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Conserved domains on  [gi|281360799|ref|NP_572868|]
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histone deacetylase 4, isoform D [Drosophila melanogaster]

Protein Classification

histone deacetylase( domain architecture ID 11731087)

class IIa histone deacetylase is a Zn-dependent enzyme that catalyzes hydrolysis of N(6)-acetyl-lysine residues of histones (EC 3.5.1.98) to yield deacetylated histones; similar to Drosophila melanogaster histone deacetylase dHDAC4, which is involved in segmentation of the Drosophila embryo and is regulated by gap and pair-rule genes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 820-1194 0e+00

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: 762.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  820 VTTGLAYDPLMLKHSCICGDNAQHPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAHAMLFGSNQcqLS 899
Cdd:cd11681     1 FTTGLAYDPLMLKHQCICGNNSSHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTLLYGTNP--LS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  900 RPKLENTLSA-----SFVRLSCGGLGVDLDTTWNEHHTATAARMAAGCVIDLALKTAKGDLRNGFAVVRPPGHHAEANLA 974
Cdd:cd11681    79 RLKLDPTKLAglpqkSFVRLPCGGIGVDSDTVWNELHTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  975 MGFCFFNSIAIAAKLLRQRMPeVRRILIVDWDVHHGNGTQQAFYQSPDILYLSIHRHDDGNFFPGTGGPTECGSGAGLGF 1054
Cdd:cd11681   159 MGFCFFNSVAIAAKQLQQKLK-LRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFPGTGAPTEVGSGAGEGF 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1055 NVNISWSGALNPPLGDAEYIAAFRTVVMPIARSFNPDIVLVSSGFDAATGHPAPLGGYHVSPACFGFMTRELLQLANGKV 1134
Cdd:cd11681   238 NVNIAWSGGLDPPMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPPPLGGYKVSPACFGYMTRQLMNLAGGKV 317

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1135 VLALEGGYDLAAICDSAQECVRALLGDPAAPIAKAELERPPCQNAINTLQKTIAIQQTHW 1194
Cdd:cd11681   318 VLALEGGYDLTAICDASEACVRALLGDELDPLSEEELERRPNPNAVTSLEKVIAIQSPYW 377
ClassIIa_HDAC_Gln-rich-N super family cl25407
Glutamine-rich N-terminal helical domain of various Class IIa histone deacetylases (HDAC4, ...
 43-97 2.47e-04

Glutamine-rich N-terminal helical domain of various Class IIa histone deacetylases (HDAC4, HDAC5 and HDCA9); This superfamily consists of a glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDAC9; it is missing in HDAC7. It is referred to as the glutamine-rich domain, and confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors. This domain is able to repress transcription independently of the HDAC's C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues.


The actual alignment was detected with superfamily member cd10164:

Pssm-ID: 421006 [Multi-domain]  Cd Length: 97  Bit Score: 41.35  E-value: 2.47e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 281360799   43 IDQQIMELKKSQELQKQRLINSFQEQSKQMELEHKLQLEH--KYQFAVNSHGAFQEL 97
Cdd:cd10164     9 LQQELLLLKQQQQLQKQLLFAEFQKQHEHLTRQHEVQLQKhlKVRAELFSEQQQQEI 65
 
Name Accession Description Interval E-value
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 820-1194 0e+00

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: 762.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  820 VTTGLAYDPLMLKHSCICGDNAQHPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAHAMLFGSNQcqLS 899
Cdd:cd11681     1 FTTGLAYDPLMLKHQCICGNNSSHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTLLYGTNP--LS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  900 RPKLENTLSA-----SFVRLSCGGLGVDLDTTWNEHHTATAARMAAGCVIDLALKTAKGDLRNGFAVVRPPGHHAEANLA 974
Cdd:cd11681    79 RLKLDPTKLAglpqkSFVRLPCGGIGVDSDTVWNELHTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  975 MGFCFFNSIAIAAKLLRQRMPeVRRILIVDWDVHHGNGTQQAFYQSPDILYLSIHRHDDGNFFPGTGGPTECGSGAGLGF 1054
Cdd:cd11681   159 MGFCFFNSVAIAAKQLQQKLK-LRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFPGTGAPTEVGSGAGEGF 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1055 NVNISWSGALNPPLGDAEYIAAFRTVVMPIARSFNPDIVLVSSGFDAATGHPAPLGGYHVSPACFGFMTRELLQLANGKV 1134
Cdd:cd11681   238 NVNIAWSGGLDPPMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPPPLGGYKVSPACFGYMTRQLMNLAGGKV 317

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1135 VLALEGGYDLAAICDSAQECVRALLGDPAAPIAKAELERPPCQNAINTLQKTIAIQQTHW 1194
Cdd:cd11681   318 VLALEGGYDLTAICDASEACVRALLGDELDPLSEEELERRPNPNAVTSLEKVIAIQSPYW 377
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 843-1158 2.47e-117

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: 366.95  E-value: 2.47e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799   843 HPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAHAMLfgsnqcqlsrpkLENTLSASFVRLSCGGLGVD 922
Cdd:pfam00850    1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEF------------LEEAAPEGGALLLLSYLSGD 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799   923 LDTtWNEHHTATAARMAAGCVIDLALKTAKGDLRNGFAVVRPPGHHAEANLAMGFCFFNSIAIAAKLLRQRMpEVRRILI 1002
Cdd:pfam00850   69 DDT-PVSPGSYEAALLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKY-GLKRVAI 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  1003 VDWDVHHGNGTQQAFYQSPDILYLSIHRHdDGNFFPGTGGPTECGSGAGLGFNVNIswsgALNPPLGDAEYIAAFRTVVM 1082
Cdd:pfam00850  147 VDFDVHHGNGTQEIFYDDPSVLTLSIHQY-PGGFYPGTGFADETGEGKGKGYTLNV----PLPPGTGDAEYLAAFEEILL 221

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281360799  1083 PIARSFNPDIVLVSSGFDAATGHpaPLGGYHVSPACFGFMTRELLQLA---NGKVVLALEGGYDLAAICDSAQECVRAL 1158
Cdd:pfam00850  222 PALEEFQPDLILVSAGFDAHAGD--PLGGLNLTTEGFAEITRILLELAdplCIRVVSVLEGGYNLDALARSATAVLAAL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 822-1160 3.56e-103

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 328.99  E-value: 3.56e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  822 TGLAYDPLMLKHSCicGDNaqHPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAH-AMLFgsnqcqlsr 900
Cdd:COG0123     1 TALIYHPDYLLHDL--GPG--HPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYvDALR--------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  901 pklENTLSASFVRLscgglgvDLDTTWNEHhTATAARMAAGCVIDLALKTAKGDLRNGFAVVRPPGHHAEANLAMGFCFF 980
Cdd:COG0123    68 ---AASLDGGYGQL-------DPDTPVSPG-TWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGFCLF 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  981 NSIAIAAKLLRQRmpEVRRILIVDWDVHHGNGTQQAFYQSPDILYLSIHRHddgNFFPGTGGPTECGSGAGLGFNVNIsw 1060
Cdd:COG0123   137 NNAAIAARYLLAK--GLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD---PLYPGTGAADETGEGAGEGSNLNV-- 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1061 sgALNPPLGDAEYIAAFRTVVMPIARSFNPDIVLVSSGFDAATGHpaPLGGYHVSPACFGFMTRELLQLA---NGKVVLA 1137
Cdd:COG0123   210 --PLPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHADD--PLGRLNLTTEGYAWRTRRVLELAdhcGGPVVSV 285

                         330       340
                  ....*....|....*....|...
gi 281360799 1138 LEGGYDLAAICDSAQECVRALLG 1160
Cdd:COG0123   286 LEGGYNLDALARSVAAHLETLLG 308
PTZ00063 PTZ00063
histone deacetylase; Provisional
 843-1104 2.17e-20

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 95.65  E-value: 2.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  843 HPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAHAMLFGS---NQC-----QLSRPKL-ENTLSASFVR 913
Cdd:PTZ00063   23 HPMKPQRIRMAHALILSYDLYKHMEIYRPHKSVEPELVLFHDEEYVDFLSSispENYrdftyQLKRFNVgEATDCPVFDG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  914 L-----SCGGLGVDLDTTWNEHHTATAARMAAGCvidlalktakgdlrngfavvrppgHHAEANLAMGFCFFNSIAIAA- 987
Cdd:PTZ00063  103 LfefqqSCAGASIDGAYKLNNHQADICVNWSGGL------------------------HHAKRSEASGFCYINDIVLGIl 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  988 KLLRQRMpevrRILIVDWDVHHGNGTQQAFYQSPDILYLSIHRHddGNFFPGTGGPTECGSGAGLGFNVNIswsgALNPP 1067
Cdd:PTZ00063  159 ELLKYHA----RVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFPGTGDVTDIGVAQGKYYSVNV----PLNDG 228

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 281360799 1068 LGDAEYIAAFRTVVMPIARSFNPDIVLVSSGFDAATG 1104
Cdd:PTZ00063  229 IDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTG 265
ClassIIa_HDAC5_Gln-rich-N cd10164
Glutamine-rich N-terminal helical domain of HDAC5, a Class IIa histone deacetylase; This ...
 43-97 2.47e-04

Glutamine-rich N-terminal helical domain of HDAC5, a Class IIa histone deacetylase; This family consists of the glutamine-rich domain of histone deacetylase 5 (HDAC5). It belongs to a superfamily that consists of the glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDCA9; it is missing from HDAC7. This domain confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors, and it is able to repress transcription independently of the HDAC C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues.


Pssm-ID: 197400 [Multi-domain]  Cd Length: 97  Bit Score: 41.35  E-value: 2.47e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 281360799   43 IDQQIMELKKSQELQKQRLINSFQEQSKQMELEHKLQLEH--KYQFAVNSHGAFQEL 97
Cdd:cd10164     9 LQQELLLLKQQQQLQKQLLFAEFQKQHEHLTRQHEVQLQKhlKVRAELFSEQQQQEI 65
 
Name Accession Description Interval E-value
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 820-1194 0e+00

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: 762.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  820 VTTGLAYDPLMLKHSCICGDNAQHPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAHAMLFGSNQcqLS 899
Cdd:cd11681     1 FTTGLAYDPLMLKHQCICGNNSSHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTLLYGTNP--LS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  900 RPKLENTLSA-----SFVRLSCGGLGVDLDTTWNEHHTATAARMAAGCVIDLALKTAKGDLRNGFAVVRPPGHHAEANLA 974
Cdd:cd11681    79 RLKLDPTKLAglpqkSFVRLPCGGIGVDSDTVWNELHTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  975 MGFCFFNSIAIAAKLLRQRMPeVRRILIVDWDVHHGNGTQQAFYQSPDILYLSIHRHDDGNFFPGTGGPTECGSGAGLGF 1054
Cdd:cd11681   159 MGFCFFNSVAIAAKQLQQKLK-LRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFPGTGAPTEVGSGAGEGF 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1055 NVNISWSGALNPPLGDAEYIAAFRTVVMPIARSFNPDIVLVSSGFDAATGHPAPLGGYHVSPACFGFMTRELLQLANGKV 1134
Cdd:cd11681   238 NVNIAWSGGLDPPMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPPPLGGYKVSPACFGYMTRQLMNLAGGKV 317

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1135 VLALEGGYDLAAICDSAQECVRALLGDPAAPIAKAELERPPCQNAINTLQKTIAIQQTHW 1194
Cdd:cd11681   318 VLALEGGYDLTAICDASEACVRALLGDELDPLSEEELERRPNPNAVTSLEKVIAIQSPYW 377
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
 819-1222 0e+00

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: 607.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  819 KVTTGLAYDPLMLKHSCICGDNAQHPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAHAMLFGSNQcqL 898
Cdd:cd10006     3 RFTTGLVYDTLMLKHQCTCGNSNSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNP--L 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  899 SRPKLEN-----TLSASFVRLSCGGLGVDLDTTWNEHHTATAARMAAGCVIDLALKTAKGDLRNGFAVVRPPGHHAEANL 973
Cdd:cd10006    81 NRQKLDSkkllgSLASVFVRLPCGGVGVDSDTIWNEVHSSGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEEST 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  974 AMGFCFFNSIAIAAKLLRQRMpEVRRILIVDWDVHHGNGTQQAFYQSPDILYLSIHRHDDGNFFPGTGGPTECGSGAGLG 1053
Cdd:cd10006   161 PMGFCYFNSVAIAAKLLQQRL-NVSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1054 FNVNISWSGALNPPLGDAEYIAAFRTVVMPIARSFNPDIVLVSSGFDAATGHPAPLGGYHVSPACFGFMTRELLQLANGK 1133
Cdd:cd10006   240 FNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSAKCFGYLTKQLMGLAGGR 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1134 VVLALEGGYDLAAICDSAQECVRALLGDPAAPIAKAELERPPCQNAINTLQKTIAIQQTHWPCVRMLEHTVGLSALETLK 1213
Cdd:cd10006   320 IVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGYSLIEAQT 399


                  ....*....
gi 281360799 1214 VEHDESETI 1222
Cdd:cd10006   400 CENEEAETV 408
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
 818-1232 0e+00

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: 603.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  818 HKVTTGLAYDPLMLKHSCICGDNAQHPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAHAMLFGS---N 894
Cdd:cd10007     1 HLFTTGLVYDTFMLKHQCTCGNTNVHPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHSEHHTLLYGTsplN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  895 QCQLSRPKLENTLSAS-FVRLSCGGLGVDLDTTWNEHHTATAARMAAGCVIDLALKTAKGDLRNGFAVVRPPGHHAEANL 973
Cdd:cd10007    81 RQKLDSKKLLGPLSQKmYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLIELAFKVAAGELKNGFAVIRPPGHHAEEST 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  974 AMGFCFFNSIAIAAKLLRQRMpEVRRILIVDWDVHHGNGTQQAFYQSPDILYLSIHRHDDGNFFPGTGGPTECGSGAGLG 1053
Cdd:cd10007   161 AMGFCFFNSVAIAAKLLQQKL-NVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGNFFPGSGAPDEVGAGPGVG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1054 FNVNISWSGALNPPLGDAEYIAAFRTVVMPIARSFNPDIVLVSSGFDAATGHPAPLGGYHVSPACFGFMTRELLQLANGK 1133
Cdd:cd10007   240 FNVNIAWTGGVDPPIGDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGHQSPLGGYSVTAKCFGHLTKQLMTLAGGR 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1134 VVLALEGGYDLAAICDSAQECVRALLGDPAAPIAKAELERPPCQNAINTLQKTIAIQQTHWPCVRMLEHTVGLSALETLK 1213
Cdd:cd10007   320 VVLALEGGHDLTAICDASEACVSALLGMELTPLDNTVLQQKPNDNAVATLERVIEIQSKHWSCLKRFAATLGFSLLEAQR 399

                         410
                  ....*....|....*....
gi 281360799 1214 VEHDESETINAMAGLSMQS 1232
Cdd:cd10007   400 GELEEAETVSAMASLSVDT 418
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
 821-1194 0e+00

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: 575.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  821 TTGLAYDPLMLKHSCICGDNAQHPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAHAMLFGSNQcqLSR 900
Cdd:cd10008     2 TTGLVYDSVMLKHQCSCGDNSNHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNP--LSR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  901 PKLENTLSAS------FVRLSCGGLGVDLDTTWNEHHTATAARMAAGCVIDLALKTAKGDLRNGFAVVRPPGHHAEANLA 974
Cdd:cd10008    80 LKLDNGKLAGllaqrmFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  975 MGFCFFNSIAIAAKLLRQRmPEVRRILIVDWDVHHGNGTQQAFYQSPDILYLSIHRHDDGNFFPGTGGPTECGSGAGLGF 1054
Cdd:cd10008   160 MGFCFFNSVAIACRQLQQQ-GKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGAGSGEGF 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1055 NVNISWSGALNPPLGDAEYIAAFRTVVMPIARSFNPDIVLVSSGFDAATGHPAPLGGYHVSPACFGFMTRELLQLANGKV 1134
Cdd:cd10008   239 NVNVAWAGGLDPPMGDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAV 318

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1135 VLALEGGYDLAAICDSAQECVRALLGDPAAPIAKAELERPPCQNAINTLQKTIAIQQTHW 1194
Cdd:cd10008   319 VLALEGGHDLTAICDASEACVAALLGNEVDPLSEESWKQKPNLNAIRSLEAVIRVHSKYW 378
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
 821-1194 9.19e-170

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: 508.02  E-value: 9.19e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  821 TTGLAYDPLMLKHSCICGDNAQHPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAHAMLFGSNQcqLSR 900
Cdd:cd10009     2 ATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNP--LDG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  901 PKLE------NTLSASFVRLSCGGLGVDLDTTWNEHHTATAARMAAGCVIDLALKTAKGDLRNGFAVVRPPGHHAEANLA 974
Cdd:cd10009    80 QKLDprillgDDSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  975 MGFCFFNSIAIAAKLLRQRMpEVRRILIVDWDVHHGNGTQQAFYQSPDILYLSIHRHDDGNFFPGTGGPTECGSGAGLGF 1054
Cdd:cd10009   160 MGFCFFNSVAITAKYLRDQL-NISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGY 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1055 NVNISWSGALNPPLGDAEYIAAFRTVVMPIARSFNPDIVLVSSGFDAATGHPAPLGGYHVSPACFGFMTRELLQLANGKV 1134
Cdd:cd10009   239 NINIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRV 318

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1135 VLALEGGYDLAAICDSAQECVRALLGDPAAPIAKAELERPPCQNAINTLQKTIAIQQTHW 1194
Cdd:cd10009   319 VLALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSKYW 378
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
 826-1198 1.17e-131

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: 407.11  E-value: 1.17e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  826 YDPLMLKHSCICgdNAQHPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAHAmlfgsnqcqlsrPKLEN 905
Cdd:cd10003     1 YDQRMMNHHNLW--DPGHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHL------------DEMKS 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  906 TLSASFVRLscGGLGVDLDTTWNEHHTATAARMAAGCVIDLALKTAKGDLRNGFAVVRPPGHHAEANLAMGFCFFNSIAI 985
Cdd:cd10003    67 LEKMKPREL--NRLGKEYDSIYIHPDSYQCALLAAGCVLQVVEAVLTGESRNGVAIVRPPGHHAEQDTACGFCFFNNVAI 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  986 AAKLLRQRMpEVRRILIVDWDVHHGNGTQQAFYQSPDILYLSIHRHDDGNFFPGT--GGPTECGSGAGLGFNVNISWSGa 1063
Cdd:cd10003   145 AARYAQKKY-GLKRILIVDWDVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSpeGNYDVVGKGKGEGFNVNIPWNK- 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1064 lnPPLGDAEYIAAFRTVVMPIARSFNPDIVLVSSGFDAATGHpaPLGGYHVSPACFGFMTRELLQLANGKVVLALEGGYD 1143
Cdd:cd10003   223 --GGMGDAEYIAAFQQVVLPIAYEFNPELVLVSAGFDAARGD--PLGGCKVTPEGYAHMTHMLMSLAGGRVIVILEGGYN 298

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 281360799 1144 LAAICDSAQECVRALLGDPAAPIakaELERPPCQNAINTLQKTIAIQQTHWPCVR 1198
Cdd:cd10003   299 LTSISESMSMCTKTLLGDPPPVL---DLPRPPCSSALKSINNVLQVHQKYWKSLR 350
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 842-1162 1.20e-128

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: 397.49  E-value: 1.20e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  842 QHPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAHaMLFGSNQCQLSRPKLENtLSASFVRLScggLGV 921
Cdd:cd11600     2 PHPEDPSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEH-WDRVEATEKMSDEQLKD-RTEIFERDS---LYV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  922 DldttwneHHTATAARMAAGCVIDLALKTAKGDLRNGFAVVRPPGHHAEANLAMGFCFFNSIAIAAKLLRQRMPE-VRRI 1000
Cdd:cd11600    77 N-------NDTAFCARLSCGGAIEACRAVAEGRVKNAFAVVRPPGHHAEPDESMGFCFFNNVAVAAKWLQTEYPDkIKKI 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1001 LIVDWDVHHGNGTQQAFYQSPDILYLSIHRHDDGNFFPGT--GGPTECGSGAGLGFNVNISWSgalNPPLGDAEYIAAFR 1078
Cdd:cd11600   150 LILDWDIHHGNGTQRAFYDDPNVLYISLHRFENGGFYPGTpyGDYESVGEGAGLGFNVNIPWP---QGGMGDADYIYAFQ 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1079 TVVMPIARSFNPDIVLVSSGFDAATGHpaPLGGYHVSPACFGFMTRELLQLANGKVVLALEGGYDLAAICDSAQECVRAL 1158
Cdd:cd11600   227 RIVMPIAYEFDPDLVIISAGFDAADGD--ELGQCHVTPAGYAHMTHMLMSLAGGKLVVALEGGYNLDAISDSALAVAKVL 304


                  ....
gi 281360799 1159 LGDP 1162
Cdd:cd11600   305 LGEA 308
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
 843-1159 1.12e-127

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: 394.17  E-value: 1.12e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  843 HPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAHAMLFGsnqcqlsrpklentlsasfvRLSCGGLGVD 922
Cdd:cd09992     1 HPERPERLLAILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYIERVE--------------------ETCEAGGGYL 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  923 LDTTWNEHHTATAARMAAGCVIDLALKTAKGDLRNGFAVVRPPGHHAEANLAMGFCFFNSIAIAAKLLRQRmPEVRRILI 1002
Cdd:cd09992    61 DPDTYVSPGSYEAALLAAGAALAAVDAVLSGEAENAFALVRPPGHHAEPDRAMGFCLFNNVAIAARYAQKR-YGLKRVLI 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1003 VDWDVHHGNGTQQAFYQSPDILYLSIHRHDdgnFFPGTGGPTECGSGAGLGFNVNIswsgALNPPLGDAEYIAAFRTVVM 1082
Cdd:cd09992   140 VDWDVHHGNGTQDIFYDDPSVLYFSIHQYP---FYPGTGAAEETGGGAGEGFTINV----PLPPGSGDAEYLAAFEEVLL 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1083 PIARSFNPDIVLVSSGFDAATGHpaPLGGYHVSPACFGFMTRELLQLA----NGKVVLALEGGYDLAAICDSAQECVRAL 1158
Cdd:cd09992   213 PIAREFQPDLVLVSAGFDAHRGD--PLGGMNLTPEGYARLTRLLKELAdehcGGRLVFVLEGGYNLEALAESVLAVLEAL 290


                  .
gi 281360799 1159 L 1159
Cdd:cd09992   291 L 291
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 843-1158 2.47e-117

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: 366.95  E-value: 2.47e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799   843 HPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAHAMLfgsnqcqlsrpkLENTLSASFVRLSCGGLGVD 922
Cdd:pfam00850    1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEF------------LEEAAPEGGALLLLSYLSGD 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799   923 LDTtWNEHHTATAARMAAGCVIDLALKTAKGDLRNGFAVVRPPGHHAEANLAMGFCFFNSIAIAAKLLRQRMpEVRRILI 1002
Cdd:pfam00850   69 DDT-PVSPGSYEAALLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKY-GLKRVAI 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  1003 VDWDVHHGNGTQQAFYQSPDILYLSIHRHdDGNFFPGTGGPTECGSGAGLGFNVNIswsgALNPPLGDAEYIAAFRTVVM 1082
Cdd:pfam00850  147 VDFDVHHGNGTQEIFYDDPSVLTLSIHQY-PGGFYPGTGFADETGEGKGKGYTLNV----PLPPGTGDAEYLAAFEEILL 221

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281360799  1083 PIARSFNPDIVLVSSGFDAATGHpaPLGGYHVSPACFGFMTRELLQLA---NGKVVLALEGGYDLAAICDSAQECVRAL 1158
Cdd:pfam00850  222 PALEEFQPDLILVSAGFDAHAGD--PLGGLNLTTEGFAEITRILLELAdplCIRVVSVLEGGYNLDALARSATAVLAAL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 822-1160 3.56e-103

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 328.99  E-value: 3.56e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  822 TGLAYDPLMLKHSCicGDNaqHPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAH-AMLFgsnqcqlsr 900
Cdd:COG0123     1 TALIYHPDYLLHDL--GPG--HPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYvDALR--------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  901 pklENTLSASFVRLscgglgvDLDTTWNEHhTATAARMAAGCVIDLALKTAKGDLRNGFAVVRPPGHHAEANLAMGFCFF 980
Cdd:COG0123    68 ---AASLDGGYGQL-------DPDTPVSPG-TWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGFCLF 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  981 NSIAIAAKLLRQRmpEVRRILIVDWDVHHGNGTQQAFYQSPDILYLSIHRHddgNFFPGTGGPTECGSGAGLGFNVNIsw 1060
Cdd:COG0123   137 NNAAIAARYLLAK--GLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD---PLYPGTGAADETGEGAGEGSNLNV-- 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1061 sgALNPPLGDAEYIAAFRTVVMPIARSFNPDIVLVSSGFDAATGHpaPLGGYHVSPACFGFMTRELLQLA---NGKVVLA 1137
Cdd:COG0123   210 --PLPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHADD--PLGRLNLTTEGYAWRTRRVLELAdhcGGPVVSV 285

                         330       340
                  ....*....|....*....|...
gi 281360799 1138 LEGGYDLAAICDSAQECVRALLG 1160
Cdd:COG0123   286 LEGGYNLDALARSVAAHLETLLG 308
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 837-1194 1.28e-101

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: 326.19  E-value: 1.28e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  837 CGDNAQHPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAH----AMLFGSNQCQLsrpkleNTLSASFv 912
Cdd:cd10002     1 CNWDSNHIECPERLEAILERLTQDGLLERCVKIPAREAEEDEILLVHSQEYidlvKSTETMEKEEL------ESLCSGY- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  913 rlscgglgvdlDTTWNEHHTATAARMAAGCVIDLALKTAKGDLRNGFAVVRPPGHHAEANLAMGFCFFNSIAIAAKLLRQ 992
Cdd:cd10002    74 -----------DSVYLCPSTYEAARLAAGSTIELVKAVMAGKIQNGFALIRPPGHHAMRNEANGYCIFNNVAIAAKYAIE 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  993 RMpEVRRILIVDWDVHHGNGTQQAFYQSPDILYLSIHRHDDGNFFPGTGGPT--ECGSGAGLGFNVNISWSGALnppLGD 1070
Cdd:cd10002   143 KL-GLKRILIVDWDVHHGQGTQQGFYEDPRVLYFSIHRYEHGRFWPHLFESDydYIGVGHGYGFNVNVPLNQTG---LGD 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1071 AEYIAAFRTVVMPIARSFNPDIVLVSSGFDAATGhpAPLGGYHVSPACFGFMTRELLQLANGKVVLALEGGYDLAAICDS 1150
Cdd:cd10002   219 ADYLAIFHHILLPLALEFQPELVLVSAGFDASIG--DPEGEMAVTPAGYAHLTRLLMGLAGGKLLLVLEGGYLLESLAES 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 281360799 1151 AQECVRALLGDPAAPIAKAElerpPCQNAINTLQKTIAIQQTHW 1194
Cdd:cd10002   297 VSMTLRGLLGDPLPPLAPPI----PIRSVLETILNAIAHLSPRW 336
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
 837-1194 2.87e-82

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: 272.88  E-value: 2.87e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  837 CGDNAQHPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAHAMLFGSNQcQLSRPKLEnTLSASFvrlsc 916
Cdd:cd11682     1 CLWDESFPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYVALMKSTQ-YMTEEELR-TLADTY----- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  917 gglgvdlDTTWNEHHTATAARMAAGCVIDLALKTAKGDLRNGFAVVRPPGHHAEANLAMGFCFFNSIAIAAKLLRQRMpE 996
Cdd:cd11682    74 -------DSVYLHPNSYSCACLAVGSVLQLVDKVLGGEIRNGLAIVRPPGHHAQHDKMDGYCMFNNVAIAARYAQQKH-G 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  997 VRRILIVDWDVHHGNGTQQAFYQSPDILYLSIHRHDDGNFFP--GTGGPTECGSGAGLGFNVNISWSGAlnpPLGDAEYI 1074
Cdd:cd11682   146 VQRVLIVDWDVHHGQGTQFIFEQDPSVLYFSIHRYEQGRFWPhlKESDSSAVGFGRGEGYNINVPWNQV---GMRDADYI 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1075 AAFRTVVMPIARSFNPDIVLVSSGFDAATGHPAplGGYHVSPACFGFMTRELLQLANGKVVLALEGGYDLAAICDSAQEC 1154
Cdd:cd11682   223 AAFLHVLLPVALEFQPQLVLVAAGFDAVIGDPK--GEMAATPACFAHLTHLLMGLAGGKLILSLEGGYNLRSLAEGVCAS 300

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 281360799 1155 VRALLGDPAAPIakaELERPPCQNAINTLQKTIAIQQTHW 1194
Cdd:cd11682   301 LKALLGDPCPML---ESPGAPCRSALASVSCTISALEPFW 337
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
 822-1145 2.31e-81

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: 270.97  E-value: 2.31e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  822 TGLAYDPLMLKH----------SCICGDNA-QHPEHSGRLQsvwaRLNE----TDLVKRCDRLRARKATQEELQTVHTEA 886
Cdd:cd09996     1 TGFVWDERYLWHdtgtgalflpVGGLLVQPgRHPENPETKR----RIKNllevSGLSDHLVLITPRPATDEELLRVHTPE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  887 HamlfgsnqcqLSRPKlenTLSASfvrlscGGLGVDLDTTWNeHHTATAARMAAGCVIDLALKTAKGDLRNGFAVVRPPG 966
Cdd:cd09996    77 Y----------IDRVK---AASAA------GGGEAGGGTPFG-PGSYEIALLAAGGAIAAVDAVLDGEVDNAYALVRPPG 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  967 HHAEANLAMGFCFFNSIAIAAKLLRQRMpEVRRILIVDWDVHHGNGTQQAFYQSPDILYLSIHRhdDGNFFPGTGGPTEC 1046
Cdd:cd09996   137 HHAEPDQGMGFCLFNNVAIAARHALAVG-GVKRVAVVDWDVHHGNGTQAIFYDDPDVLTISLHQ--DRCFPPDSGAVEER 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1047 GSGAGLGFNVNIswsgalnpPL----GDAEYIAAFRTVVMPIARSFNPDIVLVSSGFDAATGHpaPLGGYHVSPACFGFM 1122
Cdd:cd09996   214 GEGAGEGYNLNI--------PLppgsGDGAYLHAFERIVLPALRAFRPELIIVASGFDASAFD--PLGRMMLTSDGFRAL 283

                         330       340
                  ....*....|....*....|....*..
gi 281360799 1123 TRELLQLAN----GKVVLALEGGYDLA 1145
Cdd:cd09996   284 TRKLRDLADelcgGRLVMVHEGGYSEA 310
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
 849-1158 3.18e-81

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: 267.76  E-value: 3.18e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  849 RLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAHAMLFGSNQCQLSRPKlentlsasfvrlscGGLGVDLDTTWN 928
Cdd:cd09301     1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKANFAVATITE--------------SKPVIFGPNFPV 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  929 EHHTATAARMAAGCVIDLALKTAKGDLRNGFAVVRPPGHHAEANLAMGFCFFNSIAIAAKLLRQRmpEVRRILIVDWDVH 1008
Cdd:cd09301    67 QRHYFRGARLSTGGVVEAAELVAKGELERAFAVVGAGGHHAGKSRAWGFCYFNDVVLAIKFLRER--GISRILIIDTDAH 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1009 HGNGTQQAFYQSPDILYLSIHRHDDGNFfpgtggptecGSGAGLGFNVNISWSGAlnppLGDAEYIAAFRTVVMPIARSF 1088
Cdd:cd09301   145 HGDGTREAFYDDDRVLHMSFHNYDIYPF----------GRGKGKGYKINVPLEDG----LGDEEYLDAVERVISKVLEEF 210

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281360799 1089 NPDIVLVSSGFDAATGHpaPLGGYHVSPACFGFMTRELLQLANGK-VVLALEGGYDLAAICDSAQECVRAL 1158
Cdd:cd09301   211 EPEVVVLQFGHDTHEGD--RLGGFNLSEKGFVKLAEIVKEFARGGpILMVLGGGYNPEAAARIWTAIIKEL 279
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 849-1194 1.42e-77

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: 259.79  E-value: 1.42e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  849 RLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAHAMLFGSNQCQLSRPKLEntLSASFvrlscgglgvdlDTTWN 928
Cdd:cd11683    13 RLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRETQVMNKEELMA--ISGKY------------DAVYF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  929 EHHTATAARMAAGCVIDLALKTAKGDLRNGFAVVRPPGHHAEANLAMGFCFFNSIAIAAKLLRQRMpEVRRILIVDWDVH 1008
Cdd:cd11683    79 HPNTFHCARLAAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYAKKKY-GLHRILIVDWDVH 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1009 HGNGTQQAFYQSPDILYLSIHRHDDGNFFPG--TGGPTECGSGAGLGFNVNISWSGAlnpPLGDAEYIAAFRTVVMPIAR 1086
Cdd:cd11683   158 HGQGIQYIFEEDPSVLYFSWHRYEHQRFWPFlrESDYDAVGRGKGLGFNINLPWNKV---GMGNADYLAAFFHVLLPLAF 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1087 SFNPDIVLVSSGFDAATGHPAplGGYHVSPACFGFMTRELLQLANGKVVLALEGGYDLAAICDSAQECVRALLGDPAAPI 1166
Cdd:cd11683   235 EFDPELVLVSAGFDSAIGDPE--GQMCATPECFAHLTHLLMVLAGGKLCAVLEGGYHLESLAESVCMTVQTLLGDPLPRL 312

                         330       340
                  ....*....|....*....|....*...
gi 281360799 1167 AKaelERPPCQNAINTLQKTIAIQQTHW 1194
Cdd:cd11683   313 SG---EMTPCQSALESIQNVRAAQAPYW 337
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
 843-1159 2.33e-76

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: 254.36  E-value: 2.33e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  843 HPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAHAmlfgsnqcqlsrpklentlsaSFVRLSCGGLG-V 921
Cdd:cd11599     1 HPESPERLEAILDALIASGLDRLLRQLEAPPATREQLLRVHDAAYV---------------------DRLEAAAPEEGlV 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  922 DLDT-TWNEHHTATAARMAAGCVIDLALKTAKGDLRNGFAVVRPPGHHAEANLAMGFCFFNSIAIAAKLLRQRmPEVRRI 1000
Cdd:cd11599    60 QLDPdTAMSPGSLEAALRAAGAVVAAVDAVMAGEARNAFCAVRPPGHHAERDKAMGFCLFNNVAIAAAHALAH-HGLERV 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1001 LIVDWDVHHGNGTQQAFYQSPDILYLSIHRHddgNFFPGTGGPTECGSGaglgfnvNIswsgaLNPPL----GDAEYIAA 1076
Cdd:cd11599   139 AIVDFDVHHGNGTEDIFRDDPRVLFCSSHQH---PLYPGTGAPDETGHG-------NI-----VNVPLpagtGGAEFREA 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1077 FRTVVMPIARSFNPDIVLVSSGFDAatgHPA-PLGGYHVSPACFGFMTRELLQLAN----GKVVLALEGGYDLAAICDSA 1151
Cdd:cd11599   204 VEDRWLPALDAFKPDLILISAGFDA---HRDdPLAQLNLTEEDYAWITEQLMDVADrycdGRIVSVLEGGYDLSALARSV 280


                  ....*...
gi 281360799 1152 QECVRALL 1159
Cdd:cd11599   281 AAHVRALM 288
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
 826-1160 2.84e-70

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: 237.44  E-value: 2.84e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  826 YDPLMLKHS----CICGDNAQHPEHSGRLQSVWARLNETDLVkrcDRLRARKATQEELQTVHTEAHamlfgsnqcqlsrp 901
Cdd:cd10001     4 YSEDHLLHHpkteLSRGKLVPHPENPERAEAILDALKRAGLG---EVLPPRDFGLEPILAVHDPDY-------------- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  902 kLEntlsasFVRlscgglGVDLDTTWNEHhTATAARMAAGCVIDLALKTAKGDlRNGFAVVRPPGHHAEANLAMGFCFFN 981
Cdd:cd10001    67 -VD------FLE------TADTDTPISEG-TWEAALAAADTALTAADLVLEGE-RAAYALCRPPGHHAGRDRAGGFCYFN 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  982 SIAIAAKLLRQRMPevrRILIVDWDVHHGNGTQQAFYQSPDILYLSIHRhDDGNFFPGTGG-PTECGSGAGLGFNVNIsw 1060
Cdd:cd10001   132 NAAIAAQYLRDRAG---RVAILDVDVHHGNGTQEIFYERPDVLYVSIHG-DPRTFYPFFLGfADETGEGEGEGYNLNL-- 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1061 sgalnpPL----GDAEYIAAFRTVVMPIARsFNPDIVLVSSGFDAATGHpaPLGGYHVSPACFGFMTRELLQLaNGKVVL 1136
Cdd:cd10001   206 ------PLppgtGDDDYLAALDEALAAIAA-FGPDALVVSLGFDTHEGD--PLSDFKLTTEDYARIGRRIAAL-GLPTVF 275

                         330       340
                  ....*....|....*....|....
gi 281360799 1137 ALEGGYDLAAIcdsaQECVRALLG 1160
Cdd:cd10001   276 VQEGGYNVDAL----GRNAVAFLA 295
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
 824-1144 1.66e-48

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: 175.44  E-value: 1.66e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  824 LAYDPLMLKHSCicGDNaqHPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEA---HAMLFGSNQCQLSR 900
Cdd:cd09994     2 FIYSEEYLRYSF--GPN--HPFNPPRLSLTKDLLRALGLLPPVDLVPPRPATEEELLLFHTPDyieAVKEASRGQEPEGR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  901 PKLentlsasfvrlscgGLGvDLDTTWNEH-HTAtaARMAAGCVIDLALKTAKGDLRNGFAvvrPPG--HHAEANLAMGF 977
Cdd:cd09994    78 GRL--------------GLG-TEDNPVFPGmHEA--AALVVGGTLLAARLVLEGEARRAFN---PAGglHHAMRGRASGF 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  978 CFFNSIAIAAKLLRQRmpEVRRILIVDWDVHHGNGTQQAFYQSPDILYLSIHRhDDGNFFPGTGGPTECGSGAGLGFNVN 1057
Cdd:cd09994   138 CVYNDAAVAIERLRDK--GGLRVAYVDIDAHHGDGVQAAFYDDPRVLTISLHE-SGRYLFPGTGFVDEIGEGEGYGYAVN 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1058 IswsgALNPPLGDAEYIAAFRTVVMPIARSFNPDIVLVSSGFDAATGHpaPLGGYHVSPACFGFMTRELLQLA----NGK 1133
Cdd:cd09994   215 I----PLPPGTGDDEFLRAFEAVVPPLLRAFRPDVIVSQHGADAHAGD--PLTHLNLSNRAYRAAVRRIRELAdeycGGR 288

                         330
                  ....*....|.
gi 281360799 1134 VVLALEGGYDL 1144
Cdd:cd09994   289 WLALGGGGYNP 299
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 853-1149 7.04e-33

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: 129.15  E-value: 7.04e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  853 VWARLNETDLVKRCDRLRARKATQEELQTVHTEA--HAMLFGSNQCQLSR-------PKLENTlsasfVRLSCGGlgvdl 923
Cdd:cd09993    11 LREALLEEGLVLPEDIVEPEPATREDLLRVHDPEylESLKSGELSREEIRrigfpwsPELVER-----TRLAVGG----- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  924 dttwnehhTATAARMA--AGCVIDLAlktakGdlrnGFavvrppgHHAEANLAMGFCFFNSIAIAAKLLRQRmPEVRRIL 1001
Cdd:cd09993    81 --------TILAARLAleHGLAINLA-----G----GT-------HHAFPDRGEGFCVFNDIAIAARVLLAE-GLVRRVL 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1002 IVDWDVHHGNGTQQAFYQSPDILYLSIHrhdDGNFFPGTGGPtecgsgaglgfnvnISWSGALNPPLGDAEYIAAFRTVV 1081
Cdd:cd09993   136 IVDLDVHQGNGTAAIFADDPSVFTFSMH---GEKNYPFRKEP--------------SDLDVPLPDGTGDDEYLAALEEAL 198

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281360799 1082 MPIARSFNPDIVLVSSGFDAATGHpaPLGGYHVSPAcfGFMTRELLQLANGK-----VVLALEGGY--DLAAICD 1149
Cdd:cd09993   199 PRLLAEFRPDLVFYNAGVDVLAGD--RLGRLSLSLE--GLRERDRLVLRFARargipVAMVLGGGYsrDIARLVA 269
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
 862-1142 1.04e-32

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: 129.62  E-value: 1.04e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  862 LVKRCDRLRARKATQEELQTVHTEAHaMLFgsnqcqLSRPKLEN--TLSASFVRLscgGLGVD---LDTTWnehhtaTAA 936
Cdd:cd09991    34 LYKKMEIYRPRPATAEELTKFHSDDY-IDF------LRSVSPDNmkEFKKQLERF---NVGEDcpvFDGLY------EYC 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  937 RMAAGCVIDLALKTAKGDlrnGFAVVRPPG--HHAEANLAMGFCFFNSIAIAAKLLRQRMPevrRILIVDWDVHHGNGTQ 1014
Cdd:cd09991    98 QLYAGGSIAAAVKLNRGQ---ADIAINWAGglHHAKKSEASGFCYVNDIVLAILELLKYHQ---RVLYIDIDIHHGDGVE 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1015 QAFYQSPDILYLSIHRHddGNFFPGTGGPTECGSGAGLGFNVNIswsgALNPPLGDAEYIAAFRTVVMPIARSFNPDIVL 1094
Cdd:cd09991   172 EAFYTTDRVMTVSFHKF--GEYFFPGTGLRDIGAGKGKYYAVNV----PLKDGIDDESYLQIFEPVLSKVMEVFQPSAVV 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 281360799 1095 VSSGFDAATGHpaPLGGYHVSP----ACFGFMTRellqlANGKVVLALEGGY 1142
Cdd:cd09991   246 LQCGADSLAGD--RLGCFNLSIkghaKCVKFVKS-----FNIPLLVLGGGGY 290
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 862-1148 7.74e-31

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: 125.53  E-value: 7.74e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  862 LVKRCDRLRARKATQEELQTVHTEAHaMLFGSNQCQLSRPKLENTLSASFvrlscgGLGvdLDTTWNEHhTATAARMAAG 941
Cdd:cd10000    35 LLKQLRVVKPRVATEEELASFHSDEY-IQFLKKASNEGDNDEEPSEQQEF------GLG--YDCPIFEG-IYDYAAAVAG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  942 CVIDLALKTAKGDLRngFAVVRPPG-HHAEANLAMGFCFFNSIAIAAKLLRQRMpevRRILIVDWDVHHGNGTQQAFYQS 1020
Cdd:cd10000   105 ATLTAAQLLIDGKCK--VAINWFGGwHHAQRDEASGFCYVNDIVLGILKLREKF---DRVLYVDLDLHHGDGVEDAFSFT 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1021 PDILYLSIHRHDDGnFFPGTGGPTECGSGAGLGFNVNIswsgALNPPLGDAEYIAAFRTVVMPIARSFNPDIVLVSSGFD 1100
Cdd:cd10000   180 SKVMTVSLHKYSPG-FFPGTGDVSDVGLGKGKYYTVNV----PLRDGIQDEQYLQIFTAVVPEIVAAFRPEAVVLQCGAD 254

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 281360799 1101 AATGHpaPLGGYHVSPACFGFMTRELLQLANGKVVLAlEGGYDLA--AIC 1148
Cdd:cd10000   255 TLAGD--PMGAFNLTPVGIGKCLKYVLGWKLPTLILG-GGGYNLAntARC 301
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
 844-1148 9.61e-29

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: 117.75  E-value: 9.61e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  844 PEHSGRLQSVWARLNETDLVKRCDR-LRARKATQEELQTVHTEahamlfgsnqcqlsrpklentlsaSFVRLSCGGLGVD 922
Cdd:cd11680    16 PSNKGRSSLVHSLIRAYGLLQHFDEiIEPERATRKDLTKYHDK------------------------DYVDFLLKKYGLE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  923 LDTTW----NEHhtataARMAAGCVIDLAlKTAKGDLRNGFAVVRPPG-HHAEANLAMGFCFFNSIAIAAKLLRQRmpEV 997
Cdd:cd11680    72 DDCPVfpflSMY-----VQLVAGSSLALA-KHLITQVERDIAINWYGGrHHAQKSRASGFCYVNDIVLAILRLRRA--RF 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  998 RRILIVDWDVHHGNGTQQAFYQSPDILYLSIHRHDDGnFFPGTGGPTECGSgaglGFNVNIswsgALNPPLGDAEYIAAF 1077
Cdd:cd11680   144 RRVFYLDLDLHHGDGVESAFFFSKNVLTCSIHRYDPG-FFPGTGSLKNSSD----KGMLNI----PLKRGLSDKTLLRII 214

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281360799 1078 RTVVMPIARSFNPDIVLVSSGFDAATGHpaPLGGYHVSPACFGFMTRELLQLANGKVVLAL-EGGYD--LAAIC 1148
Cdd:cd11680   215 DSIVRPLIEKFEPEVIVIQCGCDGLSGD--PHKEWNLTIRGYGSVIELLLKEFKDKPTLLLgGGGYNhtEAARA 286
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
 843-1121 5.05e-28

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: 116.02  E-value: 5.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  843 HPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAH----AMLFGSNQCQLSRPKLENTlsasfvrlscgG 918
Cdd:cd11598    18 HPMKPFRLTLTKHLVMGYGLHKAMDTYEARAATREELRQFHDADYldflSKVSPENANQLRFDKAEPF-----------N 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  919 LGVDLDTTwneHHTATAARMAAGCVIDLALKTAKGdlRNGFAVVRPPG-HHAEANLAMGFCFFNSIAIAAKLLRQRMPev 997
Cdd:cd11598    87 IGDDCPVF---DGMYDYCQLYAGASLDAARKLCSG--QSDIAINWSGGlHHAKKSEASGFCYVNDIVLAILNLLRYFP-- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  998 rRILIVDWDVHHGNGTQQAFYQSPDILYLSIHRHdDGNFFPGTGGPTECGSGAGLGFNVNIswsgALNPPLGDAEYIAAF 1077
Cdd:cd11598   160 -RVLYIDIDVHHGDGVEEAFYRTDRVMTLSFHKY-NGEFFPGTGDLDDNGGTPGKHFALNV----PLEDGIDDEQYNLLF 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 281360799 1078 RTVVMPIARSFNPDIVLVSSGFDAATGHpaPLGGYHVS----PACFGF 1121
Cdd:cd11598   234 KSIIGPTIEKFQPSAIVLQCGADSLGGD--RLGQFNLNikahGACVKF 279
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 931-1158 1.92e-21

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: 93.98  E-value: 1.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  931 HTATAARMAAGCVIDLAlktakGDLRNGFAVVrppGHHAEANlamgfcffnSIAIAAKLLRQRmpevrrILIVDWDVHHG 1010
Cdd:cd09987     6 RKAEAHELLAGVVVAVL-----KDGKVPVVLG---GDHSIAN---------GAIRAVAELHPD------LGVIDVDAHHD 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1011 NGTQQAFY--------------QSPDILYLSIHRHDDGNFFPGtggptecGSGAGLGFNVNISWSGalnppLGDAEYIAA 1076
Cdd:cd09987    63 VRTPEAFGkgnhhtprhllcepLISDVHIVSIGIRGVSNGEAG-------GAYARKLGVVYFSMTE-----VDKLGLGDV 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1077 FRTVVMPIarSFNPDIVLVSSGFDAATGHPAPLGGyhvSPACFGFMTRELLQL------ANGKVVLALEGGYDLA----A 1146
Cdd:cd09987   131 FEEIVSYL--GDKGDNVYLSVDVDGLDPSFAPGTG---TPGPGGLSYREGLYIteriakTNLVVGLDIVEVNPLLdetgR 205

                         250
                  ....*....|..
gi 281360799 1147 ICDSAQECVRAL 1158
Cdd:cd09987   206 TARLAAALTLEL 217
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
 843-1104 5.05e-21

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: 96.67  E-value: 5.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  843 HPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAHAMLFGSnqcqlSRPKLENTLSASFVRLSCGGLGVD 922
Cdd:cd10010    25 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRS-----IRPDNMSEYSKQMQRFNVGEDCPV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  923 LDTTWNEHHTATAARMAAGCVIDLALKTAKGDLRNGFavvrppgHHAEANLAMGFCFFNSIAIAA-KLLRQRmpevRRIL 1001
Cdd:cd10010   100 FDGLFEFCQLSAGGSVASAVKLNKQQTDIAVNWAGGL-------HHAKKSEASGFCYVNDIVLAIlELLKYH----QRVL 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1002 IVDWDVHHGNGTQQAFYQSPDILYLSIHRHddGNFFPGTGGPTECGSGAGLGFNVNIswsgALNPPLGDAEYIAAFRTVV 1081
Cdd:cd10010   169 YIDIDIHHGDGVEEAFYTTDRVMTVSFHKY--GEYFPGTGDLRDIGAGKGKYYAVNY----PLRDGIDDESYEAIFKPVM 242

                         250       260
                  ....*....|....*....|...
gi 281360799 1082 MPIARSFNPDIVLVSSGFDAATG 1104
Cdd:cd10010   243 SKVMEMFQPSAVVLQCGADSLSG 265
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
 841-1104 1.07e-20

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: 95.64  E-value: 1.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  841 AQHPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAHAMLFG----SNQCQLSRPKLENTLSA------- 909
Cdd:cd10004    19 PGHPMKPHRIRMAHSLVMNYGLYKKMEIYRAKPATKNEMTQFHTDEYIDFLSrvtpDNMEKFQKEQVKYNVGDdcpvfdg 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  910 --SFVRLSCGGlgvdldttwnehHTATAARMAAG-CviDLALKTAKGDlrngfavvrppgHHAEANLAMGFCFFNSIAIA 986
Cdd:cd10004    99 lfEFCSISAGG------------SMEGAARLNRGkC--DIAVNWAGGL------------HHAKKSEASGFCYVNDIVLG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  987 A-KLLRQRmpevRRILIVDWDVHHGNGTQQAFYQSPDILYLSIHRHddGNFFPGTGGPTECGSGAGLGFNVNIswsgALN 1065
Cdd:cd10004   153 IlELLRYH----QRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKY--GEYFPGTGELRDIGIGTGKNYAVNV----PLR 222

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 281360799 1066 PPLGDAEYIAAFRTVVMPIARSFNPDIVLVSSGFDAATG 1104
Cdd:cd10004   223 DGIDDESYKSIFEPVIKHVMEWYQPEAVVLQCGGDSLSG 261
PTZ00063 PTZ00063
histone deacetylase; Provisional
 843-1104 2.17e-20

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 95.65  E-value: 2.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  843 HPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAHAMLFGS---NQC-----QLSRPKL-ENTLSASFVR 913
Cdd:PTZ00063   23 HPMKPQRIRMAHALILSYDLYKHMEIYRPHKSVEPELVLFHDEEYVDFLSSispENYrdftyQLKRFNVgEATDCPVFDG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  914 L-----SCGGLGVDLDTTWNEHHTATAARMAAGCvidlalktakgdlrngfavvrppgHHAEANLAMGFCFFNSIAIAA- 987
Cdd:PTZ00063  103 LfefqqSCAGASIDGAYKLNNHQADICVNWSGGL------------------------HHAKRSEASGFCYINDIVLGIl 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  988 KLLRQRMpevrRILIVDWDVHHGNGTQQAFYQSPDILYLSIHRHddGNFFPGTGGPTECGSGAGLGFNVNIswsgALNPP 1067
Cdd:PTZ00063  159 ELLKYHA----RVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFPGTGDVTDIGVAQGKYYSVNV----PLNDG 228

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 281360799 1068 LGDAEYIAAFRTVVMPIARSFNPDIVLVSSGFDAATG 1104
Cdd:PTZ00063  229 IDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTG 265
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
 944-1151 6.92e-19

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: 89.82  E-value: 6.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  944 IDLALKTAKGDLRNGFAVVRPPGHHAEANLAMGFCFFNSIAIAAK--LLRQrmpEVRRILIVDWDVHHGNGTQ------- 1014
Cdd:cd09998    97 VDSVFKPESPGTKRAFVAIRPPGHHCSESTPSGFCWVNNVHVGAAhaYLTH---GITRVVILDIDLHHGNGTQdiawrin 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1015 -----------------QAFYQSPDILYLSIHrhdDGNFFPGTGGPTECGSGAglgfNVNIS-------WSGALNPPLGD 1070
Cdd:cd09998   174 aeankqalesssyddfkPAGAPGLRIFYSSLH---DINSFPCEDGDPAKVKDA----SVSIDgahgqwiWNVHLQPWTTE 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799 1071 AEYIAAFR---TVVMPIARSF-------NPD--IVLVSSGFDAATGHPAPLG--GYHVSPACFGFMTRELLQLA----NG 1132
Cdd:cd09998   247 EDFWELYYpkyRILFEKAAEFlrlttaaTPFktLVFISAGFDASEHEYESMQrhGVNVPTSFYYRFARDAVRFAdahaHG 326

                         250
                  ....*....|....*....
gi 281360799 1133 KVVLALEGGYDLAAICDSA 1151
Cdd:cd09998   327 RLISVLEGGYSDRALCSGV 345
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
 967-1101 9.53e-18

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: 86.68  E-value: 9.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  967 HHAEANLAMGFCFFNSIAIAAKLLRQRMPevrRILIVDWDVHHGNGTQQAFYQSPDILYLSIHRHddGN-FFPGTGGPTE 1045
Cdd:cd10005   132 HHAKKFEASGFCYVNDIVIAILELLKYHP---RVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKY--GNyFFPGTGDMYE 206

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 281360799 1046 CGSGAGLGFNVNIswsgALNPPLGDAEYIAAFRTVVMPIARSFNPDIVLVSSGFDA 1101
Cdd:cd10005   207 VGAESGRYYSVNV----PLKDGIDDQSYLQLFKPVIQQVIDFYQPTCIVLQCGADS 258
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
 843-1104 4.24e-17

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: 84.73  E-value: 4.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  843 HPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAHAMLFGSnqcqlSRPKLENTLSASFVRLSCGGLGVD 922
Cdd:cd10011    21 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRS-----IRPDNMSEYSKQMQRFNVGEDCPV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  923 LDTTWNEHHTATAARMAAGCVI-----DLALKTAKGDlrngfavvrppgHHAEANLAMGFCFFNSIAIAA-KLLRQRmpe 996
Cdd:cd10011    96 FDGLFEFCQLSTGGSVAGAVKLnrqqtDMAVNWAGGL------------HHAKKSEASGFCYVNDIVLAIlELLKYH--- 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  997 vRRILIVDWDVHHGNGTQQAFYQSPDILYLSihRHDDGNFFPGTGGPTECGSGAGLGFNVNISWSGALNpplgDAEYIAA 1076
Cdd:cd10011   161 -QRVLYIDIDIHHGDGVEEAFYTTDRVMTVS--FHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGID----DESYGQI 233

                         250       260
                  ....*....|....*....|....*...
gi 281360799 1077 FRTVVMPIARSFNPDIVLVSSGFDAATG 1104
Cdd:cd10011   234 FKPIISKVMEMYQPSAVVLQCGADSLSG 261
PTZ00346 PTZ00346
histone deacetylase; Provisional
 877-1104 1.47e-16

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 83.93  E-value: 1.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  877 EELQTVHTEAHAMLFGSNQCqlsRPKLENT-LSASFVRLSCGGLgvdldTTWNEHHTATAARMAAGCVIdlaLKTAKGDL 955
Cdd:PTZ00346   77 EELMAYHTDTYLANLGLHSC---RSWLWNAeTSKVFFSGDCPPV-----EGLMEHSIATASGTLMGAVL---LNSGQVDV 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360799  956 rngfAVVRPPG-HHAEANLAMGFCFFNSIAIAA-KLLRQRmpevRRILIVDWDVHHGNGTQQAFYQSPDILYLSIHRHDD 1033
Cdd:PTZ00346  146 ----AVHWGGGmHHSKCGECSGFCYVNDIVLGIlELLKCH----DRVLYVDIDMHHGDGVDEAFCTSDRVFTLSLHKFGE 217

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281360799 1034 gNFFPGTGGPTECGSGAGLGFNVNIS-WSGalnppLGDAEYIAAFRTVVMPIARSFNPDIVLVSSGFDAATG 1104
Cdd:PTZ00346  218 -SFFPGTGHPRDVGYGRGRYYSMNLAvWDG-----ITDFYYLGLFEHALHSIVRRYSPDAIVLQCGADSLAG 283
ClassIIa_HDAC5_Gln-rich-N cd10164
Glutamine-rich N-terminal helical domain of HDAC5, a Class IIa histone deacetylase; This ...
 43-97 2.47e-04

Glutamine-rich N-terminal helical domain of HDAC5, a Class IIa histone deacetylase; This family consists of the glutamine-rich domain of histone deacetylase 5 (HDAC5). It belongs to a superfamily that consists of the glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDCA9; it is missing from HDAC7. This domain confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors, and it is able to repress transcription independently of the HDAC C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues.


Pssm-ID: 197400 [Multi-domain]  Cd Length: 97  Bit Score: 41.35  E-value: 2.47e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 281360799   43 IDQQIMELKKSQELQKQRLINSFQEQSKQMELEHKLQLEH--KYQFAVNSHGAFQEL 97
Cdd:cd10164     9 LQQELLLLKQQQQLQKQLLFAEFQKQHEHLTRQHEVQLQKhlKVRAELFSEQQQQEI 65
ClassIIa_HDAC4_Gln-rich-N cd10162
Glutamine-rich N-terminal helical domain of HDAC4, a Class IIa histone deacetylase; This ...
 43-85 5.23e-04

Glutamine-rich N-terminal helical domain of HDAC4, a Class IIa histone deacetylase; This family consists of the glutamine-rich domain of histone deacetylase 4 (HDAC4). It belongs to a superfamily that consists of the glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDCA9; it is missing from HDAC7. This domain confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors, and it is able to repress transcription independently of the HDAC C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues.


Pssm-ID: 197398 [Multi-domain]  Cd Length: 90  Bit Score: 40.18  E-value: 5.23e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 281360799   43 IDQQIMELKKSQELQKQRLINSFQEQSKQMELEHKLQL-EHKYQ 85
Cdd:cd10162     9 LQQELLALKQKQQIQRQLLIAEFQRQHEQLSRQHEAQLhEHIKQ 52
ClassIIa_HDAC_Gln-rich-N cd10149
Glutamine-rich N-terminal helical domain of various Class IIa histone deacetylases (HDAC4, ...
 43-81 1.68e-03

Glutamine-rich N-terminal helical domain of various Class IIa histone deacetylases (HDAC4, HDAC5 and HDCA9); This superfamily consists of a glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDAC9; it is missing in HDAC7. It is referred to as the glutamine-rich domain, and confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors. This domain is able to repress transcription independently of the HDAC's C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues.


Pssm-ID: 197397 [Multi-domain]  Cd Length: 90  Bit Score: 38.90  E-value: 1.68e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 281360799   43 IDQQIMELKKSQELQKQRLINSFQEQSKQMELEHKLQLE 81
Cdd:cd10149     9 LQQELLALKQQQQIQKQLLIAEFQKQHENLTRQHEAQLQ 47
ClassIIa_HDAC9_Gln-rich-N cd10163
Glutamine-rich N-terminal helical domain of HDAC9, a Class IIa histone deacetylase; This ...
 43-82 3.96e-03

Glutamine-rich N-terminal helical domain of HDAC9, a Class IIa histone deacetylase; This family consists of the glutamine-rich domain of histone deacetylase 9 (HDAC9). It belongs to a superfamily that consists of the glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDCA9; it is missing from HDAC7. This domain confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors, and it is able to repress transcription independently of the HDAC C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues.


Pssm-ID: 197399 [Multi-domain]  Cd Length: 90  Bit Score: 37.81  E-value: 3.96e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 281360799   43 IDQQIMELKKSQELQKQRLINSFQEQSKQMELEHKLQL-EH 82
Cdd:cd10163     9 LQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLqEH 49
 
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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