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Conserved domains on  [gi|1622924881|ref|XP_028701820|]
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histone deacetylase 9 isoform X22 [Macaca mulatta]

Protein Classification

histone deacetylase 9( domain architecture ID 10178373)

histone deacetylase 9 (HD9) is a Class IIa histone deacetylase responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 656-1033 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: 792.32  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  656 SATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQ 735
Cdd:cd11681      1 FTTGLAYDPLMLKHQCICGNNSSHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTLLYGTNPLSRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  736 KLDPRILLGDdSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAM 815
Cdd:cd11681     81 KLDPTKLAGL-PQKSFVRLPCGGIGVDSDTVWNELHTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQAM 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  816 GFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYNI 895
Cdd:cd11681    160 GFCFFNSVAIAAKQLQQKLKLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFPGTGAPTEVGSGAGEGFNV 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  896 NIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVL 975
Cdd:cd11681    240 NIAWSGGLDPPMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPPPLGGYKVSPACFGYMTRQLMNLAGGKVVL 319

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622924881  976 ALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSKYW 1033
Cdd:cd11681    320 ALEGGYDLTAICDASEACVRALLGDELDPLSEEELERRPNPNAVTSLEKVIAIQSPYW 377
ClassIIa_HDAC9_Gln-rich-N cd10163
Glutamine-rich N-terminal helical domain of HDAC9, a Class IIa histone deacetylase; This ...
 60-149 3.73e-23

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: 94.44  E-value: 3.73e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881   60 DPVVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIKLQQELLAIKQQQELLEKEQKLEQQRQEQE 139
Cdd:cd10163      1 DPTVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHLKLQQELLAMKQQQELLEKEQKLEQQRQEQE 80

                           90
                   ....*....|
gi 1622924881  140 VERHRREQQL 149
Cdd:cd10163     81 LERHRREQQL 90
 
Name Accession Description Interval E-value
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 656-1033 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: 792.32  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  656 SATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQ 735
Cdd:cd11681      1 FTTGLAYDPLMLKHQCICGNNSSHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTLLYGTNPLSRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  736 KLDPRILLGDdSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAM 815
Cdd:cd11681     81 KLDPTKLAGL-PQKSFVRLPCGGIGVDSDTVWNELHTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQAM 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  816 GFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYNI 895
Cdd:cd11681    160 GFCFFNSVAIAAKQLQQKLKLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFPGTGAPTEVGSGAGEGFNV 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  896 NIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVL 975
Cdd:cd11681    240 NIAWSGGLDPPMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPPPLGGYKVSPACFGYMTRQLMNLAGGKVVL 319

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622924881  976 ALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSKYW 1033
Cdd:cd11681    320 ALEGGYDLTAICDASEACVRALLGDELDPLSEEELERRPNPNAVTSLEKVIAIQSPYW 377
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 679-997 1.71e-123

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: 380.04  E-value: 1.71e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  679 HPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHH-SLLYGTNPLDGQKLDPRILLGDDSQKFFSslpcg 757
Cdd:pfam00850    1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYlEFLEEAAPEGGALLLLSYLSGDDDTPVSP----- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  758 glgvdsdtiwnelHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQLNIS 837
Cdd:pfam00850   76 -------------GSYEAALLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLK 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  838 KILIVDLDVHHGNGTQQAFYADPSILYISLHRYDeGNFFPGSGAPNEVGTGLGEGYNINIAWTGGldppMGDVEYLEAFR 917
Cdd:pfam00850  143 RVAIVDFDVHHGNGTQEIFYDDPSVLTLSIHQYP-GGFYPGTGFADETGEGKGKGYTLNVPLPPG----TGDAEYLAAFE 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  918 TIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLAD---GRVVLALEGGHDLTAICDASEACV 994
Cdd:pfam00850  218 EILLPALEEFQPDLILVSAGFDAHAGD--PLGGLNLTTEGFAEITRILLELADplcIRVVSVLEGGYNLDALARSATAVL 295


                   ...
gi 1622924881  995 NAL 997
Cdd:pfam00850  296 AAL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 658-999 7.75e-108

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 339.01  E-value: 7.75e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  658 TGIAYDPLMLKHQCvcgnSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHsllygtnpldgqkL 737
Cdd:COG0123      1 TALIYHPDYLLHDL----GPGHPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDY-------------V 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  738 DprillgddsqKFFSSLPCGGLG-VDSDTIWNElHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMG 816
Cdd:COG0123     64 D----------ALRAASLDGGYGqLDPDTPVSP-GTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMG 132

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  817 FCFFNSVAITAKYLRDQlNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdegNFFPGSGAPNEVGTGLGEGYNIN 896
Cdd:COG0123    133 FCLFNNAAIAARYLLAK-GLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD---PLYPGTGAADETGEGAGEGSNLN 208

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  897 IAwtggLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLAD---GRV 973
Cdd:COG0123    209 VP----LPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHADD--PLGRLNLTTEGYAWRTRRVLELADhcgGPV 282

                          330       340
                   ....*....|....*....|....*.
gi 1622924881  974 VLALEGGHDLTAICDASEACVNALLG 999
Cdd:COG0123    283 VSVLEGGYNLDALARSVAAHLETLLG 308
ClassIIa_HDAC9_Gln-rich-N cd10163
Glutamine-rich N-terminal helical domain of HDAC9, a Class IIa histone deacetylase; This ...
 60-149 3.73e-23

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: 94.44  E-value: 3.73e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881   60 DPVVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIKLQQELLAIKQQQELLEKEQKLEQQRQEQE 139
Cdd:cd10163      1 DPTVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHLKLQQELLAMKQQQELLEKEQKLEQQRQEQE 80

                           90
                   ....*....|
gi 1622924881  140 VERHRREQQL 149
Cdd:cd10163     81 LERHRREQQL 90
PTZ00063 PTZ00063
histone deacetylase; Provisional
 807-960 1.19e-21

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 99.11  E-value: 1.19e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  807 HHAEESTAMGFCFFNSVAITA----KYLrdqlniSKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdeGNFFPGSGAP 882
Cdd:PTZ00063   137 HHAKRSEASGFCYINDIVLGIlellKYH------ARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFPGTGDV 208

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622924881  883 NEVGTGLGEGYNINIAWTGGLDppmgDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTppLGGYKVTAKcfGH 960
Cdd:PTZ00063   209 TDIGVAQGKYYSVNVPLNDGID----DDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDR--LGRFNLTIK--GH 278
HDAC4_Gln pfam12203
Glutamine rich N terminal domain of histone deacetylase 4; This domain is found in eukaryotes, ...
 87-149 1.43e-17

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: 78.74  E-value: 1.43e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622924881   87 IAEFQKQHENLTRQHQAQLQEHIKLQQELLAIKQQQELLEKEQKLEQQRQEQEVERHRREQQL 149
Cdd:pfam12203   29 IAEFQKQHELLTRQHEAQLQEHIKQQQELLAMKQQQELLEQQRKLEQQRQEEELEKHRREQQL 91
 
Name Accession Description Interval E-value
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 656-1033 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: 792.32  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  656 SATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQ 735
Cdd:cd11681      1 FTTGLAYDPLMLKHQCICGNNSSHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTLLYGTNPLSRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  736 KLDPRILLGDdSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAM 815
Cdd:cd11681     81 KLDPTKLAGL-PQKSFVRLPCGGIGVDSDTVWNELHTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQAM 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  816 GFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYNI 895
Cdd:cd11681    160 GFCFFNSVAIAAKQLQQKLKLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFPGTGAPTEVGSGAGEGFNV 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  896 NIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVL 975
Cdd:cd11681    240 NIAWSGGLDPPMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPPPLGGYKVSPACFGYMTRQLMNLAGGKVVL 319

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622924881  976 ALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSKYW 1033
Cdd:cd11681    320 ALEGGYDLTAICDASEACVRALLGDELDPLSEEELERRPNPNAVTSLEKVIAIQSPYW 377
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
 656-1034 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: 792.29  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  656 SATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQ 735
Cdd:cd10009      1 SATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  736 KLDPRILLGDDSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAM 815
Cdd:cd10009     81 KLDPRILLGDDSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAM 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  816 GFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYNI 895
Cdd:cd10009    161 GFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYNI 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  896 NIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVL 975
Cdd:cd10009    241 NIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVL 320

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622924881  976 ALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSKYWK 1034
Cdd:cd10009    321 ALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSKYWK 379
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
 656-1071 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: 754.13  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  656 SATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQ 735
Cdd:cd10007      3 FTTGLVYDTFMLKHQCTCGNTNVHPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHSEHHTLLYGTSPLNRQ 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  736 KLDPRILLGDDSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAM 815
Cdd:cd10007     83 KLDSKKLLGPLSQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLIELAFKVAAGELKNGFAVIRPPGHHAEESTAM 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  816 GFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYNI 895
Cdd:cd10007    163 GFCFFNSVAIAAKLLQQKLNVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGNFFPGSGAPDEVGAGPGVGFNV 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  896 NIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVL 975
Cdd:cd10007    243 NIAWTGGVDPPIGDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGHQSPLGGYSVTAKCFGHLTKQLMTLAGGRVVL 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  976 ALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSKYWKSVRMVAVPRGCALAGAQLQE- 1054
Cdd:cd10007    323 ALEGGHDLTAICDASEACVSALLGMELTPLDNTVLQQKPNDNAVATLERVIEIQSKHWSCLKRFAATLGFSLLEAQRGEl 402

                          410
                   ....*....|....*...
gi 1622924881 1055 -ETETVSALASLTVDVEQ 1071
Cdd:cd10007    403 eEAETVSAMASLSVDTEQ 420
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
 653-1060 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: 712.96  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  653 QPGSATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPL 732
Cdd:cd10006      1 KPRFTTGLVYDTLMLKHQCTCGNSNSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  733 DGQKLDPRILLGDDSQkFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEES 812
Cdd:cd10006     81 NRQKLDSKKLLGSLAS-VFVRLPCGGVGVDSDTIWNEVHSSGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEES 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  813 TAMGFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEG 892
Cdd:cd10006    160 TPMGFCYFNSVAIAAKLLQQRLNVSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVG 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  893 YNINIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGR 972
Cdd:cd10006    240 FNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSAKCFGYLTKQLMGLAGGR 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  973 VVLALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSKYWKSVRMVAVPRGCALAGAQL 1052
Cdd:cd10006    320 IVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGYSLIEAQT 399

                          410
                   ....*....|
gi 1622924881 1053 --QEETETVS 1060
Cdd:cd10006    400 ceNEEAETVT 409
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
 658-1033 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: 672.49  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  658 TGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQKL 737
Cdd:cd10008      3 TGLVYDSVMLKHQCSCGDNSNHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLKL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  738 DPRILLGDDSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGF 817
Cdd:cd10008     83 DNGKLAGLLAQRMFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGF 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  818 CFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYNINI 897
Cdd:cd10008    163 CFFNSVAIACRQLQQQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGAGSGEGFNVNV 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  898 AWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVLAL 977
Cdd:cd10008    243 AWAGGLDPPMGDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVLAL 322

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622924881  978 EGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSKYW 1033
Cdd:cd10008    323 EGGHDLTAICDASEACVAALLGNEVDPLSEESWKQKPNLNAIRSLEAVIRVHSKYW 378
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
 679-998 2.36e-138

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: 418.44  E-value: 2.36e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  679 HPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHH-SLLYGTNPLDGQKLDPrillgddsqkffsslpcg 757
Cdd:cd09992      1 HPERPERLLAILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYiERVEETCEAGGGYLDP------------------ 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  758 glgvdsDTIWNElHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQLNIS 837
Cdd:cd09992     63 ------DTYVSP-GSYEAALLAAGAALAAVDAVLSGEAENAFALVRPPGHHAEPDRAMGFCLFNNVAIAARYAQKRYGLK 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  838 KILIVDLDVHHGNGTQQAFYADPSILYISLHRYDegnFFPGSGAPNEVGTGLGEGYNINIAWTGGldppMGDVEYLEAFR 917
Cdd:cd09992    136 RVLIVDWDVHHGNGTQDIFYDDPSVLYFSIHQYP---FYPGTGAAEETGGGAGEGFTINVPLPPG----SGDAEYLAAFE 208

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  918 TIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLAD----GRVVLALEGGHDLTAICDASEAC 993
Cdd:cd09992    209 EVLLPIAREFQPDLVLVSAGFDAHRGD--PLGGMNLTPEGYARLTRLLKELADehcgGRLVFVLEGGYNLEALAESVLAV 286


                   ....*
gi 1622924881  994 VNALL 998
Cdd:cd09992    287 LEALL 291
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
 662-1037 7.05e-138

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: 419.82  E-value: 7.05e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  662 YDPLMLKHQCVCgnSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHH-SLLYGTnpldgQKLDPR 740
Cdd:cd10003      1 YDQRMMNHHNLW--DPGHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHlDEMKSL-----EKMKPR 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  741 ILlgddsqkffsslpcGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFF 820
Cdd:cd10003     74 EL--------------NRLGKEYDSIYIHPDSYQCALLAAGCVLQVVEAVLTGESRNGVAIVRPPGHHAEQDTACGFCFF 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  821 NSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGS--GAPNEVGTGLGEGYNINIA 898
Cdd:cd10003    140 NNVAIAARYAQKKYGLKRILIVDWDVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSpeGNYDVVGKGKGEGFNVNIP 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  899 WTGGldpPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLADGRVVLALE 978
Cdd:cd10003    220 WNKG---GMGDAEYIAAFQQVVLPIAYEFNPELVLVSAGFDAARGD--PLGGCKVTPEGYAHMTHMLMSLAGGRVIVILE 294

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622924881  979 GGHDLTAICDASEACVNALLGNELEPLaedILHQSPNMNAVISLQKIIEIQSKYWKSVR 1037
Cdd:cd10003    295 GGYNLTSISESMSMCTKTLLGDPPPVL---DLPRPPCSSALKSINNVLQVHQKYWKSLR 350
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 679-997 1.71e-123

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: 380.04  E-value: 1.71e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  679 HPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHH-SLLYGTNPLDGQKLDPRILLGDDSQKFFSslpcg 757
Cdd:pfam00850    1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYlEFLEEAAPEGGALLLLSYLSGDDDTPVSP----- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  758 glgvdsdtiwnelHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQLNIS 837
Cdd:pfam00850   76 -------------GSYEAALLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLK 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  838 KILIVDLDVHHGNGTQQAFYADPSILYISLHRYDeGNFFPGSGAPNEVGTGLGEGYNINIAWTGGldppMGDVEYLEAFR 917
Cdd:pfam00850  143 RVAIVDFDVHHGNGTQEIFYDDPSVLTLSIHQYP-GGFYPGTGFADETGEGKGKGYTLNVPLPPG----TGDAEYLAAFE 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  918 TIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLAD---GRVVLALEGGHDLTAICDASEACV 994
Cdd:pfam00850  218 EILLPALEEFQPDLILVSAGFDAHAGD--PLGGLNLTTEGFAEITRILLELADplcIRVVSVLEGGYNLDALARSATAVL 295


                   ...
gi 1622924881  995 NAL 997
Cdd:pfam00850  296 AAL 298
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 679-1005 2.79e-119

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: 369.37  E-value: 2.79e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  679 HPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHsllygtnpLDG----QKLDPRILlgDDSQKFFSSL 754
Cdd:cd11600      3 HPEDPSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEH--------WDRveatEKMSDEQL--KDRTEIFERD 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  755 pcgGLGVDSdtiwnelHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQL 834
Cdd:cd11600     73 ---SLYVNN-------DTAFCARLSCGGAIEACRAVAEGRVKNAFAVVRPPGHHAEPDESMGFCFFNNVAVAAKWLQTEY 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  835 --NISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGS--GAPNEVGTGLGEGYNINIAWTgglDPPMGDV 910
Cdd:cd11600    143 pdKIKKILILDWDIHHGNGTQRAFYDDPNVLYISLHRFENGGFYPGTpyGDYESVGEGAGLGFNVNIPWP---QGGMGDA 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  911 EYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLADGRVVLALEGGHDLTAICDAS 990
Cdd:cd11600    220 DYIYAFQRIVMPIAYEFDPDLVIISAGFDAADGD--ELGQCHVTPAGYAHMTHMLMSLAGGKLVVALEGGYNLDAISDSA 297

                          330
                   ....*....|....*
gi 1622924881  991 EACVNALLGNELEPL 1005
Cdd:cd11600    298 LAVAKVLLGEAPPKL 312
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 658-999 7.75e-108

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 339.01  E-value: 7.75e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  658 TGIAYDPLMLKHQCvcgnSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHsllygtnpldgqkL 737
Cdd:COG0123      1 TALIYHPDYLLHDL----GPGHPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDY-------------V 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  738 DprillgddsqKFFSSLPCGGLG-VDSDTIWNElHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMG 816
Cdd:COG0123     64 D----------ALRAASLDGGYGqLDPDTPVSP-GTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMG 132

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  817 FCFFNSVAITAKYLRDQlNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdegNFFPGSGAPNEVGTGLGEGYNIN 896
Cdd:COG0123    133 FCLFNNAAIAARYLLAK-GLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD---PLYPGTGAADETGEGAGEGSNLN 208

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  897 IAwtggLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLAD---GRV 973
Cdd:COG0123    209 VP----LPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHADD--PLGRLNLTTEGYAWRTRRVLELADhcgGPV 282

                          330       340
                   ....*....|....*....|....*.
gi 1622924881  974 VLALEGGHDLTAICDASEACVNALLG 999
Cdd:COG0123    283 VSVLEGGYNLDALARSVAAHLETLLG 308
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 678-1033 4.26e-105

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: 332.74  E-value: 4.26e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  678 THPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHS-EHHSLLYGTNpldgqkldpriLLGDDSQKFFSSlpc 756
Cdd:cd10002      6 NHIECPERLEAILERLTQDGLLERCVKIPAREAEEDEILLVHSqEYIDLVKSTE-----------TMEKEELESLCS--- 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  757 gglgvDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQLNI 836
Cdd:cd10002     72 -----GYDSVYLCPSTYEAARLAAGSTIELVKAVMAGKIQNGFALIRPPGHHAMRNEANGYCIFNNVAIAAKYAIEKLGL 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  837 SKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPN--EVGTGLGEGYNINIAW--TGgldppMGDVEY 912
Cdd:cd10002    147 KRILIVDWDVHHGQGTQQGFYEDPRVLYFSIHRYEHGRFWPHLFESDydYIGVGHGYGFNVNVPLnqTG-----LGDADY 221

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  913 LEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLADGRVVLALEGGHDLTAICDASEA 992
Cdd:cd10002    222 LAIFHHILLPLALEFQPELVLVSAGFDASIGD--PEGEMAVTPAGYAHLTRLLMGLAGGKLLLVLEGGYLLESLAESVSM 299

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1622924881  993 CVNALLGNELEPLAEDIlhqsPNMNAVISLQKIIEIQSKYW 1033
Cdd:cd10002    300 TLRGLLGDPLPPLAPPI----PIRSVLETILNAIAHLSPRW 336
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
 685-997 3.08e-100

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: 317.45  E-value: 3.08e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  685 RIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQKLDprillgddsqkffsslpcGGLGVDSD 764
Cdd:cd09301      1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKANFAVATITE------------------SKPVIFGP 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  765 TIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRdQLNISKILIVDL 844
Cdd:cd09301     63 NFPVQRHYFRGARLSTGGVVEAAELVAKGELERAFAVVGAGGHHAGKSRAWGFCYFNDVVLAIKFLR-ERGISRILIIDT 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  845 DVHHGNGTQQAFYADPSILYISLHRYDEGNFfpgsgapnevGTGLGEGYNINIAWTGGldppMGDVEYLEAFRTIVKPVA 924
Cdd:cd09301    142 DAHHGDGTREAFYDDDRVLHMSFHNYDIYPF----------GRGKGKGYKINVPLEDG----LGDEEYLDAVERVISKVL 207

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622924881  925 KEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLAD-GRVVLALEGGHDLTAICDASEACVNAL 997
Cdd:cd09301    208 EEFEPEVVVLQFGHDTHEGD--RLGGFNLSEKGFVKLAEIVKEFARgGPILMVLGGGYNPEAAARIWTAIIKEL 279
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
 679-998 1.28e-84

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: 275.93  E-value: 1.28e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  679 HPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHH-SLLYGTNPLDGQKLdprillgddsqkffsslpcg 757
Cdd:cd11599      1 HPESPERLEAILDALIASGLDRLLRQLEAPPATREQLLRVHDAAYvDRLEAAAPEEGLVQ-------------------- 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  758 glgVDSDTIWNElHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQLNIS 837
Cdd:cd11599     61 ---LDPDTAMSP-GSLEAALRAAGAVVAAVDAVMAGEARNAFCAVRPPGHHAERDKAMGFCLFNNVAIAAAHALAHHGLE 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  838 KILIVDLDVHHGNGTQQAFYADPSILYISLHRYdegNFFPGSGAPNEVGTGlgegyNI-NIAwtggLDPPMGDVEYLEAF 916
Cdd:cd11599    137 RVAIVDFDVHHGNGTEDIFRDDPRVLFCSSHQH---PLYPGTGAPDETGHG-----NIvNVP----LPAGTGGAEFREAV 204

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  917 RTIVKPVAKEFDPDMVLVSAGFDAlegHT-PPLGGYKVTAKCFGHLTKQLMTLAD----GRVVLALEGGHDLTAICDASE 991
Cdd:cd11599    205 EDRWLPALDAFKPDLILISAGFDA---HRdDPLAQLNLTEEDYAWITEQLMDVADrycdGRIVSVLEGGYDLSALARSVA 281


                   ....*..
gi 1622924881  992 ACVNALL 998
Cdd:cd11599    282 AHVRALM 288
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
 658-1014 1.76e-83

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: 275.21  E-value: 1.76e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  658 TGIAYDPLMLKH--------QCVCG---NSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHsll 726
Cdd:cd09996      1 TGFVWDERYLWHdtgtgalfLPVGGllvQPGRHPENPETKRRIKNLLEVSGLSDHLVLITPRPATDEELLRVHTPEY--- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  727 ygtnpldgqkLDpRIllgddsqKFFSSLPCGGLGvdSDTIWNElHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPG 806
Cdd:cd09996     78 ----------ID-RV-------KAASAAGGGEAG--GGTPFGP-GSYEIALLAAGGAIAAVDAVLDGEVDNAYALVRPPG 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  807 HHAEESTAMGFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRydEGNFFPGSGAPNEVG 886
Cdd:cd09996    137 HHAEPDQGMGFCLFNNVAIAARHALAVGGVKRVAVVDWDVHHGNGTQAIFYDDPDVLTISLHQ--DRCFPPDSGAVEERG 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  887 TGLGEGYNINIAwtggLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDAleGHTPPLGGYKVTAKCFGHLTKQLM 966
Cdd:cd09996    215 EGAGEGYNLNIP----LPPGSGDGAYLHAFERIVLPALRAFRPELIIVASGFDA--SAFDPLGRMMLTSDGFRALTRKLR 288

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622924881  967 TLAD----GRVVLALEGGHDLT--AICDAseACVNALLGNEL---EPLAEDILHQSP 1014
Cdd:cd09996    289 DLADelcgGRLVMVHEGGYSEAyvPFCGL--AVLEELSGVRTgiaDPLLYYPEAQGG 343
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
 678-1033 4.22e-83

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: 273.65  E-value: 4.22e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  678 THPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHS-EHHSLLYGTNPLDGQKLdpRILlgddSQKFfsslpc 756
Cdd:cd11682      6 SFPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSpEYVALMKSTQYMTEEEL--RTL----ADTY------ 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  757 gglgvdsDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQLNI 836
Cdd:cd11682     74 -------DSVYLHPNSYSCACLAVGSVLQLVDKVLGGEIRNGLAIVRPPGHHAQHDKMDGYCMFNNVAIAARYAQQKHGV 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  837 SKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFP--GSGAPNEVGTGLGEGYNINIAWTgglDPPMGDVEYLE 914
Cdd:cd11682    147 QRVLIVDWDVHHGQGTQFIFEQDPSVLYFSIHRYEQGRFWPhlKESDSSAVGFGRGEGYNINVPWN---QVGMRDADYIA 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  915 AFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLADGRVVLALEGGHDLTAICDASEACV 994
Cdd:cd11682    224 AFLHVLLPVALEFQPQLVLVAAGFDAVIGD--PKGEMAATPACFAHLTHLLMGLAGGKLILSLEGGYNLRSLAEGVCASL 301

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1622924881  995 NALLGnelEPLAEDILHQSPNMNAVISLQKIIEIQSKYW 1033
Cdd:cd11682    302 KALLG---DPCPMLESPGAPCRSALASVSCTISALEPFW 337
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 685-1033 2.01e-75

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: 252.48  E-value: 2.01e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  685 RIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQKLDPRIllgddSQKFfsslpcgglgvdsD 764
Cdd:cd11683     13 RLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRETQVMNKEELMAI-----SGKY-------------D 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  765 TIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQLNISKILIVDL 844
Cdd:cd11683     75 AVYFHPNTFHCARLAAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYAKKKYGLHRILIVDW 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  845 DVHHGNGTQQAFYADPSILYISLHRYDEGNFFPG--SGAPNEVGTGLGEGYNINIAWTgglDPPMGDVEYLEAFRTIVKP 922
Cdd:cd11683    155 DVHHGQGIQYIFEEDPSVLYFSWHRYEHQRFWPFlrESDYDAVGRGKGLGFNINLPWN---KVGMGNADYLAAFFHVLLP 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  923 VAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLADGRVVLALEGGHDLTAICDASEACVNALLGNEL 1002
Cdd:cd11683    232 LAFEFDPELVLVSAGFDSAIGD--PEGQMCATPECFAHLTHLLMVLAGGKLCAVLEGGYHLESLAESVCMTVQTLLGDPL 309

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1622924881 1003 EPLAEDIlhqSPNMNAVISLQKIIEIQSKYW 1033
Cdd:cd11683    310 PRLSGEM---TPCQSALESIQNVRAAQAPYW 337
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
 660-999 1.77e-72

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: 242.83  E-value: 1.77e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  660 IAYDPLMLKHQ----CVCGNSTTHPEHAGRIQSIWSRLQETGLLnkcERIQGRKASLEEIQLVHSEHHsllygtnpldgq 735
Cdd:cd10001      2 IVYSEDHLLHHpkteLSRGKLVPHPENPERAEAILDALKRAGLG---EVLPPRDFGLEPILAVHDPDY------------ 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  736 kLDprillgddsqkFFSSLpcgglgvDSDTIWNElHSSGAARMAVGCVIELASKVASGElKNGFAVVRPPGHHAEESTAM 815
Cdd:cd10001     67 -VD-----------FLETA-------DTDTPISE-GTWEAALAAADTALTAADLVLEGE-RAAYALCRPPGHHAGRDRAG 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  816 GFCFFNSVAITAKYLRDQLniSKILIVDLDVHHGNGTQQAFYADPSILYISLHRyDEGNFFPG-SGAPNEVGTGLGEGYN 894
Cdd:cd10001    126 GFCYFNNAAIAAQYLRDRA--GRVAILDVDVHHGNGTQEIFYERPDVLYVSIHG-DPRTFYPFfLGFADETGEGEGEGYN 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  895 INIAwtggLDPPMGDVEYLEAFRTIVKPVAkEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLaDGRVV 974
Cdd:cd10001    203 LNLP----LPPGTGDDDYLAALDEALAAIA-AFGPDALVVSLGFDTHEGD--PLSDFKLTTEDYARIGRRIAAL-GLPTV 274

                          330       340
                   ....*....|....*....|....*
gi 1622924881  975 LALEGGHDLTAIcdaSEACVNALLG 999
Cdd:cd10001    275 FVQEGGYNVDAL---GRNAVAFLAG 296
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
 679-983 2.72e-53

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: 188.92  E-value: 2.72e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  679 HPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHhsllYgtnpLDGQKLDPRILLGDDSQKFfsslpcgG 758
Cdd:cd09994     17 HPFNPPRLSLTKDLLRALGLLPPVDLVPPRPATEEELLLFHTPD----Y----IEAVKEASRGQEPEGRGRL-------G 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  759 LGVDSDTIWNELHSsgAARMAVGCVIELASKVASGElknGFAVVRPPG--HHAEESTAMGFCFFNSVAITAKYLRDQlNI 836
Cdd:cd09994     82 LGTEDNPVFPGMHE--AAALVVGGTLLAARLVLEGE---ARRAFNPAGglHHAMRGRASGFCVYNDAAVAIERLRDK-GG 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  837 SKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGnFFPGSGAPNEVGTGLGEGYNINIAwtggLDPPMGDVEYLEAF 916
Cdd:cd09994    156 LRVAYVDIDAHHGDGVQAAFYDDPRVLTISLHESGRY-LFPGTGFVDEIGEGEGYGYAVNIP----LPPGTGDDEFLRAF 230

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622924881  917 RTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLAD----GRVVLALEGGHDL 983
Cdd:cd09994    231 EAVVPPLLRAFRPDVIVSQHGADAHAGD--PLTHLNLSNRAYRAAVRRIRELADeycgGRWLALGGGGYNP 299
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 672-1037 2.68e-37

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: 144.40  E-value: 2.68e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  672 VCGNSTTHPEHAGRIQSIwsrLQETGLLNKCERIQGRKASLEEIQLVHSEH--HSLLYGTNPLDGQKLDprillgDDSQK 749
Cdd:cd10000     12 LCDRLPKVPNRASMVHSL---IEAYGLLKQLRVVKPRVATEEELASFHSDEyiQFLKKASNEGDNDEEP------SEQQE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  750 FfsslpcgGLGVDSDTIWNELHssgAARMAVGCVIELASKVASGELKngFAVVRPPG-HHAEESTAMGFCFFNSVAITAK 828
Cdd:cd10000     83 F-------GLGYDCPIFEGIYD---YAAAVAGATLTAAQLLIDGKCK--VAINWFGGwHHAQRDEASGFCYVNDIVLGIL 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  829 YLRDQLniSKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGnFFPGSGAPNEVGTGLGEGYNINIAWTGGLDppmg 908
Cdd:cd10000    151 KLREKF--DRVLYVDLDLHHGDGVEDAFSFTSKVMTVSLHKYSPG-FFPGTGDVSDVGLGKGKYYTVNVPLRDGIQ---- 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  909 DVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVT----AKCFGHLTK-QLMTLADGrvvlalEGGHDL 983
Cdd:cd10000    224 DEQYLQIFTAVVPEIVAAFRPEAVVLQCGADTLAGD--PMGAFNLTpvgiGKCLKYVLGwKLPTLILG------GGGYNL 295

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622924881  984 --TAICDASeacVNALLGNelEPLAEDI--------------LHQSP----NMNAVISLQKIIEIQSKYWKSVR 1037
Cdd:cd10000    296 anTARCWTY---LTGLILG--EPLSSDIpdhefftsygpdyeLEISPslrpDLNEDQYIEKILETIKGNLKNVV 364
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 689-955 2.65e-35

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: 135.70  E-value: 2.65e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  689 IWSRLQETGLLNKCERIQGRKASLEEIQLVHSEH--HSLLYGTNPLdgqKLDPRILLgddsqkffsslPcgglgvdsdtI 766
Cdd:cd09993     11 LREALLEEGLVLPEDIVEPEPATREDLLRVHDPEylESLKSGELSR---EEIRRIGF-----------P----------W 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  767 WNELHSSgaARMAVGCVIeLASKVAsgeLKNGFAVvRPPG--HHAEESTAMGFCFFNSVAITAKYLRDQLNISKILIVDL 844
Cdd:cd09993     67 SPELVER--TRLAVGGTI-LAARLA---LEHGLAI-NLAGgtHHAFPDRGEGFCVFNDIAIAARVLLAEGLVRRVLIVDL 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  845 DVHHGNGTQQAFYADPSILYISLHryDEGNfFPGSGAPNevgtglgegyNINIawtgGLDPPMGDVEYLEAFRTIVKPVA 924
Cdd:cd09993    140 DVHQGNGTAAIFADDPSVFTFSMH--GEKN-YPFRKEPS----------DLDV----PLPDGTGDDEYLAALEEALPRLL 202

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1622924881  925 KEFDPDMVLVSAGFDALEGHtpPLGGYKVTA 955
Cdd:cd09993    203 AEFRPDLVFYNAGVDVLAGD--RLGRLSLSL 231
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
 679-963 1.64e-30

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: 122.69  E-value: 1.64e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  679 HPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHH-SLLYGTNPLDGQKLdprillGDDSQKFfsslpcg 757
Cdd:cd09991     15 HPMKPHRIRMTHSLILSYGLYKKMEIYRPRPATAEELTKFHSDDYiDFLRSVSPDNMKEF------KKQLERF------- 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  758 GLGVD---SDTIWNelhssgAARMAVGCVIELASKVASGELKngfAVVRPPG--HHAEESTAMGFCFFNSVAITAKYLRD 832
Cdd:cd09991     82 NVGEDcpvFDGLYE------YCQLYAGGSIAAAVKLNRGQAD---IAINWAGglHHAKKSEASGFCYVNDIVLAILELLK 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  833 QLniSKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGnfFPGSGAPNEVGTGLGEGYNINIAwtggLDPPMGDVEY 912
Cdd:cd09991    153 YH--QRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKFGEY--FFPGTGLRDIGAGKGKYYAVNVP----LKDGIDDESY 224

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622924881  913 LEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVT----AKCFGHLTK 963
Cdd:cd09991    225 LQIFEPVLSKVMEVFQPSAVVLQCGADSLAGD--RLGCFNLSikghAKCVKFVKS 277
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
 807-987 3.23e-29

Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is responsible for Smc3 deacetylation. Smc3 is an important player during the establishment of sister chromatid cohesion. Hos1 belongs to the class I histone deacetylases (HDACs). HDACs are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues in histone amino termini to yield a deacetylated histone (EC 3.5.1.98). Enzymes belonging to this group participate in regulation of a number of processes through protein (mostly different histones) modification (deacetylation). Class I histone deacetylases in general act via the formation of large multiprotein complexes. Other class I HDACs are animal HDAC1, HDAC2, HDAC3, HDAC8, fungal RPD3 and HOS2, plant HDA9, protist, archaeal and bacterial (AcuC) deacetylases. Members of this class are involved in cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and in posttranslational control of the acetyl coenzyme A synthetase.


Pssm-ID: 212543 [Multi-domain]  Cd Length: 294  Bit Score: 118.91  E-value: 3.23e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  807 HHAEESTAMGFCFFNSVAITAKYLRdQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGnFFPGSGAPNEVG 886
Cdd:cd11680    115 HHAQKSRASGFCYVNDIVLAILRLR-RARFRRVFYLDLDLHHGDGVESAFFFSKNVLTCSIHRYDPG-FFPGTGSLKNSS 192

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  887 TglgeGYNINIAWTGGLDppmgDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLM 966
Cdd:cd11680    193 D----KGMLNIPLKRGLS----DKTLLRIIDSIVRPLIEKFEPEVIVIQCGCDGLSGD--PHKEWNLTIRGYGSVIELLL 262

                          170       180
                   ....*....|....*....|....
gi 1622924881  967 TLADGRVVLALEGG---HDLTAIC 987
Cdd:cd11680    263 KEFKDKPTLLLGGGgynHTEAARA 286
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
 779-997 2.28e-27

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: 114.86  E-value: 2.28e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  779 AVGCVIELASKVASGEL---KNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQ-- 853
Cdd:cd09998     89 ALGAVCEAVDSVFKPESpgtKRAFVAIRPPGHHCSESTPSGFCWVNNVHVGAAHAYLTHGITRVVILDIDLHHGNGTQdi 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  854 ----------------------QAFYADPSILYISLHrydEGNFFP-GSGAPNEV---GTGLGEGYNINIaWTGGLDPPM 907
Cdd:cd09998    169 awrinaeankqalesssyddfkPAGAPGLRIFYSSLH---DINSFPcEDGDPAKVkdaSVSIDGAHGQWI-WNVHLQPWT 244

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  908 GDVEYLEAFR---TIVKPVAKEF-------DPD--MVLVSAGFDALEGHTPPLG--GYKVTAKCFGHLTKQLMTLAD--- 970
Cdd:cd09998    245 TEEDFWELYYpkyRILFEKAAEFlrlttaaTPFktLVFISAGFDASEHEYESMQrhGVNVPTSFYYRFARDAVRFADaha 324

                          250       260
                   ....*....|....*....|....*...
gi 1622924881  971 -GRVVLALEGGHDLTAICDASEACVNAL 997
Cdd:cd09998    325 hGRLISVLEGGYSDRALCSGVLAHLTGL 352
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
 677-960 9.02e-27

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: 113.75  E-value: 9.02e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  677 TTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHS-EHHSLLYGTNPLDGQKLDPRIL---LGDDSQKF-- 750
Cdd:cd10004     19 PGHPMKPHRIRMAHSLVMNYGLYKKMEIYRAKPATKNEMTQFHTdEYIDFLSRVTPDNMEKFQKEQVkynVGDDCPVFdg 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  751 ---FSSLPCGGlgvdsdtiwnelHSSGAARMAVG-CviELASKVASGElkngfavvrppgHHAEESTAMGFCFFNSVAIT 826
Cdd:cd10004     99 lfeFCSISAGG------------SMEGAARLNRGkC--DIAVNWAGGL------------HHAKKSEASGFCYVNDIVLG 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  827 A-KYLRDQlniSKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdeGNFFPGSGAPNEVGTGLGEGYNINIAWTGGLDp 905
Cdd:cd10004    153 IlELLRYH---QRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKY--GEYFPGTGELRDIGIGTGKNYAVNVPLRDGID- 226

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622924881  906 pmgDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTppLGGYKVTAKcfGH 960
Cdd:cd10004    227 ---DESYKSIFEPVIKHVMEWYQPEAVVLQCGGDSLSGDR--LGCFNLSMK--GH 274
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
 807-963 9.65e-26

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: 109.08  E-value: 9.65e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  807 HHAEESTAMGFCFFNSVAITakyLRDQLNI-SKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDeGNFFPGSGAPNEV 885
Cdd:cd11598    131 HHAKKSEASGFCYVNDIVLA---ILNLLRYfPRVLYIDIDVHHGDGVEEAFYRTDRVMTLSFHKYN-GEFFPGTGDLDDN 206

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622924881  886 GTGLGEGYNINIAWTGGLDppmgDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTppLGGYKVTAKCFGHLTK 963
Cdd:cd11598    207 GGTPGKHFALNVPLEDGID----DEQYNLLFKSIIGPTIEKFQPSAIVLQCGADSLGGDR--LGQFNLNIKAHGACVK 278
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 770-997 1.41e-25

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: 105.92  E-value: 1.41e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  770 LHSSGAARMAVGCVIELASKVasgelKNGFAVVrppGHHAEestamgfcfFNSVAITAKYLRdqlniSKILIVDLDVHHG 849
Cdd:cd09987      5 IRKAEAHELLAGVVVAVLKDG-----KVPVVLG---GDHSI---------ANGAIRAVAELH-----PDLGVIDVDAHHD 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  850 NGTQQAFYA--------------DPSILYISLHRYDEGNFFPGsgapnevGTGLGEGYNINIAWTGGLDPPMGDVeylea 915
Cdd:cd09987     63 VRTPEAFGKgnhhtprhllceplISDVHIVSIGIRGVSNGEAG-------GAYARKLGVVYFSMTEVDKLGLGDV----- 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  916 FRTIVKPVakEFDPDMVLVSAGFDALEGH----TPPLGGYKVTAKCFGHLTKQLMTLAdGRVVLALEGGHDL----TAIC 987
Cdd:cd09987    131 FEEIVSYL--GDKGDNVYLSVDVDGLDPSfapgTGTPGPGGLSYREGLYITERIAKTN-LVVGLDIVEVNPLldetGRTA 207

                          250
                   ....*....|
gi 1622924881  988 DASEACVNAL 997
Cdd:cd09987    208 RLAAALTLEL 217
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
 679-1039 2.93e-25

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: 109.00  E-value: 2.93e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  679 HPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHH-SLLYGTNP---LDGQKLDPRILLGDDSQKF---- 750
Cdd:cd10010     25 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYiKFLRSIRPdnmSEYSKQMQRFNVGEDCPVFdglf 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  751 -FSSLPCGGlgvdsdtiwnelhssgaarmavgcviELASKVASGELKNGFAVVRPPG-HHAEESTAMGFCFFNSVAITAK 828
Cdd:cd10010    105 eFCQLSAGG--------------------------SVASAVKLNKQQTDIAVNWAGGlHHAKKSEASGFCYVNDIVLAIL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  829 YLRDQLNisKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdeGNFFPGSGAPNEVGTGLGEGYNINIAWTGGLDppmg 908
Cdd:cd10010    159 ELLKYHQ--RVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKY--GEYFPGTGDLRDIGAGKGKYYAVNYPLRDGID---- 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  909 DVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTppLGGYKVTAKCFGHLTKQLMTLADGRVVLAlEGGHDL--TAI 986
Cdd:cd10010    231 DESYEAIFKPVMSKVMEMFQPSAVVLQCGADSLSGDR--LGCFNLTIKGHAKCVEFVKSFNLPMLMLG-GGGYTIrnVAR 307

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622924881  987 CDASEACV--NALLGNEL------EPLAEDI-LHQSP-NMNAVISLQKIIEIQSKYWKSVRMV 1039
Cdd:cd10010    308 CWTYETAValDSEIPNELpyndyfEYFGPDFkLHISPsNMTNQNTNEYLEKIKQRLFENLRML 370
ClassIIa_HDAC9_Gln-rich-N cd10163
Glutamine-rich N-terminal helical domain of HDAC9, a Class IIa histone deacetylase; This ...
 60-149 3.73e-23

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: 94.44  E-value: 3.73e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881   60 DPVVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIKLQQELLAIKQQQELLEKEQKLEQQRQEQE 139
Cdd:cd10163      1 DPTVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHLKLQQELLAMKQQQELLEKEQKLEQQRQEQE 80

                           90
                   ....*....|
gi 1622924881  140 VERHRREQQL 149
Cdd:cd10163     81 LERHRREQQL 90
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
 807-960 7.80e-22

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: 99.01  E-value: 7.80e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  807 HHAEESTAMGFCFFNSVAITAKYLRDQLNisKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdeGN-FFPGSGAPNEV 885
Cdd:cd10005    132 HHAKKFEASGFCYVNDIVIAILELLKYHP--RVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKY--GNyFFPGTGDMYEV 207

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622924881  886 GTGLGEGYNINIAWTGGLDppmgDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTppLGGYKVTAKcfGH 960
Cdd:cd10005    208 GAESGRYYSVNVPLKDGID----DQSYLQLFKPVIQQVIDFYQPTCIVLQCGADSLGCDR--LGCFNLSIK--GH 274
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
 679-1039 1.17e-21

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: 98.21  E-value: 1.17e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  679 HPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHS-EHHSLLYGTNP---LDGQKLDPRILLGDDSQKF---- 750
Cdd:cd10011     21 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSdEYIKFLRSIRPdnmSEYSKQMQRFNVGEDCPVFdglf 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  751 -FSSLPCGGlGVDSDTIWNELHSSGAARMAVGCvielaskvasgelkngfavvrppgHHAEESTAMGFCFFNSVAITAKY 829
Cdd:cd10011    101 eFCQLSTGG-SVAGAVKLNRQQTDMAVNWAGGL------------------------HHAKKSEASGFCYVNDIVLAILE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  830 LRDQLNisKILIVDLDVHHGNGTQQAFYADPSILYISlhRYDEGNFFPGSGAPNEVGTGLGEGYNINIAWTGGLDppmgD 909
Cdd:cd10011    156 LLKYHQ--RVLYIDIDIHHGDGVEEAFYTTDRVMTVS--FHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGID----D 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  910 VEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTppLGGYKVTAKcfGHlTKQLMTLADGRVVLALEGGHDLT----A 985
Cdd:cd10011    228 ESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDR--LGCFNLTVK--GH-AKCVEVVKTFNLPLLMLGGGGYTirnvA 302

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622924881  986 ICDASEACV--NALLGNEL------EPLAEDI-LHQSP-NMNAVISLQKIIEIQSKYWKSVRMV 1039
Cdd:cd10011    303 RCWTYETAValDCEIPNELpyndyfEYFGPDFkLHISPsNMTNQNTPEYMEKIKQRLFENLRML 366
PTZ00063 PTZ00063
histone deacetylase; Provisional
 807-960 1.19e-21

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 99.11  E-value: 1.19e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  807 HHAEESTAMGFCFFNSVAITA----KYLrdqlniSKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdeGNFFPGSGAP 882
Cdd:PTZ00063   137 HHAKRSEASGFCYINDIVLGIlellKYH------ARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFPGTGDV 208

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622924881  883 NEVGTGLGEGYNINIAWTGGLDppmgDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTppLGGYKVTAKcfGH 960
Cdd:PTZ00063   209 TDIGVAQGKYYSVNVPLNDGID----DDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDR--LGRFNLTIK--GH 278
ClassIIa_HDAC_Gln-rich-N cd10149
Glutamine-rich N-terminal helical domain of various Class IIa histone deacetylases (HDAC4, ...
 60-149 7.40e-20

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: 85.13  E-value: 7.40e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881   60 DPVVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIKLQQELLAIKQQQELLEKEQKLEQQRQEQE 139
Cdd:cd10149      1 DPVLREQQLQQELLALKQQQQIQKQLLIAEFQKQHENLTRQHEAQLQEHIKQQQEMLAIKQQQELLEKQRKLEQQRQEQE 80

                           90
                   ....*....|
gi 1622924881  140 VERHRREQQL 149
Cdd:cd10149     81 LEKQRREQQL 90
PTZ00346 PTZ00346
histone deacetylase; Provisional
 807-980 6.66e-18

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 87.78  E-value: 6.66e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  807 HHAEESTAMGFCFFNSVAITAKYLRDQLNisKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEgNFFPGSGAPNEVG 886
Cdd:PTZ00346   154 HHSKCGECSGFCYVNDIVLGILELLKCHD--RVLYVDIDMHHGDGVDEAFCTSDRVFTLSLHKFGE-SFFPGTGHPRDVG 230

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881  887 TGLGEGYNINIA-WTGgldppMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTppLGGYKVTAKCFGHLTKQL 965
Cdd:PTZ00346   231 YGRGRYYSMNLAvWDG-----ITDFYYLGLFEHALHSIVRRYSPDAIVLQCGADSLAGDR--LGLLNLSSFGHGQCVQAV 303

                          170
                   ....*....|....*
gi 1622924881  966 MTLadGRVVLALEGG 980
Cdd:PTZ00346   304 RDL--GIPMLALGGG 316
HDAC4_Gln pfam12203
Glutamine rich N terminal domain of histone deacetylase 4; This domain is found in eukaryotes, ...
 87-149 1.43e-17

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: 78.74  E-value: 1.43e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622924881   87 IAEFQKQHENLTRQHQAQLQEHIKLQQELLAIKQQQELLEKEQKLEQQRQEQEVERHRREQQL 149
Cdd:pfam12203   29 IAEFQKQHELLTRQHEAQLQEHIKQQQELLAMKQQQELLEQQRKLEQQRQEEELEKHRREQQL 91
ClassIIa_HDAC4_Gln-rich-N cd10162
Glutamine-rich N-terminal helical domain of HDAC4, a Class IIa histone deacetylase; This ...
 87-149 4.04e-15

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: 71.77  E-value: 4.04e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622924881   87 IAEFQKQHENLTRQHQAQLQEHIKLQQELLAIKQQQELLEKEQKLEQQRQEQEVERHRREQQL 149
Cdd:cd10162     28 IAEFQRQHEQLSRQHEAQLHEHIKQQQELLAMKHQQELLEHQRKLERHRQEQEMEKQQREQKL 90
ClassIIa_HDAC5_Gln-rich-N cd10164
Glutamine-rich N-terminal helical domain of HDAC5, a Class IIa histone deacetylase; This ...
 60-172 9.64e-13

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: 65.23  E-value: 9.64e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622924881   60 DPVVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIKLQQELLAIKQQQELLEKeqkleqqrqeqe 139
Cdd:cd10164      1 DPSLREQQLQQELLLLKQQQQLQKQLLFAEFQKQHEHLTRQHEVQLQKHLKVRAELFSEQQQQEILAA------------ 68

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1622924881  140 verhRREQQLPPLRGKDRGRERAVASTEVKQKL 172
Cdd:cd10164     69 ----KRQQELEQQRKREQQRQEELEKQRLEQQL 97
 
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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