NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|281306754|ref|NP_445902|]
View 

histone deacetylase 5 [Rattus norvegicus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Arginase_HDAC super family cl17011
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 670-1086 0e+00

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.


The actual alignment was detected with superfamily member cd10007:

Pssm-ID: 450134 [Multi-domain]  Cd Length: 420  Bit Score: 882.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  670 HLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLN 749
Cdd:cd10007     1 HLFTTGLVYDTFMLKHQCTCGNTNVHPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHSEHHTLLYGTSPLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  750 RQKLDSKKLLGPISQKMYAMLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLVELAFKVAAGELKNGFAIIRPPGHHAEEST 829
Cdd:cd10007    81 RQKLDSKKLLGPLSQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLIELAFKVAAGELKNGFAVIRPPGHHAEEST 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  830 AMGFCFFNSVAITAKLLQQKLSVGKVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGY 909
Cdd:cd10007   161 AMGFCFFNSVAIAAKLLQQKLNVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGNFFPGSGAPDEVGAGPGVGF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  910 NVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRV 989
Cdd:cd10007   241 NVNIAWTGGVDPPIGDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGHQSPLGGYSVTAKCFGHLTKQLMTLAGGRV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  990 VLALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPSVNAVATLEKVIEIQSKHWSCVQRFATGLGCSLREAQTG 1069
Cdd:cd10007   321 VLALEGGHDLTAICDASEACVSALLGMELTPLDNTVLQQKPNDNAVATLERVIEIQSKHWSCLKRFAATLGFSLLEAQRG 400

                         410
                  ....*....|....*..
gi 281306754 1070 EKEEAETVSAMALLSMG 1086
Cdd:cd10007   401 ELEEAETVSAMASLSVD 417
ClassIIa_HDAC_Gln-rich-N super family cl25407
Glutamine-rich N-terminal helical domain of various Class IIa histone deacetylases (HDAC4, ...
 68-155 1.54e-09

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: 55.99  E-value: 1.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754   68 DPALREQQLQQELLVLKQQQQLQKQLLFAEFQKQHDHLTRQHEV---------QLQKHLKQQQEMLAAKRQQELEQQRQR 138
Cdd:cd10164     1 DPSLREQQLQQELLLLKQQQQLQKQLLFAEFQKQHEHLTRQHEVqlqkhlkvrAELFSEQQQQEILAAKRQQELEQQRKR 80

                          90
                  ....*....|....*..
gi 281306754  139 EQQRQEELEKQRLEQQL 155
Cdd:cd10164    81 EQQRQEELEKQRLEQQL 97
 
Name Accession Description Interval E-value
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
 670-1086 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: 882.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  670 HLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLN 749
Cdd:cd10007     1 HLFTTGLVYDTFMLKHQCTCGNTNVHPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHSEHHTLLYGTSPLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  750 RQKLDSKKLLGPISQKMYAMLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLVELAFKVAAGELKNGFAIIRPPGHHAEEST 829
Cdd:cd10007    81 RQKLDSKKLLGPLSQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLIELAFKVAAGELKNGFAVIRPPGHHAEEST 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  830 AMGFCFFNSVAITAKLLQQKLSVGKVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGY 909
Cdd:cd10007   161 AMGFCFFNSVAIAAKLLQQKLNVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGNFFPGSGAPDEVGAGPGVGF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  910 NVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRV 989
Cdd:cd10007   241 NVNIAWTGGVDPPIGDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGHQSPLGGYSVTAKCFGHLTKQLMTLAGGRV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  990 VLALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPSVNAVATLEKVIEIQSKHWSCVQRFATGLGCSLREAQTG 1069
Cdd:cd10007   321 VLALEGGHDLTAICDASEACVSALLGMELTPLDNTVLQQKPNDNAVATLERVIEIQSKHWSCLKRFAATLGFSLLEAQRG 400

                         410
                  ....*....|....*..
gi 281306754 1070 EKEEAETVSAMALLSMG 1086
Cdd:cd10007   401 ELEEAETVSAMASLSVD 417
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 695-1013 8.30e-113

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: 352.31  E-value: 8.30e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754   695 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSplnrqkldskkllgpiSQKMYAMLPCGG 774
Cdd:pfam00850    1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEA----------------APEGGALLLLSY 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754   775 IGVDSDTVWNEmHSSSAVRMAVGCLVELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLSVGK 854
Cdd:pfam00850   65 LSGDDDTPVSP-GSYEAALLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLKR 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754   855 VLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYDnGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGvdppIGDVEYLTAFRT 934
Cdd:pfam00850  144 VAIVDFDVHHGNGTQEIFYDDPSVLTLSIHQYP-GGFYPGTGFADETGEGKGKGYTLNVPLPPG----TGDAEYLAAFEE 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754   935 VVMPIAHEFSPDVVLVSAGFDAVEGHlsPLGGYSVTARCFGHLTRQLMTLA---GGRVVLALEGGHDLTAICDASEACVS 1011
Cdd:pfam00850  219 ILLPALEEFQPDLILVSAGFDAHAGD--PLGGLNLTTEGFAEITRILLELAdplCIRVVSVLEGGYNLDALARSATAVLA 296


                   ..
gi 281306754  1012 AL 1013
Cdd:pfam00850  297 AL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 674-1014 2.12e-92

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 297.79  E-value: 2.12e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  674 TGVVYDTFMLKHQCmcGNTHvhPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHS-EYHTLLYGTSPLNRqk 752
Cdd:COG0123     1 TALIYHPDYLLHDL--GPGH--PEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTpDYVDALRAASLDGG-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  753 ldskkllgpisqkmYAMLpcggigvDSDTVWNEmHSSSAVRMAVGCLVELAFKVAAGELKNGFAIIRPPGHHAEESTAMG 832
Cdd:COG0123    75 --------------YGQL-------DPDTPVSP-GTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMG 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  833 FCFFNSVAITAKLLQQKlSVGKVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYdngNFFPGSGAPEEVGGGPGVGYNVN 912
Cdd:COG0123   133 FCLFNNAAIAARYLLAK-GLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD---PLYPGTGAADETGEGAGEGSNLN 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  913 VAwtggVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLMTLA---GGRV 989
Cdd:COG0123   209 VP----LPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHAD--DPLGRLNLTTEGYAWRTRRVLELAdhcGGPV 282

                         330       340
                  ....*....|....*....|....*
gi 281306754  990 VLALEGGHDLTAICDASEACVSALL 1014
Cdd:COG0123   283 VSVLEGGYNLDALARSVAAHLETLL 307
PTZ00063 PTZ00063
histone deacetylase; Provisional
 823-987 1.63e-19

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 92.57  E-value: 1.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  823 HHAEESTAMGFCFFNSVAI-TAKLLQQKlsvGKVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYdnGNFFPGSGAPEEV 901
Cdd:PTZ00063  137 HHAKRSEASGFCYINDIVLgILELLKYH---ARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFPGTGDVTDI 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  902 GGGPGVGYNVNVAWTGGVDppigDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVT----ARCFGH- 976
Cdd:PTZ00063  212 GVAQGKYYSVNVPLNDGID----DDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTG--DRLGRFNLTikghAACVEFv 285

                         170
                  ....*....|...
gi 281306754  977 --LTRQLMTLAGG 987
Cdd:PTZ00063  286 rsLNIPLLVLGGG 298
ClassIIa_HDAC5_Gln-rich-N cd10164
Glutamine-rich N-terminal helical domain of HDAC5, a Class IIa histone deacetylase; This ...
 68-155 1.54e-09

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: 55.99  E-value: 1.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754   68 DPALREQQLQQELLVLKQQQQLQKQLLFAEFQKQHDHLTRQHEV---------QLQKHLKQQQEMLAAKRQQELEQQRQR 138
Cdd:cd10164     1 DPSLREQQLQQELLLLKQQQQLQKQLLFAEFQKQHEHLTRQHEVqlqkhlkvrAELFSEQQQQEILAAKRQQELEQQRKR 80

                          90
                  ....*....|....*..
gi 281306754  139 EQQRQEELEKQRLEQQL 155
Cdd:cd10164    81 EQQRQEELEKQRLEQQL 97
HDAC4_Gln pfam12203
Glutamine rich N terminal domain of histone deacetylase 4; This domain is found in eukaryotes, ...
 95-155 1.07e-03

Glutamine rich N terminal domain of histone deacetylase 4; This domain is found in eukaryotes, and is approximately 90 amino acids in length. The family is found in association with pfam00850. The domain forms an alpha helix which complexes to form a tetramer. The glutamine rich domains have many intra- and inter-helical interactions which are thought to be involved in reversible assembly and disassembly of proteins. The domain is part of histone deacetylase 4 (HDAC4) which removes acetyl groups from histones. This restores their positive charge to allow stronger DNA binding thus restricting transcriptional activity.


Pssm-ID: 403429 [Multi-domain]  Cd Length: 91  Bit Score: 39.45  E-value: 1.07e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281306754    95 FAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKRQQELEQQ--RQREQQRQEELEKQRLEQQL 155
Cdd:pfam12203   29 IAEFQKQHELLTRQHEAQLQEHIKQQQELLAMKQQQELLEQqrKLEQQRQEEELEKHRREQQL 91
 
Name Accession Description Interval E-value
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
 670-1086 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: 882.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  670 HLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLN 749
Cdd:cd10007     1 HLFTTGLVYDTFMLKHQCTCGNTNVHPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHSEHHTLLYGTSPLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  750 RQKLDSKKLLGPISQKMYAMLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLVELAFKVAAGELKNGFAIIRPPGHHAEEST 829
Cdd:cd10007    81 RQKLDSKKLLGPLSQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLIELAFKVAAGELKNGFAVIRPPGHHAEEST 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  830 AMGFCFFNSVAITAKLLQQKLSVGKVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGY 909
Cdd:cd10007   161 AMGFCFFNSVAIAAKLLQQKLNVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGNFFPGSGAPDEVGAGPGVGF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  910 NVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRV 989
Cdd:cd10007   241 NVNIAWTGGVDPPIGDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGHQSPLGGYSVTAKCFGHLTKQLMTLAGGRV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  990 VLALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPSVNAVATLEKVIEIQSKHWSCVQRFATGLGCSLREAQTG 1069
Cdd:cd10007   321 VLALEGGHDLTAICDASEACVSALLGMELTPLDNTVLQQKPNDNAVATLERVIEIQSKHWSCLKRFAATLGFSLLEAQRG 400

                         410
                  ....*....|....*..
gi 281306754 1070 EKEEAETVSAMALLSMG 1086
Cdd:cd10007   401 ELEEAETVSAMASLSVD 417
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 672-1049 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: 758.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  672 FTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQ 751
Cdd:cd11681     1 FTTGLAYDPLMLKHQCICGNNSSHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTLLYGTNPLSRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  752 KLDSKKLLGpISQKMYAMLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLVELAFKVAAGELKNGFAIIRPPGHHAEESTAM 831
Cdd:cd11681    81 KLDPTKLAG-LPQKSFVRLPCGGIGVDSDTVWNELHTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQAM 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  832 GFCFFNSVAITAKLLQQKLSVGKVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGYNV 911
Cdd:cd11681   160 GFCFFNSVAIAAKQLQQKLKLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFPGTGAPTEVGSGAGEGFNV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  912 NVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRVVL 991
Cdd:cd11681   240 NIAWSGGLDPPMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPPPLGGYKVSPACFGYMTRQLMNLAGGKVVL 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 281306754  992 ALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPSVNAVATLEKVIEIQSKHW 1049
Cdd:cd11681   320 ALEGGYDLTAICDASEACVRALLGDELDPLSEEELERRPNPNAVTSLEKVIAIQSPYW 377
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
 669-1078 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: 743.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  669 KHLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPL 748
Cdd:cd10006     1 KPRFTTGLVYDTLMLKHQCTCGNSNSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  749 NRQKLDSKKLLGPISQkMYAMLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLVELAFKVAAGELKNGFAIIRPPGHHAEES 828
Cdd:cd10006    81 NRQKLDSKKLLGSLAS-VFVRLPCGGVGVDSDTIWNEVHSSGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEES 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  829 TAMGFCFFNSVAITAKLLQQKLSVGKVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVG 908
Cdd:cd10006   160 TPMGFCYFNSVAIAAKLLQQRLNVSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  909 YNVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGR 988
Cdd:cd10006   240 FNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSAKCFGYLTKQLMGLAGGR 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  989 VVLALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPSVNAVATLEKVIEIQSKHWSCVQRFATGLGCSLREAQT 1068
Cdd:cd10006   320 IVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGYSLIEAQT 399

                         410
                  ....*....|
gi 281306754 1069 GEKEEAETVS 1078
Cdd:cd10006   400 CENEEAETVT 409
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
 672-1049 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: 675.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  672 FTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQ 751
Cdd:cd10008     1 FTTGLVYDSVMLKHQCSCGDNSNHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  752 KLDSKKLLGPISQKMYAMLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLVELAFKVAAGELKNGFAIIRPPGHHAEESTAM 831
Cdd:cd10008    81 KLDNGKLAGLLAQRMFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  832 GFCFFNSVAITAKLLQQKLSVGKVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGYNV 911
Cdd:cd10008   161 GFCFFNSVAIACRQLQQQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGAGSGEGFNV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  912 NVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRVVL 991
Cdd:cd10008   241 NVAWAGGLDPPMGDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVL 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 281306754  992 ALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPSVNAVATLEKVIEIQSKHW 1049
Cdd:cd10008   321 ALEGGHDLTAICDASEACVAALLGNEVDPLSEESWKQKPNLNAIRSLEAVIRVHSKYW 378
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
 672-1049 0e+00

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: 644.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  672 FTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQ 751
Cdd:cd10009     1 SATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  752 KLDSKKLLGPISQKMYAMLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLVELAFKVAAGELKNGFAIIRPPGHHAEESTAM 831
Cdd:cd10009    81 KLDPRILLGDDSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  832 GFCFFNSVAITAKLLQQKLSVGKVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGYNV 911
Cdd:cd10009   161 GFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYNI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  912 NVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRVVL 991
Cdd:cd10009   241 NIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVL 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 281306754  992 ALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPSVNAVATLEKVIEIQSKHW 1049
Cdd:cd10009   321 ALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSKYW 378
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
 678-1051 9.39e-130

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: 399.02  E-value: 9.39e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  678 YDTFMLKHQCMCgNTHvHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHtllygtspLNRQKLDSKK 757
Cdd:cd10003     1 YDQRMMNHHNLW-DPG-HPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEH--------LDEMKSLEKM 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  758 LLGPISQKmyamlpcggiGVDSDTVWNEMHSSSAVRMAVGCLVELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFN 837
Cdd:cd10003    71 KPRELNRL----------GKEYDSIYIHPDSYQCALLAAGCVLQVVEAVLTGESRNGVAIVRPPGHHAEQDTACGFCFFN 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  838 SVAITAKLLQQKLSVGKVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYDNGNFFPGS--GAPEEVGGGPGVGYNVNVAW 915
Cdd:cd10003   141 NVAIAARYAQKKYGLKRILIVDWDVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSpeGNYDVVGKGKGEGFNVNIPW 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  916 TGGvdpPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEG 995
Cdd:cd10003   221 NKG---GMGDAEYIAAFQQVVLPIAYEFNPELVLVSAGFDAARG--DPLGGCKVTPEGYAHMTHMLMSLAGGRVIVILEG 295

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 281306754  996 GHDLTAICDASEACVSALLSVELQPLDeavLQQKPSVNAVATLEKVIEIQSKHWSC 1051
Cdd:cd10003   296 GYNLTSISESMSMCTKTLLGDPPPVLD---LPRPPCSSALKSINNVLQVHQKYWKS 348
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
 695-1014 9.66e-128

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: 391.48  E-value: 9.66e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  695 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTllygtsplnrqkldskkllgpisQKMYAMLPCGG 774
Cdd:cd09992     1 HPERPERLLAILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYI-----------------------ERVEETCEAGG 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  775 IGVDSDTVWNEmHSSSAVRMAVGCLVELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLSVGK 854
Cdd:cd09992    58 GYLDPDTYVSP-GSYEAALLAAGAALAAVDAVLSGEAENAFALVRPPGHHAEPDRAMGFCLFNNVAIAARYAQKRYGLKR 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  855 VLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYDngnFFPGSGAPEEVGGGPGVGYNVNVAWTGGvdppIGDVEYLTAFRT 934
Cdd:cd09992   137 VLIVDWDVHHGNGTQDIFYDDPSVLYFSIHQYP---FYPGTGAAEETGGGAGEGFTINVPLPPG----SGDAEYLAAFEE 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  935 VVMPIAHEFSPDVVLVSAGFDAVEGHlsPLGGYSVTARCFGHLTRQLMTLA----GGRVVLALEGGHDLTAICDASEACV 1010
Cdd:cd09992   210 VLLPIAREFQPDLVLVSAGFDAHRGD--PLGGMNLTPEGYARLTRLLKELAdehcGGRLVFVLEGGYNLEALAESVLAVL 287


                  ....
gi 281306754 1011 SALL 1014
Cdd:cd09992   288 EALL 291
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 695-1013 8.30e-113

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: 352.31  E-value: 8.30e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754   695 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSplnrqkldskkllgpiSQKMYAMLPCGG 774
Cdd:pfam00850    1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEA----------------APEGGALLLLSY 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754   775 IGVDSDTVWNEmHSSSAVRMAVGCLVELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLSVGK 854
Cdd:pfam00850   65 LSGDDDTPVSP-GSYEAALLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLKR 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754   855 VLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYDnGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGvdppIGDVEYLTAFRT 934
Cdd:pfam00850  144 VAIVDFDVHHGNGTQEIFYDDPSVLTLSIHQYP-GGFYPGTGFADETGEGKGKGYTLNVPLPPG----TGDAEYLAAFEE 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754   935 VVMPIAHEFSPDVVLVSAGFDAVEGHlsPLGGYSVTARCFGHLTRQLMTLA---GGRVVLALEGGHDLTAICDASEACVS 1011
Cdd:pfam00850  219 ILLPALEEFQPDLILVSAGFDAHAGD--PLGGLNLTTEGFAEITRILLELAdplCIRVVSVLEGGYNLDALARSATAVLA 296


                   ..
gi 281306754  1012 AL 1013
Cdd:pfam00850  297 AL 298
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 695-1015 4.39e-111

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: 348.18  E-value: 4.39e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  695 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYH-TLLYGTSPLNRQKLDSKKllgpisqKMYamlpcg 773
Cdd:cd11600     3 HPEDPSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEHwDRVEATEKMSDEQLKDRT-------EIF------ 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  774 gigvDSDTVWNEMHSSSAVRMAVGCLVELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKL--S 851
Cdd:cd11600    70 ----ERDSLYVNNDTAFCARLSCGGAIEACRAVAEGRVKNAFAVVRPPGHHAEPDESMGFCFFNNVAVAAKWLQTEYpdK 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  852 VGKVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYDNGNFFPGS--GAPEEVGGGPGVGYNVNVAWTggvDPPIGDVEYL 929
Cdd:cd11600   146 IKKILILDWDIHHGNGTQRAFYDDPNVLYISLHRFENGGFYPGTpyGDYESVGEGAGLGFNVNIPWP---QGGMGDADYI 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  930 TAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTAICDASEAC 1009
Cdd:cd11600   223 YAFQRIVMPIAYEFDPDLVIISAGFDAADG--DELGQCHVTPAGYAHMTHMLMSLAGGKLVVALEGGYNLDAISDSALAV 300


                  ....*.
gi 281306754 1010 VSALLS 1015
Cdd:cd11600   301 AKVLLG 306
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
 701-1013 1.06e-98

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: 313.99  E-value: 1.06e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  701 RIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQKLDSKKllgpisqkmyamlpcggiGVDSD 780
Cdd:cd09301     1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKANFAVATITESKP------------------VIFGP 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  781 TVWNEMHSSSAVRMAVGCLVELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKlSVGKVLIVDW 860
Cdd:cd09301    63 NFPVQRHYFRGARLSTGGVVEAAELVAKGELERAFAVVGAGGHHAGKSRAWGFCYFNDVVLAIKFLRER-GISRILIIDT 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  861 DIHHGNGTQQAFYDDPSVLYISLHRYDNGNFFPGSGapeevgggpgVGYNVNVAWTGGvdppIGDVEYLTAFRTVVMPIA 940
Cdd:cd09301   142 DAHHGDGTREAFYDDDRVLHMSFHNYDIYPFGRGKG----------KGYKINVPLEDG----LGDEEYLDAVERVISKVL 207

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281306754  941 HEFSPDVVLVSAGFDAVEGHlsPLGGYSVTARCFGHLTRQLMTLA-GGRVVLALEGGHDLTAICDASEACVSAL 1013
Cdd:cd09301   208 EEFEPEVVVLQFGHDTHEGD--RLGGFNLSEKGFVKLAEIVKEFArGGPILMVLGGGYNPEAAARIWTAIIKEL 279
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 695-1049 1.81e-96

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: 310.01  E-value: 1.81e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  695 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHS-EYHTLLYGTSPLNRQKLDSKkllgpisqkmyamlpCG 773
Cdd:cd10002     7 HIECPERLEAILERLTQDGLLERCVKIPAREAEEDEILLVHSqEYIDLVKSTETMEKEELESL---------------CS 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  774 GIgvdsDTVWNEMHSSSAVRMAVGCLVELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLSVG 853
Cdd:cd10002    72 GY----DSVYLCPSTYEAARLAAGSTIELVKAVMAGKIQNGFALIRPPGHHAMRNEANGYCIFNNVAIAAKYAIEKLGLK 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  854 KVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYDNGNFFP----------GSGApeevgggpGVGYNVNVAW--TGgvdp 921
Cdd:cd10002   148 RILIVDWDVHHGQGTQQGFYEDPRVLYFSIHRYEHGRFWPhlfesdydyiGVGH--------GYGFNVNVPLnqTG---- 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  922 pIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTA 1001
Cdd:cd10002   216 -LGDADYLAIFHHILLPLALEFQPELVLVSAGFDASIG--DPEGEMAVTPAGYAHLTRLLMGLAGGKLLLVLEGGYLLES 292

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 281306754 1002 ICDASEACVSALLSVELQPLDeavlQQKPSVNAVATLEKVIEIQSKHW 1049
Cdd:cd10002   293 LAESVSMTLRGLLGDPLPPLA----PPIPIRSVLETILNAIAHLSPRW 336
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 674-1014 2.12e-92

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 297.79  E-value: 2.12e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  674 TGVVYDTFMLKHQCmcGNTHvhPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHS-EYHTLLYGTSPLNRqk 752
Cdd:COG0123     1 TALIYHPDYLLHDL--GPGH--PEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTpDYVDALRAASLDGG-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  753 ldskkllgpisqkmYAMLpcggigvDSDTVWNEmHSSSAVRMAVGCLVELAFKVAAGELKNGFAIIRPPGHHAEESTAMG 832
Cdd:COG0123    75 --------------YGQL-------DPDTPVSP-GTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMG 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  833 FCFFNSVAITAKLLQQKlSVGKVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYdngNFFPGSGAPEEVGGGPGVGYNVN 912
Cdd:COG0123   133 FCLFNNAAIAARYLLAK-GLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD---PLYPGTGAADETGEGAGEGSNLN 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  913 VAwtggVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLMTLA---GGRV 989
Cdd:COG0123   209 VP----LPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHAD--DPLGRLNLTTEGYAWRTRRVLELAdhcGGPV 282

                         330       340
                  ....*....|....*....|....*
gi 281306754  990 VLALEGGHDLTAICDASEACVSALL 1014
Cdd:COG0123   283 VSVLEGGYNLDALARSVAAHLETLL 307
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
 695-1049 1.24e-79

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: 264.41  E-value: 1.24e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  695 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHS-EYHTLLYGTSPLNRQKLDSkkllgpISQKMyamlpcg 773
Cdd:cd11682     7 FPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSpEYVALMKSTQYMTEEELRT------LADTY------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  774 gigvdsDTVWNEMHSSSAVRMAVGCLVELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLSVG 853
Cdd:cd11682    74 ------DSVYLHPNSYSCACLAVGSVLQLVDKVLGGEIRNGLAIVRPPGHHAQHDKMDGYCMFNNVAIAARYAQQKHGVQ 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  854 KVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYDNGNFFP--GSGAPEEVGGGPGVGYNVNVAWTggvDPPIGDVEYLTA 931
Cdd:cd11682   148 RVLIVDWDVHHGQGTQFIFEQDPSVLYFSIHRYEQGRFWPhlKESDSSAVGFGRGEGYNINVPWN---QVGMRDADYIAA 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  932 FRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTAICDASEACVS 1011
Cdd:cd11682   225 FLHVLLPVALEFQPQLVLVAAGFDAVIG--DPKGEMAATPACFAHLTHLLMGLAGGKLILSLEGGYNLRSLAEGVCASLK 302

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 281306754 1012 ALLSvelQPLDEAVLQQKPSVNAVATLEKVIEIQSKHW 1049
Cdd:cd11682   303 ALLG---DPCPMLESPGAPCRSALASVSCTISALEPFW 337
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
 695-1014 1.89e-77

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: 256.28  E-value: 1.89e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  695 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTllygtsplnrqkldskkllgpisQKMYAMLPCGG 774
Cdd:cd11599     1 HPESPERLEAILDALIASGLDRLLRQLEAPPATREQLLRVHDAAYV-----------------------DRLEAAAPEEG 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  775 IG-VDSDTVWNEmHSSSAVRMAVGCLVELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLSVG 853
Cdd:cd11599    58 LVqLDPDTAMSP-GSLEAALRAAGAVVAAVDAVMAGEARNAFCAVRPPGHHAERDKAMGFCLFNNVAIAAAHALAHHGLE 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  854 KVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYdngNFFPGSGAPEEVGGGpgvgyN-VNVAWTGGVDPPigdvEYLTAF 932
Cdd:cd11599   137 RVAIVDFDVHHGNGTEDIFRDDPRVLFCSSHQH---PLYPGTGAPDETGHG-----NiVNVPLPAGTGGA----EFREAV 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  933 RTVVMPIAHEFSPDVVLVSAGFDAvegHLS-PLGGYSVTARCFGHLTRQLMTLA----GGRVVLALEGGHDLTAICDASE 1007
Cdd:cd11599   205 EDRWLPALDAFKPDLILISAGFDA---HRDdPLAQLNLTEEDYAWITEQLMDVAdrycDGRIVSVLEGGYDLSALARSVA 281


                  ....*..
gi 281306754 1008 ACVSALL 1014
Cdd:cd11599   282 AHVRALM 288
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
 674-1000 8.74e-75

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: 251.71  E-value: 8.74e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  674 TGVVYDTFMLKHQcmcGNTHV--------------HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYH 739
Cdd:cd09996     1 TGFVWDERYLWHD---TGTGAlflpvggllvqpgrHPENPETKRRIKNLLEVSGLSDHLVLITPRPATDEELLRVHTPEY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  740 tllygtspLNRQKLDSKKllgpisqkmyamlpcGGIGVDSDTVWNEmHSSSAVRMAVGCLVELAFKVAAGELKNGFAIIR 819
Cdd:cd09996    78 --------IDRVKAASAA---------------GGGEAGGGTPFGP-GSYEIALLAAGGAIAAVDAVLDGEVDNAYALVR 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  820 PPGHHAEESTAMGFCFFNSVAITAKLLQQKLSVGKVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRydNGNFFPGSGAPE 899
Cdd:cd09996   134 PPGHHAEPDQGMGFCLFNNVAIAARHALAVGGVKRVAVVDWDVHHGNGTQAIFYDDPDVLTISLHQ--DRCFPPDSGAVE 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  900 EVGGGPGVGYNVNVAWtggvdPP-IGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAveGHLSPLGGYSVTARCFGHLT 978
Cdd:cd09996   212 ERGEGAGEGYNLNIPL-----PPgSGDGAYLHAFERIVLPALRAFRPELIIVASGFDA--SAFDPLGRMMLTSDGFRALT 284

                         330       340
                  ....*....|....*....|....*.
gi 281306754  979 RQLMTLA----GGRVVLALEGGHDLT 1000
Cdd:cd09996   285 RKLRDLAdelcGGRLVMVHEGGYSEA 310
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 701-1049 1.67e-66

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: 227.82  E-value: 1.67e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  701 RIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSplnrQKLDSKKLLGpISQKMyamlpcggigvdsD 780
Cdd:cd11683    13 RLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRET----QVMNKEELMA-ISGKY-------------D 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  781 TVWNEMHSSSAVRMAVGCLVELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLSVGKVLIVDW 860
Cdd:cd11683    75 AVYFHPNTFHCARLAAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYAKKKYGLHRILIVDW 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  861 DIHHGNGTQQAFYDDPSVLYISLHRYDNGNFFPG--SGAPEEVGGGPGVGYNVNVAWTggvDPPIGDVEYLTAFRTVVMP 938
Cdd:cd11683   155 DVHHGQGIQYIFEEDPSVLYFSWHRYEHQRFWPFlrESDYDAVGRGKGLGFNINLPWN---KVGMGNADYLAAFFHVLLP 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  939 IAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTAICDASEACVSALLSvel 1018
Cdd:cd11683   232 LAFEFDPELVLVSAGFDSAIG--DPEGQMCATPECFAHLTHLLMVLAGGKLCAVLEGGYHLESLAESVCMTVQTLLG--- 306

                         330       340       350
                  ....*....|....*....|....*....|.
gi 281306754 1019 QPLDEAVLQQKPSVNAVATLEKVIEIQSKHW 1049
Cdd:cd11683   307 DPLPRLSGEMTPCQSALESIQNVRAAQAPYW 337
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
 695-1015 2.58e-55

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: 194.29  E-value: 2.58e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  695 HPEHAGRIQSIWSRLQETGLLskcERIRGRKATLDEIQTVHS-EYHTLLYGtsplnrqkldskkllgpisqkmyamlpcg 773
Cdd:cd10001    25 HPENPERAEAILDALKRAGLG---EVLPPRDFGLEPILAVHDpDYVDFLET----------------------------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  774 gigVDSDTVWNEmHSSSAVRMAVGCLVELAFKVAAGElKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKlsVG 853
Cdd:cd10001    73 ---ADTDTPISE-GTWEAALAAADTALTAADLVLEGE-RAAYALCRPPGHHAGRDRAGGFCYFNNAAIAAQYLRDR--AG 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  854 KVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRyDNGNFFP---------GSGApeevgggpGVGYNVNVAwtggVDPPIG 924
Cdd:cd10001   146 RVAILDVDVHHGNGTQEIFYERPDVLYVSIHG-DPRTFYPfflgfadetGEGE--------GEGYNLNLP----LPPGTG 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  925 DVEYLTAFRTVVMPIAhEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLMTLaGGRVVLALEGGHDLTAIcd 1004
Cdd:cd10001   213 DDDYLAALDEALAAIA-AFGPDALVVSLGFDTHEG--DPLSDFKLTTEDYARIGRRIAAL-GLPTVFVQEGGYNVDAL-- 286

                         330
                  ....*....|.
gi 281306754 1005 asEACVSALLS 1015
Cdd:cd10001   287 --GRNAVAFLA 295
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
 695-999 5.99e-43

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: 159.26  E-value: 5.99e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  695 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHS-EYHTLLYGTSPlNRQKLDSKKLlgpisqkmyamlpcg 773
Cdd:cd09994    17 HPFNPPRLSLTKDLLRALGLLPPVDLVPPRPATEEELLLFHTpDYIEAVKEASR-GQEPEGRGRL--------------- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  774 GIGVDSDTVWNEMHSSSAvrMAVGCLVELAFKVAAGELKNGFAIIrppG--HHAEESTAMGFCFFNSVAITAKLLQQKlS 851
Cdd:cd09994    81 GLGTEDNPVFPGMHEAAA--LVVGGTLLAARLVLEGEARRAFNPA---GglHHAMRGRASGFCVYNDAAVAIERLRDK-G 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  852 VGKVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRyDNGNFFPGSGAPEEVGGGPGVGYNVNVAwtggVDPPIGDVEYLTA 931
Cdd:cd09994   155 GLRVAYVDIDAHHGDGVQAAFYDDPRVLTISLHE-SGRYLFPGTGFVDEIGEGEGYGYAVNIP----LPPGTGDDEFLRA 229

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281306754  932 FRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLMTLA----GGRVVLALEGGHDL 999
Cdd:cd09994   230 FEAVVPPLLRAFRPDVIVSQHGADAHAG--DPLTHLNLSNRAYRAAVRRIRELAdeycGGRWLALGGGGYNP 299
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 688-1003 9.44e-29

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: 119.37  E-value: 9.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  688 MCGNTHVHPEHAGRIQSIwsrLQETGLLSKCERIRGRKATLDEIQTVHS-EYHTLLYGTSplnrQKLDSkkllgpisQKM 766
Cdd:cd10000    12 LCDRLPKVPNRASMVHSL---IEAYGLLKQLRVVKPRVATEEELASFHSdEYIQFLKKAS----NEGDN--------DEE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  767 YAMLPCGGIGVDSDTVWNEMhssSAVRMAVGCLVELAFKVAAGELKngFAIIRPPG-HHAEESTAMGFCFFNSVAITAKL 845
Cdd:cd10000    77 PSEQQEFGLGYDCPIFEGIY---DYAAAVAGATLTAAQLLIDGKCK--VAINWFGGwHHAQRDEASGFCYVNDIVLGILK 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  846 LQQKLSvgKVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYDNGnFFPGSGAPEEVGGGPGVGYNVNVAWTGGVDppigD 925
Cdd:cd10000   152 LREKFD--RVLYVDLDLHHGDGVEDAFSFTSKVMTVSLHKYSPG-FFPGTGDVSDVGLGKGKYYTVNVPLRDGIQ----D 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  926 VEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVT----ARCFGH-LTRQLMTL-AGGrvvlaleGGHDL 999
Cdd:cd10000   225 EQYLQIFTAVVPEIVAAFRPEAVVLQCGADTLAG--DPMGAFNLTpvgiGKCLKYvLGWKLPTLiLGG-------GGYNL 295


                  ....*.
gi 281306754 1000 --TAIC 1003
Cdd:cd10000   296 anTARC 301
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 705-987 1.31e-28

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: 116.44  E-value: 1.31e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  705 IWSRLQETGLLSKCERIRGRKATLDEIQTVHS-EY-HTLLYGTSPLNRQKLdskkllgpisqkmyAMLPcggigvdsdtv 782
Cdd:cd09993    11 LREALLEEGLVLPEDIVEPEPATREDLLRVHDpEYlESLKSGELSREEIRR--------------IGFP----------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  783 WNEmHSSSAVRMAVGCLVeLAFKVAageLKNGFAIiRPPG--HHAEESTAMGFCFFNSVAITAKLLQQKLSVGKVLIVDW 860
Cdd:cd09993    66 WSP-ELVERTRLAVGGTI-LAARLA---LEHGLAI-NLAGgtHHAFPDRGEGFCVFNDIAIAARVLLAEGLVRRVLIVDL 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  861 DIHHGNGTQQAFYDDPSVLYISLHrydNGNFFPGSGAPEevgggpgvgyNVNVawtgGVDPPIGDVEYLTAFRTVVMPIA 940
Cdd:cd09993   140 DVHQGNGTAAIFADDPSVFTFSMH---GEKNYPFRKEPS----------DLDV----PLPDGTGDDEYLAALEEALPRLL 202

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 281306754  941 HEFSPDVVLVSAGFDAVEGhlSPLGGYSVT-----AR-------CFGHLTRQLMTLAGG 987
Cdd:cd09993   203 AEFRPDLVFYNAGVDVLAG--DRLGRLSLSleglrERdrlvlrfARARGIPVAMVLGGG 259
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
 823-1003 1.86e-26

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: 110.82  E-value: 1.86e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  823 HHAEESTAMGFCFFNSVAITAKLLQQKlSVGKVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYDNGnFFPGSGApeevG 902
Cdd:cd11680   115 HHAQKSRASGFCYVNDIVLAILRLRRA-RFRRVFYLDLDLHHGDGVESAFFFSKNVLTCSIHRYDPG-FFPGTGS----L 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  903 GGPGVGYNVNVAWTGGVDppigDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLM 982
Cdd:cd11680   189 KNSSDKGMLNIPLKRGLS----DKTLLRIIDSIVRPLIEKFEPEVIVIQCGCDGLSG--DPHKEWNLTIRGYGSVIELLL 262

                         170       180
                  ....*....|....*....|....
gi 281306754  983 TLAGGRVVLALEGG---HDLTAIC 1003
Cdd:cd11680   263 KEFKDKPTLLLGGGgynHTEAARA 286
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
 688-987 6.32e-25

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: 106.51  E-value: 6.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  688 MCGNTHV---HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHS-EYHTLLYGTSPLNRQKLdsKKLLgpis 763
Cdd:cd09991     5 DVGNYYYgqgHPMKPHRIRMTHSLILSYGLYKKMEIYRPRPATAEELTKFHSdDYIDFLRSVSPDNMKEF--KKQL---- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  764 qKMYamlpcgGIGVDSdTVWNEMHSssAVRMAVGCLVELAFKVAAGELKNGfaiIRPPG--HHAEESTAMGFCFFNSV-- 839
Cdd:cd09991    79 -ERF------NVGEDC-PVFDGLYE--YCQLYAGGSIAAAVKLNRGQADIA---INWAGglHHAKKSEASGFCYVNDIvl 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  840 AITaKLLQQKlsvGKVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYdnGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGV 919
Cdd:cd09991   146 AIL-ELLKYH---QRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKF--GEYFFPGTGLRDIGAGKGKYYAVNVPLKDGI 219

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281306754  920 DppigDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVT----ARCFGHLTR---QLMTLAGG 987
Cdd:cd09991   220 D----DESYLQIFEPVLSKVMEVFQPSAVVLQCGADSLAG--DRLGCFNLSikghAKCVKFVKSfniPLLVLGGG 288
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 786-1013 4.05e-24

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: 101.68  E-value: 4.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  786 MHSSSAVRMAVGCLVELAFKVaagelKNGFAIIrppGHHAEestamgfcfFNSVAITAKLLQqklsvGKVLIVDWDIHHG 865
Cdd:cd09987     5 IRKAEAHELLAGVVVAVLKDG-----KVPVVLG---GDHSI---------ANGAIRAVAELH-----PDLGVIDVDAHHD 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  866 NGTQQAFYD--------------DPSVLYISLHRYDNGNFFPGsgapeevgGGPGVGYNVNVAWTGGVDppigDVEYLTA 931
Cdd:cd09987    63 VRTPEAFGKgnhhtprhllceplISDVHIVSIGIRGVSNGEAG--------GAYARKLGVVYFSMTEVD----KLGLGDV 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  932 FRTVVMPIahEFSPDVVLVSAGFDAVEGHLSP----LGGYSVTARCFGHLTRQLMTLaGGRVVLALEGGHDL----TAIC 1003
Cdd:cd09987   131 FEEIVSYL--GDKGDNVYLSVDVDGLDPSFAPgtgtPGPGGLSYREGLYITERIAKT-NLVVGLDIVEVNPLldetGRTA 207

                         250
                  ....*....|
gi 281306754 1004 DASEACVSAL 1013
Cdd:cd09987   208 RLAAALTLEL 217
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
 724-979 1.60e-23

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: 102.53  E-value: 1.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  724 RKATLDEIQTVHSE-YHTLLYGTSPLNRQKLDSKKL----LG---PISQKMYAMLpcggigvdsdtvwnemhsssavRMA 795
Cdd:cd11598    47 RAATREELRQFHDAdYLDFLSKVSPENANQLRFDKAepfnIGddcPVFDGMYDYC----------------------QLY 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  796 VGCLVELAFKVAAGelKNGFAIIRPPG-HHAEESTAMGFCFFNSVAITakLLQQKLSVGKVLIVDWDIHHGNGTQQAFYD 874
Cdd:cd11598   105 AGASLDAARKLCSG--QSDIAINWSGGlHHAKKSEASGFCYVNDIVLA--ILNLLRYFPRVLYIDIDVHHGDGVEEAFYR 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  875 DPSVLYISLHRYdNGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGvdppIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGF 954
Cdd:cd11598   181 TDRVMTLSFHKY-NGEFFPGTGDLDDNGGTPGKHFALNVPLEDG----IDDEQYNLLFKSIIGPTIEKFQPSAIVLQCGA 255

                         250       260
                  ....*....|....*....|....*
gi 281306754  955 DAVEGhlSPLGGYSVTARCFGHLTR 979
Cdd:cd11598   256 DSLGG--DRLGQFNLNIKAHGACVK 278
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
 690-976 2.16e-21

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: 97.57  E-value: 2.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  690 GNTHV---HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHS-EYHTLLYGTSPLNR---QKLDSKKLLG-- 760
Cdd:cd10004    13 GNYAYgpgHPMKPHRIRMAHSLVMNYGLYKKMEIYRAKPATKNEMTQFHTdEYIDFLSRVTPDNMekfQKEQVKYNVGdd 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  761 -PISQKMYAMlpCGGIGVDSDTVWNEMHSSSAvrmavgclvELAFKVAAGElkngfaiirppgHHAEESTAMGFCFFNSV 839
Cdd:cd10004    93 cPVFDGLFEF--CSISAGGSMEGAARLNRGKC---------DIAVNWAGGL------------HHAKKSEASGFCYVNDI 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  840 AITA-KLLQQKlsvGKVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYdnGNFFPGSGAPEEVGGGPGVGYNVNVAWTGG 918
Cdd:cd10004   150 VLGIlELLRYH---QRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKY--GEYFPGTGELRDIGIGTGKNYAVNVPLRDG 224

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 281306754  919 VDppigDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARcfGH 976
Cdd:cd10004   225 ID----DESYKSIFEPVIKHVMEWYQPEAVVLQCGGDSLSG--DRLGCFNLSMK--GH 274
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
 695-976 2.23e-20

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: 94.36  E-value: 2.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  695 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSE-YHTLLYGTSPLNRQKLdSKKL----LG---PISQKM 766
Cdd:cd10010    25 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDdYIKFLRSIRPDNMSEY-SKQMqrfnVGedcPVFDGL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  767 Y--AMLPCGGiGVDSDTVWNEMHSSSAVRMAVGClvelafkvaagelkngfaiirppgHHAEESTAMGFCFFNSVAITak 844
Cdd:cd10010   104 FefCQLSAGG-SVASAVKLNKQQTDIAVNWAGGL------------------------HHAKKSEASGFCYVNDIVLA-- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  845 LLQQKLSVGKVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYdnGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGVDppig 924
Cdd:cd10010   157 ILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKY--GEYFPGTGDLRDIGAGKGKYYAVNYPLRDGID---- 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 281306754  925 DVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARcfGH 976
Cdd:cd10010   231 DESYEAIFKPVMSKVMEMFQPSAVVLQCGADSLSG--DRLGCFNLTIK--GH 278
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
 788-1013 2.86e-20

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: 93.67  E-value: 2.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  788 SSSAVRMAVGCL---VELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLSVGKVLIVDWDIHH 864
Cdd:cd09998    82 SLDAIQGALGAVceaVDSVFKPESPGTKRAFVAIRPPGHHCSESTPSGFCWVNNVHVGAAHAYLTHGITRVVILDIDLHH 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  865 GNGTQ------------------------QAFYDDPSVLYISLHrydNGNFFP---GSGAPEEVGggpgvgyNVNVA--- 914
Cdd:cd09998   162 GNGTQdiawrinaeankqalesssyddfkPAGAPGLRIFYSSLH---DINSFPcedGDPAKVKDA-------SVSIDgah 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  915 ----WTGGVDPPIGDVEYLTAFR---TVVMPIAHEF-------SPD--VVLVSAGFDAVEGHLSPLGGYS--VTARCFGH 976
Cdd:cd09998   232 gqwiWNVHLQPWTTEEDFWELYYpkyRILFEKAAEFlrlttaaTPFktLVFISAGFDASEHEYESMQRHGvnVPTSFYYR 311

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 281306754  977 LTRQLMTLA----GGRVVLALEGGHDLTAICDASEACVSAL 1013
Cdd:cd09998   312 FARDAVRFAdahaHGRLISVLEGGYSDRALCSGVLAHLTGL 352
PTZ00063 PTZ00063
histone deacetylase; Provisional
 823-987 1.63e-19

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 92.57  E-value: 1.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  823 HHAEESTAMGFCFFNSVAI-TAKLLQQKlsvGKVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYdnGNFFPGSGAPEEV 901
Cdd:PTZ00063  137 HHAKRSEASGFCYINDIVLgILELLKYH---ARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFPGTGDVTDI 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  902 GGGPGVGYNVNVAWTGGVDppigDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVT----ARCFGH- 976
Cdd:PTZ00063  212 GVAQGKYYSVNVPLNDGID----DDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTG--DRLGRFNLTikghAACVEFv 285

                         170
                  ....*....|...
gi 281306754  977 --LTRQLMTLAGG 987
Cdd:PTZ00063  286 rsLNIPLLVLGGG 298
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
 823-978 5.92e-19

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: 90.15  E-value: 5.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  823 HHAEESTAMGFCFFNSVAITA-KLLQQKlsvGKVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYDNgNFFPGSGAPEEV 901
Cdd:cd10005   132 HHAKKFEASGFCYVNDIVIAIlELLKYH---PRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGN-YFFPGTGDMYEV 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  902 GGGPGVGYNVNVAWTGGVDppigDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDA------------VEGHLS------- 962
Cdd:cd10005   208 GAESGRYYSVNVPLKDGID----DQSYLQLFKPVIQQVIDFYQPTCIVLQCGADSlgcdrlgcfnlsIKGHGEcvefvks 283

                         170       180
                  ....*....|....*....|....*.
gi 281306754  963 ---PL-----GGYSV--TARCFGHLT 978
Cdd:cd10005   284 fniPLlvlggGGYTVrnVARCWTYET 309
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
 695-976 2.88e-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: 85.11  E-value: 2.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  695 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHS-EYHTLLYGTSPLNRQKLdSKKL----LG---PISQKM 766
Cdd:cd10011    21 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSdEYIKFLRSIRPDNMSEY-SKQMqrfnVGedcPVFDGL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  767 Y--AMLPCGGiGVDSDTVWNEMHSSSAVRMAVGClvelafkvaagelkngfaiirppgHHAEESTAMGFCFFNSVAITak 844
Cdd:cd10011   100 FefCQLSTGG-SVAGAVKLNRQQTDMAVNWAGGL------------------------HHAKKSEASGFCYVNDIVLA-- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  845 LLQQKLSVGKVLIVDWDIHHGNGTQQAFYDDPSVLYISlhRYDNGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGVDppig 924
Cdd:cd10011   153 ILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVS--FHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGID---- 226

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 281306754  925 DVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARcfGH 976
Cdd:cd10011   227 DESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSG--DRLGCFNLTVK--GH 274
PTZ00346 PTZ00346
histone deacetylase; Provisional
 823-996 2.40e-13

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 73.53  E-value: 2.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  823 HHAEESTAMGFCFFNSVAItaKLLQQKLSVGKVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYDNgNFFPGSGAPEEVG 902
Cdd:PTZ00346  154 HHSKCGECSGFCYVNDIVL--GILELLKCHDRVLYVDIDMHHGDGVDEAFCTSDRVFTLSLHKFGE-SFFPGTGHPRDVG 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754  903 GGPGVGYNVNVA-WTGgvdppIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQL 981
Cdd:PTZ00346  231 YGRGRYYSMNLAvWDG-----ITDFYYLGLFEHALHSIVRRYSPDAIVLQCGADSLAG--DRLGLLNLSSFGHGQCVQAV 303

                         170
                  ....*....|....*
gi 281306754  982 MTLagGRVVLALEGG 996
Cdd:PTZ00346  304 RDL--GIPMLALGGG 316
ClassIIa_HDAC5_Gln-rich-N cd10164
Glutamine-rich N-terminal helical domain of HDAC5, a Class IIa histone deacetylase; This ...
 68-155 1.54e-09

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: 55.99  E-value: 1.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754   68 DPALREQQLQQELLVLKQQQQLQKQLLFAEFQKQHDHLTRQHEV---------QLQKHLKQQQEMLAAKRQQELEQQRQR 138
Cdd:cd10164     1 DPSLREQQLQQELLLLKQQQQLQKQLLFAEFQKQHEHLTRQHEVqlqkhlkvrAELFSEQQQQEILAAKRQQELEQQRKR 80

                          90
                  ....*....|....*..
gi 281306754  139 EQQRQEELEKQRLEQQL 155
Cdd:cd10164    81 EQQRQEELEKQRLEQQL 97
ClassIIa_HDAC_Gln-rich-N cd10149
Glutamine-rich N-terminal helical domain of various Class IIa histone deacetylases (HDAC4, ...
 68-155 6.95e-08

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: 51.23  E-value: 6.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754   68 DPALREQQLQQELLVLKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKRQQ--ELEQQRQREQQRQEE 145
Cdd:cd10149     1 DPVLREQQLQQELLALKQQQQIQKQLLIAEFQKQHENLTRQHEAQLQEHIKQQQEMLAIKQQQelLEKQRKLEQQRQEQE 80

                          90
                  ....*....|
gi 281306754  146 LEKQRLEQQL 155
Cdd:cd10149    81 LEKQRREQQL 90
HDAC4_Gln pfam12203
Glutamine rich N terminal domain of histone deacetylase 4; This domain is found in eukaryotes, ...
 95-155 1.07e-03

Glutamine rich N terminal domain of histone deacetylase 4; This domain is found in eukaryotes, and is approximately 90 amino acids in length. The family is found in association with pfam00850. The domain forms an alpha helix which complexes to form a tetramer. The glutamine rich domains have many intra- and inter-helical interactions which are thought to be involved in reversible assembly and disassembly of proteins. The domain is part of histone deacetylase 4 (HDAC4) which removes acetyl groups from histones. This restores their positive charge to allow stronger DNA binding thus restricting transcriptional activity.


Pssm-ID: 403429 [Multi-domain]  Cd Length: 91  Bit Score: 39.45  E-value: 1.07e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281306754    95 FAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKRQQELEQQ--RQREQQRQEELEKQRLEQQL 155
Cdd:pfam12203   29 IAEFQKQHELLTRQHEAQLQEHIKQQQELLAMKQQQELLEQqrKLEQQRQEEELEKHRREQQL 91
ClassIIa_HDAC9_Gln-rich-N cd10163
Glutamine-rich N-terminal helical domain of HDAC9, a Class IIa histone deacetylase; This ...
 96-127 5.24e-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: 37.43  E-value: 5.24e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 281306754   96 AEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAK 127
Cdd:cd10163    29 AEFQKQHENLTRQHQAQLQEHLKLQQELLAMK 60
ClassIIa_HDAC4_Gln-rich-N cd10162
Glutamine-rich N-terminal helical domain of HDAC4, a Class IIa histone deacetylase; This ...
 68-127 6.95e-03

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: 37.10  E-value: 6.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 281306754   68 DPALREQQLQQELLVLKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAK 127
Cdd:cd10162     1 EPALREQQLQQELLALKQKQQIQRQLLIAEFQRQHEQLSRQHEAQLHEHIKQQQELLAMK 60
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH