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Conserved domains on  [gi|1838744837|ref|NP_001369322|]
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histone deacetylase 5 isoform 1 [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 ...
 679-1095 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 1838744837  679 HLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLN 758
Cdd:cd10007      1 HLFTTGLVYDTFMLKHQCTCGNTNVHPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHSEHHTLLYGTSPLN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  759 RQKLDSKKLLGPISQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEEST 838
Cdd:cd10007     81 RQKLDSKKLLGPLSQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLIELAFKVAAGELKNGFAVIRPPGHHAEEST 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  839 AMGFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGY 918
Cdd:cd10007    161 AMGFCFFNSVAIAAKLLQQKLNVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGNFFPGSGAPDEVGAGPGVGF 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  919 NVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRV 998
Cdd:cd10007    241 NVNIAWTGGVDPPIGDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGHQSPLGGYSVTAKCFGHLTKQLMTLAGGRV 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  999 VLALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPNINAVATLEKVIEIQSKHWSCVQKFAAGLGRSLREAQAG 1078
Cdd:cd10007    321 VLALEGGHDLTAICDASEACVSALLGMELTPLDNTVLQQKPNDNAVATLERVIEIQSKHWSCLKRFAATLGFSLLEAQRG 400

                          410
                   ....*....|....*..
gi 1838744837 1079 ETEEAETVSAMALLSVG 1095
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 ...
 68-164 1.91e-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: 75.63  E-value: 1.91e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837   68 DPTLREQQLQQELLALKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEMLAAKRQQELEQQRQR 147
Cdd:cd10164      1 DPSLREQQLQQELLLLKQQQQLQKQLLFAEFQKQHEHLTRQHEVQLQKHLKVRAELFSEQQQQEILAAKRQQELEQQRKR 80

                           90
                   ....*....|....*..
gi 1838744837  148 EQQRQEELEKQRLEQQL 164
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 ...
 679-1095 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 1838744837  679 HLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLN 758
Cdd:cd10007      1 HLFTTGLVYDTFMLKHQCTCGNTNVHPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHSEHHTLLYGTSPLN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  759 RQKLDSKKLLGPISQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEEST 838
Cdd:cd10007     81 RQKLDSKKLLGPLSQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLIELAFKVAAGELKNGFAVIRPPGHHAEEST 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  839 AMGFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGY 918
Cdd:cd10007    161 AMGFCFFNSVAIAAKLLQQKLNVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGNFFPGSGAPDEVGAGPGVGF 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  919 NVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRV 998
Cdd:cd10007    241 NVNIAWTGGVDPPIGDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGHQSPLGGYSVTAKCFGHLTKQLMTLAGGRV 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  999 VLALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPNINAVATLEKVIEIQSKHWSCVQKFAAGLGRSLREAQAG 1078
Cdd:cd10007    321 VLALEGGHDLTAICDASEACVSALLGMELTPLDNTVLQQKPNDNAVATLERVIEIQSKHWSCLKRFAATLGFSLLEAQRG 400

                          410
                   ....*....|....*..
gi 1838744837 1079 ETEEAETVSAMALLSVG 1095
Cdd:cd10007    401 ELEEAETVSAMASLSVD 417
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 704-1022 4.23e-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: 4.23e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  704 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQKLDSKKLLGpisqkmyavlpcgg 783
Cdd:pfam00850    1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAAPEGGALLLLSYLS-------------- 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  784 igvDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVGK 863
Cdd:pfam00850   67 ---GDDDTPVSPGSYEAALLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLKR 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  864 VLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDnGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGvdppIGDVEYLTAFRT 943
Cdd:pfam00850  144 VAIVDFDVHHGNGTQEIFYDDPSVLTLSIHQYP-GGFYPGTGFADETGEGKGKGYTLNVPLPPG----TGDAEYLAAFEE 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  944 VVMPIAHEFSPDVVLVSAGFDAVEGHlsPLGGYSVTARCFGHLTRQLMTLA---GGRVVLALEGGHDLTAICDASEACVS 1020
Cdd:pfam00850  219 ILLPALEEFQPDLILVSAGFDAHAGD--PLGGLNLTTEGFAEITRILLELAdplCIRVVSVLEGGYNLDALARSATAVLA 296


                   ..
gi 1838744837 1021 AL 1022
Cdd:pfam00850  297 AL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 683-1023 5.14e-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: 5.14e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  683 TGVVYDTFMLKHQCmcGNTHvhPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHtllygtsplnrqkL 762
Cdd:COG0123      1 TALIYHPDYLLHDL--GPGH--PEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDY-------------V 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  763 DskkllgpisqKMYAVLPCGGIG-VDSDTVWNEmHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMG 841
Cdd:COG0123     64 D----------ALRAASLDGGYGqLDPDTPVSP-GTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMG 132

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  842 FCFFNSVAITAKLLQQKlNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYdngNFFPGSGAPEEVGGGPGVGYNVN 921
Cdd:COG0123    133 FCLFNNAAIAARYLLAK-GLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD---PLYPGTGAADETGEGAGEGSNLN 208

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  922 VAwtggVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLMTLA---GGRV 998
Cdd:COG0123    209 VP----LPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHAD--DPLGRLNLTTEGYAWRTRRVLELAdhcGGPV 282

                          330       340
                   ....*....|....*....|....*
gi 1838744837  999 VLALEGGHDLTAICDASEACVSALL 1023
Cdd:COG0123    283 VSVLEGGYNLDALARSVAAHLETLL 307
PTZ00063 PTZ00063
histone deacetylase; Provisional
 832-996 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 1838744837  832 HHAEESTAMGFCFFNSVAI-TAKLLQQKlnvGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYdnGNFFPGSGAPEEV 910
Cdd:PTZ00063   137 HHAKRSEASGFCYINDIVLgILELLKYH---ARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFPGTGDVTDI 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  911 GGGPGVGYNVNVAWTGGVDppigDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVT----ARCFGH- 985
Cdd:PTZ00063   212 GVAQGKYYSVNVPLNDGID----DDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTG--DRLGRFNLTikghAACVEFv 285

                          170
                   ....*....|...
gi 1838744837  986 --LTRQLMTLAGG 996
Cdd:PTZ00063   286 rsLNIPLLVLGGG 298
ClassIIa_HDAC5_Gln-rich-N cd10164
Glutamine-rich N-terminal helical domain of HDAC5, a Class IIa histone deacetylase; This ...
 68-164 1.91e-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: 75.63  E-value: 1.91e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837   68 DPTLREQQLQQELLALKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEMLAAKRQQELEQQRQR 147
Cdd:cd10164      1 DPSLREQQLQQELLLLKQQQQLQKQLLFAEFQKQHEHLTRQHEVQLQKHLKVRAELFSEQQQQEILAAKRQQELEQQRKR 80

                           90
                   ....*....|....*..
gi 1838744837  148 EQQRQEELEKQRLEQQL 164
Cdd:cd10164     81 EQQRQEELEKQRLEQQL 97
HDAC4_Gln pfam12203
Glutamine rich N terminal domain of histone deacetylase 4; This domain is found in eukaryotes, ...
 95-164 4.04e-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: 4.04e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837   95 FAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEMLAAKrqqeleqQRQREQQRQEELEKQRLEQQL 164
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 ...
 679-1095 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 1838744837  679 HLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLN 758
Cdd:cd10007      1 HLFTTGLVYDTFMLKHQCTCGNTNVHPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHSEHHTLLYGTSPLN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  759 RQKLDSKKLLGPISQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEEST 838
Cdd:cd10007     81 RQKLDSKKLLGPLSQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLIELAFKVAAGELKNGFAVIRPPGHHAEEST 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  839 AMGFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGY 918
Cdd:cd10007    161 AMGFCFFNSVAIAAKLLQQKLNVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGNFFPGSGAPDEVGAGPGVGF 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  919 NVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRV 998
Cdd:cd10007    241 NVNIAWTGGVDPPIGDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGHQSPLGGYSVTAKCFGHLTKQLMTLAGGRV 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  999 VLALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPNINAVATLEKVIEIQSKHWSCVQKFAAGLGRSLREAQAG 1078
Cdd:cd10007    321 VLALEGGHDLTAICDASEACVSALLGMELTPLDNTVLQQKPNDNAVATLERVIEIQSKHWSCLKRFAATLGFSLLEAQRG 400

                          410
                   ....*....|....*..
gi 1838744837 1079 ETEEAETVSAMALLSVG 1095
Cdd:cd10007    401 ELEEAETVSAMASLSVD 417
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 681-1058 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 1838744837  681 FTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQ 760
Cdd:cd11681      1 FTTGLAYDPLMLKHQCICGNNSSHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTLLYGTNPLSRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  761 KLDSKKLLGpISQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAM 840
Cdd:cd11681     81 KLDPTKLAG-LPQKSFVRLPCGGIGVDSDTVWNELHTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQAM 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  841 GFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGYNV 920
Cdd:cd11681    160 GFCFFNSVAIAAKQLQQKLKLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFPGTGAPTEVGSGAGEGFNV 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  921 NVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRVVL 1000
Cdd:cd11681    240 NIAWSGGLDPPMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPPPLGGYKVSPACFGYMTRQLMNLAGGKVVL 319

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1838744837 1001 ALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPNINAVATLEKVIEIQSKHW 1058
Cdd:cd11681    320 ALEGGYDLTAICDASEACVRALLGDELDPLSEEELERRPNPNAVTSLEKVIAIQSPYW 377
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
 678-1087 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 1838744837  678 KHLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPL 757
Cdd:cd10006      1 KPRFTTGLVYDTLMLKHQCTCGNSNSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  758 NRQKLDSKKLLGPISQkMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEES 837
Cdd:cd10006     81 NRQKLDSKKLLGSLAS-VFVRLPCGGVGVDSDTIWNEVHSSGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEES 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  838 TAMGFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVG 917
Cdd:cd10006    160 TPMGFCYFNSVAIAAKLLQQRLNVSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVG 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  918 YNVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGR 997
Cdd:cd10006    240 FNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSAKCFGYLTKQLMGLAGGR 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  998 VVLALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPNINAVATLEKVIEIQSKHWSCVQKFAAGLGRSLREAQA 1077
Cdd:cd10006    320 IVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGYSLIEAQT 399

                          410
                   ....*....|
gi 1838744837 1078 GETEEAETVS 1087
Cdd:cd10006    400 CENEEAETVT 409
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
 681-1058 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 1838744837  681 FTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQ 760
Cdd:cd10008      1 FTTGLVYDSVMLKHQCSCGDNSNHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  761 KLDSKKLLGPISQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAM 840
Cdd:cd10008     81 KLDNGKLAGLLAQRMFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAM 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  841 GFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGYNV 920
Cdd:cd10008    161 GFCFFNSVAIACRQLQQQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGAGSGEGFNV 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  921 NVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRVVL 1000
Cdd:cd10008    241 NVAWAGGLDPPMGDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVL 320

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1838744837 1001 ALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPNINAVATLEKVIEIQSKHW 1058
Cdd:cd10008    321 ALEGGHDLTAICDASEACVAALLGNEVDPLSEESWKQKPNLNAIRSLEAVIRVHSKYW 378
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
 681-1058 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 1838744837  681 FTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQ 760
Cdd:cd10009      1 SATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  761 KLDSKKLLGPISQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAM 840
Cdd:cd10009     81 KLDPRILLGDDSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAM 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  841 GFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGYNV 920
Cdd:cd10009    161 GFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYNI 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  921 NVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRVVL 1000
Cdd:cd10009    241 NIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVL 320

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1838744837 1001 ALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPNINAVATLEKVIEIQSKHW 1058
Cdd:cd10009    321 ALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSKYW 378
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
 687-1060 1.16e-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: 1.16e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  687 YDTFMLKHQCMCgNTHvHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHtllygtspLNRQKLDSKK 766
Cdd:cd10003      1 YDQRMMNHHNLW-DPG-HPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEH--------LDEMKSLEKM 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  767 LLGPISQKmyavlpcggiGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFN 846
Cdd:cd10003     71 KPRELNRL----------GKEYDSIYIHPDSYQCALLAAGCVLQVVEAVLTGESRNGVAIVRPPGHHAEQDTACGFCFFN 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  847 SVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGS--GAPEEVGGGPGVGYNVNVAW 924
Cdd:cd10003    141 NVAIAARYAQKKYGLKRILIVDWDVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSpeGNYDVVGKGKGEGFNVNIPW 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  925 TGGvdpPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEG 1004
Cdd:cd10003    221 NKG---GMGDAEYIAAFQQVVLPIAYEFNPELVLVSAGFDAARG--DPLGGCKVTPEGYAHMTHMLMSLAGGRVIVILEG 295

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1838744837 1005 GHDLTAICDASEACVSALLSVELQPLDeavLQQKPNINAVATLEKVIEIQSKHWSC 1060
Cdd:cd10003    296 GYNLTSISESMSMCTKTLLGDPPPVLD---LPRPPCSSALKSINNVLQVHQKYWKS 348
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
 704-1023 1.91e-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: 1.91e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  704 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTllygtsplnrqkldskkllgpisQKMYAVLPCGG 783
Cdd:cd09992      1 HPERPERLLAILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYI-----------------------ERVEETCEAGG 57

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  784 IGVDSDTVWNEmHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVGK 863
Cdd:cd09992     58 GYLDPDTYVSP-GSYEAALLAAGAALAAVDAVLSGEAENAFALVRPPGHHAEPDRAMGFCLFNNVAIAARYAQKRYGLKR 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  864 VLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDngnFFPGSGAPEEVGGGPGVGYNVNVAWTGGvdppIGDVEYLTAFRT 943
Cdd:cd09992    137 VLIVDWDVHHGNGTQDIFYDDPSVLYFSIHQYP---FYPGTGAAEETGGGAGEGFTINVPLPPG----SGDAEYLAAFEE 209

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  944 VVMPIAHEFSPDVVLVSAGFDAVEGHlsPLGGYSVTARCFGHLTRQLMTLA----GGRVVLALEGGHDLTAICDASEACV 1019
Cdd:cd09992    210 VLLPIAREFQPDLVLVSAGFDAHRGD--PLGGMNLTPEGYARLTRLLKELAdehcGGRLVFVLEGGYNLEALAESVLAVL 287


                   ....
gi 1838744837 1020 SALL 1023
Cdd:cd09992    288 EALL 291
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 704-1022 4.23e-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: 4.23e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  704 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQKLDSKKLLGpisqkmyavlpcgg 783
Cdd:pfam00850    1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAAPEGGALLLLSYLS-------------- 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  784 igvDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVGK 863
Cdd:pfam00850   67 ---GDDDTPVSPGSYEAALLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLKR 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  864 VLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDnGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGvdppIGDVEYLTAFRT 943
Cdd:pfam00850  144 VAIVDFDVHHGNGTQEIFYDDPSVLTLSIHQYP-GGFYPGTGFADETGEGKGKGYTLNVPLPPG----TGDAEYLAAFEE 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  944 VVMPIAHEFSPDVVLVSAGFDAVEGHlsPLGGYSVTARCFGHLTRQLMTLA---GGRVVLALEGGHDLTAICDASEACVS 1020
Cdd:pfam00850  219 ILLPALEEFQPDLILVSAGFDAHAGD--PLGGLNLTTEGFAEITRILLELAdplCIRVVSVLEGGYNLDALARSATAVLA 296


                   ..
gi 1838744837 1021 AL 1022
Cdd:pfam00850  297 AL 298
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 704-1024 1.36e-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: 1.36e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  704 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYH-TLLYGTSPLNRQKLDSKKllgpisqKMYavlpcg 782
Cdd:cd11600      3 HPEDPSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEHwDRVEATEKMSDEQLKDRT-------EIF------ 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  783 gigvDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKL--N 860
Cdd:cd11600     70 ----ERDSLYVNNDTAFCARLSCGGAIEACRAVAEGRVKNAFAVVRPPGHHAEPDESMGFCFFNNVAVAAKWLQTEYpdK 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  861 VGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGS--GAPEEVGGGPGVGYNVNVAWTggvDPPIGDVEYL 938
Cdd:cd11600    146 IKKILILDWDIHHGNGTQRAFYDDPNVLYISLHRFENGGFYPGTpyGDYESVGEGAGLGFNVNIPWP---QGGMGDADYI 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  939 TAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTAICDASEAC 1018
Cdd:cd11600    223 YAFQRIVMPIAYEFDPDLVIISAGFDAADG--DELGQCHVTPAGYAHMTHMLMSLAGGKLVVALEGGYNLDAISDSALAV 300


                   ....*.
gi 1838744837 1019 VSALLS 1024
Cdd:cd11600    301 AKVLLG 306
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 704-1058 4.58e-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: 4.58e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  704 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHS-EYHTLLYGTSPLNRQKLDSKkllgpisqkmyavlpCG 782
Cdd:cd10002      7 HIECPERLEAILERLTQDGLLERCVKIPAREAEEDEILLVHSqEYIDLVKSTETMEKEELESL---------------CS 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  783 GIgvdsDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVG 862
Cdd:cd10002     72 GY----DSVYLCPSTYEAARLAAGSTIELVKAVMAGKIQNGFALIRPPGHHAMRNEANGYCIFNNVAIAAKYAIEKLGLK 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  863 KVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFP----------GSGApeevgggpGVGYNVNVAW--TGgvdp 930
Cdd:cd10002    148 RILIVDWDVHHGQGTQQGFYEDPRVLYFSIHRYEHGRFWPhlfesdydyiGVGH--------GYGFNVNVPLnqTG---- 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  931 pIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTA 1010
Cdd:cd10002    216 -LGDADYLAIFHHILLPLALEFQPELVLVSAGFDASIG--DPEGEMAVTPAGYAHLTRLLMGLAGGKLLLVLEGGYLLES 292

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1838744837 1011 ICDASEACVSALLSVELQPLDeavlQQKPNINAVATLEKVIEIQSKHW 1058
Cdd:cd10002    293 LAESVSMTLRGLLGDPLPPLA----PPIPIRSVLETILNAIAHLSPRW 336
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
 710-1022 2.43e-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: 2.43e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  710 RIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQKLDSKKllgpisqkmyavlpcggiGVDSD 789
Cdd:cd09301      1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKANFAVATITESKP------------------VIFGP 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  790 TVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKlNVGKVLIVDW 869
Cdd:cd09301     63 NFPVQRHYFRGARLSTGGVVEAAELVAKGELERAFAVVGAGGHHAGKSRAWGFCYFNDVVLAIKFLRER-GISRILIIDT 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  870 DIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGSGapeevgggpgVGYNVNVAWTGGvdppIGDVEYLTAFRTVVMPIA 949
Cdd:cd09301    142 DAHHGDGTREAFYDDDRVLHMSFHNYDIYPFGRGKG----------KGYKINVPLEDG----LGDEEYLDAVERVISKVL 207

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838744837  950 HEFSPDVVLVSAGFDAVEGHlsPLGGYSVTARCFGHLTRQLMTLA-GGRVVLALEGGHDLTAICDASEACVSAL 1022
Cdd:cd09301    208 EEFEPEVVVLQFGHDTHEGD--RLGGFNLSEKGFVKLAEIVKEFArGGPILMVLGGGYNPEAAARIWTAIIKEL 279
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 683-1023 5.14e-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: 5.14e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  683 TGVVYDTFMLKHQCmcGNTHvhPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHtllygtsplnrqkL 762
Cdd:COG0123      1 TALIYHPDYLLHDL--GPGH--PEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDY-------------V 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  763 DskkllgpisqKMYAVLPCGGIG-VDSDTVWNEmHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMG 841
Cdd:COG0123     64 D----------ALRAASLDGGYGqLDPDTPVSP-GTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMG 132

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  842 FCFFNSVAITAKLLQQKlNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYdngNFFPGSGAPEEVGGGPGVGYNVN 921
Cdd:COG0123    133 FCLFNNAAIAARYLLAK-GLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD---PLYPGTGAADETGEGAGEGSNLN 208

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  922 VAwtggVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLMTLA---GGRV 998
Cdd:COG0123    209 VP----LPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHAD--DPLGRLNLTTEGYAWRTRRVLELAdhcGGPV 282

                          330       340
                   ....*....|....*....|....*
gi 1838744837  999 VLALEGGHDLTAICDASEACVSALL 1023
Cdd:COG0123    283 VSVLEGGYNLDALARSVAAHLETLL 307
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
 704-1058 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 1838744837  704 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHS-EYHTLLYGTSPLNRQKLDSkkllgpISQKMyavlpcg 782
Cdd:cd11682      7 FPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSpEYVALMKSTQYMTEEELRT------LADTY------- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  783 gigvdsDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVG 862
Cdd:cd11682     74 ------DSVYLHPNSYSCACLAVGSVLQLVDKVLGGEIRNGLAIVRPPGHHAQHDKMDGYCMFNNVAIAARYAQQKHGVQ 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  863 KVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFP--GSGAPEEVGGGPGVGYNVNVAWTggvDPPIGDVEYLTA 940
Cdd:cd11682    148 RVLIVDWDVHHGQGTQFIFEQDPSVLYFSIHRYEQGRFWPhlKESDSSAVGFGRGEGYNINVPWN---QVGMRDADYIAA 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  941 FRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTAICDASEACVS 1020
Cdd:cd11682    225 FLHVLLPVALEFQPQLVLVAAGFDAVIG--DPKGEMAATPACFAHLTHLLMGLAGGKLILSLEGGYNLRSLAEGVCASLK 302

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1838744837 1021 ALLSvelQPLDEAVLQQKPNINAVATLEKVIEIQSKHW 1058
Cdd:cd11682    303 ALLG---DPCPMLESPGAPCRSALASVSCTISALEPFW 337
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
 704-1023 2.46e-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: 2.46e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  704 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHtllygtsplnrqkldskkllgpISQKMYAVLPCGG 783
Cdd:cd11599      1 HPESPERLEAILDALIASGLDRLLRQLEAPPATREQLLRVHDAAY----------------------VDRLEAAAPEEGL 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  784 IGVDSDTVWNEmHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVGK 863
Cdd:cd11599     59 VQLDPDTAMSP-GSLEAALRAAGAVVAAVDAVMAGEARNAFCAVRPPGHHAERDKAMGFCLFNNVAIAAAHALAHHGLER 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  864 VLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYdngNFFPGSGAPEEVGGGpgvgyN-VNVAWTGGVDPPigdvEYLTAFR 942
Cdd:cd11599    138 VAIVDFDVHHGNGTEDIFRDDPRVLFCSSHQH---PLYPGTGAPDETGHG-----NiVNVPLPAGTGGA----EFREAVE 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  943 TVVMPIAHEFSPDVVLVSAGFDAvegHLS-PLGGYSVTARCFGHLTRQLMTLA----GGRVVLALEGGHDLTAICDASEA 1017
Cdd:cd11599    206 DRWLPALDAFKPDLILISAGFDA---HRDdPLAQLNLTEEDYAWITEQLMDVAdrycDGRIVSVLEGGYDLSALARSVAA 282


                   ....*.
gi 1838744837 1018 CVSALL 1023
Cdd:cd11599    283 HVRALM 288
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
 683-1009 2.60e-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: 250.56  E-value: 2.60e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  683 TGVVYDTFMLKHQcmcGNTHV--------------HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYH 748
Cdd:cd09996      1 TGFVWDERYLWHD---TGTGAlflpvggllvqpgrHPENPETKRRIKNLLEVSGLSDHLVLITPRPATDEELLRVHTPEY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  749 tllygtspLNRQKLDSKKllgpisqkmyavlpcGGIGVDSDTVWNEmHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIR 828
Cdd:cd09996     78 --------IDRVKAASAA---------------GGGEAGGGTPFGP-GSYEIALLAAGGAIAAVDAVLDGEVDNAYALVR 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  829 PPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRydNGNFFPGSGAPE 908
Cdd:cd09996    134 PPGHHAEPDQGMGFCLFNNVAIAARHALAVGGVKRVAVVDWDVHHGNGTQAIFYDDPDVLTISLHQ--DRCFPPDSGAVE 211

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  909 EVGGGPGVGYNVNVAWtggvdPP-IGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAveGHLSPLGGYSVTARCFGHLT 987
Cdd:cd09996    212 ERGEGAGEGYNLNIPL-----PPgSGDGAYLHAFERIVLPALRAFRPELIIVASGFDA--SAFDPLGRMMLTSDGFRALT 284

                          330       340
                   ....*....|....*....|....*.
gi 1838744837  988 RQLMTLA----GGRVVLALEGGHDLT 1009
Cdd:cd09996    285 RKLRDLAdelcGGRLVMVHEGGYSEA 310
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 710-1058 8.50e-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: 8.50e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  710 RIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSplnrQKLDSKKLLGpISQKMyavlpcggigvdsD 789
Cdd:cd11683     13 RLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRET----QVMNKEELMA-ISGKY-------------D 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  790 TVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVGKVLIVDW 869
Cdd:cd11683     75 AVYFHPNTFHCARLAAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYAKKKYGLHRILIVDW 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  870 DIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPG--SGAPEEVGGGPGVGYNVNVAWTggvDPPIGDVEYLTAFRTVVMP 947
Cdd:cd11683    155 DVHHGQGIQYIFEEDPSVLYFSWHRYEHQRFWPFlrESDYDAVGRGKGLGFNINLPWN---KVGMGNADYLAAFFHVLLP 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  948 IAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTAICDASEACVSALLSvel 1027
Cdd:cd11683    232 LAFEFDPELVLVSAGFDSAIG--DPEGQMCATPECFAHLTHLLMVLAGGKLCAVLEGGYHLESLAESVCMTVQTLLG--- 306

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1838744837 1028 QPLDEAVLQQKPNINAVATLEKVIEIQSKHW 1058
Cdd:cd11683    307 DPLPRLSGEMTPCQSALESIQNVRAAQAPYW 337
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
 704-1024 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 1838744837  704 HPEHAGRIQSIWSRLQETGLLskcERIRGRKATLDEIQTVHS-EYHTLLYGtsplnrqkldskkllgpisqkmyavlpcg 782
Cdd:cd10001     25 HPENPERAEAILDALKRAGLG---EVLPPRDFGLEPILAVHDpDYVDFLET----------------------------- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  783 gigVDSDTVWNEmHSSSAVRMAVGCLLELAFKVAAGElKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKlnVG 862
Cdd:cd10001     73 ---ADTDTPISE-GTWEAALAAADTALTAADLVLEGE-RAAYALCRPPGHHAGRDRAGGFCYFNNAAIAAQYLRDR--AG 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  863 KVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRyDNGNFFP---------GSGApeevgggpGVGYNVNVAwtggVDPPIG 933
Cdd:cd10001    146 RVAILDVDVHHGNGTQEIFYERPDVLYVSIHG-DPRTFYPfflgfadetGEGE--------GEGYNLNLP----LPPGTG 212

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  934 DVEYLTAFRTVVMPIAhEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLMTLaGGRVVLALEGGHDLTAIcd 1013
Cdd:cd10001    213 DDDYLAALDEALAAIA-AFGPDALVVSLGFDTHEG--DPLSDFKLTTEDYARIGRRIAAL-GLPTVFVQEGGYNVDAL-- 286

                          330
                   ....*....|.
gi 1838744837 1014 asEACVSALLS 1024
Cdd:cd10001    287 --GRNAVAFLA 295
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
 704-1008 2.18e-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: 2.18e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  704 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHS-EYHTLLYGTSPlNRQKLDSKKLlgpisqkmyavlpcg 782
Cdd:cd09994     17 HPFNPPRLSLTKDLLRALGLLPPVDLVPPRPATEEELLLFHTpDYIEAVKEASR-GQEPEGRGRL--------------- 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  783 GIGVDSDTVWNEMHSSSAvrMAVGCLLELAFKVAAGELKNGFAIIrppG--HHAEESTAMGFCFFNSVAITAKLLQQKlN 860
Cdd:cd09994     81 GLGTEDNPVFPGMHEAAA--LVVGGTLLAARLVLEGEARRAFNPA---GglHHAMRGRASGFCVYNDAAVAIERLRDK-G 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  861 VGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRyDNGNFFPGSGAPEEVGGGPGVGYNVNVAwtggVDPPIGDVEYLTA 940
Cdd:cd09994    155 GLRVAYVDIDAHHGDGVQAAFYDDPRVLTISLHE-SGRYLFPGTGFVDEIGEGEGYGYAVNIP----LPPGTGDDEFLRA 229

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838744837  941 FRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLMTLA----GGRVVLALEGGHDL 1008
Cdd:cd09994    230 FEAVVPPLLRAFRPDVIVSQHGADAHAG--DPLTHLNLSNRAYRAAVRRIRELAdeycGGRWLALGGGGYNP 299
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 697-1012 2.66e-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: 2.66e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  697 MCGNTHVHPEHAGRIQSIwsrLQETGLLSKCERIRGRKATLDEIQTVHS-EYHTLLYGTSplnrQKLDSkkllgpisQKM 775
Cdd:cd10000     12 LCDRLPKVPNRASMVHSL---IEAYGLLKQLRVVKPRVATEEELASFHSdEYIQFLKKAS----NEGDN--------DEE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  776 YAVLPCGGIGVDSDTVWNEMhssSAVRMAVGCLLELAFKVAAGELKngFAIIRPPG-HHAEESTAMGFCFFNSVAITAKL 854
Cdd:cd10000     77 PSEQQEFGLGYDCPIFEGIY---DYAAAVAGATLTAAQLLIDGKCK--VAINWFGGwHHAQRDEASGFCYVNDIVLGILK 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  855 LQQKLNvgKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGnFFPGSGAPEEVGGGPGVGYNVNVAWTGGVDppigD 934
Cdd:cd10000    152 LREKFD--RVLYVDLDLHHGDGVEDAFSFTSKVMTVSLHKYSPG-FFPGTGDVSDVGLGKGKYYTVNVPLRDGIQ----D 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  935 VEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVT----ARCFGH-LTRQLMTL-AGGrvvlaleGGHDL 1008
Cdd:cd10000    225 EQYLQIFTAVVPEIVAAFRPEAVVLQCGADTLAG--DPMGAFNLTpvgiGKCLKYvLGWKLPTLiLGG-------GGYNL 295


                   ....*.
gi 1838744837 1009 --TAIC 1012
Cdd:cd10000    296 anTARC 301
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 714-996 2.32e-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: 2.32e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  714 IWSRLQETGLLSKCERIRGRKATLDEIQTVHS-EY-HTLLYGTspLNRQKLDSKKLlgPISQKMyaVLPcggigvdsdtv 791
Cdd:cd09993     11 LREALLEEGLVLPEDIVEPEPATREDLLRVHDpEYlESLKSGE--LSREEIRRIGF--PWSPEL--VER----------- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  792 wnemhsssaVRMAVGCLLeLAFKVAageLKNGFAIiRPPG--HHAEESTAMGFCFFNSVAITAKLLQQKLNVGKVLIVDW 869
Cdd:cd09993     74 ---------TRLAVGGTI-LAARLA---LEHGLAI-NLAGgtHHAFPDRGEGFCVFNDIAIAARVLLAEGLVRRVLIVDL 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  870 DIHHGNGTQQAFYNDPSVLYISLHrydNGNFFPGSGAPEevgggpgvgyNVNVawtgGVDPPIGDVEYLTAFRTVVMPIA 949
Cdd:cd09993    140 DVHQGNGTAAIFADDPSVFTFSMH---GEKNYPFRKEPS----------DLDV----PLPDGTGDDEYLAALEEALPRLL 202

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1838744837  950 HEFSPDVVLVSAGFDAVEGhlSPLGGYSVT-----AR-------CFGHLTRQLMTLAGG 996
Cdd:cd09993    203 AEFRPDLVFYNAGVDVLAG--DRLGRLSLSleglrERdrlvlrfARARGIPVAMVLGGG 259
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
 832-1012 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 1838744837  832 HHAEESTAMGFCFFNSVAITAKLLQQKlNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGnFFPGSGApeevG 911
Cdd:cd11680    115 HHAQKSRASGFCYVNDIVLAILRLRRA-RFRRVFYLDLDLHHGDGVESAFFFSKNVLTCSIHRYDPG-FFPGTGS----L 188

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  912 GGPGVGYNVNVAWTGGVDppigDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQLM 991
Cdd:cd11680    189 KNSSDKGMLNIPLKRGLS----DKTLLRIIDSIVRPLIEKFEPEVIVIQCGCDGLSG--DPHKEWNLTIRGYGSVIELLL 262

                          170       180
                   ....*....|....*....|....
gi 1838744837  992 TLAGGRVVLALEGG---HDLTAIC 1012
Cdd:cd11680    263 KEFKDKPTLLLGGGgynHTEAARA 286
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
 697-996 2.39e-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: 2.39e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  697 MCGNTHV---HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHS-EYHTLLYGTSPLNRQKLdsKKLLgpis 772
Cdd:cd09991      5 DVGNYYYgqgHPMKPHRIRMTHSLILSYGLYKKMEIYRPRPATAEELTKFHSdDYIDFLRSVSPDNMKEF--KKQL---- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  773 qKMYavlpcgGIGVDSdTVWNEMHSssAVRMAVGCLLELAFKVAAGELKNGfaiIRPPG--HHAEESTAMGFCFFNSV-- 848
Cdd:cd09991     79 -ERF------NVGEDC-PVFDGLYE--YCQLYAGGSIAAAVKLNRGQADIA---INWAGglHHAKKSEASGFCYVNDIvl 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  849 AITaKLLQQKlnvGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYdnGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGV 928
Cdd:cd09991    146 AIL-ELLKYH---QRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKF--GEYFFPGTGLRDIGAGKGKYYAVNVPLKDGI 219

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1838744837  929 DppigDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVT----ARCFGHLTR---QLMTLAGG 996
Cdd:cd09991    220 D----DESYLQIFEPVLSKVMEVFQPSAVVLQCGADSLAG--DRLGCFNLSikghAKCVKFVKSfniPLLVLGGG 288
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
 733-988 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 1838744837  733 RKATLDEIQTVHSE-YHTLLYGTSPLNRQKLDSKKL----LG---PISQKMYAVLpcggigvdsdtvwnemhsssavRMA 804
Cdd:cd11598     47 RAATREELRQFHDAdYLDFLSKVSPENANQLRFDKAepfnIGddcPVFDGMYDYC----------------------QLY 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  805 VGCLLELAFKVAAGelKNGFAIIRPPG-HHAEESTAMGFCFFNSVAITakLLQQKLNVGKVLIVDWDIHHGNGTQQAFYN 883
Cdd:cd11598    105 AGASLDAARKLCSG--QSDIAINWSGGlHHAKKSEASGFCYVNDIVLA--ILNLLRYFPRVLYIDIDVHHGDGVEEAFYR 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  884 DPSVLYISLHRYdNGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGvdppIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGF 963
Cdd:cd11598    181 TDRVMTLSFHKY-NGEFFPGTGDLDDNGGTPGKHFALNVPLEDG----IDDEQYNLLFKSIIGPTIEKFQPSAIVLQCGA 255

                          250       260
                   ....*....|....*....|....*
gi 1838744837  964 DAVEGhlSPLGGYSVTARCFGHLTR 988
Cdd:cd11598    256 DSLGG--DRLGQFNLNIKAHGACVK 278
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 795-1022 2.25e-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: 99.76  E-value: 2.25e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  795 MHSSSAVRMAVGCLLELAFKVaagelKNGFAIIrppGHHAEestamgfcfFNSVAITAKLLQqklnvGKVLIVDWDIHHG 874
Cdd:cd09987      5 IRKAEAHELLAGVVVAVLKDG-----KVPVVLG---GDHSI---------ANGAIRAVAELH-----PDLGVIDVDAHHD 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  875 NGTQQAFYN--------------DPSVLYISLHRYDNGNFFPGsgapeevgGGPGVGYNVNVAWTGGVDppigDVEYLTA 940
Cdd:cd09987     63 VRTPEAFGKgnhhtprhllceplISDVHIVSIGIRGVSNGEAG--------GAYARKLGVVYFSMTEVD----KLGLGDV 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  941 FRTVVMPIahEFSPDVVLVSAGFDAVEGHLSP----LGGYSVTARCFGHLTRQLMTLaGGRVVLALEGGHDL----TAIC 1012
Cdd:cd09987    131 FEEIVSYL--GDKGDNVYLSVDVDGLDPSFAPgtgtPGPGGLSYREGLYITERIAKT-NLVVGLDIVEVNPLldetGRTA 207

                          250
                   ....*....|
gi 1838744837 1013 DASEACVSAL 1022
Cdd:cd09987    208 RLAAALTLEL 217
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
 699-985 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 1838744837  699 GNTHV---HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHS-EYHTLLYGTSPLNR---QKLDSKKLLG-- 769
Cdd:cd10004     13 GNYAYgpgHPMKPHRIRMAHSLVMNYGLYKKMEIYRAKPATKNEMTQFHTdEYIDFLSRVTPDNMekfQKEQVKYNVGdd 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  770 -PISQKMYavlpcggigvdsdtvwnEMHSSSAvrmavGCLLELAFKVAAGelKNGFAIIRPPG-HHAEESTAMGFCFFNS 847
Cdd:cd10004     93 cPVFDGLF-----------------EFCSISA-----GGSMEGAARLNRG--KCDIAVNWAGGlHHAKKSEASGFCYVND 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  848 VAITA-KLLQQKlnvGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYdnGNFFPGSGAPEEVGGGPGVGYNVNVAWTG 926
Cdd:cd10004    149 IVLGIlELLRYH---QRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKY--GEYFPGTGELRDIGIGTGKNYAVNVPLRD 223

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1838744837  927 GVDppigDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARcfGH 985
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 ...
 704-985 2.50e-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: 2.50e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  704 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSE-YHTLLYGTSPLNRQKLdSKKL----LG---PISQKM 775
Cdd:cd10010     25 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDdYIKFLRSIRPDNMSEY-SKQMqrfnVGedcPVFDGL 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  776 YAV--LPCGGiGVDSDTVWNEMHSSSAVRMAVGCllelafkvaagelkngfaiirppgHHAEESTAMGFCFFNSVAITak 853
Cdd:cd10010    104 FEFcqLSAGG-SVASAVKLNKQQTDIAVNWAGGL------------------------HHAKKSEASGFCYVNDIVLA-- 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  854 LLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYdnGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGVDppig 933
Cdd:cd10010    157 ILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKY--GEYFPGTGDLRDIGAGKGKYYAVNYPLRDGID---- 230

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1838744837  934 DVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARcfGH 985
Cdd:cd10010    231 DESYEAIFKPVMSKVMEMFQPSAVVLQCGADSLSG--DRLGCFNLTIK--GH 278
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
 812-1022 3.41e-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: 3.41e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  812 AFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQ------------- 878
Cdd:cd09998    100 VFKPESPGTKRAFVAIRPPGHHCSESTPSGFCWVNNVHVGAAHAYLTHGITRVVILDIDLHHGNGTQdiawrinaeankq 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  879 -----------QAFYNDPSVLYISLHrydNGNFFP---GSGAPEEVGggpgvgyNVNVA-------WTGGVDPPIGDVEY 937
Cdd:cd09998    180 alesssyddfkPAGAPGLRIFYSSLH---DINSFPcedGDPAKVKDA-------SVSIDgahgqwiWNVHLQPWTTEEDF 249

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  938 LTAFR---TVVMPIAHEF-------SPD--VVLVSAGFDAVEGHLSPLGGYS--VTARCFGHLTRQLMTLA----GGRVV 999
Cdd:cd09998    250 WELYYpkyRILFEKAAEFlrlttaaTPFktLVFISAGFDASEHEYESMQRHGvnVPTSFYYRFARDAVRFAdahaHGRLI 329

                          250       260
                   ....*....|....*....|...
gi 1838744837 1000 LALEGGHDLTAICDASEACVSAL 1022
Cdd:cd09998    330 SVLEGGYSDRALCSGVLAHLTGL 352
PTZ00063 PTZ00063
histone deacetylase; Provisional
 832-996 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 1838744837  832 HHAEESTAMGFCFFNSVAI-TAKLLQQKlnvGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYdnGNFFPGSGAPEEV 910
Cdd:PTZ00063   137 HHAKRSEASGFCYINDIVLgILELLKYH---ARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFPGTGDVTDI 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  911 GGGPGVGYNVNVAWTGGVDppigDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVT----ARCFGH- 985
Cdd:PTZ00063   212 GVAQGKYYSVNVPLNDGID----DDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTG--DRLGRFNLTikghAACVEFv 285

                          170
                   ....*....|...
gi 1838744837  986 --LTRQLMTLAGG 996
Cdd:PTZ00063   286 rsLNIPLLVLGGG 298
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
 699-987 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 1838744837  699 GNTHV---HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSE-YHTLLYGTSPLNRQKLdsKKLLGPISqk 774
Cdd:cd10005     12 GNFHYgpgHPMKPHRLALTHSLVLHYGLYKKMQVYKPYRASAHDMCRFHSEdYIDFLQRVTPQNIQGF--TKSLNQFN-- 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  775 myavlpcggIGVDSdTVWNEMHSSSAvrMAVGCLLELAFKVAAGELKngFAIIRPPG-HHAEESTAMGFCFFNSVAITA- 852
Cdd:cd10005     88 ---------VGDDC-PVFPGLFDFCS--MYTGASLEGATKLNHKICD--IAINWSGGlHHAKKFEASGFCYVNDIVIAIl 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  853 KLLQQKlnvGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNgNFFPGSGAPEEVGGGPGVGYNVNVAWTGGVDppi 932
Cdd:cd10005    154 ELLKYH---PRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGN-YFFPGTGDMYEVGAESGRYYSVNVPLKDGID--- 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  933 gDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDA------------VEGHLS----------PL-----GGYSV--TARCF 983
Cdd:cd10005    227 -DQSYLQLFKPVIQQVIDFYQPTCIVLQCGADSlgcdrlgcfnlsIKGHGEcvefvksfniPLlvlggGGYTVrnVARCW 305


                   ....
gi 1838744837  984 GHLT 987
Cdd:cd10005    306 TYET 309
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
 704-985 3.25e-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: 3.25e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  704 HPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHS-EYHTLLYGTSPLNRQKLdSKKL----LG---PISQKM 775
Cdd:cd10011     21 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSdEYIKFLRSIRPDNMSEY-SKQMqrfnVGedcPVFDGL 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  776 YAV--LPCGGiGVDSDTVWNEMHSSSAVRMAVGCllelafkvaagelkngfaiirppgHHAEESTAMGFCFFNSVAITak 853
Cdd:cd10011    100 FEFcqLSTGG-SVAGAVKLNRQQTDMAVNWAGGL------------------------HHAKKSEASGFCYVNDIVLA-- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  854 LLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISlhRYDNGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGVDppig 933
Cdd:cd10011    153 ILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVS--FHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGID---- 226

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1838744837  934 DVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARcfGH 985
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 ...
 68-164 1.91e-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: 75.63  E-value: 1.91e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837   68 DPTLREQQLQQELLALKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEMLAAKRQQELEQQRQR 147
Cdd:cd10164      1 DPSLREQQLQQELLLLKQQQQLQKQLLFAEFQKQHEHLTRQHEVQLQKHLKVRAELFSEQQQQEILAAKRQQELEQQRKR 80

                           90
                   ....*....|....*..
gi 1838744837  148 EQQRQEELEKQRLEQQL 164
Cdd:cd10164     81 EQQRQEELEKQRLEQQL 97
PTZ00346 PTZ00346
histone deacetylase; Provisional
 832-1005 2.80e-13

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 73.53  E-value: 2.80e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  832 HHAEESTAMGFCFFNSVAItaKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNgNFFPGSGAPEEVG 911
Cdd:PTZ00346   154 HHSKCGECSGFCYVNDIVL--GILELLKCHDRVLYVDIDMHHGDGVDEAFCTSDRVFTLSLHKFGE-SFFPGTGHPRDVG 230

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837  912 GGPGVGYNVNVA-WTGgvdppIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGhlSPLGGYSVTARCFGHLTRQL 990
Cdd:PTZ00346   231 YGRGRYYSMNLAvWDG-----ITDFYYLGLFEHALHSIVRRYSPDAIVLQCGADSLAG--DRLGLLNLSSFGHGQCVQAV 303

                          170
                   ....*....|....*
gi 1838744837  991 MTLagGRVVLALEGG 1005
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, ...
 68-164 2.26e-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: 2.26e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837   68 DPTLREQQLQQELLALKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEMLAAKrqqeleqQRQR 147
Cdd:cd10149      1 DPVLREQQLQQELLALKQQQQIQKQLLIAEFQKQHENLTRQHEAQLQEHIKQQQEMLAIKQQQELLEKQ-------RKLE 73

                           90
                   ....*....|....*..
gi 1838744837  148 EQQRQEELEKQRLEQQL 164
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 ...
 68-133 3.93e-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: 3.93e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838744837   68 DPTLREQQLQQELLALKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEML 133
Cdd:cd10163      1 DPTVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHLKLQQELLAMKQQQELL 66
HDAC4_Gln pfam12203
Glutamine rich N terminal domain of histone deacetylase 4; This domain is found in eukaryotes, ...
 95-164 4.04e-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: 4.04e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744837   95 FAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEMLAAKrqqeleqQRQREQQRQEELEKQRLEQQL 164
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 ...
 68-133 1.19e-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: 1.19e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838744837   68 DPTLREQQLQQELLALKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEML 133
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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