLAILELLK-YH---QRVLYIDIDIHH 180
Cdd:cd11600   80 TAFCaRLSCGGAIeaCRAVAEGRVKNAFAVVRPPG-HHAEPDESMGFCFFNNVAVAAKWLQTeYPdkiKKILILDWDIHH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 181 GDGVEEAFYTTDRVMTVSFHKY--GEYFPGT--GDLRDIGAGKGKYYAVNYPLRD-GIDDESYEAIFKPI-MSKVMEmYQ 254
Cdd:cd11600  159 GNGTQRAFYDDPNVLYISLHRFenGGFYPGTpyGDYESVGEGAGLGFNVNIPWPQgGMGDADYIYAFQRIvMPIAYE-FD 237

                        250       260
                 ....*....|....*....|....*....
gi 528510099 255 PSAVVLQCGADSLSGDRLGCFNLTIKGHA 283
Cdd:cd11600  238 PDLVIISAGFDAADGDELGQCHVTPAGYA 266
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 29-289 4.71e-33

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: 129.00  E-value: 4.71e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  29 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSirpdnmseysKQMQRFNVGEDCPVFDGLF 108
Cdd:cd11681   24 HPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTLLYGT----------NPLSRLKLDPTKLAGLPQK 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 109 EFCQLSTGG-SVAGAVKLNKQQTDIAINWAGGL------------------------HHAKKSEASGFCYVNDIVLA--I 161
Cdd:cd11681   94 SFVRLPCGGiGVDSDTVWNELHTSNAARMAVGCvidlafkvatgelkngfavvrppgHHAEPSQAMGFCFFNSVAIAakQ 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 162 LELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKY--GEYFPGTGDLRDIGAGKGKYYAVNYPLRDGID----D 235
Cdd:cd11681  174 LQQKLKLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYddGNFFPGTGAPTEVGSGAGEGFNVNIAWSGGLDppmgD 253

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 528510099 236 ESYEAIFKPIMSKVMEMYQPSAVVLQCGADSLSG--DRLGCFNLTikghAKCVEYM 289
Cdd:cd11681  254 AEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGhpPPLGGYKVS----PACFGYM 305
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
 29-289 7.28e-29

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: 117.42  E-value: 7.28e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  29 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKF-----LRSIRPDNMSEYSKQMQRFnvgedcpv 103
Cdd:cd10008   24 HPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLygtnpLSRLKLDNGKLAGLLAQRM-------- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 104 fdglfeFCQLSTGG-SVAGAVKLNKQQTDIAINWAGGL------------------------HHAKKSEASGFCYVNDIV 158
Cdd:cd10008   96 ------FVMLPCGGvGVDTDTIWNELHSSNAARWAAGSvtdlafkvasrelkngfavvrppgHHADHSTAMGFCFFNSVA 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 159 LAI--LELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKY--GEYFPGTGDLRDIGAGKGKYYAVNYPLRDGID 234
Cdd:cd10008  170 IACrqLQQQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHddGNFFPGSGAVDEVGAGSGEGFNVNVAWAGGLD 249

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528510099 235 ----DESYEAIFKPIMSKVMEMYQPSAVVLQCGADSLSGD--RLGCFNLTikghAKCVEYM 289
Cdd:cd10008  250 ppmgDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHpaPLGGYHVS----AKCFGYM 306
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
 29-289 6.46e-28

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: 115.13  E-value: 6.46e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  29 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIkFLRSIRPDNMSEYSKQMQRFNVGEdcpvfdglf 108
Cdd:cd10006   27 HPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHT-LLYGTNPLNRQKLDSKKLLGSLAS--------- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 109 EFCQLSTGG------------SVAGAVKLN-KQQTDIAINWAGGL------------HHAKKSEASGFCYVNDIVLA--I 161
Cdd:cd10006   97 VFVRLPCGGvgvdsdtiwnevHSSGAARLAvGCVVELVFKVATGElkngfavvrppgHHAEESTPMGFCYFNSVAIAakL 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 162 LELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKY--GEYFPGTGDLRDIGAGKGKYYAVNYPLRDGID----D 235
Cdd:cd10006  177 LQQRLNVSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYddGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDppmgD 256

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 528510099 236 ESYEAIFKPIMSKVMEMYQPSAVVLQCGADSLSGD--RLGCFNLTikghAKCVEYM 289
Cdd:cd10006  257 AEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHptPLGGYNLS----AKCFGYL 308
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
 29-282 9.51e-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: 108.92  E-value: 9.51e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  29 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDdYIKFLRSIRPDNMSEY-SKQMqrfnVGedcPVFDGL 107
Cdd:cd10007   26 HPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHSE-HHTLLYGTSPLNRQKLdSKKL----LG---PLSQKM 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 108 FEFcqLSTGG-SVAGAVKLNKQQTDIAINWAGGL------------------------HHAKKSEASGFCYVNDIVLAIl 162
Cdd:cd10007   98 YAV--LPCGGiGVDSDTVWNEMHSSSAVRMAVGClielafkvaagelkngfavirppgHHAEESTAMGFCFFNSVAIAA- 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 163 ELLKYH---QRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKY--GEYFPGTGDLRDIGAGKGKYYAVNYPLRDGID--- 234
Cdd:cd10007  175 KLLQQKlnvGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYddGNFFPGSGAPDEVGAGPGVGFNVNIAWTGGVDppi 254

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 528510099 235 -DESYEAIFKPIMSKVMEMYQPSAVVLQCGADSLSGDR--LGCFNLTIK--GH 282
Cdd:cd10007  255 gDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGHQspLGGYSVTAKcfGH 307
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
 29-278 5.23e-24

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: 101.43  E-value: 5.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  29 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYskqmqrfnVGEDCPVFDGLF 108
Cdd:cd11599    1 HPESPERLEAILDALIASGLDRLLRQLEAPPATREQLLRVHDAAYVDRLEAAAPEEGLVQ--------LDPDTAMSPGSL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 109 EFCQLSTGGSVAG--AVkLNKQQTD--IAINWAGglHHAKKSEASGFCYVNDIVLAILELLKYH--QRVLYIDIDIHHGD 182
Cdd:cd11599   73 EAALRAAGAVVAAvdAV-MAGEARNafCAVRPPG--HHAERDKAMGFCLFNNVAIAAAHALAHHglERVAIVDFDVHHGN 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 183 GVEEAFYTTDRVMTVSFHKYgEYFPGTGDLRDIGAGkgkyYAVNYPLRDGIDDESYEAIFKPIMSKVMEMYQPSAVVLQC 262
Cdd:cd11599  150 GTEDIFRDDPRVLFCSSHQH-PLYPGTGAPDETGHG----NIVNVPLPAGTGGAEFREAVEDRWLPALDAFKPDLILISA 224

                        250
                 ....*....|....*.
gi 528510099 263 GADSLSGDRLGCFNLT 278
Cdd:cd11599  225 GFDAHRDDPLAQLNLT 240
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
 21-282 9.91e-24

Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. Class IIa histone deacetylases are signal-dependent co-repressors, they have N-terminal regulatory domain with two or three conserved serine residues, phosphorylation of these residues is important for ability to shuttle between the nucleus and cytoplasm and act as transcriptional co-repressors. HDAC9 is involved in regulation of gene expression and dendritic growth in developing cortical neurons. It also plays a role in hematopoiesis. Its deregulated expression may be associated with some human cancers. HDAC5 and HDAC9 have been found to be significantly up-regulated in high-risk medulloblastoma compared with low-risk and may potentially be novel drug targets.


Pssm-ID: 212533 [Multi-domain]  Cd Length: 379  Bit Score: 102.40  E-value: 9.91e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  21 GNYyygQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYiKFLRSIRPDNMSEYSKqmqRFNVGED 100
Cdd:cd10009   19 GNS---TTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHH-SLLYGTNPLDGQKLDP---RILLGDD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 101 CPVFdglfeFCQLSTGG--------------------------SVAGAVKLNKQQTDIAINWAGGlHHAKKSEASGFCYV 154
Cdd:cd10009   92 SQKF-----FSSLPCGGlgvdsdtiwnelhssgaarmavgcviELASKVASGELKNGFAVVRPPG-HHAEESTAMGFCFF 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 155 NDIVLAIlellKYHQ------RVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKY--GEYFPGTGDLRDIGAGKGKYYAVN 226
Cdd:cd10009  166 NSVAITA----KYLRdqlnisKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdeGNFFPGSGAPNEVGTGLGEGYNIN 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528510099 227 YPLRDGID----DESYEAIFKPIMSKVMEMYQPSAVVLQCGADSLSGDR--LGCFNLTIK--GH 282
Cdd:cd10009  242 IAWTGGLDppmgDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTppLGGYKVTAKcfGH 305
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 33-278 3.54e-21

Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. HDACs usually act via association with DNA binding proteins to target specific chromatin regions. HDAC10 has an N-terminal deacetylase domain and a C-terminal pseudo-repeat that shares significant similarity with its catalytic domain. It is located in the nucleus and cytoplasm, and is involved in regulation of melanogenesis. It transcriptionally down-regulates thioredoxin-interacting protein (TXNIP), leading to altered reactive oxygen species (ROS) signaling in human gastric cancer cells. Known interaction partners of HDAC10 are Pax3, KAP1, hsc70 and HDAC3 proteins.


Pssm-ID: 212546 [Multi-domain]  Cd Length: 337  Bit Score: 94.54  E-value: 3.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  33 PHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNmseySKQMQRFNVGEDCPVF-DGLFEFC 111
Cdd:cd11683   11 PERLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRETQVMN----KEELMAISGKYDAVYFhPNTFHCA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 112 QLSTGGSV--AGAVKLNKQQTDIAINWAGGlHHAKKSEASGFCYVNDIVLAILELLKYH--QRVLYIDIDIHHGDGVEEA 187
Cdd:cd11683   87 RLAAGATLqlVDAVLTGEVQNGMALVRPPG-HHSQRNAANGFCVFNNVAIAAEYAKKKYglHRILIVDWDVHHGQGIQYI 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 188 FYTTDRVMTVSFHKY--GEYFPG--TGDLRDIGAGKGKYYAVNYPLRD-GIDDESYEAIFKPIMSKVMEMYQPSAVVLQC 262
Cdd:cd11683  166 FEEDPSVLYFSWHRYehQRFWPFlrESDYDAVGRGKGLGFNINLPWNKvGMGNADYLAAFFHVLLPLAFEFDPELVLVSA 245

                        250
                 ....*....|....*.
gi 528510099 263 GADSLSGDRLGCFNLT 278
Cdd:cd11683  246 GFDSAIGDPEGQMCAT 261
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
 29-273 4.83e-21

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: 94.15  E-value: 4.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099  29 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFdglF 108
Cdd:cd11682    7 FPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYVALMKSTQYMTEEELRTLADTYDSVYLHPNS---Y 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 109 EFCQLSTGG--SVAGAVKLNKQQTDIAINWAGGlHHAKKSEASGFCYVNDIVLAILELLKYH--QRVLYIDIDIHHGDGV 184
Cdd:cd11682   84 SCACLAVGSvlQLVDKVLGGEIRNGLAIVRPPG-HHAQHDKMDGYCMFNNVAIAARYAQQKHgvQRVLIVDWDVHHGQGT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510099 185 EEAFYTTDRVMTVSFHKY--GEYFP--GTGDLRDIGAGKGKYYAVNYPL-RDGIDDESYEAIFKPIMSKVMEMYQPSAVV 259
Cdd:cd11682  163 QFIFEQDPSVLYFSIHRYeqGRFWPhlKESDSSAVGFGRGEGYNINVPWnQVGMRDADYIAAFLHVLLPVALEFQPQLVL 242

                        250
                 ....*....|....
gi 528510099 260 LQCGADSLSGDRLG 273
Cdd:cd11682  243 VAAGFDAVIGDPKG 256
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
 141-186 3.10e-07

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: 52.45  E-value: 3.10e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 528510099 141 HHAKKSEASGFCYVNDIVLAILE-LLKYH-QRVLYIDIDIHHGDGVEE 186
Cdd:cd09998  120 HHCSESTPSGFCWVNNVHVGAAHaYLTHGiTRVVILDIDLHHGNGTQD 167
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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