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Conserved domains on  [gi|30795202|ref|NP_848510|]
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histone deacetylase 9 isoform 4 [Homo sapiens]

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 ...
631-1008 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 30795202  631 SATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQ 710
Cdd:cd11681    1 FTTGLAYDPLMLKHQCICGNNSSHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTLLYGTNPLSRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  711 KLDPRILLGDdSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAM 790
Cdd:cd11681   81 KLDPTKLAGL-PQKSFVRLPCGGIGVDSDTVWNELHTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQAM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  791 GFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYNI 870
Cdd:cd11681  160 GFCFFNSVAIAAKQLQQKLKLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFPGTGAPTEVGSGAGEGFNV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  871 NIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVL 950
Cdd:cd11681  240 NIAWSGGLDPPMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPPPLGGYKVSPACFGYMTRQLMNLAGGKVVL 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 30795202  951 ALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSKYW 1008
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 ...
38-124 5.48e-20

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: 85.58  E-value: 5.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202   38 DPVVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIK---ELLAIKQQQELLEKEQKLEQQRQEQE 114
Cdd:cd10163    1 DPTVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHLKlqqELLAMKQQQELLEKEQKLEQQRQEQE 80
                         90
                 ....*....|
gi 30795202  115 VERHRREQQL 124
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 ...
631-1008 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 30795202  631 SATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQ 710
Cdd:cd11681    1 FTTGLAYDPLMLKHQCICGNNSSHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTLLYGTNPLSRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  711 KLDPRILLGDdSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAM 790
Cdd:cd11681   81 KLDPTKLAGL-PQKSFVRLPCGGIGVDSDTVWNELHTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQAM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  791 GFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYNI 870
Cdd:cd11681  160 GFCFFNSVAIAAKQLQQKLKLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFPGTGAPTEVGSGAGEGFNV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  871 NIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVL 950
Cdd:cd11681  240 NIAWSGGLDPPMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPPPLGGYKVSPACFGYMTRQLMNLAGGKVVL 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 30795202  951 ALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSKYW 1008
Cdd:cd11681  320 ALEGGYDLTAICDASEACVRALLGDELDPLSEEELERRPNPNAVTSLEKVIAIQSPYW 377
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
654-972 1.05e-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: 1.05e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202    654 HPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHH-SLLYGTNPLDGQKLDPRILLGDDSQKFFSslpcg 732
Cdd:pfam00850    1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYlEFLEEAAPEGGALLLLSYLSGDDDTPVSP----- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202    733 glgvdsdtiwnelHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQLNIS 812
Cdd:pfam00850   76 -------------GSYEAALLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLK 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202    813 KILIVDLDVHHGNGTQQAFYADPSILYISLHRYDeGNFFPGSGAPNEVGTGLGEGYNINIAWTGGldppMGDVEYLEAFR 892
Cdd:pfam00850  143 RVAIVDFDVHHGNGTQEIFYDDPSVLTLSIHQYP-GGFYPGTGFADETGEGKGKGYTLNVPLPPG----TGDAEYLAAFE 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202    893 TIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLAD---GRVVLALEGGHDLTAICDASEACV 969
Cdd:pfam00850  218 EILLPALEEFQPDLILVSAGFDAHAGD--PLGGLNLTTEGFAEITRILLELADplcIRVVSVLEGGYNLDALARSATAVL 295

                   ...
gi 30795202    970 NAL 972
Cdd:pfam00850  296 AAL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
633-974 5.10e-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: 5.10e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  633 TGIAYDPLMLKHQCvcgnSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHsllygtnpldgqkL 712
Cdd:COG0123    1 TALIYHPDYLLHDL----GPGHPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDY-------------V 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  713 DprillgddsqKFFSSLPCGGLG-VDSDTIWNElHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMG 791
Cdd:COG0123   64 D----------ALRAASLDGGYGqLDPDTPVSP-GTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMG 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  792 FCFFNSVAITAKYLRDQlNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdegNFFPGSGAPNEVGTGLGEGYNIN 871
Cdd:COG0123  133 FCLFNNAAIAARYLLAK-GLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD---PLYPGTGAADETGEGAGEGSNLN 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  872 IAwtggLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLAD---GRV 948
Cdd:COG0123  209 VP----LPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHADD--PLGRLNLTTEGYAWRTRRVLELADhcgGPV 282
                        330       340
                 ....*....|....*....|....*.
gi 30795202  949 VLALEGGHDLTAICDASEACVNALLG 974
Cdd:COG0123  283 VSVLEGGYNLDALARSVAAHLETLLG 308
PTZ00063 PTZ00063
histone deacetylase; Provisional
782-935 1.15e-21

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 99.11  E-value: 1.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202   782 HHAEESTAMGFCFFNSVAITA----KYLrdqlniSKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdeGNFFPGSGAP 857
Cdd:PTZ00063  137 HHAKRSEASGFCYINDIVLGIlellKYH------ARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFPGTGDV 208
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30795202   858 NEVGTGLGEGYNINIAWTGGLDppmgDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTppLGGYKVTAKcfGH 935
Cdd:PTZ00063  209 TDIGVAQGKYYSVNVPLNDGID----DDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDR--LGRFNLTIK--GH 278
ClassIIa_HDAC9_Gln-rich-N cd10163
Glutamine-rich N-terminal helical domain of HDAC9, a Class IIa histone deacetylase; This ...
38-124 5.48e-20

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: 85.58  E-value: 5.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202   38 DPVVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIK---ELLAIKQQQELLEKEQKLEQQRQEQE 114
Cdd:cd10163    1 DPTVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHLKlqqELLAMKQQQELLEKEQKLEQQRQEQE 80
                         90
                 ....*....|
gi 30795202  115 VERHRREQQL 124
Cdd:cd10163   81 LERHRREQQL 90
HDAC4_Gln pfam12203
Glutamine rich N terminal domain of histone deacetylase 4; This domain is found in eukaryotes, ...
65-124 1.32e-14

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: 70.27  E-value: 1.32e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30795202     65 IAEFQKQHENLTRQHQAQLQEHIK---ELLAIKQQQELLEKEQKLEQQRQEQEVERHRREQQL 124
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 ...
631-1008 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 30795202  631 SATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQ 710
Cdd:cd11681    1 FTTGLAYDPLMLKHQCICGNNSSHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTLLYGTNPLSRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  711 KLDPRILLGDdSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAM 790
Cdd:cd11681   81 KLDPTKLAGL-PQKSFVRLPCGGIGVDSDTVWNELHTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQAM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  791 GFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYNI 870
Cdd:cd11681  160 GFCFFNSVAIAAKQLQQKLKLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFPGTGAPTEVGSGAGEGFNV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  871 NIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVL 950
Cdd:cd11681  240 NIAWSGGLDPPMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPPPLGGYKVSPACFGYMTRQLMNLAGGKVVL 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 30795202  951 ALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSKYW 1008
Cdd:cd11681  320 ALEGGYDLTAICDASEACVRALLGDELDPLSEEELERRPNPNAVTSLEKVIAIQSPYW 377
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
631-1009 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 30795202  631 SATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQ 710
Cdd:cd10009    1 SATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  711 KLDPRILLGDDSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAM 790
Cdd:cd10009   81 KLDPRILLGDDSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  791 GFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYNI 870
Cdd:cd10009  161 GFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYNI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  871 NIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVL 950
Cdd:cd10009  241 NIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVL 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 30795202  951 ALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSKYWK 1009
Cdd:cd10009  321 ALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSKYWK 379
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
631-1046 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: 754.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  631 SATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQ 710
Cdd:cd10007    3 FTTGLVYDTFMLKHQCTCGNTNVHPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHSEHHTLLYGTSPLNRQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  711 KLDPRILLGDDSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAM 790
Cdd:cd10007   83 KLDSKKLLGPLSQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLIELAFKVAAGELKNGFAVIRPPGHHAEESTAM 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  791 GFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYNI 870
Cdd:cd10007  163 GFCFFNSVAIAAKLLQQKLNVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGNFFPGSGAPDEVGAGPGVGFNV 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  871 NIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVL 950
Cdd:cd10007  243 NIAWTGGVDPPIGDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGHQSPLGGYSVTAKCFGHLTKQLMTLAGGRVVL 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  951 ALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSKYWKSVRMVAVPRGCALAGAQLQE- 1029
Cdd:cd10007  323 ALEGGHDLTAICDASEACVSALLGMELTPLDNTVLQQKPNDNAVATLERVIEIQSKHWSCLKRFAATLGFSLLEAQRGEl 402
                        410
                 ....*....|....*...
gi 30795202 1030 -ETETVSALASLTVDVEQ 1046
Cdd:cd10007  403 eEAETVSAMASLSVDTEQ 420
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
628-1035 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 30795202  628 QPGSATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPL 707
Cdd:cd10006    1 KPRFTTGLVYDTLMLKHQCTCGNSNSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  708 DGQKLDPRILLGDDSQkFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEES 787
Cdd:cd10006   81 NRQKLDSKKLLGSLAS-VFVRLPCGGVGVDSDTIWNEVHSSGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEES 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  788 TAMGFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEG 867
Cdd:cd10006  160 TPMGFCYFNSVAIAAKLLQQRLNVSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  868 YNINIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGR 947
Cdd:cd10006  240 FNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSAKCFGYLTKQLMGLAGGR 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  948 VVLALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSKYWKSVRMVAVPRGCALAGAQL 1027
Cdd:cd10006  320 IVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGYSLIEAQT 399
                        410
                 ....*....|
gi 30795202 1028 --QEETETVS 1035
Cdd:cd10006  400 ceNEEAETVT 409
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
633-1008 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 30795202  633 TGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQKL 712
Cdd:cd10008    3 TGLVYDSVMLKHQCSCGDNSNHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLKL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  713 DPRILLGDDSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGF 792
Cdd:cd10008   83 DNGKLAGLLAQRMFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  793 CFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYNINI 872
Cdd:cd10008  163 CFFNSVAIACRQLQQQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGAGSGEGFNVNV 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  873 AWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVLAL 952
Cdd:cd10008  243 AWAGGLDPPMGDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVLAL 322
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 30795202  953 EGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSKYW 1008
Cdd:cd10008  323 EGGHDLTAICDASEACVAALLGNEVDPLSEESWKQKPNLNAIRSLEAVIRVHSKYW 378
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
654-973 1.65e-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: 1.65e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  654 HPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHH-SLLYGTNPLDGQKLDPrillgddsqkffsslpcg 732
Cdd:cd09992    1 HPERPERLLAILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYiERVEETCEAGGGYLDP------------------ 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  733 glgvdsDTIWNElHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQLNIS 812
Cdd:cd09992   63 ------DTYVSP-GSYEAALLAAGAALAAVDAVLSGEAENAFALVRPPGHHAEPDRAMGFCLFNNVAIAARYAQKRYGLK 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  813 KILIVDLDVHHGNGTQQAFYADPSILYISLHRYDegnFFPGSGAPNEVGTGLGEGYNINIAWTGGldppMGDVEYLEAFR 892
Cdd:cd09992  136 RVLIVDWDVHHGNGTQDIFYDDPSVLYFSIHQYP---FYPGTGAAEETGGGAGEGFTINVPLPPG----SGDAEYLAAFE 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  893 TIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLAD----GRVVLALEGGHDLTAICDASEAC 968
Cdd:cd09992  209 EVLLPIAREFQPDLVLVSAGFDAHRGD--PLGGMNLTPEGYARLTRLLKELADehcgGRLVFVLEGGYNLEALAESVLAV 286

                 ....*
gi 30795202  969 VNALL 973
Cdd:cd09992  287 LEALL 291
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
637-1012 4.98e-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: 419.44  E-value: 4.98e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  637 YDPLMLKHQCVCgnSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHH-SLLYGTnpldgQKLDPR 715
Cdd:cd10003    1 YDQRMMNHHNLW--DPGHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHlDEMKSL-----EKMKPR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  716 ILlgddsqkffsslpcGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFF 795
Cdd:cd10003   74 EL--------------NRLGKEYDSIYIHPDSYQCALLAAGCVLQVVEAVLTGESRNGVAIVRPPGHHAEQDTACGFCFF 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  796 NSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGS--GAPNEVGTGLGEGYNINIA 873
Cdd:cd10003  140 NNVAIAARYAQKKYGLKRILIVDWDVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSpeGNYDVVGKGKGEGFNVNIP 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  874 WTGGldpPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLADGRVVLALE 953
Cdd:cd10003  220 WNKG---GMGDAEYIAAFQQVVLPIAYEFNPELVLVSAGFDAARGD--PLGGCKVTPEGYAHMTHMLMSLAGGRVIVILE 294
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 30795202  954 GGHDLTAICDASEACVNALLGNELEPLaedILHQSPNMNAVISLQKIIEIQSKYWKSVR 1012
Cdd:cd10003  295 GGYNLTSISESMSMCTKTLLGDPPPVL---DLPRPPCSSALKSINNVLQVHQKYWKSLR 350
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
654-972 1.05e-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: 1.05e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202    654 HPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHH-SLLYGTNPLDGQKLDPRILLGDDSQKFFSslpcg 732
Cdd:pfam00850    1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYlEFLEEAAPEGGALLLLSYLSGDDDTPVSP----- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202    733 glgvdsdtiwnelHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQLNIS 812
Cdd:pfam00850   76 -------------GSYEAALLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLK 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202    813 KILIVDLDVHHGNGTQQAFYADPSILYISLHRYDeGNFFPGSGAPNEVGTGLGEGYNINIAWTGGldppMGDVEYLEAFR 892
Cdd:pfam00850  143 RVAIVDFDVHHGNGTQEIFYDDPSVLTLSIHQYP-GGFYPGTGFADETGEGKGKGYTLNVPLPPG----TGDAEYLAAFE 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202    893 TIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLAD---GRVVLALEGGHDLTAICDASEACV 969
Cdd:pfam00850  218 EILLPALEEFQPDLILVSAGFDAHAGD--PLGGLNLTTEGFAEITRILLELADplcIRVVSVLEGGYNLDALARSATAVL 295

                   ...
gi 30795202    970 NAL 972
Cdd:pfam00850  296 AAL 298
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
654-980 1.73e-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: 1.73e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  654 HPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHsllygtnpLDG----QKLDPRILlgDDSQKFFSSL 729
Cdd:cd11600    3 HPEDPSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEH--------WDRveatEKMSDEQL--KDRTEIFERD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  730 pcgGLGVDSdtiwnelHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQL 809
Cdd:cd11600   73 ---SLYVNN-------DTAFCARLSCGGAIEACRAVAEGRVKNAFAVVRPPGHHAEPDESMGFCFFNNVAVAAKWLQTEY 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  810 --NISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGS--GAPNEVGTGLGEGYNINIAWTgglDPPMGDV 885
Cdd:cd11600  143 pdKIKKILILDWDIHHGNGTQRAFYDDPNVLYISLHRFENGGFYPGTpyGDYESVGEGAGLGFNVNIPWP---QGGMGDA 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  886 EYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLADGRVVLALEGGHDLTAICDAS 965
Cdd:cd11600  220 DYIYAFQRIVMPIAYEFDPDLVIISAGFDAADGD--ELGQCHVTPAGYAHMTHMLMSLAGGKLVVALEGGYNLDAISDSA 297
                        330
                 ....*....|....*
gi 30795202  966 EACVNALLGNELEPL 980
Cdd:cd11600  298 LAVAKVLLGEAPPKL 312
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
633-974 5.10e-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: 5.10e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  633 TGIAYDPLMLKHQCvcgnSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHsllygtnpldgqkL 712
Cdd:COG0123    1 TALIYHPDYLLHDL----GPGHPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDY-------------V 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  713 DprillgddsqKFFSSLPCGGLG-VDSDTIWNElHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMG 791
Cdd:COG0123   64 D----------ALRAASLDGGYGqLDPDTPVSP-GTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMG 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  792 FCFFNSVAITAKYLRDQlNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdegNFFPGSGAPNEVGTGLGEGYNIN 871
Cdd:COG0123  133 FCLFNNAAIAARYLLAK-GLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD---PLYPGTGAADETGEGAGEGSNLN 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  872 IAwtggLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLAD---GRV 948
Cdd:COG0123  209 VP----LPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHADD--PLGRLNLTTEGYAWRTRRVLELADhcgGPV 282
                        330       340
                 ....*....|....*....|....*.
gi 30795202  949 VLALEGGHDLTAICDASEACVNALLG 974
Cdd:COG0123  283 VSVLEGGYNLDALARSVAAHLETLLG 308
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
653-1008 3.08e-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: 3.08e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  653 THPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHS-EHHSLLYGTNpldgqkldpriLLGDDSQKFFSSlpc 731
Cdd:cd10002    6 NHIECPERLEAILERLTQDGLLERCVKIPAREAEEDEILLVHSqEYIDLVKSTE-----------TMEKEELESLCS--- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  732 gglgvDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQLNI 811
Cdd:cd10002   72 -----GYDSVYLCPSTYEAARLAAGSTIELVKAVMAGKIQNGFALIRPPGHHAMRNEANGYCIFNNVAIAAKYAIEKLGL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  812 SKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPN--EVGTGLGEGYNINIAW--TGgldppMGDVEY 887
Cdd:cd10002  147 KRILIVDWDVHHGQGTQQGFYEDPRVLYFSIHRYEHGRFWPHLFESDydYIGVGHGYGFNVNVPLnqTG-----LGDADY 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  888 LEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLADGRVVLALEGGHDLTAICDASEA 967
Cdd:cd10002  222 LAIFHHILLPLALEFQPELVLVSAGFDASIGD--PEGEMAVTPAGYAHLTRLLMGLAGGKLLLVLEGGYLLESLAESVSM 299
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 30795202  968 CVNALLGNELEPLAEDIlhqsPNMNAVISLQKIIEIQSKYW 1008
Cdd:cd10002  300 TLRGLLGDPLPPLAPPI----PIRSVLETILNAIAHLSPRW 336
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
660-972 2.12e-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: 2.12e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  660 RIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQKLDprillgddsqkffsslpcGGLGVDSD 739
Cdd:cd09301    1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKANFAVATITE------------------SKPVIFGP 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  740 TIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRdQLNISKILIVDL 819
Cdd:cd09301   63 NFPVQRHYFRGARLSTGGVVEAAELVAKGELERAFAVVGAGGHHAGKSRAWGFCYFNDVVLAIKFLR-ERGISRILIIDT 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  820 DVHHGNGTQQAFYADPSILYISLHRYDEGNFfpgsgapnevGTGLGEGYNINIAWTGGldppMGDVEYLEAFRTIVKPVA 899
Cdd:cd09301  142 DAHHGDGTREAFYDDDRVLHMSFHNYDIYPF----------GRGKGKGYKINVPLEDG----LGDEEYLDAVERVISKVL 207
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30795202  900 KEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLAD-GRVVLALEGGHDLTAICDASEACVNAL 972
Cdd:cd09301  208 EEFEPEVVVLQFGHDTHEGD--RLGGFNLSEKGFVKLAEIVKEFARgGPILMVLGGGYNPEAAARIWTAIIKEL 279
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
654-973 8.85e-85

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: 8.85e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  654 HPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHH-SLLYGTNPLDGQKLdprillgddsqkffsslpcg 732
Cdd:cd11599    1 HPESPERLEAILDALIASGLDRLLRQLEAPPATREQLLRVHDAAYvDRLEAAAPEEGLVQ-------------------- 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  733 glgVDSDTIWNElHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQLNIS 812
Cdd:cd11599   61 ---LDPDTAMSP-GSLEAALRAAGAVVAAVDAVMAGEARNAFCAVRPPGHHAERDKAMGFCLFNNVAIAAAHALAHHGLE 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  813 KILIVDLDVHHGNGTQQAFYADPSILYISLHRYdegNFFPGSGAPNEVGTGlgegyNI-NIAwtggLDPPMGDVEYLEAF 891
Cdd:cd11599  137 RVAIVDFDVHHGNGTEDIFRDDPRVLFCSSHQH---PLYPGTGAPDETGHG-----NIvNVP----LPAGTGGAEFREAV 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  892 RTIVKPVAKEFDPDMVLVSAGFDAlegHT-PPLGGYKVTAKCFGHLTKQLMTLAD----GRVVLALEGGHDLTAICDASE 966
Cdd:cd11599  205 EDRWLPALDAFKPDLILISAGFDA---HRdDPLAQLNLTEEDYAWITEQLMDVADrycdGRIVSVLEGGYDLSALARSVA 281

                 ....*..
gi 30795202  967 ACVNALL 973
Cdd:cd11599  282 AHVRALM 288
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
633-989 1.03e-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: 275.59  E-value: 1.03e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  633 TGIAYDPLMLKH--------QCVCG---NSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHsll 701
Cdd:cd09996    1 TGFVWDERYLWHdtgtgalfLPVGGllvQPGRHPENPETKRRIKNLLEVSGLSDHLVLITPRPATDEELLRVHTPEY--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  702 ygtnpldgqkLDpRIllgddsqKFFSSLPCGGLGvdSDTIWNElHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPG 781
Cdd:cd09996   78 ----------ID-RV-------KAASAAGGGEAG--GGTPFGP-GSYEIALLAAGGAIAAVDAVLDGEVDNAYALVRPPG 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  782 HHAEESTAMGFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRydEGNFFPGSGAPNEVG 861
Cdd:cd09996  137 HHAEPDQGMGFCLFNNVAIAARHALAVGGVKRVAVVDWDVHHGNGTQAIFYDDPDVLTISLHQ--DRCFPPDSGAVEERG 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  862 TGLGEGYNINIAwtggLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDAleGHTPPLGGYKVTAKCFGHLTKQLM 941
Cdd:cd09996  215 EGAGEGYNLNIP----LPPGSGDGAYLHAFERIVLPALRAFRPELIIVASGFDA--SAFDPLGRMMLTSDGFRALTRKLR 288
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 30795202  942 TLAD----GRVVLALEGGHDLT--AICDAseACVNALLGNEL---EPLAEDILHQSP 989
Cdd:cd09996  289 DLADelcgGRLVMVHEGGYSEAyvPFCGL--AVLEELSGVRTgiaDPLLYYPEAQGG 343
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
653-1008 2.24e-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: 274.04  E-value: 2.24e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  653 THPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHS-EHHSLLYGTNPLDGQKLdpRILlgddSQKFfsslpc 731
Cdd:cd11682    6 SFPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSpEYVALMKSTQYMTEEEL--RTL----ADTY------ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  732 gglgvdsDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQLNI 811
Cdd:cd11682   74 -------DSVYLHPNSYSCACLAVGSVLQLVDKVLGGEIRNGLAIVRPPGHHAQHDKMDGYCMFNNVAIAARYAQQKHGV 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  812 SKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFP--GSGAPNEVGTGLGEGYNINIAWTgglDPPMGDVEYLE 889
Cdd:cd11682  147 QRVLIVDWDVHHGQGTQFIFEQDPSVLYFSIHRYEQGRFWPhlKESDSSAVGFGRGEGYNINVPWN---QVGMRDADYIA 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  890 AFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLADGRVVLALEGGHDLTAICDASEACV 969
Cdd:cd11682  224 AFLHVLLPVALEFQPQLVLVAAGFDAVIGD--PKGEMAATPACFAHLTHLLMGLAGGKLILSLEGGYNLRSLAEGVCASL 301
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 30795202  970 NALLGnelEPLAEDILHQSPNMNAVISLQKIIEIQSKYW 1008
Cdd:cd11682  302 KALLG---DPCPMLESPGAPCRSALASVSCTISALEPFW 337
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
660-1008 1.46e-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: 1.46e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  660 RIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQKLDPRIllgddSQKFfsslpcgglgvdsD 739
Cdd:cd11683   13 RLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRETQVMNKEELMAI-----SGKY-------------D 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  740 TIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQLNISKILIVDL 819
Cdd:cd11683   75 AVYFHPNTFHCARLAAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYAKKKYGLHRILIVDW 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  820 DVHHGNGTQQAFYADPSILYISLHRYDEGNFFPG--SGAPNEVGTGLGEGYNINIAWTgglDPPMGDVEYLEAFRTIVKP 897
Cdd:cd11683  155 DVHHGQGIQYIFEEDPSVLYFSWHRYEHQRFWPFlrESDYDAVGRGKGLGFNINLPWN---KVGMGNADYLAAFFHVLLP 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  898 VAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLADGRVVLALEGGHDLTAICDASEACVNALLGNEL 977
Cdd:cd11683  232 LAFEFDPELVLVSAGFDSAIGD--PEGQMCATPECFAHLTHLLMVLAGGKLCAVLEGGYHLESLAESVCMTVQTLLGDPL 309
                        330       340       350
                 ....*....|....*....|....*....|.
gi 30795202  978 EPLAEDIlhqSPNMNAVISLQKIIEIQSKYW 1008
Cdd:cd11683  310 PRLSGEM---TPCQSALESIQNVRAAQAPYW 337
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
635-974 1.47e-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: 1.47e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  635 IAYDPLMLKHQ----CVCGNSTTHPEHAGRIQSIWSRLQETGLLnkcERIQGRKASLEEIQLVHSEHHsllygtnpldgq 710
Cdd:cd10001    2 IVYSEDHLLHHpkteLSRGKLVPHPENPERAEAILDALKRAGLG---EVLPPRDFGLEPILAVHDPDY------------ 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  711 kLDprillgddsqkFFSSLpcgglgvDSDTIWNElHSSGAARMAVGCVIELASKVASGElKNGFAVVRPPGHHAEESTAM 790
Cdd:cd10001   67 -VD-----------FLETA-------DTDTPISE-GTWEAALAAADTALTAADLVLEGE-RAAYALCRPPGHHAGRDRAG 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  791 GFCFFNSVAITAKYLRDQLniSKILIVDLDVHHGNGTQQAFYADPSILYISLHRyDEGNFFPG-SGAPNEVGTGLGEGYN 869
Cdd:cd10001  126 GFCYFNNAAIAAQYLRDRA--GRVAILDVDVHHGNGTQEIFYERPDVLYVSIHG-DPRTFYPFfLGFADETGEGEGEGYN 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  870 INIAwtggLDPPMGDVEYLEAFRTIVKPVAkEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLaDGRVV 949
Cdd:cd10001  203 LNLP----LPPGTGDDDYLAALDEALAAIA-AFGPDALVVSLGFDTHEGD--PLSDFKLTTEDYARIGRRIAAL-GLPTV 274
                        330       340
                 ....*....|....*....|....*
gi 30795202  950 LALEGGHDLTAIcdaSEACVNALLG 974
Cdd:cd10001  275 FVQEGGYNVDAL---GRNAVAFLAG 296
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
654-958 2.58e-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: 2.58e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  654 HPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHhsllYgtnpLDGQKLDPRILLGDDSQKFfsslpcgG 733
Cdd:cd09994   17 HPFNPPRLSLTKDLLRALGLLPPVDLVPPRPATEEELLLFHTPD----Y----IEAVKEASRGQEPEGRGRL-------G 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  734 LGVDSDTIWNELHSsgAARMAVGCVIELASKVASGElknGFAVVRPPG--HHAEESTAMGFCFFNSVAITAKYLRDQlNI 811
Cdd:cd09994   82 LGTEDNPVFPGMHE--AAALVVGGTLLAARLVLEGE---ARRAFNPAGglHHAMRGRASGFCVYNDAAVAIERLRDK-GG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  812 SKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGnFFPGSGAPNEVGTGLGEGYNINIAwtggLDPPMGDVEYLEAF 891
Cdd:cd09994  156 LRVAYVDIDAHHGDGVQAAFYDDPRVLTISLHESGRY-LFPGTGFVDEIGEGEGYGYAVNIP----LPPGTGDDEFLRAF 230
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30795202  892 RTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLAD----GRVVLALEGGHDL 958
Cdd:cd09994  231 EAVVPPLLRAFRPDVIVSQHGADAHAGD--PLTHLNLSNRAYRAAVRRIRELADeycgGRWLALGGGGYNP 299
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
647-1012 2.59e-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: 2.59e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  647 VCGNSTTHPEHAGRIQSIwsrLQETGLLNKCERIQGRKASLEEIQLVHSEH--HSLLYGTNPLDGQKLDprillgDDSQK 724
Cdd:cd10000   12 LCDRLPKVPNRASMVHSL---IEAYGLLKQLRVVKPRVATEEELASFHSDEyiQFLKKASNEGDNDEEP------SEQQE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  725 FfsslpcgGLGVDSDTIWNELHssgAARMAVGCVIELASKVASGELKngFAVVRPPG-HHAEESTAMGFCFFNSVAITAK 803
Cdd:cd10000   83 F-------GLGYDCPIFEGIYD---YAAAVAGATLTAAQLLIDGKCK--VAINWFGGwHHAQRDEASGFCYVNDIVLGIL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  804 YLRDQLniSKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGnFFPGSGAPNEVGTGLGEGYNINIAWTGGLDppmg 883
Cdd:cd10000  151 KLREKF--DRVLYVDLDLHHGDGVEDAFSFTSKVMTVSLHKYSPG-FFPGTGDVSDVGLGKGKYYTVNVPLRDGIQ---- 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  884 DVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVT----AKCFGHLTK-QLMTLADGrvvlalEGGHDL 958
Cdd:cd10000  224 DEQYLQIFTAVVPEIVAAFRPEAVVLQCGADTLAGD--PMGAFNLTpvgiGKCLKYVLGwKLPTLILG------GGGYNL 295
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30795202  959 --TAICDASeacVNALLGNelEPLAEDI--------------LHQSP----NMNAVISLQKIIEIQSKYWKSVR 1012
Cdd:cd10000  296 anTARCWTY---LTGLILG--EPLSSDIpdhefftsygpdyeLEISPslrpDLNEDQYIEKILETIKGNLKNVV 364
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
664-930 2.58e-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: 2.58e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  664 IWSRLQETGLLNKCERIQGRKASLEEIQLVHSEH--HSLLYGTNPLdgqKLDPRILLgddsqkffsslPcgglgvdsdtI 741
Cdd:cd09993   11 LREALLEEGLVLPEDIVEPEPATREDLLRVHDPEylESLKSGELSR---EEIRRIGF-----------P----------W 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  742 WNELHSSgaARMAVGCVIeLASKVAsgeLKNGFAVvRPPG--HHAEESTAMGFCFFNSVAITAKYLRDQLNISKILIVDL 819
Cdd:cd09993   67 SPELVER--TRLAVGGTI-LAARLA---LEHGLAI-NLAGgtHHAFPDRGEGFCVFNDIAIAARVLLAEGLVRRVLIVDL 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  820 DVHHGNGTQQAFYADPSILYISLHryDEGNfFPGSGAPNevgtglgegyNINIawtgGLDPPMGDVEYLEAFRTIVKPVA 899
Cdd:cd09993  140 DVHQGNGTAAIFADDPSVFTFSMH--GEKN-YPFRKEPS----------DLDV----PLPDGTGDDEYLAALEEALPRLL 202
                        250       260       270
                 ....*....|....*....|....*....|.
gi 30795202  900 KEFDPDMVLVSAGFDALEGHtpPLGGYKVTA 930
Cdd:cd09993  203 AEFRPDLVFYNAGVDVLAGD--RLGRLSLSL 231
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
654-938 1.59e-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: 1.59e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  654 HPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHH-SLLYGTNPLDGQKLdprillGDDSQKFfsslpcg 732
Cdd:cd09991   15 HPMKPHRIRMTHSLILSYGLYKKMEIYRPRPATAEELTKFHSDDYiDFLRSVSPDNMKEF------KKQLERF------- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  733 GLGVD---SDTIWNelhssgAARMAVGCVIELASKVASGELKngfAVVRPPG--HHAEESTAMGFCFFNSVAITAKYLRD 807
Cdd:cd09991   82 NVGEDcpvFDGLYE------YCQLYAGGSIAAAVKLNRGQAD---IAINWAGglHHAKKSEASGFCYVNDIVLAILELLK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  808 QLniSKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGnfFPGSGAPNEVGTGLGEGYNINIAwtggLDPPMGDVEY 887
Cdd:cd09991  153 YH--QRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKFGEY--FFPGTGLRDIGAGKGKYYAVNVP----LKDGIDDESY 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 30795202  888 LEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVT----AKCFGHLTK 938
Cdd:cd09991  225 LQIFEPVLSKVMEVFQPSAVVLQCGADSLAGD--RLGCFNLSikghAKCVKFVKS 277
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
782-962 3.14e-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: 3.14e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  782 HHAEESTAMGFCFFNSVAITAKYLRdQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGnFFPGSGAPNEVG 861
Cdd:cd11680  115 HHAQKSRASGFCYVNDIVLAILRLR-RARFRRVFYLDLDLHHGDGVESAFFFSKNVLTCSIHRYDPG-FFPGTGSLKNSS 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  862 TglgeGYNINIAWTGGLDppmgDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLM 941
Cdd:cd11680  193 D----KGMLNIPLKRGLS----DKTLLRIIDSIVRPLIEKFEPEVIVIQCGCDGLSGD--PHKEWNLTIRGYGSVIELLL 262
                        170       180
                 ....*....|....*....|....
gi 30795202  942 TLADGRVVLALEGG---HDLTAIC 962
Cdd:cd11680  263 KEFKDKPTLLLGGGgynHTEAARA 286
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
754-972 2.69e-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: 114.47  E-value: 2.69e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  754 AVGCVIELASKVASGEL---KNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQ-- 828
Cdd:cd09998   89 ALGAVCEAVDSVFKPESpgtKRAFVAIRPPGHHCSESTPSGFCWVNNVHVGAAHAYLTHGITRVVILDIDLHHGNGTQdi 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  829 ----------------------QAFYADPSILYISLHrydEGNFFP-GSGAPNEV---GTGLGEGYNINIaWTGGLDPPM 882
Cdd:cd09998  169 awrinaeankqalesssyddfkPAGAPGLRIFYSSLH---DINSFPcEDGDPAKVkdaSVSIDGAHGQWI-WNVHLQPWT 244
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  883 GDVEYLEAFR---TIVKPVAKEF-------DPD--MVLVSAGFDALEGHTPPLG--GYKVTAKCFGHLTKQLMTLAD--- 945
Cdd:cd09998  245 TEEDFWELYYpkyRILFEKAAEFlrlttaaTPFktLVFISAGFDASEHEYESMQrhGVNVPTSFYYRFARDAVRFADaha 324
                        250       260
                 ....*....|....*....|....*...
gi 30795202  946 -GRVVLALEGGHDLTAICDASEACVNAL 972
Cdd:cd09998  325 hGRLISVLEGGYSDRALCSGVLAHLTGL 352
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
652-935 1.13e-26

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: 113.36  E-value: 1.13e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  652 TTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHS-EHHSLLYGTNPLDGQKLDPRIL---LGDDSQKF-- 725
Cdd:cd10004   19 PGHPMKPHRIRMAHSLVMNYGLYKKMEIYRAKPATKNEMTQFHTdEYIDFLSRVTPDNMEKFQKEQVkynVGDDCPVFdg 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  726 ---FSSLPCGGlgvdsdtiwnelHSSGAARMAVG-CviELASKVASGElkngfavvrppgHHAEESTAMGFCFFNSVAIT 801
Cdd:cd10004   99 lfeFCSISAGG------------SMEGAARLNRGkC--DIAVNWAGGL------------HHAKKSEASGFCYVNDIVLG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  802 A-KYLRDQlniSKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdeGNFFPGSGAPNEVGTGLGEGYNINIAWTGGLDp 880
Cdd:cd10004  153 IlELLRYH---QRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKY--GEYFPGTGELRDIGIGTGKNYAVNVPLRDGID- 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 30795202  881 pmgDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTppLGGYKVTAKcfGH 935
Cdd:cd10004  227 ---DESYKSIFEPVIKHVMEWYQPEAVVLQCGGDSLSGDR--LGCFNLSMK--GH 274
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
782-938 9.37e-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: 9.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  782 HHAEESTAMGFCFFNSVAITakyLRDQLNI-SKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDeGNFFPGSGAPNEV 860
Cdd:cd11598  131 HHAKKSEASGFCYVNDIVLA---ILNLLRYfPRVLYIDIDVHHGDGVEEAFYRTDRVMTLSFHKYN-GEFFPGTGDLDDN 206
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30795202  861 GTGLGEGYNINIAWTGGLDppmgDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTppLGGYKVTAKCFGHLTK 938
Cdd:cd11598  207 GGTPGKHFALNVPLEDGID----DEQYNLLFKSIIGPTIEKFQPSAIVLQCGADSLGGDR--LGQFNLNIKAHGACVK 278
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
745-972 1.60e-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: 105.54  E-value: 1.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  745 LHSSGAARMAVGCVIELASKVasgelKNGFAVVrppGHHAEestamgfcfFNSVAITAKYLRdqlniSKILIVDLDVHHG 824
Cdd:cd09987    5 IRKAEAHELLAGVVVAVLKDG-----KVPVVLG---GDHSI---------ANGAIRAVAELH-----PDLGVIDVDAHHD 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  825 NGTQQAFYA--------------DPSILYISLHRYDEGNFFPGsgapnevGTGLGEGYNINIAWTGGLDPPMGDVeylea 890
Cdd:cd09987   63 VRTPEAFGKgnhhtprhllceplISDVHIVSIGIRGVSNGEAG-------GAYARKLGVVYFSMTEVDKLGLGDV----- 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  891 FRTIVKPVakEFDPDMVLVSAGFDALEGH----TPPLGGYKVTAKCFGHLTKQLMTLAdGRVVLALEGGHDL----TAIC 962
Cdd:cd09987  131 FEEIVSYL--GDKGDNVYLSVDVDGLDPSfapgTGTPGPGGLSYREGLYITERIAKTN-LVVGLDIVEVNPLldetGRTA 207
                        250
                 ....*....|
gi 30795202  963 DASEACVNAL 972
Cdd:cd09987  208 RLAAALTLEL 217
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
654-1014 2.84e-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: 2.84e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  654 HPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHH-SLLYGTNP---LDGQKLDPRILLGDDSQKF---- 725
Cdd:cd10010   25 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYiKFLRSIRPdnmSEYSKQMQRFNVGEDCPVFdglf 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  726 -FSSLPCGGlgvdsdtiwnelhssgaarmavgcviELASKVASGELKNGFAVVRPPG-HHAEESTAMGFCFFNSVAITAK 803
Cdd:cd10010  105 eFCQLSAGG--------------------------SVASAVKLNKQQTDIAVNWAGGlHHAKKSEASGFCYVNDIVLAIL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  804 YLRDQLNisKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdeGNFFPGSGAPNEVGTGLGEGYNINIAWTGGLDppmg 883
Cdd:cd10010  159 ELLKYHQ--RVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKY--GEYFPGTGDLRDIGAGKGKYYAVNYPLRDGID---- 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  884 DVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTppLGGYKVTAKCFGHLTKQLMTLADGRVVLAlEGGHDL--TAI 961
Cdd:cd10010  231 DESYEAIFKPVMSKVMEMFQPSAVVLQCGADSLSGDR--LGCFNLTIKGHAKCVEFVKSFNLPMLMLG-GGGYTIrnVAR 307
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30795202  962 CDASEACV--NALLGNEL------EPLAEDI-LHQSP-NMNAVISLQKIIEIQSKYWKSVRMV 1014
Cdd:cd10010  308 CWTYETAValDSEIPNELpyndyfEYFGPDFkLHISPsNMTNQNTNEYLEKIKQRLFENLRML 370
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
782-935 7.56e-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: 7.56e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  782 HHAEESTAMGFCFFNSVAITAKYLRDQLNisKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdeGN-FFPGSGAPNEV 860
Cdd:cd10005  132 HHAKKFEASGFCYVNDIVIAILELLKYHP--RVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKY--GNyFFPGTGDMYEV 207
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30795202  861 GTGLGEGYNINIAWTGGLDppmgDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTppLGGYKVTAKcfGH 935
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 ...
654-1014 1.13e-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: 1.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  654 HPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHS-EHHSLLYGTNP---LDGQKLDPRILLGDDSQKF---- 725
Cdd:cd10011   21 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSdEYIKFLRSIRPdnmSEYSKQMQRFNVGEDCPVFdglf 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  726 -FSSLPCGGlGVDSDTIWNELHSSGAARMAVGCvielaskvasgelkngfavvrppgHHAEESTAMGFCFFNSVAITAKY 804
Cdd:cd10011  101 eFCQLSTGG-SVAGAVKLNRQQTDMAVNWAGGL------------------------HHAKKSEASGFCYVNDIVLAILE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  805 LRDQLNisKILIVDLDVHHGNGTQQAFYADPSILYISlhRYDEGNFFPGSGAPNEVGTGLGEGYNINIAWTGGLDppmgD 884
Cdd:cd10011  156 LLKYHQ--RVLYIDIDIHHGDGVEEAFYTTDRVMTVS--FHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGID----D 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202  885 VEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTppLGGYKVTAKcfGHlTKQLMTLADGRVVLALEGGHDLT----A 960
Cdd:cd10011  228 ESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDR--LGCFNLTVK--GH-AKCVEVVKTFNLPLLMLGGGGYTirnvA 302
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30795202  961 ICDASEACV--NALLGNEL------EPLAEDI-LHQSP-NMNAVISLQKIIEIQSKYWKSVRMV 1014
Cdd:cd10011  303 RCWTYETAValDCEIPNELpyndyfEYFGPDFkLHISPsNMTNQNTPEYMEKIKQRLFENLRML 366
PTZ00063 PTZ00063
histone deacetylase; Provisional
782-935 1.15e-21

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 99.11  E-value: 1.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202   782 HHAEESTAMGFCFFNSVAITA----KYLrdqlniSKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdeGNFFPGSGAP 857
Cdd:PTZ00063  137 HHAKRSEASGFCYINDIVLGIlellKYH------ARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFPGTGDV 208
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30795202   858 NEVGTGLGEGYNINIAWTGGLDppmgDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTppLGGYKVTAKcfGH 935
Cdd:PTZ00063  209 TDIGVAQGKYYSVNVPLNDGID----DDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDR--LGRFNLTIK--GH 278
ClassIIa_HDAC9_Gln-rich-N cd10163
Glutamine-rich N-terminal helical domain of HDAC9, a Class IIa histone deacetylase; This ...
38-124 5.48e-20

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: 85.58  E-value: 5.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202   38 DPVVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIK---ELLAIKQQQELLEKEQKLEQQRQEQE 114
Cdd:cd10163    1 DPTVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHLKlqqELLAMKQQQELLEKEQKLEQQRQEQE 80
                         90
                 ....*....|
gi 30795202  115 VERHRREQQL 124
Cdd:cd10163   81 LERHRREQQL 90
PTZ00346 PTZ00346
histone deacetylase; Provisional
782-955 6.40e-18

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 87.78  E-value: 6.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202   782 HHAEESTAMGFCFFNSVAITAKYLRDQLNisKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEgNFFPGSGAPNEVG 861
Cdd:PTZ00346  154 HHSKCGECSGFCYVNDIVLGILELLKCHD--RVLYVDIDMHHGDGVDEAFCTSDRVFTLSLHKFGE-SFFPGTGHPRDVG 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202   862 TGLGEGYNINIA-WTGgldppMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTppLGGYKVTAKCFGHLTKQL 940
Cdd:PTZ00346  231 YGRGRYYSMNLAvWDG-----ITDFYYLGLFEHALHSIVRRYSPDAIVLQCGADSLAGDR--LGLLNLSSFGHGQCVQAV 303
                         170
                  ....*....|....*
gi 30795202   941 MTLadGRVVLALEGG 955
Cdd:PTZ00346  304 RDL--GIPMLALGGG 316
ClassIIa_HDAC_Gln-rich-N cd10149
Glutamine-rich N-terminal helical domain of various Class IIa histone deacetylases (HDAC4, ...
38-124 2.46e-17

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: 77.81  E-value: 2.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202   38 DPVVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIK---ELLAIKQQQELLEKEQKLEQQRQEQE 114
Cdd:cd10149    1 DPVLREQQLQQELLALKQQQQIQKQLLIAEFQKQHENLTRQHEAQLQEHIKqqqEMLAIKQQQELLEKQRKLEQQRQEQE 80
                         90
                 ....*....|
gi 30795202  115 VERHRREQQL 124
Cdd:cd10149   81 LEKQRREQQL 90
HDAC4_Gln pfam12203
Glutamine rich N terminal domain of histone deacetylase 4; This domain is found in eukaryotes, ...
65-124 1.32e-14

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: 70.27  E-value: 1.32e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30795202     65 IAEFQKQHENLTRQHQAQLQEHIK---ELLAIKQQQELLEKEQKLEQQRQEQEVERHRREQQL 124
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 ...
65-124 1.98e-12

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: 64.06  E-value: 1.98e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30795202   65 IAEFQKQHENLTRQHQAQLQEHIK---ELLAIKQQQELLEKEQKLEQQRQEQEVERHRREQQL 124
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 ...
38-147 1.23e-10

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: 59.07  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795202   38 DPVVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIK---ELLAIKQQQELLEKeqkleqqrqeqe 114
Cdd:cd10164    1 DPSLREQQLQQELLLLKQQQQLQKQLLFAEFQKQHEHLTRQHEVQLQKHLKvraELFSEQQQQEILAA------------ 68
                         90       100       110
                 ....*....|....*....|....*....|...
gi 30795202  115 verhRREQQLPPLRGKDRGRERAVASTEVKQKL 147
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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