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Conserved domains on  [gi|62750349|ref|NP_001015053|]
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histone deacetylase 5 isoform 3 [Homo sapiens]

Protein Classification

histone deacetylase 5( domain architecture ID 10178376)

histone deacetylase 5 (HD5) 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)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
 680-1096 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: 892.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  680 HLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLN 759
Cdd:cd10007    1 HLFTTGLVYDTFMLKHQCTCGNTNVHPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHSEHHTLLYGTSPLN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  760 RQKLDSKKLLGPISQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEEST 839
Cdd:cd10007   81 RQKLDSKKLLGPLSQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLIELAFKVAAGELKNGFAVIRPPGHHAEEST 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  840 AMGFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGY 919
Cdd:cd10007  161 AMGFCFFNSVAIAAKLLQQKLNVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGNFFPGSGAPDEVGAGPGVGF 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  920 NVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRV 999
Cdd:cd10007  241 NVNIAWTGGVDPPIGDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGHQSPLGGYSVTAKCFGHLTKQLMTLAGGRV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349 1000 VLALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPNINAVATLEKVIEIQSKHWSCVQKFAAGLGRSLREAQAG 1079
Cdd:cd10007  321 VLALEGGHDLTAICDASEACVSALLGMELTPLDNTVLQQKPNDNAVATLERVIEIQSKHWSCLKRFAATLGFSLLEAQRG 400

                        410
                 ....*....|....*..
gi 62750349 1080 ETEEAETVSAMALLSVG 1096
Cdd:cd10007  401 ELEEAETVSAMASLSVD 417
ClassIIa_HDAC5_Gln-rich-N cd10164
Glutamine-rich N-terminal helical domain of HDAC5, a Class IIa histone deacetylase; This ...
 69-165 1.80e-16

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: 76.02  E-value: 1.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349   69 DPTLREQQLQQELLALKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEMLAAKRQQELEQQRQR 148
Cdd:cd10164    1 DPSLREQQLQQELLLLKQQQQLQKQLLFAEFQKQHEHLTRQHEVQLQKHLKVRAELFSEQQQQEILAAKRQQELEQQRKR 80

                         90
                 ....*....|....*..
gi 62750349  149 EQQRQEELEKQRLEQQL 165
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 ...
 680-1096 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: 892.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  680 HLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLN 759
Cdd:cd10007    1 HLFTTGLVYDTFMLKHQCTCGNTNVHPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHSEHHTLLYGTSPLN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  760 RQKLDSKKLLGPISQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEEST 839
Cdd:cd10007   81 RQKLDSKKLLGPLSQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLIELAFKVAAGELKNGFAVIRPPGHHAEEST 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  840 AMGFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGY 919
Cdd:cd10007  161 AMGFCFFNSVAIAAKLLQQKLNVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGNFFPGSGAPDEVGAGPGVGF 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  920 NVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRV 999
Cdd:cd10007  241 NVNIAWTGGVDPPIGDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGHQSPLGGYSVTAKCFGHLTKQLMTLAGGRV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349 1000 VLALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPNINAVATLEKVIEIQSKHWSCVQKFAAGLGRSLREAQAG 1079
Cdd:cd10007  321 VLALEGGHDLTAICDASEACVSALLGMELTPLDNTVLQQKPNDNAVATLERVIEIQSKHWSCLKRFAATLGFSLLEAQRG 400

                        410
                 ....*....|....*..
gi 62750349 1080 ETEEAETVSAMALLSVG 1096
Cdd:cd10007  401 ELEEAETVSAMASLSVD 417
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 705-1023 4.21e-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: 353.08  E-value: 4.21e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349    705 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQKLDSKKLLGpisqkmyavlpcgg 784
Cdd:pfam00850    1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAAPEGGALLLLSYLS-------------- 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349    785 igvDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVGK 864
Cdd:pfam00850   67 ---GDDDTPVSPGSYEAALLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLKR 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349    865 VLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDnGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGvdppIGDVEYLTAFRT 944
Cdd:pfam00850  144 VAIVDFDVHHGNGTQEIFYDDPSVLTLSIHQYP-GGFYPGTGFADETGEGKGKGYTLNVPLPPG----TGDAEYLAAFEE 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349    945 VVMPIAHEFSPDVVLVSAGFDAVEGHlsPLGGYSVTARCFGHLTRQLMTLA---GGRVVLALEGGHDLTAICDASEACVS 1021
Cdd:pfam00850  219 ILLPALEEFQPDLILVSAGFDAHAGD--PLGGLNLTTEGFAEITRILLELAdplCIRVVSVLEGGYNLDALARSATAVLA 296


                   ..
gi 62750349   1022 AL 1023
Cdd:pfam00850  297 AL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 684-1024 6.12e-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: 297.02  E-value: 6.12e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  684 TGVVYDTFMLKHQCmcGNTHvhPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHtllygtsplnrqkL 763
Cdd:COG0123    1 TALIYHPDYLLHDL--GPGH--PEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDY-------------V 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  764 DskkllgpisqKMYAVLPCGGIG-VDSDTVWNEmHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMG 842
Cdd:COG0123   64 D----------ALRAASLDGGYGqLDPDTPVSP-GTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMG 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  843 FCFFNSVAITAKLLQQKlNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYdngNFFPGSGAPEEVGGGPGVGYNVN 922
Cdd:COG0123  133 FCLFNNAAIAARYLLAK-GLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD---PLYPGTGAADETGEGAGEGSNLN 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  923 VAwtggVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLMTLA---GGRV 999
Cdd:COG0123  209 VP----LPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHAD--DPLGRLNLTTEGYAWRTRRVLELAdhcGGPV 282

                        330       340
                 ....*....|....*....|....*
gi 62750349 1000 VLALEGGHDLTAICDASEACVSALL 1024
Cdd:COG0123  283 VSVLEGGYNLDALARSVAAHLETLL 307
PTZ00063 PTZ00063
histone deacetylase; Provisional
 833-997 1.58e-19

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 92.95  E-value: 1.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349   833 HHAEESTAMGFCFFNSVAI-TAKLLQQKlnvGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYdnGNFFPGSGAPEEV 911
Cdd:PTZ00063  137 HHAKRSEASGFCYINDIVLgILELLKYH---ARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFPGTGDVTDI 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349   912 GGGPGVGYNVNVAWTGGVDppigDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVT----ARCFGH- 986
Cdd:PTZ00063  212 GVAQGKYYSVNVPLNDGID----DDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTG--DRLGRFNLTikghAACVEFv 285

                         170
                  ....*....|...
gi 62750349   987 --LTRQLMTLAGG 997
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 ...
 69-165 1.80e-16

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: 76.02  E-value: 1.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349   69 DPTLREQQLQQELLALKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEMLAAKRQQELEQQRQR 148
Cdd:cd10164    1 DPSLREQQLQQELLLLKQQQQLQKQLLFAEFQKQHEHLTRQHEVQLQKHLKVRAELFSEQQQQEILAAKRQQELEQQRKR 80

                         90
                 ....*....|....*..
gi 62750349  149 EQQRQEELEKQRLEQQL 165
Cdd:cd10164   81 EQQRQEELEKQRLEQQL 97
HDAC4_Gln pfam12203
Glutamine rich N terminal domain of histone deacetylase 4; This domain is found in eukaryotes, ...
 96-165 4.00e-07

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: 49.08  E-value: 4.00e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349     96 FAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEMLAAKrqqeleqQRQREQQRQEELEKQRLEQQL 165
Cdd:pfam12203   29 IAEFQKQHELLTRQHEAQLQEHIKQQQELLAMKQQQELLEQQ-------RKLEQQRQEEELEKHRREQQL 91
 
Name Accession Description Interval E-value
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
 680-1096 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: 892.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  680 HLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLN 759
Cdd:cd10007    1 HLFTTGLVYDTFMLKHQCTCGNTNVHPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHSEHHTLLYGTSPLN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  760 RQKLDSKKLLGPISQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEEST 839
Cdd:cd10007   81 RQKLDSKKLLGPLSQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLIELAFKVAAGELKNGFAVIRPPGHHAEEST 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  840 AMGFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGY 919
Cdd:cd10007  161 AMGFCFFNSVAIAAKLLQQKLNVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGNFFPGSGAPDEVGAGPGVGF 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  920 NVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRV 999
Cdd:cd10007  241 NVNIAWTGGVDPPIGDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGHQSPLGGYSVTAKCFGHLTKQLMTLAGGRV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349 1000 VLALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPNINAVATLEKVIEIQSKHWSCVQKFAAGLGRSLREAQAG 1079
Cdd:cd10007  321 VLALEGGHDLTAICDASEACVSALLGMELTPLDNTVLQQKPNDNAVATLERVIEIQSKHWSCLKRFAATLGFSLLEAQRG 400

                        410
                 ....*....|....*..
gi 62750349 1080 ETEEAETVSAMALLSVG 1096
Cdd:cd10007  401 ELEEAETVSAMASLSVD 417
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 682-1059 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: 757.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  682 FTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQ 761
Cdd:cd11681    1 FTTGLAYDPLMLKHQCICGNNSSHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTLLYGTNPLSRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  762 KLDSKKLLGpISQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAM 841
Cdd:cd11681   81 KLDPTKLAG-LPQKSFVRLPCGGIGVDSDTVWNELHTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQAM 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  842 GFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGYNV 921
Cdd:cd11681  160 GFCFFNSVAIAAKQLQQKLKLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFPGTGAPTEVGSGAGEGFNV 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  922 NVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRVVL 1001
Cdd:cd11681  240 NIAWSGGLDPPMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPPPLGGYKVSPACFGYMTRQLMNLAGGKVVL 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 62750349 1002 ALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPNINAVATLEKVIEIQSKHW 1059
Cdd:cd11681  320 ALEGGYDLTAICDASEACVRALLGDELDPLSEEELERRPNPNAVTSLEKVIAIQSPYW 377
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
 679-1088 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: 745.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  679 KHLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPL 758
Cdd:cd10006    1 KPRFTTGLVYDTLMLKHQCTCGNSNSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  759 NRQKLDSKKLLGPISQkMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEES 838
Cdd:cd10006   81 NRQKLDSKKLLGSLAS-VFVRLPCGGVGVDSDTIWNEVHSSGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEES 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  839 TAMGFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVG 918
Cdd:cd10006  160 TPMGFCYFNSVAIAAKLLQQRLNVSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  919 YNVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGR 998
Cdd:cd10006  240 FNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSAKCFGYLTKQLMGLAGGR 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  999 VVLALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPNINAVATLEKVIEIQSKHWSCVQKFAAGLGRSLREAQA 1078
Cdd:cd10006  320 IVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGYSLIEAQT 399

                        410
                 ....*....|
gi 62750349 1079 GETEEAETVS 1088
Cdd:cd10006  400 CENEEAETVT 409
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
 682-1059 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 62750349  682 FTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQ 761
Cdd:cd10008    1 FTTGLVYDSVMLKHQCSCGDNSNHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  762 KLDSKKLLGPISQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAM 841
Cdd:cd10008   81 KLDNGKLAGLLAQRMFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  842 GFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGYNV 921
Cdd:cd10008  161 GFCFFNSVAIACRQLQQQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGAGSGEGFNV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  922 NVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRVVL 1001
Cdd:cd10008  241 NVAWAGGLDPPMGDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVL 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 62750349 1002 ALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPNINAVATLEKVIEIQSKHW 1059
Cdd:cd10008  321 ALEGGHDLTAICDASEACVAALLGNEVDPLSEESWKQKPNLNAIRSLEAVIRVHSKYW 378
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
 682-1059 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: 647.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  682 FTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQ 761
Cdd:cd10009    1 SATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  762 KLDSKKLLGPISQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAM 841
Cdd:cd10009   81 KLDPRILLGDDSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  842 GFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGYNV 921
Cdd:cd10009  161 GFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYNI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  922 NVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRVVL 1001
Cdd:cd10009  241 NIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVL 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 62750349 1002 ALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPNINAVATLEKVIEIQSKHW 1059
Cdd:cd10009  321 ALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSKYW 378
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
 688-1061 1.21e-129

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: 1.21e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  688 YDTFMLKHQCMCgNTHvHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHtllygtspLNRQKLDSKK 767
Cdd:cd10003    1 YDQRMMNHHNLW-DPG-HPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEH--------LDEMKSLEKM 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  768 LLGPISQKmyavlpcggiGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFN 847
Cdd:cd10003   71 KPRELNRL----------GKEYDSIYIHPDSYQCALLAAGCVLQVVEAVLTGESRNGVAIVRPPGHHAEQDTACGFCFFN 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  848 SVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGS--GAPEEVGGGPGVGYNVNVAW 925
Cdd:cd10003  141 NVAIAARYAQKKYGLKRILIVDWDVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSpeGNYDVVGKGKGEGFNVNIPW 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  926 TGGvdpPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEG 1005
Cdd:cd10003  221 NKG---GMGDAEYIAAFQQVVLPIAYEFNPELVLVSAGFDAARG--DPLGGCKVTPEGYAHMTHMLMSLAGGRVIVILEG 295

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 62750349 1006 GHDLTAICDASEACVSALLSVELQPLDeavLQQKPNINAVATLEKVIEIQSKHWSC 1061
Cdd:cd10003  296 GYNLTSISESMSMCTKTLLGDPPPVLD---LPRPPCSSALKSINNVLQVHQKYWKS 348
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
 705-1024 2.23e-127

Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues of histones (EC 3.5.1.98) and possibly other proteins to yield deacetylated histones/other proteins. This group includes animal HDAC4,5,6,7,8,9,10, fungal HOS3 and HDA1, plant HDA5 and HDA15 as well as other eukaryotes, archaeal and bacterial histone-like deacetylases. Eukaryotic deacetylases mostly use histones (H2, H3, H4) as substrates for deacetylation; however, non-histone substrates are known (for example, tubulin). Substrates for prokaryotic histone-like deacetylases are not known. Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. Interaction partners of class II deacetylases include 14-3-3 proteins, MEF2 family of transcriptional factors, CtBP, calmodulin (CaM), SMRT, N-CoR, BCL6, HP1alpha and SUMO. Histone deacetylases play a role in the regulation of cell cycle, cell differentiation and survival. Class II mammalian HDACs are differentially inhibited by structurally diverse compounds with known antitumor activities, thus presenting them as potential drug targets for human diseases resulting from aberrant acetylation.


Pssm-ID: 212518 [Multi-domain]  Cd Length: 291  Bit Score: 390.71  E-value: 2.23e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  705 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTllygtsplnrqkldskkllgpisQKMYAVLPCGG 784
Cdd:cd09992    1 HPERPERLLAILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYI-----------------------ERVEETCEAGG 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  785 IGVDSDTVWNEmHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVGK 864
Cdd:cd09992   58 GYLDPDTYVSP-GSYEAALLAAGAALAAVDAVLSGEAENAFALVRPPGHHAEPDRAMGFCLFNNVAIAARYAQKRYGLKR 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  865 VLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDngnFFPGSGAPEEVGGGPGVGYNVNVAWTGGvdppIGDVEYLTAFRT 944
Cdd:cd09992  137 VLIVDWDVHHGNGTQDIFYDDPSVLYFSIHQYP---FYPGTGAAEETGGGAGEGFTINVPLPPG----SGDAEYLAAFEE 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  945 VVMPIAHEFSPDVVLVSAGFDAVEGHlsPLGGYSVTARCFGHLTRQLMTLA----GGRVVLALEGGHDLTAICDASEACV 1020
Cdd:cd09992  210 VLLPIAREFQPDLVLVSAGFDAHRGD--PLGGMNLTPEGYARLTRLLKELAdehcGGRLVFVLEGGYNLEALAESVLAVL 287


                 ....
gi 62750349 1021 SALL 1024
Cdd:cd09992  288 EALL 291
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 705-1023 4.21e-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: 353.08  E-value: 4.21e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349    705 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQKLDSKKLLGpisqkmyavlpcgg 784
Cdd:pfam00850    1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAAPEGGALLLLSYLS-------------- 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349    785 igvDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVGK 864
Cdd:pfam00850   67 ---GDDDTPVSPGSYEAALLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLKR 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349    865 VLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDnGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGvdppIGDVEYLTAFRT 944
Cdd:pfam00850  144 VAIVDFDVHHGNGTQEIFYDDPSVLTLSIHQYP-GGFYPGTGFADETGEGKGKGYTLNVPLPPG----TGDAEYLAAFEE 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349    945 VVMPIAHEFSPDVVLVSAGFDAVEGHlsPLGGYSVTARCFGHLTRQLMTLA---GGRVVLALEGGHDLTAICDASEACVS 1021
Cdd:pfam00850  219 ILLPALEEFQPDLILVSAGFDAHAGD--PLGGLNLTTEGFAEITRILLELAdplCIRVVSVLEGGYNLDALARSATAVLA 296


                   ..
gi 62750349   1022 AL 1023
Cdd:pfam00850  297 AL 298
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 705-1025 1.38e-110

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: 347.02  E-value: 1.38e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  705 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYH-TLLYGTSPLNRQKLDSKKllgpisqKMYavlpcg 783
Cdd:cd11600    3 HPEDPSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEHwDRVEATEKMSDEQLKDRT-------EIF------ 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  784 gigvDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKL--N 861
Cdd:cd11600   70 ----ERDSLYVNNDTAFCARLSCGGAIEACRAVAEGRVKNAFAVVRPPGHHAEPDESMGFCFFNNVAVAAKWLQTEYpdK 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  862 VGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGS--GAPEEVGGGPGVGYNVNVAWTggvDPPIGDVEYL 939
Cdd:cd11600  146 IKKILILDWDIHHGNGTQRAFYDDPNVLYISLHRFENGGFYPGTpyGDYESVGEGAGLGFNVNIPWP---QGGMGDADYI 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  940 TAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTAICDASEAC 1019
Cdd:cd11600  223 YAFQRIVMPIAYEFDPDLVIISAGFDAADG--DELGQCHVTPAGYAHMTHMLMSLAGGKLVVALEGGYNLDAISDSALAV 300


                 ....*.
gi 62750349 1020 VSALLS 1025
Cdd:cd11600  301 AKVLLG 306
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 705-1059 4.79e-97

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: 311.94  E-value: 4.79e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  705 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHS-EYHTLLYGTSPLNRQKLDSKkllgpisqkmyavlpCG 783
Cdd:cd10002    7 HIECPERLEAILERLTQDGLLERCVKIPAREAEEDEILLVHSqEYIDLVKSTETMEKEELESL---------------CS 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  784 GIgvdsDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVG 863
Cdd:cd10002   72 GY----DSVYLCPSTYEAARLAAGSTIELVKAVMAGKIQNGFALIRPPGHHAMRNEANGYCIFNNVAIAAKYAIEKLGLK 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  864 KVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFP----------GSGApeevgggpGVGYNVNVAW--TGgvdp 931
Cdd:cd10002  148 RILIVDWDVHHGQGTQQGFYEDPRVLYFSIHRYEHGRFWPhlfesdydyiGVGH--------GYGFNVNVPLnqTG---- 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  932 pIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTA 1011
Cdd:cd10002  216 -LGDADYLAIFHHILLPLALEFQPELVLVSAGFDASIG--DPEGEMAVTPAGYAHLTRLLMGLAGGKLLLVLEGGYLLES 292

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 62750349 1012 ICDASEACVSALLSVELQPLDeavlQQKPNINAVATLEKVIEIQSKHW 1059
Cdd:cd10002  293 LAESVSMTLRGLLGDPLPPLA----PPIPIRSVLETILNAIAHLSPRW 336
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
 711-1023 2.46e-96

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: 307.82  E-value: 2.46e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  711 RIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQKLDSKKllgpisqkmyavlpcggiGVDSD 790
Cdd:cd09301    1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKANFAVATITESKP------------------VIFGP 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  791 TVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKlNVGKVLIVDW 870
Cdd:cd09301   63 NFPVQRHYFRGARLSTGGVVEAAELVAKGELERAFAVVGAGGHHAGKSRAWGFCYFNDVVLAIKFLRER-GISRILIIDT 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  871 DIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGSGapeevgggpgVGYNVNVAWTGGvdppIGDVEYLTAFRTVVMPIA 950
Cdd:cd09301  142 DAHHGDGTREAFYDDDRVLHMSFHNYDIYPFGRGKG----------KGYKINVPLEDG----LGDEEYLDAVERVISKVL 207

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62750349  951 HEFSPDVVLVSAGFDAVEGHlsPLGGYSVTARCFGHLTRQLMTLA-GGRVVLALEGGHDLTAICDASEACVSAL 1023
Cdd:cd09301  208 EEFEPEVVVLQFGHDTHEGD--RLGGFNLSEKGFVKLAEIVKEFArGGPILMVLGGGYNPEAAARIWTAIIKEL 279
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 684-1024 6.12e-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: 297.02  E-value: 6.12e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  684 TGVVYDTFMLKHQCmcGNTHvhPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHtllygtsplnrqkL 763
Cdd:COG0123    1 TALIYHPDYLLHDL--GPGH--PEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDY-------------V 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  764 DskkllgpisqKMYAVLPCGGIG-VDSDTVWNEmHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMG 842
Cdd:COG0123   64 D----------ALRAASLDGGYGqLDPDTPVSP-GTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMG 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  843 FCFFNSVAITAKLLQQKlNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYdngNFFPGSGAPEEVGGGPGVGYNVN 922
Cdd:COG0123  133 FCLFNNAAIAARYLLAK-GLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD---PLYPGTGAADETGEGAGEGSNLN 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  923 VAwtggVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLMTLA---GGRV 999
Cdd:COG0123  209 VP----LPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHAD--DPLGRLNLTTEGYAWRTRRVLELAdhcGGPV 282

                        330       340
                 ....*....|....*....|....*
gi 62750349 1000 VLALEGGHDLTAICDASEACVSALL 1024
Cdd:COG0123  283 VSVLEGGYNLDALARSVAAHLETLL 307
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
 705-1059 1.57e-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: 264.02  E-value: 1.57e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  705 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHS-EYHTLLYGTSPLNRQKLDSkkllgpISQKMyavlpcg 783
Cdd:cd11682    7 FPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSpEYVALMKSTQYMTEEELRT------LADTY------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  784 gigvdsDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVG 863
Cdd:cd11682   74 ------DSVYLHPNSYSCACLAVGSVLQLVDKVLGGEIRNGLAIVRPPGHHAQHDKMDGYCMFNNVAIAARYAQQKHGVQ 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  864 KVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFP--GSGAPEEVGGGPGVGYNVNVAWTggvDPPIGDVEYLTA 941
Cdd:cd11682  148 RVLIVDWDVHHGQGTQFIFEQDPSVLYFSIHRYEQGRFWPhlKESDSSAVGFGRGEGYNINVPWN---QVGMRDADYIAA 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  942 FRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTAICDASEACVS 1021
Cdd:cd11682  225 FLHVLLPVALEFQPQLVLVAAGFDAVIG--DPKGEMAATPACFAHLTHLLMGLAGGKLILSLEGGYNLRSLAEGVCASLK 302

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 62750349 1022 ALLSvelQPLDEAVLQQKPNINAVATLEKVIEIQSKHW 1059
Cdd:cd11682  303 ALLG---DPCPMLESPGAPCRSALASVSCTISALEPFW 337
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
 705-1024 2.82e-76

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


Pssm-ID: 212541 [Multi-domain]  Cd Length: 288  Bit Score: 253.20  E-value: 2.82e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  705 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHtllygtsplnrqkldskkllgpISQKMYAVLPCGG 784
Cdd:cd11599    1 HPESPERLEAILDALIASGLDRLLRQLEAPPATREQLLRVHDAAY----------------------VDRLEAAAPEEGL 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  785 IGVDSDTVWNEmHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVGK 864
Cdd:cd11599   59 VQLDPDTAMSP-GSLEAALRAAGAVVAAVDAVMAGEARNAFCAVRPPGHHAERDKAMGFCLFNNVAIAAAHALAHHGLER 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  865 VLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYdngNFFPGSGAPEEVGGGpgvgyN-VNVAWTGGVDPPigdvEYLTAFR 943
Cdd:cd11599  138 VAIVDFDVHHGNGTEDIFRDDPRVLFCSSHQH---PLYPGTGAPDETGHG-----NiVNVPLPAGTGGA----EFREAVE 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  944 TVVMPIAHEFSPDVVLVSAGFDAvegHLS-PLGGYSVTARCFGHLTRQLMTLA----GGRVVLALEGGHDLTAICDASEA 1018
Cdd:cd11599  206 DRWLPALDAFKPDLILISAGFDA---HRDdPLAQLNLTEEDYAWITEQLMDVAdrycDGRIVSVLEGGYDLSALARSVAA 282


                 ....*.
gi 62750349 1019 CVSALL 1024
Cdd:cd11599  283 HVRALM 288
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
 684-1010 3.19e-74

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: 250.17  E-value: 3.19e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  684 TGVVYDTFMLKHQcmcGNTHV--------------HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYH 749
Cdd:cd09996    1 TGFVWDERYLWHD---TGTGAlflpvggllvqpgrHPENPETKRRIKNLLEVSGLSDHLVLITPRPATDEELLRVHTPEY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  750 tllygtspLNRQKLDSKKllgpisqkmyavlpcGGIGVDSDTVWNEmHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIR 829
Cdd:cd09996   78 --------IDRVKAASAA---------------GGGEAGGGTPFGP-GSYEIALLAAGGAIAAVDAVLDGEVDNAYALVR 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  830 PPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRydNGNFFPGSGAPE 909
Cdd:cd09996  134 PPGHHAEPDQGMGFCLFNNVAIAARHALAVGGVKRVAVVDWDVHHGNGTQAIFYDDPDVLTISLHQ--DRCFPPDSGAVE 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  910 EVGGGPGVGYNVNVAWtggvdPP-IGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAveGHLSPLGGYSVTARCFGHLT 988
Cdd:cd09996  212 ERGEGAGEGYNLNIPL-----PPgSGDGAYLHAFERIVLPALRAFRPELIIVASGFDA--SAFDPLGRMMLTSDGFRALT 284

                        330       340
                 ....*....|....*....|....*.
gi 62750349  989 RQLMTLA----GGRVVLALEGGHDLT 1010
Cdd:cd09996  285 RKLRDLAdelcGGRLVMVHEGGYSEA 310
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 711-1059 8.13e-67

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: 228.59  E-value: 8.13e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  711 RIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSplnrQKLDSKKLLGpISQKMyavlpcggigvdsD 790
Cdd:cd11683   13 RLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRET----QVMNKEELMA-ISGKY-------------D 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  791 TVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVGKVLIVDW 870
Cdd:cd11683   75 AVYFHPNTFHCARLAAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYAKKKYGLHRILIVDW 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  871 DIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPG--SGAPEEVGGGPGVGYNVNVAWTggvDPPIGDVEYLTAFRTVVMP 948
Cdd:cd11683  155 DVHHGQGIQYIFEEDPSVLYFSWHRYEHQRFWPFlrESDYDAVGRGKGLGFNINLPWN---KVGMGNADYLAAFFHVLLP 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  949 IAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTAICDASEACVSALLSvel 1028
Cdd:cd11683  232 LAFEFDPELVLVSAGFDSAIG--DPEGQMCATPECFAHLTHLLMVLAGGKLCAVLEGGYHLESLAESVCMTVQTLLG--- 306

                        330       340       350
                 ....*....|....*....|....*....|.
gi 62750349 1029 QPLDEAVLQQKPNINAVATLEKVIEIQSKHW 1059
Cdd:cd11683  307 DPLPRLSGEMTPCQSALESIQNVRAAQAPYW 337
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
 705-1025 4.06e-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: 193.91  E-value: 4.06e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  705 HPEHAGRIQSIWSRLQETGLLskcERIRGRKATLDEIQTVHS-EYHTLLYGtsplnrqkldskkllgpisqkmyavlpcg 783
Cdd:cd10001   25 HPENPERAEAILDALKRAGLG---EVLPPRDFGLEPILAVHDpDYVDFLET----------------------------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  784 gigVDSDTVWNEmHSSSAVRMAVGCLLELAFKVAAGElKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKlnVG 863
Cdd:cd10001   73 ---ADTDTPISE-GTWEAALAAADTALTAADLVLEGE-RAAYALCRPPGHHAGRDRAGGFCYFNNAAIAAQYLRDR--AG 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  864 KVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRyDNGNFFP---------GSGApeevgggpGVGYNVNVAwtggVDPPIG 934
Cdd:cd10001  146 RVAILDVDVHHGNGTQEIFYERPDVLYVSIHG-DPRTFYPfflgfadetGEGE--------GEGYNLNLP----LPPGTG 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  935 DVEYLTAFRTVVMPIAhEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLMTLaGGRVVLALEGGHDLTAIcd 1014
Cdd:cd10001  213 DDDYLAALDEALAAIA-AFGPDALVVSLGFDTHEG--DPLSDFKLTTEDYARIGRRIAAL-GLPTVFVQEGGYNVDAL-- 286

                        330
                 ....*....|.
gi 62750349 1015 asEACVSALLS 1025
Cdd:cd10001  287 --GRNAVAFLA 295
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
 705-1009 2.27e-42

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: 157.72  E-value: 2.27e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  705 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHS-EYHTLLYGTSPlNRQKLDSKKLlgpisqkmyavlpcg 783
Cdd:cd09994   17 HPFNPPRLSLTKDLLRALGLLPPVDLVPPRPATEEELLLFHTpDYIEAVKEASR-GQEPEGRGRL--------------- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  784 GIGVDSDTVWNEMHSSSAvrMAVGCLLELAFKVAAGELKNGFAIIrppG--HHAEESTAMGFCFFNSVAITAKLLQQKlN 861
Cdd:cd09994   81 GLGTEDNPVFPGMHEAAA--LVVGGTLLAARLVLEGEARRAFNPA---GglHHAMRGRASGFCVYNDAAVAIERLRDK-G 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  862 VGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRyDNGNFFPGSGAPEEVGGGPGVGYNVNVAwtggVDPPIGDVEYLTA 941
Cdd:cd09994  155 GLRVAYVDIDAHHGDGVQAAFYDDPRVLTISLHE-SGRYLFPGTGFVDEIGEGEGYGYAVNIP----LPPGTGDDEFLRA 229

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62750349  942 FRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLMTLA----GGRVVLALEGGHDL 1009
Cdd:cd09994  230 FEAVVPPLLRAFRPDVIVSQHGADAHAG--DPLTHLNLSNRAYRAAVRRIRELAdeycGGRWLALGGGGYNP 299
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 698-1013 2.67e-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: 120.91  E-value: 2.67e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  698 MCGNTHVHPEHAGRIQSIwsrLQETGLLSKCERIRGRKATLDEIQTVHS-EYHTLLYGTSplnrQKLDSkkllgpisQKM 776
Cdd:cd10000   12 LCDRLPKVPNRASMVHSL---IEAYGLLKQLRVVKPRVATEEELASFHSdEYIQFLKKAS----NEGDN--------DEE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  777 YAVLPCGGIGVDSDTVWNEMhssSAVRMAVGCLLELAFKVAAGELKngFAIIRPPG-HHAEESTAMGFCFFNSVAITAKL 855
Cdd:cd10000   77 PSEQQEFGLGYDCPIFEGIY---DYAAAVAGATLTAAQLLIDGKCK--VAINWFGGwHHAQRDEASGFCYVNDIVLGILK 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  856 LQQKLNvgKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGnFFPGSGAPEEVGGGPGVGYNVNVAWTGGVDppigD 935
Cdd:cd10000  152 LREKFD--RVLYVDLDLHHGDGVEDAFSFTSKVMTVSLHKYSPG-FFPGTGDVSDVGLGKGKYYTVNVPLRDGIQ----D 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  936 VEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVT----ARCFGH-LTRQLMTL-AGGrvvlaleGGHDL 1009
Cdd:cd10000  225 EQYLQIFTAVVPEIVAAFRPEAVVLQCGADTLAG--DPMGAFNLTpvgiGKCLKYvLGWKLPTLiLGG-------GGYNL 295


                 ....*.
gi 62750349 1010 --TAIC 1013
Cdd:cd10000  296 anTARC 301
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 715-997 2.30e-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: 115.67  E-value: 2.30e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  715 IWSRLQETGLLSKCERIRGRKATLDEIQTVHS-EY-HTLLYGTspLNRQKLDSKKLlgPISQKMyaVLPcggigvdsdtv 792
Cdd:cd09993   11 LREALLEEGLVLPEDIVEPEPATREDLLRVHDpEYlESLKSGE--LSREEIRRIGF--PWSPEL--VER----------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  793 wnemhsssaVRMAVGCLLeLAFKVAageLKNGFAIiRPPG--HHAEESTAMGFCFFNSVAITAKLLQQKLNVGKVLIVDW 870
Cdd:cd09993   74 ---------TRLAVGGTI-LAARLA---LEHGLAI-NLAGgtHHAFPDRGEGFCVFNDIAIAARVLLAEGLVRRVLIVDL 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  871 DIHHGNGTQQAFYNDPSVLYISLHrydNGNFFPGSGAPEevgggpgvgyNVNVawtgGVDPPIGDVEYLTAFRTVVMPIA 950
Cdd:cd09993  140 DVHQGNGTAAIFADDPSVFTFSMH---GEKNYPFRKEPS----------DLDV----PLPDGTGDDEYLAALEEALPRLL 202

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 62750349  951 HEFSPDVVLVSAGFDAVEGhlSPLGGYSVT-----AR-------CFGHLTRQLMTLAGG 997
Cdd:cd09993  203 AEFRPDLVFYNAGVDVLAG--DRLGRLSLSleglrERdrlvlrfARARGIPVAMVLGGG 259
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
 833-1013 2.47e-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: 110.43  E-value: 2.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  833 HHAEESTAMGFCFFNSVAITAKLLQQKlNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGnFFPGSGApeevG 912
Cdd:cd11680  115 HHAQKSRASGFCYVNDIVLAILRLRRA-RFRRVFYLDLDLHHGDGVESAFFFSKNVLTCSIHRYDPG-FFPGTGS----L 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  913 GGPGVGYNVNVAWTGGVDppigDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLM 992
Cdd:cd11680  189 KNSSDKGMLNIPLKRGLS----DKTLLRIIDSIVRPLIEKFEPEVIVIQCGCDGLSG--DPHKEWNLTIRGYGSVIELLL 262

                        170       180
                 ....*....|....*....|....
gi 62750349  993 TLAGGRVVLALEGG---HDLTAIC 1013
Cdd:cd11680  263 KEFKDKPTLLLGGGgynHTEAARA 286
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
 698-997 2.42e-24

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: 104.97  E-value: 2.42e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  698 MCGNTHV---HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHS-EYHTLLYGTSPLNRQKLdsKKLLgpis 773
Cdd:cd09991    5 DVGNYYYgqgHPMKPHRIRMTHSLILSYGLYKKMEIYRPRPATAEELTKFHSdDYIDFLRSVSPDNMKEF--KKQL---- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  774 qKMYavlpcgGIGVDSdTVWNEMHSssAVRMAVGCLLELAFKVAAGELKNGfaiIRPPG--HHAEESTAMGFCFFNSV-- 849
Cdd:cd09991   79 -ERF------NVGEDC-PVFDGLYE--YCQLYAGGSIAAAVKLNRGQADIA---INWAGglHHAKKSEASGFCYVNDIvl 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  850 AITaKLLQQKlnvGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYdnGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGV 929
Cdd:cd09991  146 AIL-ELLKYH---QRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKF--GEYFFPGTGLRDIGAGKGKYYAVNVPLKDGI 219

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62750349  930 DppigDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVT----ARCFGHLTR---QLMTLAGG 997
Cdd:cd09991  220 D----DESYLQIFEPVLSKVMEVFQPSAVVLQCGADSLAG--DRLGCFNLSikghAKCVKFVKSfniPLLVLGGG 288
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
 734-989 4.86e-24

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: 104.07  E-value: 4.86e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  734 RKATLDEIQTVHSE-YHTLLYGTSPLNRQKLDSKKL----LG---PISQKMYAVLpcggigvdsdtvwnemhsssavRMA 805
Cdd:cd11598   47 RAATREELRQFHDAdYLDFLSKVSPENANQLRFDKAepfnIGddcPVFDGMYDYC----------------------QLY 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  806 VGCLLELAFKVAAGelKNGFAIIRPPG-HHAEESTAMGFCFFNSVAITakLLQQKLNVGKVLIVDWDIHHGNGTQQAFYN 884
Cdd:cd11598  105 AGASLDAARKLCSG--QSDIAINWSGGlHHAKKSEASGFCYVNDIVLA--ILNLLRYFPRVLYIDIDVHHGDGVEEAFYR 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  885 DPSVLYISLHRYdNGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGvdppIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGF 964
Cdd:cd11598  181 TDRVMTLSFHKY-NGEFFPGTGDLDDNGGTPGKHFALNVPLEDG----IDDEQYNLLFKSIIGPTIEKFQPSAIVLQCGA 255

                        250       260
                 ....*....|....*....|....*
gi 62750349  965 DAVEGhlSPLGGYSVTARCFGHLTR 989
Cdd:cd11598  256 DSLGG--DRLGQFNLNIKAHGACVK 278
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 796-1023 2.32e-23

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: 99.37  E-value: 2.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  796 MHSSSAVRMAVGCLLELAFKVaagelKNGFAIIrppGHHAEestamgfcfFNSVAITAKLLQqklnvGKVLIVDWDIHHG 875
Cdd:cd09987    5 IRKAEAHELLAGVVVAVLKDG-----KVPVVLG---GDHSI---------ANGAIRAVAELH-----PDLGVIDVDAHHD 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  876 NGTQQAFYN--------------DPSVLYISLHRYDNGNFFPGsgapeevgGGPGVGYNVNVAWTGGVDppigDVEYLTA 941
Cdd:cd09987   63 VRTPEAFGKgnhhtprhllceplISDVHIVSIGIRGVSNGEAG--------GAYARKLGVVYFSMTEVD----KLGLGDV 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  942 FRTVVMPIahEFSPDVVLVSAGFDAVEGHLSP----LGGYSVTARCFGHLTRQLMTLaGGRVVLALEGGHDL----TAIC 1013
Cdd:cd09987  131 FEEIVSYL--GDKGDNVYLSVDVDGLDPSFAPgtgtPGPGGLSYREGLYITERIAKT-NLVVGLDIVEVNPLldetGRTA 207

                        250
                 ....*....|
gi 62750349 1014 DASEACVSAL 1023
Cdd:cd09987  208 RLAAALTLEL 217
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
 700-986 1.83e-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: 97.96  E-value: 1.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  700 GNTHV---HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHS-EYHTLLYGTSPLNR---QKLDSKKLLG-- 770
Cdd:cd10004   13 GNYAYgpgHPMKPHRIRMAHSLVMNYGLYKKMEIYRAKPATKNEMTQFHTdEYIDFLSRVTPDNMekfQKEQVKYNVGdd 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  771 -PISQKMYavlpcggigvdsdtvwnEMHSSSAvrmavGCLLELAFKVAAGelKNGFAIIRPPG-HHAEESTAMGFCFFNS 848
Cdd:cd10004   93 cPVFDGLF-----------------EFCSISA-----GGSMEGAARLNRG--KCDIAVNWAGGlHHAKKSEASGFCYVND 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  849 VAITA-KLLQQKlnvGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYdnGNFFPGSGAPEEVGGGPGVGYNVNVAWTG 927
Cdd:cd10004  149 IVLGIlELLRYH---QRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKY--GEYFPGTGELRDIGIGTGKNYAVNVPLRD 223

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 62750349  928 GVDppigDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARcfGH 986
Cdd:cd10004  224 GID----DESYKSIFEPVIKHVMEWYQPEAVVLQCGGDSLSG--DRLGCFNLSMK--GH 274
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
 705-986 2.48e-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: 2.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  705 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSE-YHTLLYGTSPLNRQKLdSKKL----LG---PISQKM 776
Cdd:cd10010   25 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDdYIKFLRSIRPDNMSEY-SKQMqrfnVGedcPVFDGL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  777 YAV--LPCGGiGVDSDTVWNEMHSSSAVRMAVGCllelafkvaagelkngfaiirppgHHAEESTAMGFCFFNSVAITak 854
Cdd:cd10010  104 FEFcqLSAGG-SVASAVKLNKQQTDIAVNWAGGL------------------------HHAKKSEASGFCYVNDIVLA-- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  855 LLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYdnGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGVDppig 934
Cdd:cd10010  157 ILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKY--GEYFPGTGDLRDIGAGKGKYYAVNYPLRDGID---- 230

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 62750349  935 DVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARcfGH 986
Cdd:cd10010  231 DESYEAIFKPVMSKVMEMFQPSAVVLQCGADSLSG--DRLGCFNLTIK--GH 278
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
 813-1023 3.42e-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: 3.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  813 AFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQ------------- 879
Cdd:cd09998  100 VFKPESPGTKRAFVAIRPPGHHCSESTPSGFCWVNNVHVGAAHAYLTHGITRVVILDIDLHHGNGTQdiawrinaeankq 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  880 -----------QAFYNDPSVLYISLHrydNGNFFP---GSGAPEEVGggpgvgyNVNVA-------WTGGVDPPIGDVEY 938
Cdd:cd09998  180 alesssyddfkPAGAPGLRIFYSSLH---DINSFPcedGDPAKVKDA-------SVSIDgahgqwiWNVHLQPWTTEEDF 249

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  939 LTAFR---TVVMPIAHEF-------SPD--VVLVSAGFDAVEGHLSPLGGYS--VTARCFGHLTRQLMTLA----GGRVV 1000
Cdd:cd09998  250 WELYYpkyRILFEKAAEFlrlttaaTPFktLVFISAGFDASEHEYESMQRHGvnVPTSFYYRFARDAVRFAdahaHGRLI 329

                        250       260
                 ....*....|....*....|...
gi 62750349 1001 LALEGGHDLTAICDASEACVSAL 1023
Cdd:cd09998  330 SVLEGGYSDRALCSGVLAHLTGL 352
PTZ00063 PTZ00063
histone deacetylase; Provisional
 833-997 1.58e-19

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 92.95  E-value: 1.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349   833 HHAEESTAMGFCFFNSVAI-TAKLLQQKlnvGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYdnGNFFPGSGAPEEV 911
Cdd:PTZ00063  137 HHAKRSEASGFCYINDIVLgILELLKYH---ARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFPGTGDVTDI 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349   912 GGGPGVGYNVNVAWTGGVDppigDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVT----ARCFGH- 986
Cdd:PTZ00063  212 GVAQGKYYSVNVPLNDGID----DDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTG--DRLGRFNLTikghAACVEFv 285

                         170
                  ....*....|...
gi 62750349   987 --LTRQLMTLAGG 997
Cdd:PTZ00063  286 rsLNIPLLVLGGG 298
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
 700-988 3.37e-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: 90.92  E-value: 3.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  700 GNTHV---HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSE-YHTLLYGTSPLNRQKLdsKKLLGPISqk 775
Cdd:cd10005   12 GNFHYgpgHPMKPHRLALTHSLVLHYGLYKKMQVYKPYRASAHDMCRFHSEdYIDFLQRVTPQNIQGF--TKSLNQFN-- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  776 myavlpcggIGVDSdTVWNEMHSSSAvrMAVGCLLELAFKVAAGELKngFAIIRPPG-HHAEESTAMGFCFFNSVAITA- 853
Cdd:cd10005   88 ---------VGDDC-PVFPGLFDFCS--MYTGASLEGATKLNHKICD--IAINWSGGlHHAKKFEASGFCYVNDIVIAIl 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  854 KLLQQKlnvGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNgNFFPGSGAPEEVGGGPGVGYNVNVAWTGGVDppi 933
Cdd:cd10005  154 ELLKYH---PRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGN-YFFPGTGDMYEVGAESGRYYSVNVPLKDGID--- 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  934 gDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDA------------VEGHLS----------PL-----GGYSV--TARCF 984
Cdd:cd10005  227 -DQSYLQLFKPVIQQVIDFYQPTCIVLQCGADSlgcdrlgcfnlsIKGHGEcvefvksfniPLlvlggGGYTVrnVARCW 305


                 ....
gi 62750349  985 GHLT 988
Cdd:cd10005  306 TYET 309
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
 705-986 3.22e-17

Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme that catalyzes hydrolysis of N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. HDAC2 is involved in regulation through association with DNA binding proteins to target specific chromatin regions. It forms transcriptional repressor complexes by associating with several proteins, including the mammalian zinc-finger transcription factor YY1, thus playing an important role in transcriptional regulation, cell cycle progression and developmental events. Additionally, a few non-histone HDAC2 substrates have been found. HDAC2 plays a role in embryonic development and cytokine signaling important for immune response, and is over-expressed in several solid tumors including oral, prostate, ovarian, endometrial and gastric cancer. It participates in DNA-damage response, along with HDAC1; together, they can promote DNA non-homologous end-joining. HDAC2 is considered an important cancer prognostic marker. Inhibitors specifically targeting HDAC2 could be a therapeutic drug option.


Pssm-ID: 212535 [Multi-domain]  Cd Length: 366  Bit Score: 84.73  E-value: 3.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  705 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHS-EYHTLLYGTSPLNRQKLdSKKL----LG---PISQKM 776
Cdd:cd10011   21 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSdEYIKFLRSIRPDNMSEY-SKQMqrfnVGedcPVFDGL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  777 YAV--LPCGGiGVDSDTVWNEMHSSSAVRMAVGCllelafkvaagelkngfaiirppgHHAEESTAMGFCFFNSVAITak 854
Cdd:cd10011  100 FEFcqLSTGG-SVAGAVKLNRQQTDMAVNWAGGL------------------------HHAKKSEASGFCYVNDIVLA-- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349  855 LLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISlhRYDNGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGVDppig 934
Cdd:cd10011  153 ILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVS--FHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGID---- 226

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 62750349  935 DVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARcfGH 986
Cdd:cd10011  227 DESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSG--DRLGCFNLTVK--GH 274
ClassIIa_HDAC5_Gln-rich-N cd10164
Glutamine-rich N-terminal helical domain of HDAC5, a Class IIa histone deacetylase; This ...
 69-165 1.80e-16

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: 76.02  E-value: 1.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349   69 DPTLREQQLQQELLALKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEMLAAKRQQELEQQRQR 148
Cdd:cd10164    1 DPSLREQQLQQELLLLKQQQQLQKQLLFAEFQKQHEHLTRQHEVQLQKHLKVRAELFSEQQQQEILAAKRQQELEQQRKR 80

                         90
                 ....*....|....*..
gi 62750349  149 EQQRQEELEKQRLEQQL 165
Cdd:cd10164   81 EQQRQEELEKQRLEQQL 97
PTZ00346 PTZ00346
histone deacetylase; Provisional
 833-1006 2.83e-13

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 73.14  E-value: 2.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349   833 HHAEESTAMGFCFFNSVAItaKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNgNFFPGSGAPEEVG 912
Cdd:PTZ00346  154 HHSKCGECSGFCYVNDIVL--GILELLKCHDRVLYVDIDMHHGDGVDEAFCTSDRVFTLSLHKFGE-SFFPGTGHPRDVG 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349   913 GGPGVGYNVNVA-WTGgvdppIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQL 991
Cdd:PTZ00346  231 YGRGRYYSMNLAvWDG-----ITDFYYLGLFEHALHSIVRRYSPDAIVLQCGADSLAG--DRLGLLNLSSFGHGQCVQAV 303

                         170
                  ....*....|....*
gi 62750349   992 MTLagGRVVLALEGG 1006
Cdd:PTZ00346  304 RDL--GIPMLALGGG 316
ClassIIa_HDAC_Gln-rich-N cd10149
Glutamine-rich N-terminal helical domain of various Class IIa histone deacetylases (HDAC4, ...
 69-165 2.33e-11

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: 61.25  E-value: 2.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349   69 DPTLREQQLQQELLALKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEMLAAKrqqeleqQRQR 148
Cdd:cd10149    1 DPVLREQQLQQELLALKQQQQIQKQLLIAEFQKQHENLTRQHEAQLQEHIKQQQEMLAIKQQQELLEKQ-------RKLE 73

                         90
                 ....*....|....*..
gi 62750349  149 EQQRQEELEKQRLEQQL 165
Cdd:cd10149   74 QQRQEQELEKQRREQQL 90
ClassIIa_HDAC9_Gln-rich-N cd10163
Glutamine-rich N-terminal helical domain of HDAC9, a Class IIa histone deacetylase; This ...
 69-134 3.90e-07

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: 48.98  E-value: 3.90e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62750349   69 DPTLREQQLQQELLALKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEML 134
Cdd:cd10163    1 DPTVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHLKLQQELLAMKQQQELL 66
HDAC4_Gln pfam12203
Glutamine rich N terminal domain of histone deacetylase 4; This domain is found in eukaryotes, ...
 96-165 4.00e-07

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: 49.08  E-value: 4.00e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62750349     96 FAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEMLAAKrqqeleqQRQREQQRQEELEKQRLEQQL 165
Cdd:pfam12203   29 IAEFQKQHELLTRQHEAQLQEHIKQQQELLAMKQQQELLEQQ-------RKLEQQRQEEELEKHRREQQL 91
ClassIIa_HDAC4_Gln-rich-N cd10162
Glutamine-rich N-terminal helical domain of HDAC4, a Class IIa histone deacetylase; This ...
 69-134 1.15e-05

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: 44.80  E-value: 1.15e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62750349   69 DPTLREQQLQQELLALKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEML 134
Cdd:cd10162    1 EPALREQQLQQELLALKQKQQIQRQLLIAEFQRQHEQLSRQHEAQLHEHIKQQQELLAMKHQQELL 66
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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