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Conserved domains on  [gi|6325325|ref|NP_015393|]
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histone deacetylase [Saccharomyces cerevisiae S288C]

Protein Classification

Hos1 family histone deacetylase( domain architecture ID 10184832)

Hos1 family histone deacetylase similar to Saccharomyces cerevisiae histone deacetylase HOS1, which is a Zn-dependent class I histone deacetylase responsible for Smc3 deacetylation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
 5-390 9.02e-160

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: 453.65  E-value: 9.02e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325    5 VISTSIFQSQVADLLPCNNhQKSQLTYSLINAYDLLQHFDEVLTFPYARKDDLLEFHSKSYIDYLINgrfnkmmaqdvnn 84
Cdd:cd11680   1 ILSVSEELTKIADLLPSNK-GRSSLVHSLIRAYGLLQHFDEIIEPERATRKDLTKYHDKDYVDFLLK------------- 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325   85 pmveskwselseladnwnekidynpsqdlqrfttrenlynyylnhsqalennmdcinnsevptndkptdtyilnsetkQY 164
Cdd:cd11680  67 ------------------------------------------------------------------------------KY 68

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  165 NLEGDCPIFSYLPMYCQVITGATLNLLDHLSP-TERLIGINWDGGRHHAFKQRASGFCYINDVVLLIQRLRKAKLNKITY 243
Cdd:cd11680  69 GLEDDCPVFPFLSMYVQLVAGSSLALAKHLITqVERDIAINWYGGRHHAQKSRASGFCYVNDIVLAILRLRRARFRRVFY 148

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  244 VDFDLHHGDGVEKAFQYSKQIQTISVHLYEPGFFPGTGSLsDSRKDKNVVNIPLKHGCDDNYLELIASKIVNPLIERHEP 323
Cdd:cd11680 149 LDLDLHHGDGVESAFFFSKNVLTCSIHRYDPGFFPGTGSL-KNSSDKGMLNIPLKRGLSDKTLLRIIDSIVRPLIEKFEP 227

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6325325  324 EALIIECGGDGLLGDRFNEWQLTIRGLSRIIINIMKSYPRAHIFLLGGGGYNDLLMSRFYTYLTWCV 390
Cdd:cd11680 228 EVIVIQCGCDGLSGDPHKEWNLTIRGYGSVIELLLKEFKDKPTLLLGGGGYNHTEAARAWTYLTSMV 294
 
Name Accession Description Interval E-value
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
 5-390 9.02e-160

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: 453.65  E-value: 9.02e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325    5 VISTSIFQSQVADLLPCNNhQKSQLTYSLINAYDLLQHFDEVLTFPYARKDDLLEFHSKSYIDYLINgrfnkmmaqdvnn 84
Cdd:cd11680   1 ILSVSEELTKIADLLPSNK-GRSSLVHSLIRAYGLLQHFDEIIEPERATRKDLTKYHDKDYVDFLLK------------- 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325   85 pmveskwselseladnwnekidynpsqdlqrfttrenlynyylnhsqalennmdcinnsevptndkptdtyilnsetkQY 164
Cdd:cd11680  67 ------------------------------------------------------------------------------KY 68

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  165 NLEGDCPIFSYLPMYCQVITGATLNLLDHLSP-TERLIGINWDGGRHHAFKQRASGFCYINDVVLLIQRLRKAKLNKITY 243
Cdd:cd11680  69 GLEDDCPVFPFLSMYVQLVAGSSLALAKHLITqVERDIAINWYGGRHHAQKSRASGFCYVNDIVLAILRLRRARFRRVFY 148

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  244 VDFDLHHGDGVEKAFQYSKQIQTISVHLYEPGFFPGTGSLsDSRKDKNVVNIPLKHGCDDNYLELIASKIVNPLIERHEP 323
Cdd:cd11680 149 LDLDLHHGDGVESAFFFSKNVLTCSIHRYDPGFFPGTGSL-KNSSDKGMLNIPLKRGLSDKTLLRIIDSIVRPLIEKFEP 227

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6325325  324 EALIIECGGDGLLGDRFNEWQLTIRGLSRIIINIMKSYPRAHIFLLGGGGYNDLLMSRFYTYLTWCV 390
Cdd:cd11680 228 EVIVIQCGCDGLSGDPHKEWNLTIRGYGSVIELLLKEFKDKPTLLLGGGGYNHTEAARAWTYLTSMV 294
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 23-388 3.19e-68

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: 219.80  E-value: 3.19e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325     23 NHQKSQLTYSLINAYDLLQHFdEVLTFPYARKDDLLEFHSKSYIDYLingrfnkmmaqdvnnpmvESKWSELSELADNWN 102
Cdd:pfam00850   4 NPERLKAILEALREAGLLPDL-EIIAPRPATEEELLLVHSPEYLEFL------------------EEAAPEGGALLLLSY 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325    103 EKIDynpsqdlqrfttrenlynyylnhsqalennmdcinnsevptndkptdtyilnsetkqynleGDCPIFSYLPMYCQV 182
Cdd:pfam00850  65 LSGD-------------------------------------------------------------DDTPVSPGSYEAALL 83

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325    183 ITGATLNLLDHLSPTERLIG--INWdGGRHHAFKQRASGFCYINDVVLLIQRLRKA-KLNKITYVDFDLHHGDGVEKAFQ 259
Cdd:pfam00850  84 AAGGTLAAADAVLSGEARNAfaLVR-PPGHHAERDRASGFCIFNNVAIAAKYLREKyGLKRVAIVDFDVHHGNGTQEIFY 162

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325    260 YSKQIQTISVHLYEPGFFPGTGSLSDSRKDK---NVVNIPLKHGCDDNYLELIASKIVNPLIERHEPEALIIECGGDGLL 336
Cdd:pfam00850 163 DDPSVLTLSIHQYPGGFYPGTGFADETGEGKgkgYTLNVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAGFDAHA 242

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 6325325    337 GDRFNEWQLTIRGLSRIIINIMKSYPRAHIFLL--GGGGYNDLLMSRFYTYLTW 388
Cdd:pfam00850 243 GDPLGGLNLTTEGFAEITRILLELADPLCIRVVsvLEGGYNLDALARSATAVLA 296
PTZ00063 PTZ00063
histone deacetylase; Provisional
 162-387 1.93e-46

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 166.52  E-value: 1.93e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325   162 KQYNL--EGDCPIFSYLPMYCQVITGATLNLLDHLSPTERLIGINWDGGRHHAFKQRASGFCYINDVVLLIQRLRKAKLn 239
Cdd:PTZ00063  87 KRFNVgeATDCPVFDGLFEFQQSCAGASIDGAYKLNNHQADICVNWSGGLHHAKRSEASGFCYINDIVLGILELLKYHA- 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325   240 KITYVDFDLHHGDGVEKAFQYSKQIQTISVHLYEpGFFPGTGSLSD---SRKDKNVVNIPLKHGCDDNYLELIASKIVNP 316
Cdd:PTZ00063 166 RVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKFG-DFFPGTGDVTDigvAQGKYYSVNVPLNDGIDDDSFVDLFKPVISK 244

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325325   317 LIERHEPEALIIECGGDGLLGDRFNEWQLTIRGLSRIIINIMK-SYPrahIFLLGGGGYNDLLMSRFYTYLT 387
Cdd:PTZ00063 245 CVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAACVEFVRSlNIP---LLVLGGGGYTIRNVARCWAYET 313
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 207-375 3.12e-43

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 154.49  E-value: 3.12e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  207 GGRHHAFKQRASGFCYINDVVLLIQRLRKAKLNKITYVDFDLHHGDGVEKAFQYSKQIQTISVHlyEPGFFPGTGSLSDS 286
Cdd:COG0123 120 PPGHHAERDRAMGFCLFNNAAIAARYLLAKGLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIH--QDPLYPGTGAADET 197

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  287 RKDK---NVVNIPLKHGCDDN-YLELIAsKIVNPLIERHEPEALIIECGGDGLLGDRFNEWQLTIRGLSRIIINIMKSYP 362
Cdd:COG0123 198 GEGAgegSNLNVPLPPGTGDAeYLAALE-EALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELAD 276

                       170
                ....*....|....*
gi 6325325  363 RAH--IFLLGGGGYN 375
Cdd:COG0123 277 HCGgpVVSVLEGGYN 291
 
Name Accession Description Interval E-value
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
 5-390 9.02e-160

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: 453.65  E-value: 9.02e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325    5 VISTSIFQSQVADLLPCNNhQKSQLTYSLINAYDLLQHFDEVLTFPYARKDDLLEFHSKSYIDYLINgrfnkmmaqdvnn 84
Cdd:cd11680   1 ILSVSEELTKIADLLPSNK-GRSSLVHSLIRAYGLLQHFDEIIEPERATRKDLTKYHDKDYVDFLLK------------- 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325   85 pmveskwselseladnwnekidynpsqdlqrfttrenlynyylnhsqalennmdcinnsevptndkptdtyilnsetkQY 164
Cdd:cd11680  67 ------------------------------------------------------------------------------KY 68

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  165 NLEGDCPIFSYLPMYCQVITGATLNLLDHLSP-TERLIGINWDGGRHHAFKQRASGFCYINDVVLLIQRLRKAKLNKITY 243
Cdd:cd11680  69 GLEDDCPVFPFLSMYVQLVAGSSLALAKHLITqVERDIAINWYGGRHHAQKSRASGFCYVNDIVLAILRLRRARFRRVFY 148

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  244 VDFDLHHGDGVEKAFQYSKQIQTISVHLYEPGFFPGTGSLsDSRKDKNVVNIPLKHGCDDNYLELIASKIVNPLIERHEP 323
Cdd:cd11680 149 LDLDLHHGDGVESAFFFSKNVLTCSIHRYDPGFFPGTGSL-KNSSDKGMLNIPLKRGLSDKTLLRIIDSIVRPLIEKFEP 227

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6325325  324 EALIIECGGDGLLGDRFNEWQLTIRGLSRIIINIMKSYPRAHIFLLGGGGYNDLLMSRFYTYLTWCV 390
Cdd:cd11680 228 EVIVIQCGCDGLSGDPHKEWNLTIRGYGSVIELLLKEFKDKPTLLLGGGGYNHTEAARAWTYLTSMV 294
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
 23-387 1.38e-77

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: 244.41  E-value: 1.38e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325   23 NHQKSQLTYSLINAYDLLQHFdEVLTFPYARKDDLLEFHSKSYIDYLingrfnkmmaQDVNNpmveskwselselaDNWN 102
Cdd:cd09991  18 KPHRIRMTHSLILSYGLYKKM-EIYRPRPATAEELTKFHSDDYIDFL----------RSVSP--------------DNMK 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  103 EkidynPSQDLQRFttrenlynyylnhsqalennmdcinnsevptndkptdtyilnsetkqyNLEGDCPIFSYLPMYCQV 182
Cdd:cd09991  73 E-----FKKQLERF------------------------------------------------NVGEDCPVFDGLYEYCQL 99

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  183 ITGATLNLLDHLSPTERLIGINWDGGRHHAFKQRASGFCYINDVVLLIQRLRKaKLNKITYVDFDLHHGDGVEKAFQYSK 262
Cdd:cd09991 100 YAGGSIAAAVKLNRGQADIAINWAGGLHHAKKSEASGFCYVNDIVLAILELLK-YHQRVLYIDIDIHHGDGVEEAFYTTD 178

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  263 QIQTISVHLYEPGFFPGTGsLSD--SRKDKN-VVNIPLKHGCDDNYLELIASKIVNPLIERHEPEALIIECGGDGLLGDR 339
Cdd:cd09991 179 RVMTVSFHKFGEYFFPGTG-LRDigAGKGKYyAVNVPLKDGIDDESYLQIFEPVLSKVMEVFQPSAVVLQCGADSLAGDR 257

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 6325325  340 FNEWQLTIRGLSRiIINIMKSYPRAHIfLLGGGGYNDLLMSRFYTYLT 387
Cdd:cd09991 258 LGCFNLSIKGHAK-CVKFVKSFNIPLL-VLGGGGYTLRNVARCWTYET 303
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 26-387 1.51e-70

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: 227.99  E-value: 1.51e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325   26 KSQLTYSLINAYDLLQHFdEVLTFPYARKDDLLEFHSKSYIDYLingrfNKMmaqdvnnpmveskwselseladnwneki 105
Cdd:cd10000  22 RASMVHSLIEAYGLLKQL-RVVKPRVATEEELASFHSDEYIQFL-----KKA---------------------------- 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  106 dyNPSQDlqrfttrenlynyylnhsqalennmdcinnsevptNDKPTDtyilnsETKQYNLEGDCPIFSYLPMYCQVITG 185
Cdd:cd10000  68 --SNEGD-----------------------------------NDEEPS------EQQEFGLGYDCPIFEGIYDYAAAVAG 104

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  186 ATLNLLDHLSPTERLIGINWDGGRHHAFKQRASGFCYINDVVLLIQRLRKaKLNKITYVDFDLHHGDGVEKAFQYSKQIQ 265
Cdd:cd10000 105 ATLTAAQLLIDGKCKVAINWFGGWHHAQRDEASGFCYVNDIVLGILKLRE-KFDRVLYVDLDLHHGDGVEDAFSFTSKVM 183

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  266 TISVHLYEPGFFPGTGSLSDSRKDKN---VVNIPLKHGCDDNYLELIASKIVNPLIERHEPEALIIECGGDGLLGDRFNE 342
Cdd:cd10000 184 TVSLHKYSPGFFPGTGDVSDVGLGKGkyyTVNVPLRDGIQDEQYLQIFTAVVPEIVAAFRPEAVVLQCGADTLAGDPMGA 263

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 6325325  343 WQLTIRGLSRIIINIMK-SYPrahIFLLGGGGYNDLLMSRFYTYLT 387
Cdd:cd10000 264 FNLTPVGIGKCLKYVLGwKLP---TLILGGGGYNLANTARCWTYLT 306
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 23-388 3.19e-68

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: 219.80  E-value: 3.19e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325     23 NHQKSQLTYSLINAYDLLQHFdEVLTFPYARKDDLLEFHSKSYIDYLingrfnkmmaqdvnnpmvESKWSELSELADNWN 102
Cdd:pfam00850   4 NPERLKAILEALREAGLLPDL-EIIAPRPATEEELLLVHSPEYLEFL------------------EEAAPEGGALLLLSY 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325    103 EKIDynpsqdlqrfttrenlynyylnhsqalennmdcinnsevptndkptdtyilnsetkqynleGDCPIFSYLPMYCQV 182
Cdd:pfam00850  65 LSGD-------------------------------------------------------------DDTPVSPGSYEAALL 83

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325    183 ITGATLNLLDHLSPTERLIG--INWdGGRHHAFKQRASGFCYINDVVLLIQRLRKA-KLNKITYVDFDLHHGDGVEKAFQ 259
Cdd:pfam00850  84 AAGGTLAAADAVLSGEARNAfaLVR-PPGHHAERDRASGFCIFNNVAIAAKYLREKyGLKRVAIVDFDVHHGNGTQEIFY 162

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325    260 YSKQIQTISVHLYEPGFFPGTGSLSDSRKDK---NVVNIPLKHGCDDNYLELIASKIVNPLIERHEPEALIIECGGDGLL 336
Cdd:pfam00850 163 DDPSVLTLSIHQYPGGFYPGTGFADETGEGKgkgYTLNVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAGFDAHA 242

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 6325325    337 GDRFNEWQLTIRGLSRIIINIMKSYPRAHIFLL--GGGGYNDLLMSRFYTYLTW 388
Cdd:pfam00850 243 GDPLGGLNLTTEGFAEITRILLELADPLCIRVVsvLEGGYNLDALARSATAVLA 296
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
 160-387 1.03e-56

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: 190.36  E-value: 1.03e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  160 ETKQYNLEGDCPIFSYLPMYCQVITGATLNLLDHLSPTERLIGINWDGGRHHAFKQRASGFCYINDVVLLIQRLRKAkLN 239
Cdd:cd11598  81 KAEPFNIGDDCPVFDGMYDYCQLYAGASLDAARKLCSGQSDIAINWSGGLHHAKKSEASGFCYVNDIVLAILNLLRY-FP 159

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  240 KITYVDFDLHHGDGVEKAFQYSKQIQTISVHLYEPGFFPGTGSLSDSRKDKN---VVNIPLKHGCDDN-YLELIASkIVN 315
Cdd:cd11598 160 RVLYIDIDVHHGDGVEEAFYRTDRVMTLSFHKYNGEFFPGTGDLDDNGGTPGkhfALNVPLEDGIDDEqYNLLFKS-IIG 238

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325325  316 PLIERHEPEALIIECGGDGLLGDRFNEWQLTIRGLSRiIINIMKSYpRAHIFLLGGGGYNDLLMSRFYTYLT 387
Cdd:cd11598 239 PTIEKFQPSAIVLQCGADSLGGDRLGQFNLNIKAHGA-CVKFVKSF-GIPMLVVGGGGYTPRNVARAWCYET 308
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
 183-375 1.36e-49

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: 171.59  E-value: 1.36e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  183 ITGATLNLLDHLSPTERLIGINWDGGRHHAFKQRASGFCYINDVVLLIQRLRKAKLNKITYVDFDLHHGDGVEKAFQYSK 262
Cdd:cd09994 100 VVGGTLLAARLVLEGEARRAFNPAGGLHHAMRGRASGFCVYNDAAVAIERLRDKGGLRVAYVDIDAHHGDGVQAAFYDDP 179

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  263 QIQTISVHLYEPGFFPGTGSLSDSRKDK---NVVNIPL-KHGCDDNYLELIAsKIVNPLIERHEPEALIIECGGDGLLGD 338
Cdd:cd09994 180 RVLTISLHESGRYLFPGTGFVDEIGEGEgygYAVNIPLpPGTGDDEFLRAFE-AVVPPLLRAFRPDVIVSQHGADAHAGD 258

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 6325325  339 RFNEWQLTIRGLSRI---IINIMKSYPRAHIFLLGGGGYN 375
Cdd:cd09994 259 PLTHLNLSNRAYRAAvrrIRELADEYCGGRWLALGGGGYN 298
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
 150-387 2.51e-49

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: 172.94  E-value: 2.51e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  150 KPTDTYILNSETKQYNLEGDCPIFSYLPMYCQVITGATLNLLDHLSPTERLIGINWDGGRHHAFKQRASGFCYINDVVLL 229
Cdd:cd10010  77 RPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSAGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLA 156

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  230 IQRLRKAKlNKITYVDFDLHHGDGVEKAFQYSKQIQTISVHLYEPgFFPGTGSLSDSRKDKN---VVNIPLKHGCDDNYL 306
Cdd:cd10010 157 ILELLKYH-QRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGE-YFPGTGDLRDIGAGKGkyyAVNYPLRDGIDDESY 234

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  307 ELIASKIVNPLIERHEPEALIIECGGDGLLGDRFNEWQLTIRGLSRiIINIMKSYpRAHIFLLGGGGYNDLLMSRFYTYL 386
Cdd:cd10010 235 EAIFKPVMSKVMEMFQPSAVVLQCGADSLSGDRLGCFNLTIKGHAK-CVEFVKSF-NLPMLMLGGGGYTIRNVARCWTYE 312


                .
gi 6325325  387 T 387
Cdd:cd10010 313 T 313
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
 162-396 1.58e-48

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: 170.66  E-value: 1.58e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  162 KQYNLEGDCPIFSYLPMYCQVITGATLNLLDHLSPTERLIGINWDGGRHHAFKQRASGFCYINDVVLLIQRLRKAKlNKI 241
Cdd:cd10005  84 NQFNVGDDCPVFPGLFDFCSMYTGASLEGATKLNHKICDIAINWSGGLHHAKKFEASGFCYVNDIVIAILELLKYH-PRV 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  242 TYVDFDLHHGDGVEKAFQYSKQIQTISVHLYEPGFFPGTGSLSDSRKDKN---VVNIPLKHGCDD-NYLELIaSKIVNPL 317
Cdd:cd10005 163 LYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGryySVNVPLKDGIDDqSYLQLF-KPVIQQV 241

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  318 IERHEPEALIIECGGDGLLGDRFNEWQLTIRGLSRiIINIMKSYpRAHIFLLGGGGYNDLLMSRFYTYLT-WCVTKQFSN 396
Cdd:cd10005 242 IDFYQPTCIVLQCGADSLGCDRLGCFNLSIKGHGE-CVEFVKSF-NIPLLVLGGGGYTVRNVARCWTYETsLLVDEEISN 319
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
 160-387 7.41e-48

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: 168.83  E-value: 7.41e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  160 ETKQYNLEGDCPIFSYLPMYCQVITGATLNLLDHLSPTERLIGINWDGGRHHAFKQRASGFCYINDVVLLIQRLRKAKlN 239
Cdd:cd10004  83 EQVKYNVGDDCPVFDGLFEFCSISAGGSMEGAARLNRGKCDIAVNWAGGLHHAKKSEASGFCYVNDIVLGILELLRYH-Q 161

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  240 KITYVDFDLHHGDGVEKAFQYSKQIQTISVHLYEPgFFPGTGSLSDS--RKDKN-VVNIPLKHGCDDNYLELIASKIVNP 316
Cdd:cd10004 162 RVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYGE-YFPGTGELRDIgiGTGKNyAVNVPLRDGIDDESYKSIFEPVIKH 240

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6325325  317 LIERHEPEALIIECGGDGLLGDRFNEWQLTIRGLSRiIINIMKSYpRAHIFLLGGGGYNDLLMSRFYTYLT 387
Cdd:cd10004 241 VMEWYQPEAVVLQCGGDSLSGDRLGCFNLSMKGHAN-CVNFVKSF-NLPMLVLGGGGYTMRNVARTWAFET 309
PTZ00063 PTZ00063
histone deacetylase; Provisional
 162-387 1.93e-46

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 166.52  E-value: 1.93e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325   162 KQYNL--EGDCPIFSYLPMYCQVITGATLNLLDHLSPTERLIGINWDGGRHHAFKQRASGFCYINDVVLLIQRLRKAKLn 239
Cdd:PTZ00063  87 KRFNVgeATDCPVFDGLFEFQQSCAGASIDGAYKLNNHQADICVNWSGGLHHAKRSEASGFCYINDIVLGILELLKYHA- 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325   240 KITYVDFDLHHGDGVEKAFQYSKQIQTISVHLYEpGFFPGTGSLSD---SRKDKNVVNIPLKHGCDDNYLELIASKIVNP 316
Cdd:PTZ00063 166 RVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKFG-DFFPGTGDVTDigvAQGKYYSVNVPLNDGIDDDSFVDLFKPVISK 244

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325325   317 LIERHEPEALIIECGGDGLLGDRFNEWQLTIRGLSRIIINIMK-SYPrahIFLLGGGGYNDLLMSRFYTYLT 387
Cdd:PTZ00063 245 CVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAACVEFVRSlNIP---LLVLGGGGYTIRNVARCWAYET 313
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
 150-387 8.46e-46

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: 163.31  E-value: 8.46e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  150 KPTDTYILNSETKQYNLEGDCPIFSYLPMYCQVITGATLNLLDHLSPTERLIGINWDGGRHHAFKQRASGFCYINDVVLL 229
Cdd:cd10011  73 RPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLA 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  230 IQRLRKAKlNKITYVDFDLHHGDGVEKAFQYSKQIQTISvHLYEPGFFPGTGSLSDSRKDKN---VVNIPLKHGCDDNYL 306
Cdd:cd10011 153 ILELLKYH-QRVLYIDIDIHHGDGVEEAFYTTDRVMTVS-FHKYGEYFPGTGDLRDIGAGKGkyyAVNFPMRDGIDDESY 230

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  307 ELIASKIVNPLIERHEPEALIIECGGDGLLGDRFNEWQLTIRGLSRiIINIMKSYpRAHIFLLGGGGYNDLLMSRFYTYL 386
Cdd:cd10011 231 GQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAK-CVEVVKTF-NLPLLMLGGGGYTIRNVARCWTYE 308


                .
gi 6325325  387 T 387
Cdd:cd10011 309 T 309
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 207-375 3.12e-43

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 154.49  E-value: 3.12e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  207 GGRHHAFKQRASGFCYINDVVLLIQRLRKAKLNKITYVDFDLHHGDGVEKAFQYSKQIQTISVHlyEPGFFPGTGSLSDS 286
Cdd:COG0123 120 PPGHHAERDRAMGFCLFNNAAIAARYLLAKGLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIH--QDPLYPGTGAADET 197

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  287 RKDK---NVVNIPLKHGCDDN-YLELIAsKIVNPLIERHEPEALIIECGGDGLLGDRFNEWQLTIRGLSRIIINIMKSYP 362
Cdd:COG0123 198 GEGAgegSNLNVPLPPGTGDAeYLAALE-EALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELAD 276

                       170
                ....*....|....*
gi 6325325  363 RAH--IFLLGGGGYN 375
Cdd:COG0123 277 HCGgpVVSVLEGGYN 291
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
 160-390 9.32e-39

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: 141.80  E-value: 9.32e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  160 ETKQYNLEGDCPIFSYLPMYCQVITGATLNLLDHLSPTERLIGINW-DGGRHHAFKQRASGFCYINDVVLLIQRLRKAKL 238
Cdd:cd09301  54 ESKPVIFGPNFPVQRHYFRGARLSTGGVVEAAELVAKGELERAFAVvGAGGHHAGKSRAWGFCYFNDVVLAIKFLRERGI 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  239 NKITYVDFDLHHGDGVEKAFQYSKQIQTISVHLYEPGFFpgtgslsDSRKDKNV-VNIPLKHGCDDN-YLELIaSKIVNP 316
Cdd:cd09301 134 SRILIIDTDAHHGDGTREAFYDDDRVLHMSFHNYDIYPF-------GRGKGKGYkINVPLEDGLGDEeYLDAV-ERVISK 205

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6325325  317 LIERHEPEALIIECGGDGLLGDRFNEWQLTIRGLSRIIINIMKSYPRAHIFLLGGGGYNDLLMSRFYTYlTWCV 390
Cdd:cd09301 206 VLEEFEPEVVVLQFGHDTHEGDRLGGFNLSEKGFVKLAEIVKEFARGGPILMVLGGGYNPEAAARIWTA-IIKE 278
PTZ00346 PTZ00346
histone deacetylase; Provisional
 154-391 1.54e-33

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 131.31  E-value: 1.54e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325   154 TYILNSETKQYNLEGDCPIFSYLPMYCQVITGATLNLLDHLSPTERLIGINWDGGRHHAFKQRASGFCYINDVVLLIQRL 233
Cdd:PTZ00346  98 SWLWNAETSKVFFSGDCPPVEGLMEHSIATASGTLMGAVLLNSGQVDVAVHWGGGMHHSKCGECSGFCYVNDIVLGILEL 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325   234 RKAKlNKITYVDFDLHHGDGVEKAFQYSKQIQTISVHLYEPGFFPGTGSLSD---SRKDKNVVNIPLKHGCDDNYLELIA 310
Cdd:PTZ00346 178 LKCH-DRVLYVDIDMHHGDGVDEAFCTSDRVFTLSLHKFGESFFPGTGHPRDvgyGRGRYYSMNLAVWDGITDFYYLGLF 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325   311 SKIVNPLIERHEPEALIIECGGDGLLGDRFNEWQLTIRGLSRIIINIMK-SYPrahIFLLGGGGYNDLLMSRFYTYLTWC 389
Cdd:PTZ00346 257 EHALHSIVRRYSPDAIVLQCGADSLAGDRLGLLNLSSFGHGQCVQAVRDlGIP---MLALGGGGYTIRNVAKLWAYETSI 333


                 ..
gi 6325325   390 VT 391
Cdd:PTZ00346 334 LT 335
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
 210-375 3.49e-28

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: 113.36  E-value: 3.49e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  210 HHAFKQRASGFCYINDVVLLIQRLRKAK-LNKITYVDFDLHHGDGVEKAFQYSKQIQTISVHLYepGFFPGTGSLSDSRK 288
Cdd:cd09992 105 HHAEPDRAMGFCLFNNVAIAARYAQKRYgLKRVLIVDWDVHHGNGTQDIFYDDPSVLYFSIHQY--PFYPGTGAAEETGG 182

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  289 DK---NVVNIPLKHGCDDN-YLELIaSKIVNPLIERHEPEALIIECGGDGLLGDRFNEWQLTIRG---LSRIIINIMKSY 361
Cdd:cd09992 183 GAgegFTINVPLPPGSGDAeYLAAF-EEVLLPIAREFQPDLVLVSAGFDAHRGDPLGGMNLTPEGyarLTRLLKELADEH 261

                       170
                ....*....|....
gi 6325325  362 PRAHIFLLGGGGYN 375
Cdd:cd09992 262 CGGRLVFVLEGGYN 275
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 198-375 1.85e-27

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: 110.67  E-value: 1.85e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  198 ERLIGINWDGGRHHAFKQRASGFCYINDVVLLIQRLRKAKL-NKITYVDFDLHHGDGVEKAFQYSKQIQTISVHlyEPGF 276
Cdd:cd09993  90 EHGLAINLAGGTHHAFPDRGEGFCVFNDIAIAARVLLAEGLvRRVLIVDLDVHQGNGTAAIFADDPSVFTFSMH--GEKN 167

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  277 FPGTGSLSDsrkdknvVNIPLKHGCDDN-YLELIASkIVNPLIERHEPEALIIECGGDGLLGDRFNEWQLTIRGLS---R 352
Cdd:cd09993 168 YPFRKEPSD-------LDVPLPDGTGDDeYLAALEE-ALPRLLAEFRPDLVFYNAGVDVLAGDRLGRLSLSLEGLRerdR 239

                       170       180
                ....*....|....*....|....*
gi 6325325  353 IIINIMKSY--PrahIFLLGGGGYN 375
Cdd:cd09993 240 LVLRFARARgiP---VAMVLGGGYS 261
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
 210-346 2.14e-22

Histone deacetylases and histone-like deacetylases, classII; This subfamily includes eukaryotic as well as bacterial Class II histone deacetylase (HDAC) and related proteins. Deacetylases of class II are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues of histones (EC 3.5.1.98) and possibly other proteins to yield deacetylated histones/other proteins. In D. discoideum, where four homologs (HdaA, HdaB, HdaC, HdaD) have been identified, HDAC activity is important for regulating the timing of gene expression during development. Also, inhibition of HDAC activity by trichostatin A is shown to cause hyperacetylation of the histone and a delay in cell aggregation and differentiation.


Pssm-ID: 212541 [Multi-domain]  Cd Length: 288  Bit Score: 96.81  E-value: 2.14e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  210 HHAFKQRASGFCYINDV-VLLIQRLRKAKLNKITYVDFDLHHGDGVEKAFQYSKQIQTISVHLYEpgFFPGTGSLSDSRK 288
Cdd:cd11599 106 HHAERDKAMGFCLFNNVaIAAAHALAHHGLERVAIVDFDVHHGNGTEDIFRDDPRVLFCSSHQHP--LYPGTGAPDETGH 183

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6325325  289 DkNVVNIPLKHGCD-DNYLELIASKIVnPLIERHEPEALIIECGGDGLLGDRFNEWQLT 346
Cdd:cd11599 184 G-NIVNVPLPAGTGgAEFREAVEDRWL-PALDAFKPDLILISAGFDAHRDDPLAQLNLT 240
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
 210-353 5.54e-21

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: 92.99  E-value: 5.54e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  210 HHAFKQRASGFCYINDVVLLIQRLRKaKLNKITYVDFDLHHGDGVEKAFQYSKQIQTISVHLYEPGFFPGTGSLSDSR-- 287
Cdd:cd10001 117 HHAGRDRAGGFCYFNNAAIAAQYLRD-RAGRVAILDVDVHHGNGTQEIFYERPDVLYVSIHGDPRTFYPFFLGFADETge 195

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  288 ---KDKNvVNIPLKHGCDDN-YLELIAsKIVNPlIERHEPEALIIECGGDGLLGDRFNEWQLTIRGLSRI 353
Cdd:cd10001 196 gegEGYN-LNLPLPPGTGDDdYLAALD-EALAA-IAAFGPDALVVSLGFDTHEGDPLSDFKLTTEDYARI 262
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 210-337 1.08e-19

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: 90.48  E-value: 1.08e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  210 HHAFKQRASGFCYINDVVLLIQRLR-KAKLNKITYVDFDLHHGDGVEKAFQYSKQIQTISVHLYEPG-FFPGTGSL---- 283
Cdd:cd11681 151 HHAEPSQAMGFCFFNSVAIAAKQLQqKLKLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGnFFPGTGAPtevg 230

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6325325  284 SDSRKDKNvVNIPLKHGCDDN-----YLELIASkIVNPLIERHEPEALIIECGGDGLLG 337
Cdd:cd11681 231 SGAGEGFN-VNIAWSGGLDPPmgdaeYLAAFRT-VVMPIAREFSPDIVLVSAGFDAAEG 287
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 210-375 2.00e-19

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: 88.56  E-value: 2.00e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  210 HHAFKQRASGFCYINDVVL---LIQRLRKAKLNKITYVDFDLHHGDGVEKAFQYSKQIQTISVHLYEPG-FFPGT--GSL 283
Cdd:cd11600 115 HHAEPDESMGFCFFNNVAVaakWLQTEYPDKIKKILILDWDIHHGNGTQRAFYDDPNVLYISLHRFENGgFYPGTpyGDY 194

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  284 SDSRKDKNV---VNIPLKHG--CDDNYLELIaSKIVNPLIERHEPEALIIECGGDGLLGDRFNEWQLTIRGLSRiIINIM 358
Cdd:cd11600 195 ESVGEGAGLgfnVNIPWPQGgmGDADYIYAF-QRIVMPIAYEFDPDLVIISAGFDAADGDELGQCHVTPAGYAH-MTHML 272

                       170
                ....*....|....*..
gi 6325325  359 KSYPRAHIFLLGGGGYN 375
Cdd:cd11600 273 MSLAGGKLVVALEGGYN 289
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
 210-333 4.93e-19

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: 88.39  E-value: 4.93e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  210 HHAFKQRASGFCYINDVVLLIQRLRKA-KLNKITYVDFDLHHGDGVEKAFQYSKQIQTISVHLYEPgFFPGTGSLSDSRK 288
Cdd:cd09996 137 HHAEPDQGMGFCLFNNVAIAARHALAVgGVKRVAVVDWDVHHGNGTQAIFYDDPDVLTISLHQDRC-FPPDSGAVEERGE 215

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 6325325  289 DKNV---VNIPLKHGC-DDNYLELIaSKIVNPLIERHEPEALIIECGGD 333
Cdd:cd09996 216 GAGEgynLNIPLPPGSgDGAYLHAF-ERIVLPALRAFRPELIIVASGFD 263
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 210-375 9.65e-19

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: 86.98  E-value: 9.65e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  210 HHAFKQRASGFCYINDVVLLIQR-LRKAKLNKITYVDFDLHHGDGVEKAFQYSKQIQTISVHLYEPG-FFPGtgsLSDSR 287
Cdd:cd10002 117 HHAMRNEANGYCIFNNVAIAAKYaIEKLGLKRILIVDWDVHHGQGTQQGFYEDPRVLYFSIHRYEHGrFWPH---LFESD 193

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  288 KD--------KNVVNIPL-KHGC-DDNYLElIASKIVNPLIERHEPEALIIECGGDGLLGDRFNEWQLTIRGLSRiIINI 357
Cdd:cd10002 194 YDyigvghgyGFNVNVPLnQTGLgDADYLA-IFHHILLPLALEFQPELVLVSAGFDASIGDPEGEMAVTPAGYAH-LTRL 271

                       170
                ....*....|....*...
gi 6325325  358 MKSYPRAHIFLLGGGGYN 375
Cdd:cd10002 272 LMGLAGGKLLLVLEGGYL 289
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
 210-337 1.07e-15

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: 78.52  E-value: 1.07e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  210 HHAFKQRASGFCYINDVVLLIQRLR-KAKLNKITYVDFDLHHGDGVEKAFQYSKQIQTISVHLYEPG-FFPGTGS---LS 284
Cdd:cd10009 152 HHAEESTAMGFCFFNSVAITAKYLRdQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGnFFPGSGApneVG 231

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6325325  285 DSRKDKNVVNIPLKHGCDD-----NYLELIASkIVNPLIERHEPEALIIECGGDGLLG 337
Cdd:cd10009 232 TGLGEGYNINIAWTGGLDPpmgdvEYLEAFRT-IVKPVAKEFDPDMVLVSAGFDALEG 288
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
 210-337 2.66e-15

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: 77.38  E-value: 2.66e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  210 HHAFKQRASGFCYINDVV----LLIQRLrkaKLNKITYVDFDLHHGDGVEKAFQYSKQIQTISVHLYEPG-FFPGTGSLS 284
Cdd:cd10006 154 HHAEESTPMGFCYFNSVAiaakLLQQRL---NVSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYDDGnFFPGSGAPD 230

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6325325  285 DSRKDKNV---VNIPLKHGC-----DDNYLELIASkIVNPLIERHEPEALIIECGGDGLLG 337
Cdd:cd10006 231 EVGTGPGVgfnVNMAFTGGLdppmgDAEYLAAFRT-VVMPIASEFAPDVVLVSSGFDAVEG 290
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
 210-337 3.31e-15

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: 77.33  E-value: 3.31e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  210 HHAFKQRASGFCYINDVVLLIQRLR-KAKLNKITYVDFDLHHGDGVEKAFQYSKQIQTISVHLYEPG-FFPGTGSLSDSR 287
Cdd:cd10007 154 HHAEESTAMGFCFFNSVAIAAKLLQqKLNVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGnFFPGSGAPDEVG 233

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6325325  288 KDKNV---VNIPLKHGCDD-----NYLELIASkIVNPLIERHEPEALIIECGGDGLLG 337
Cdd:cd10007 234 AGPGVgfnVNIAWTGGVDPpigdvEYLTAFRT-VVMPIANEFSPDVVLVSAGFDAVEG 290
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
 210-337 2.49e-14

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: 74.28  E-value: 2.49e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  210 HHAFKQRASGFCYINDVVLLIQRLR-KAKLNKITYVDFDLHHGDGVEKAFQYSKQIQTISVHLYEPG-FFPGTGSLSD-- 285
Cdd:cd10008 152 HHADHSTAMGFCFFNSVAIACRQLQqQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGnFFPGSGAVDEvg 231

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6325325  286 -SRKDKNVVNIPLKHGCDD-----NYLELIASkIVNPLIERHEPEALIIECGGDGLLG 337
Cdd:cd10008 232 aGSGEGFNVNVAWAGGLDPpmgdpEYLAAFRI-VVMPIAREFSPDLVLVSAGFDAAEG 288
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
 210-375 1.48e-13

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: 71.60  E-value: 1.48e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  210 HHAFKQRASGFCYINDVVLLIQ-RLRKAKLNKITYVDFDLHHGDGVEKAFQYSKQIQTISVHLYEPG-FFPGT--GSLSD 285
Cdd:cd10003 126 HHAEQDTACGFCFFNNVAIAARyAQKKYGLKRILIVDWDVHHGNGTQHMFESDPSVLYISLHRYDNGsFFPNSpeGNYDV 205

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  286 SRKDKN---VVNIP--LKHGCDDNYLeLIASKIVNPLIERHEPEALIIECGGDGLLGDRFNEWQLTIRGLSRiIINIMKS 360
Cdd:cd10003 206 VGKGKGegfNVNIPwnKGGMGDAEYI-AAFQQVVLPIAYEFNPELVLVSAGFDAARGDPLGGCKVTPEGYAH-MTHMLMS 283

                       170
                ....*....|....*
gi 6325325  361 YPRAHIFLLGGGGYN 375
Cdd:cd10003 284 LAGGRVIVILEGGYN 298
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
 210-375 5.94e-10

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: 60.64  E-value: 5.94e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  210 HHAFKQRASGFCYINDVVLLIQRLR-KAKLNKITYVDFDLHHGDGVEKAFQYSKQIQTISVHLYEPG-FFP-----GTGS 282
Cdd:cd11682 117 HHAQHDKMDGYCMFNNVAIAARYAQqKHGVQRVLIVDWDVHHGQGTQFIFEQDPSVLYFSIHRYEQGrFWPhlkesDSSA 196

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  283 LSDSRKDKNVVNIPL-KHGCDD-NYLELIAsKIVNPLIERHEPEALIIECGGDGLLGDRFNEWQLTIRGLSrIIINIMKS 360
Cdd:cd11682 197 VGFGRGEGYNINVPWnQVGMRDaDYIAAFL-HVLLPVALEFQPQLVLVAAGFDAVIGDPKGEMAATPACFA-HLTHLLMG 274

                       170
                ....*....|....*
gi 6325325  361 YPRAHIFLLGGGGYN 375
Cdd:cd11682 275 LAGGKLILSLEGGYN 289
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 210-338 6.11e-08

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: 54.48  E-value: 6.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  210 HHAFKQRASGFCYINDVVLLIQRLR-KAKLNKITYVDFDLHHGDGVEKAFQYSKQIQTISVHLYEPG-FFPgtgSLSDSR 287
Cdd:cd11683 117 HHSQRNAANGFCVFNNVAIAAEYAKkKYGLHRILIVDWDVHHGQGIQYIFEEDPSVLYFSWHRYEHQrFWP---FLRESD 193

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325325  288 KDKN--------VVNIPLKHGCDDNYLELIA-SKIVNPLIERHEPEALIIECGGDGLLGD 338
Cdd:cd11683 194 YDAVgrgkglgfNINLPWNKVGMGNADYLAAfFHVLLPLAFEFDPELVLVSAGFDSAIGD 253
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
 210-253 3.35e-05

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: 45.91  E-value: 3.35e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 6325325  210 HHAFKQRASGFCYINDVVLLIQR-LRKAKLNKITYVDFDLHHGDG 253
Cdd:cd09998 120 HHCSESTPSGFCWVNNVHVGAAHaYLTHGITRVVILDIDLHHGNG 164
 
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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