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Conserved domains on  [gi|767920762|ref|XP_011510528|]
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histone deacetylase 4 isoform X17 [Homo sapiens]

Protein Classification

histone deacetylase 4( domain architecture ID 10178366)

histone deacetylase 4 (HD4) is a class IIa histone deacetylase that is 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
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
 630-1038 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: 929.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  630 KPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPL 709
Cdd:cd10006     1 KPRFTTGLVYDTLMLKHQCTCGNSNSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  710 NRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEEST 789
Cdd:cd10006    81 NRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSSGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEEST 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  790 PMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGF 869
Cdd:cd10006   161 PMGFCYFNSVAIAAKLLQQRLNVSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  870 NVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRI 949
Cdd:cd10006   241 NVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSAKCFGYLTKQLMGLAGGRI 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  950 VLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTC 1029
Cdd:cd10006   321 VLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGYSLIEAQTC 400


                  ....*....
gi 767920762 1030 ENEEAETVT 1038
Cdd:cd10006   401 ENEEAETVT 409
ClassIIa_HDAC4_Gln-rich-N cd10162
Glutamine-rich N-terminal helical domain of HDAC4, a Class IIa histone deacetylase; This ...
 67-128 1.98e-32

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: 121.07  E-value: 1.98e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920762   67 AEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKL 128
Cdd:cd10162    29 AEFQRQHEQLSRQHEAQLHEHIKQQQELLAMKHQQELLEHQRKLERHRQEQEMEKQQREQKL 90
 
Name Accession Description Interval E-value
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
 630-1038 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: 929.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  630 KPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPL 709
Cdd:cd10006     1 KPRFTTGLVYDTLMLKHQCTCGNSNSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  710 NRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEEST 789
Cdd:cd10006    81 NRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSSGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEEST 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  790 PMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGF 869
Cdd:cd10006   161 PMGFCYFNSVAIAAKLLQQRLNVSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  870 NVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRI 949
Cdd:cd10006   241 NVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSAKCFGYLTKQLMGLAGGRI 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  950 VLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTC 1029
Cdd:cd10006   321 VLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGYSLIEAQTC 400


                  ....*....
gi 767920762 1030 ENEEAETVT 1038
Cdd:cd10006   401 ENEEAETVT 409
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 656-973 7.61e-126

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: 385.44  E-value: 7.61e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762   656 HPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHtllygtnpLNRqkldskklLGSLASVFVRLPCGGV 735
Cdd:pfam00850    1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEY--------LEF--------LEEAAPEGGALLLLSY 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762   736 GVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKI 815
Cdd:pfam00850   65 LSGDDDTPVSPGSYEAALLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLKRV 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762   816 LIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYdDGNFFPGSGAPDEVGTGPGVGFNVNMAftggLDPPMGDAEYLAAFRTV 895
Cdd:pfam00850  145 AIVDFDVHHGNGTQEIFYDDPSVLTLSIHQY-PGGFYPGTGFADETGEGKGKGYTLNVP----LPPGTGDAEYLAAFEEI 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762   896 VMPIASEFAPDVVLVSSGFDAVEGHptPLGGYNLSARCFGYLTKQLMGLA---GGRIVLALEGGHDLTAICDASEACVSA 972
Cdd:pfam00850  220 LLPALEEFQPDLILVSAGFDAHAGD--PLGGLNLTTEGFAEITRILLELAdplCIRVVSVLEGGYNLDALARSATAVLAA 297


                   .
gi 767920762   973 L 973
Cdd:pfam00850  298 L 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 635-975 2.77e-102

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 323.60  E-value: 2.77e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  635 TGLVYDTLMLKHQCtcgsSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHtllygtnplnrqkl 714
Cdd:COG0123     1 TALIYHPDYLLHDL----GPGHPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDY-------------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  715 dskkllgsLASVFVRLPCGGVG-VDSDTIWNEvHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGF 793
Cdd:COG0123    63 --------VDALRAASLDGGYGqLDPDTPVSP-GTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGF 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  794 CYFNSVAVAAKLLQQRlSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYddgNFFPGSGAPDEVGTGPGVGFNVNM 873
Cdd:COG0123   134 CLFNNAAIAARYLLAK-GLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD---PLYPGTGAADETGEGAGEGSNLNV 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  874 AftggLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGhpTPLGGYNLSARCFGYLTKQLMGLA---GGRIV 950
Cdd:COG0123   210 P----LPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHAD--DPLGRLNLTTEGYAWRTRRVLELAdhcGGPVV 283

                         330       340
                  ....*....|....*....|....*
gi 767920762  951 LALEGGHDLTAICDASEACVSALLG 975
Cdd:COG0123   284 SVLEGGYNLDALARSVAAHLETLLG 308
ClassIIa_HDAC4_Gln-rich-N cd10162
Glutamine-rich N-terminal helical domain of HDAC4, a Class IIa histone deacetylase; This ...
 67-128 1.98e-32

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: 121.07  E-value: 1.98e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920762   67 AEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKL 128
Cdd:cd10162    29 AEFQRQHEQLSRQHEAQLHEHIKQQQELLAMKHQQELLEHQRKLERHRQEQEMEKQQREQKL 90
HDAC4_Gln pfam12203
Glutamine rich N terminal domain of histone deacetylase 4; This domain is found in eukaryotes, ...
 67-128 8.31e-25

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: 99.16  E-value: 8.31e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920762    67 AEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKL 128
Cdd:pfam12203   30 AEFQKQHELLTRQHEAQLQEHIKQQQELLAMKQQQELLEQQRKLEQQRQEEELEKHRREQQL 91
PTZ00063 PTZ00063
histone deacetylase; Provisional
 783-947 2.03e-22

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 101.43  E-value: 2.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  783 HHAEESTPMGFCYFNSVAVAA-KLLQQRlsvSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYddGNFFPGSGAPDEV 861
Cdd:PTZ00063  137 HHAKRSEASGFCYINDIVLGIlELLKYH---ARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFPGTGDVTDI 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  862 GTGPGVGFNVNMAFTGGLDppmgDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGhpTPLGGYNLS----ARCFGYL 937
Cdd:PTZ00063  212 GVAQGKYYSVNVPLNDGID----DDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTG--DRLGRFNLTikghAACVEFV 285

                         170
                  ....*....|...
gi 767920762  938 TK---QLMGLAGG 947
Cdd:PTZ00063  286 RSlniPLLVLGGG 298
fliH PRK06800
flagellar assembly protein H; Validated
 68-173 6.59e-05

flagellar assembly protein H; Validated


Pssm-ID: 180700  Cd Length: 228  Bit Score: 45.63  E-value: 6.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762   68 EFQRQHEQLsRQHEAQLHEH---IKQQQEMLAMKHQQeLLEHQRKLERHRQEQELEKQHREQKLQQLKnkekgkesavas 144
Cdd:PRK06800   35 EIQKDHEEL-LAQQKSLHKElnqLRQEQQKLERERQQ-LLADREQFQEHVQQQMKEIEAARQQFQKEQ------------ 100

                          90       100
                  ....*....|....*....|....*....
gi 767920762  145 TEVKMKLQEFVLNKKKALAHRNLNHCISS 173
Cdd:PRK06800  101 QETAYEWTELLWDQSFQLAEKIVNQAVDT 129
FliJ COG2882
Flagellar biosynthesis chaperone FliJ [Cell motility];
82-129 6.99e-04

Flagellar biosynthesis chaperone FliJ [Cell motility];


Pssm-ID: 442129 [Multi-domain]  Cd Length: 142  Bit Score: 41.04  E-value: 6.99e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920762   82 AQLHEHIKQQQEMLAM------KHQQELLEHQRKL-------ERHRQEQELEKQHREQKLQ 129
Cdd:COG2882    74 ARLDEAIEQQQQQVAQaeqqveQARQAWLEARQERkaleklkERRREEERQEENRREQKEL 134
 
Name Accession Description Interval E-value
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
 630-1038 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: 929.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  630 KPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPL 709
Cdd:cd10006     1 KPRFTTGLVYDTLMLKHQCTCGNSNSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  710 NRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEEST 789
Cdd:cd10006    81 NRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSSGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEEST 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  790 PMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGF 869
Cdd:cd10006   161 PMGFCYFNSVAIAAKLLQQRLNVSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  870 NVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRI 949
Cdd:cd10006   241 NVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSAKCFGYLTKQLMGLAGGRI 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  950 VLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTC 1029
Cdd:cd10006   321 VLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGYSLIEAQTC 400


                  ....*....
gi 767920762 1030 ENEEAETVT 1038
Cdd:cd10006   401 ENEEAETVT 409
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 633-1009 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: 806.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  633 FTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQ 712
Cdd:cd11681     1 FTTGLAYDPLMLKHQCICGNNSSHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTLLYGTNPLSRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  713 KLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMG 792
Cdd:cd11681    81 KLDPTKLAGLPQKSFVRLPCGGIGVDSDTVWNELHTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQAMG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  793 FCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVN 872
Cdd:cd11681   161 FCFFNSVAIAAKQLQQKLKLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFPGTGAPTEVGSGAGEGFNVN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  873 MAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLA 952
Cdd:cd11681   241 IAWSGGLDPPMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPPPLGGYKVSPACFGYMTRQLMNLAGGKVVLA 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767920762  953 LEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYW 1009
Cdd:cd11681   321 LEGGYDLTAICDASEACVRALLGDELDPLSEEELERRPNPNAVTSLEKVIAIQSPYW 377
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
 633-1046 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: 793.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  633 FTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQ 712
Cdd:cd10007     3 FTTGLVYDTFMLKHQCTCGNTNVHPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHSEHHTLLYGTSPLNRQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  713 KLDSKKLLGSLAS-VFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPM 791
Cdd:cd10007    83 KLDSKKLLGPLSQkMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLIELAFKVAAGELKNGFAVIRPPGHHAEESTAM 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  792 GFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNV 871
Cdd:cd10007   163 GFCFFNSVAIAAKLLQQKLNVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGNFFPGSGAPDEVGAGPGVGFNV 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  872 NMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVL 951
Cdd:cd10007   243 NIAWTGGVDPPIGDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGHQSPLGGYSVTAKCFGHLTKQLMTLAGGRVVL 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  952 ALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCEN 1031
Cdd:cd10007   323 ALEGGHDLTAICDASEACVSALLGMELTPLDNTVLQQKPNDNAVATLERVIEIQSKHWSCLKRFAATLGFSLLEAQRGEL 402

                         410
                  ....*....|....*
gi 767920762 1032 EEAETVTAMASLSVG 1046
Cdd:cd10007   403 EEAETVSAMASLSVD 417
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
 633-1009 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: 726.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  633 FTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQ 712
Cdd:cd10008     1 FTTGLVYDSVMLKHQCSCGDNSNHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  713 KLDSKKLLGSLAS-VFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPM 791
Cdd:cd10008    81 KLDNGKLAGLLAQrMFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  792 GFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNV 871
Cdd:cd10008   161 GFCFFNSVAIACRQLQQQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGAGSGEGFNV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  872 NMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVL 951
Cdd:cd10008   241 NVAWAGGLDPPMGDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVL 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767920762  952 ALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYW 1009
Cdd:cd10008   321 ALEGGHDLTAICDASEACVAALLGNEVDPLSEESWKQKPNLNAIRSLEAVIRVHSKYW 378
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
 633-1010 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: 642.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  633 FTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQ 712
Cdd:cd10009     1 SATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  713 KLDSKKLLGSLAS-VFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPM 791
Cdd:cd10009    81 KLDPRILLGDDSQkFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  792 GFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNV 871
Cdd:cd10009   161 GFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYNI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  872 NMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVL 951
Cdd:cd10009   241 NIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVL 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767920762  952 ALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWR 1010
Cdd:cd10009   321 ALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSKYWK 379
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
 656-974 2.68e-137

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: 415.36  E-value: 2.68e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  656 HPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHtllygtnplnrqkldskkllgsLASVFVRLPCGGV 735
Cdd:cd09992     1 HPERPERLLAILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEY----------------------IERVEETCEAGGG 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  736 GVDSDTIWNEvHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKI 815
Cdd:cd09992    59 YLDPDTYVSP-GSYEAALLAAGAALAAVDAVLSGEAENAFALVRPPGHHAEPDRAMGFCLFNNVAIAARYAQKRYGLKRV 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  816 LIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDdgnFFPGSGAPDEVGTGPGVGFNVNMAFTGGldppMGDAEYLAAFRTV 895
Cdd:cd09992   138 LIVDWDVHHGNGTQDIFYDDPSVLYFSIHQYP---FYPGTGAAEETGGGAGEGFTINVPLPPG----SGDAEYLAAFEEV 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  896 VMPIASEFAPDVVLVSSGFDAVEGHptPLGGYNLSARCFGYLTKQLMGLA----GGRIVLALEGGHDLTAICDASEACVS 971
Cdd:cd09992   211 LLPIAREFQPDLVLVSAGFDAHRGD--PLGGMNLTPEGYARLTRLLKELAdehcGGRLVFVLEGGYNLEALAESVLAVLE 288


                  ...
gi 767920762  972 ALL 974
Cdd:cd09992   289 ALL 291
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
 639-1012 2.87e-137

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: 417.51  E-value: 2.87e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  639 YDTLMLKHQCTCgsSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYgtnplnrQKLDSKK 718
Cdd:cd10003     1 YDQRMMNHHNLW--DPGHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHLDEM-------KSLEKMK 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  719 L--LGSLASVFvrlpcggvgvdsDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYF 796
Cdd:cd10003    72 PreLNRLGKEY------------DSIYIHPDSYQCALLAAGCVLQVVEAVLTGESRNGVAIVRPPGHHAEQDTACGFCFF 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  797 NSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGS--GAPDEVGTGPGVGFNVNMA 874
Cdd:cd10003   140 NNVAIAARYAQKKYGLKRILIVDWDVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSpeGNYDVVGKGKGEGFNVNIP 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  875 FTGGldpPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGhpTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALE 954
Cdd:cd10003   220 WNKG---GMGDAEYIAAFQQVVLPIAYEFNPELVLVSAGFDAARG--DPLGGCKVTPEGYAHMTHMLMSLAGGRVIVILE 294

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767920762  955 GGHDLTAICDASEACVSALLGnelDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCL 1012
Cdd:cd10003   295 GGYNLTSISESMSMCTKTLLG---DPPPVLDLPRPPCSSALKSINNVLQVHQKYWKSL 349
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 656-973 7.61e-126

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: 385.44  E-value: 7.61e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762   656 HPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHtllygtnpLNRqkldskklLGSLASVFVRLPCGGV 735
Cdd:pfam00850    1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEY--------LEF--------LEEAAPEGGALLLLSY 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762   736 GVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKI 815
Cdd:pfam00850   65 LSGDDDTPVSPGSYEAALLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLKRV 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762   816 LIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYdDGNFFPGSGAPDEVGTGPGVGFNVNMAftggLDPPMGDAEYLAAFRTV 895
Cdd:pfam00850  145 AIVDFDVHHGNGTQEIFYDDPSVLTLSIHQY-PGGFYPGTGFADETGEGKGKGYTLNVP----LPPGTGDAEYLAAFEEI 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762   896 VMPIASEFAPDVVLVSSGFDAVEGHptPLGGYNLSARCFGYLTKQLMGLA---GGRIVLALEGGHDLTAICDASEACVSA 972
Cdd:pfam00850  220 LLPALEEFQPDLILVSAGFDAHAGD--PLGGLNLTTEGFAEITRILLELAdplCIRVVSVLEGGYNLDALARSATAVLAA 297


                   .
gi 767920762   973 L 973
Cdd:pfam00850  298 L 298
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
 662-973 8.35e-119

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: 366.37  E-value: 8.35e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  662 RIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKllgslasvfvrlpcggvGVDSDT 741
Cdd:cd09301     1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKANFAVATITESKP-----------------VIFGPN 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  742 IWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRlSVSKILIVDWD 821
Cdd:cd09301    64 FPVQRHYFRGARLSTGGVVEAAELVAKGELERAFAVVGAGGHHAGKSRAWGFCYFNDVVLAIKFLRER-GISRILIIDTD 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  822 VHHGNGTQQAFYSDPSVLYMSLHRYDDGNFfpgsgapdevGTGPGVGFNVNMAFTGGldppMGDAEYLAAFRTVVMPIAS 901
Cdd:cd09301   143 AHHGDGTREAFYDDDRVLHMSFHNYDIYPF----------GRGKGKGYKINVPLEDG----LGDEEYLDAVERVISKVLE 208

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920762  902 EFAPDVVLVSSGFDAVEGHptPLGGYNLSARCFGYLTKQLMGLA-GGRIVLALEGGHDLTAICDASEACVSAL 973
Cdd:cd09301   209 EFEPEVVVLQFGHDTHEGD--RLGGFNLSEKGFVKLAEIVKEFArGGPILMVLGGGYNPEAAARIWTAIIKEL 279
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 656-982 4.18e-118

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: 365.90  E-value: 4.18e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  656 HPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAH-TLLYGTNPLNRQKLDSKKLLGSLASVFVrlpcgg 734
Cdd:cd11600     3 HPEDPSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEHwDRVEATEKMSDEQLKDRTEIFERDSLYV------ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  735 vgvdsdtiwNEvHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRL--SV 812
Cdd:cd11600    77 ---------NN-DTAFCARLSCGGAIEACRAVAEGRVKNAFAVVRPPGHHAEPDESMGFCFFNNVAVAAKWLQTEYpdKI 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  813 SKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGS--GAPDEVGTGPGVGFNVNMAFTgglDPPMGDAEYLA 890
Cdd:cd11600   147 KKILILDWDIHHGNGTQRAFYDDPNVLYISLHRFENGGFYPGTpyGDYESVGEGAGLGFNVNIPWP---QGGMGDADYIY 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  891 AFRTVVMPIASEFAPDVVLVSSGFDAVEGhpTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACV 970
Cdd:cd11600   224 AFQRIVMPIAYEFDPDLVIISAGFDAADG--DELGQCHVTPAGYAHMTHMLMSLAGGKLVVALEGGYNLDAISDSALAVA 301

                         330
                  ....*....|..
gi 767920762  971 SALLGNELDPLP 982
Cdd:cd11600   302 KVLLGEAPPKLP 313
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 635-975 2.77e-102

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 323.60  E-value: 2.77e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  635 TGLVYDTLMLKHQCtcgsSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHtllygtnplnrqkl 714
Cdd:COG0123     1 TALIYHPDYLLHDL----GPGHPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDY-------------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  715 dskkllgsLASVFVRLPCGGVG-VDSDTIWNEvHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGF 793
Cdd:COG0123    63 --------VDALRAASLDGGYGqLDPDTPVSP-GTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGF 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  794 CYFNSVAVAAKLLQQRlSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYddgNFFPGSGAPDEVGTGPGVGFNVNM 873
Cdd:COG0123   134 CLFNNAAIAARYLLAK-GLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD---PLYPGTGAADETGEGAGEGSNLNV 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  874 AftggLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGhpTPLGGYNLSARCFGYLTKQLMGLA---GGRIV 950
Cdd:COG0123   210 P----LPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHAD--DPLGRLNLTTEGYAWRTRRVLELAdhcGGPVV 283

                         330       340
                  ....*....|....*....|....*
gi 767920762  951 LALEGGHDLTAICDASEACVSALLG 975
Cdd:COG0123   284 SVLEGGYNLDALARSVAAHLETLLG 308
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 650-1009 5.04e-101

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: 321.57  E-value: 5.04e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  650 CGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLygtnpLNRQKLDSKKLLGSLASVFvr 729
Cdd:cd10002     1 CNWDSNHIECPERLEAILERLTQDGLLERCVKIPAREAEEDEILLVHSQEYIDL-----VKSTETMEKEELESLCSGY-- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  730 lpcggvgvdsDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQR 809
Cdd:cd10002    74 ----------DSVYLCPSTYEAARLAAGSTIELVKAVMAGKIQNGFALIRPPGHHAMRNEANGYCIFNNVAIAAKYAIEK 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  810 LSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAP--DEVGTGPGVGFNVNMAF--TGgldppMGD 885
Cdd:cd10002   144 LGLKRILIVDWDVHHGQGTQQGFYEDPRVLYFSIHRYEHGRFWPHLFESdyDYIGVGHGYGFNVNVPLnqTG-----LGD 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  886 AEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGhpTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDA 965
Cdd:cd10002   219 ADYLAIFHHILLPLALEFQPELVLVSAGFDASIG--DPEGEMAVTPAGYAHLTRLLMGLAGGKLLLVLEGGYLLESLAES 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 767920762  966 SEACVSALLGnelDPLPEKVLQQRPNAnAVRSMEKVMEIHSKYW 1009
Cdd:cd10002   297 VSMTLRGLLG---DPLPPLAPPIPIRS-VLETILNAIAHLSPRW 336
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
 635-988 2.12e-89

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: 291.00  E-value: 2.12e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  635 TGLVYDTLMLKHqcTCGSSSS-------------HPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHt 701
Cdd:cd09996     1 TGFVWDERYLWH--DTGTGALflpvggllvqpgrHPENPETKRRIKNLLEVSGLSDHLVLITPRPATDEELLRVHTPEY- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  702 llygtnpLNRQKLDSKKllgslasvfvrlpcGGVGVDSDTIWNEvHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPP 781
Cdd:cd09996    78 -------IDRVKAASAA--------------GGGEAGGGTPFGP-GSYEIALLAAGGAIAAVDAVLDGEVDNAYALVRPP 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  782 GHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRydDGNFFPGSGAPDEV 861
Cdd:cd09996   136 GHHAEPDQGMGFCLFNNVAIAARHALAVGGVKRVAVVDWDVHHGNGTQAIFYDDPDVLTISLHQ--DRCFPPDSGAVEER 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  862 GTGPGVGFNVNMAftggLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAveGHPTPLGGYNLSARCFGYLTKQL 941
Cdd:cd09996   214 GEGAGEGYNLNIP----LPPGSGDGAYLHAFERIVLPALRAFRPELIIVASGFDA--SAFDPLGRMMLTSDGFRALTRKL 287

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920762  942 MGLA----GGRIVLALEGGHDL------------------TAICDASEACVSALLGNELDPLPEKVLQQ 988
Cdd:cd09996   288 RDLAdelcGGRLVMVHEGGYSEayvpfcglavleelsgvrTGIADPLLYYPEAQGGQELQPHQRAAIDA 356
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
 650-1009 3.36e-87

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: 284.44  E-value: 3.36e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  650 CGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNplnrQKLdSKKLLGSLASVFvr 729
Cdd:cd11682     1 CLWDESFPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYVALMKST----QYM-TEEELRTLADTY-- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  730 lpcggvgvdsDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQR 809
Cdd:cd11682    74 ----------DSVYLHPNSYSCACLAVGSVLQLVDKVLGGEIRNGLAIVRPPGHHAQHDKMDGYCMFNNVAIAARYAQQK 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  810 LSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDE--VGTGPGVGFNVNMAFTgglDPPMGDAE 887
Cdd:cd11682   144 HGVQRVLIVDWDVHHGQGTQFIFEQDPSVLYFSIHRYEQGRFWPHLKESDSsaVGFGRGEGYNINVPWN---QVGMRDAD 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  888 YLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTplGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASE 967
Cdd:cd11682   221 YIAAFLHVLLPVALEFQPQLVLVAAGFDAVIGDPK--GEMAATPACFAHLTHLLMGLAGGKLILSLEGGYNLRSLAEGVC 298

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 767920762  968 ACVSALLGnelDPLPEKVLQQRPNANAVRSMEKVMEIHSKYW 1009
Cdd:cd11682   299 ASLKALLG---DPCPMLESPGAPCRSALASVSCTISALEPFW 337
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
 656-974 2.36e-81

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: 266.69  E-value: 2.36e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  656 HPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTllygtnplnrqkldsKKLLGSLASVfvrlpcGGV 735
Cdd:cd11599     1 HPESPERLEAILDALIASGLDRLLRQLEAPPATREQLLRVHDAAYV---------------DRLEAAAPEE------GLV 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  736 GVDSDTIWNEvHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKI 815
Cdd:cd11599    60 QLDPDTAMSP-GSLEAALRAAGAVVAAVDAVMAGEARNAFCAVRPPGHHAERDKAMGFCLFNNVAIAAAHALAHHGLERV 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  816 LIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYddgNFFPGSGAPDEvgTGPGVGFNVNM-AFTGGldppmgdAEYLAAFRT 894
Cdd:cd11599   139 AIVDFDVHHGNGTEDIFRDDPRVLFCSSHQH---PLYPGTGAPDE--TGHGNIVNVPLpAGTGG-------AEFREAVED 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  895 VVMPIASEFAPDVVLVSSGFDAvegHPT-PLGGYNLSARCFGYLTKQLMGLA----GGRIVLALEGGHDLTAICDASEAC 969
Cdd:cd11599   207 RWLPALDAFKPDLILISAGFDA---HRDdPLAQLNLTEEDYAWITEQLMDVAdrycDGRIVSVLEGGYDLSALARSVAAH 283


                  ....*
gi 767920762  970 VSALL 974
Cdd:cd11599   284 VRALM 288
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 662-1009 5.95e-74

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: 248.24  E-value: 5.95e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  662 RIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNP-LNRQKLdsKKLLGSLASVFVRLpcggvgvdsd 740
Cdd:cd11683    13 RLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRETQvMNKEEL--MAISGKYDAVYFHP---------- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  741 tiwNEVHsagAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDW 820
Cdd:cd11683    81 ---NTFH---CARLAAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYAKKKYGLHRILIVDW 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  821 DVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPG--SGAPDEVGTGPGVGFNVNMAFTgglDPPMGDAEYLAAFRTVVMP 898
Cdd:cd11683   155 DVHHGQGIQYIFEEDPSVLYFSWHRYEHQRFWPFlrESDYDAVGRGKGLGFNINLPWN---KVGMGNADYLAAFFHVLLP 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  899 IASEFAPDVVLVSSGFDAVEGHPTplGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGnel 978
Cdd:cd11683   232 LAFEFDPELVLVSAGFDSAIGDPE--GQMCATPECFAHLTHLLMVLAGGKLCAVLEGGYHLESLAESVCMTVQTLLG--- 306

                         330       340       350
                  ....*....|....*....|....*....|.
gi 767920762  979 DPLPEKVLQQRPNANAVRSMEKVMEIHSKYW 1009
Cdd:cd11683   307 DPLPRLSGEMTPCQSALESIQNVRAAQAPYW 337
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
 637-975 9.55e-68

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: 229.35  E-value: 9.55e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  637 LVYDTLMLKHQ----CTCGSSSSHPEHAGRIQSIWSRLQETGLRGKcecIRGRKATLEELQTVHSEAHtllygtnplnrq 712
Cdd:cd10001     2 IVYSEDHLLHHpkteLSRGKLVPHPENPERAEAILDALKRAGLGEV---LPPRDFGLEPILAVHDPDY------------ 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  713 kLDskkllgslasvFVRlpcggvGVDSDTIWNEvHSAGAARLAVGCVVELVFKVATGElKNGFAVVRPPGHHAEESTPMG 792
Cdd:cd10001    67 -VD-----------FLE------TADTDTPISE-GTWEAALAAADTALTAADLVLEGE-RAAYALCRPPGHHAGRDRAGG 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  793 FCYFNSVAVAAKLLQQRlsVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRyDDGNFFPG-SGAPDEVGTGPGVGFNV 871
Cdd:cd10001   127 FCYFNNAAIAAQYLRDR--AGRVAILDVDVHHGNGTQEIFYERPDVLYVSIHG-DPRTFYPFfLGFADETGEGEGEGYNL 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  872 NMAftggLDPPMGDAEYLAAFRTVVMPIAsEFAPDVVLVSSGFDAVEGhpTPLGGYNLSARCFGYLTKQLMGLaGGRIVL 951
Cdd:cd10001   204 NLP----LPPGTGDDDYLAALDEALAAIA-AFGPDALVVSLGFDTHEG--DPLSDFKLTTEDYARIGRRIAAL-GLPTVF 275

                         330       340
                  ....*....|....*....|....
gi 767920762  952 ALEGGHDLTAIcdaSEACVSALLG 975
Cdd:cd10001   276 VQEGGYNVDAL---GRNAVAFLAG 296
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
 656-959 4.07e-48

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: 174.29  E-value: 4.07e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  656 HPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHtllygtnpLNRQKLDSKkllGSLASVFVRLpcgGV 735
Cdd:cd09994    17 HPFNPPRLSLTKDLLRALGLLPPVDLVPPRPATEEELLLFHTPDY--------IEAVKEASR---GQEPEGRGRL---GL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  736 GVDSDTIWNEVHSAgaARLAVGCVVELVFKVATGElknGFAVVRPPG--HHAEESTPMGFCYFNSVAVAAKLLQqRLSVS 813
Cdd:cd09994    83 GTEDNPVFPGMHEA--AALVVGGTLLAARLVLEGE---ARRAFNPAGglHHAMRGRASGFCVYNDAAVAIERLR-DKGGL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  814 KILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRyDDGNFFPGSGAPDEVGTGPGVGFNVNMAftggLDPPMGDAEYLAAFR 893
Cdd:cd09994   157 RVAYVDIDAHHGDGVQAAFYDDPRVLTISLHE-SGRYLFPGTGFVDEIGEGEGYGYAVNIP----LPPGTGDDEFLRAFE 231

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  894 TVVMPIASEFAPDVVLVSSGFDAVEGhpTPLGGYNLSARCFGYLTKQLMGLA----GGRIVLALEGGHDL 959
Cdd:cd09994   232 AVVPPLLRAFRPDVIVSQHGADAHAG--DPLTHLNLSNRAYRAAVRRIRELAdeycGGRWLALGGGGYNP 299
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 747-973 2.48e-39

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: 145.60  E-value: 2.48e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  747 HSAGAARLAVGCVVELVFKVatgelKNGFAVVrppGHHAEestpmgfcyFNSVAVAAKLLQQRlsvskILIVDWDVHHGN 826
Cdd:cd09987     6 RKAEAHELLAGVVVAVLKDG-----KVPVVLG---GDHSI---------ANGAIRAVAELHPD-----LGVIDVDAHHDV 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  827 GTQQAFY--------------SDPSVLYMSLHRYDDGNFFPGsgapdevGTGPGVGFNVNMAFTGGLdppmgDAEYLAAF 892
Cdd:cd09987    64 RTPEAFGkgnhhtprhllcepLISDVHIVSIGIRGVSNGEAG-------GAYARKLGVVYFSMTEVD-----KLGLGDVF 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  893 RTVVMPIasEFAPDVVLVSSGFDAVEGHPTP----LGGYNLSARCFGYLTKQLMGLaGGRIVLALEGGHDL----TAICD 964
Cdd:cd09987   132 EEIVSYL--GDKGDNVYLSVDVDGLDPSFAPgtgtPGPGGLSYREGLYITERIAKT-NLVVGLDIVEVNPLldetGRTAR 208


                  ....*....
gi 767920762  965 ASEACVSAL 973
Cdd:cd09987   209 LAAALTLEL 217
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 649-943 1.70e-34

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: 135.93  E-value: 1.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  649 TCGSSSSHPEHAGRIQSIwsrLQETGLRGKCECIRGRKATLEELQTVHSEAHTllygtNPLNR--QKLDSKKLLGSLASV 726
Cdd:cd10000    12 LCDRLPKVPNRASMVHSL---IEAYGLLKQLRVVKPRVATEEELASFHSDEYI-----QFLKKasNEGDNDEEPSEQQEF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  727 fvrlpcgGVGVDS---DTIWNEVHS-AGAARLAVGCVVELVFKVAtgelkngfavVRPPG--HHAEESTPMGFCYFNSVA 800
Cdd:cd10000    84 -------GLGYDCpifEGIYDYAAAvAGATLTAAQLLIDGKCKVA----------INWFGgwHHAQRDEASGFCYVNDIV 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  801 VAAKLLQQRLSvsKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGnFFPGSGAPDEVGTGPGVGFNVNMAFTGGLD 880
Cdd:cd10000   147 LGILKLREKFD--RVLYVDLDLHHGDGVEDAFSFTSKVMTVSLHKYSPG-FFPGTGDVSDVGLGKGKYYTVNVPLRDGIQ 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  881 ppmgDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHP------TPL---------------------GGYNLS--A 931
Cdd:cd10000   224 ----DEQYLQIFTAVVPEIVAAFRPEAVVLQCGADTLAGDPmgafnlTPVgigkclkyvlgwklptlilggGGYNLAntA 299

                         330
                  ....*....|..
gi 767920762  932 RCFGYLTKQLMG 943
Cdd:cd10000   300 RCWTYLTGLILG 311
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
 656-947 1.91e-33

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: 131.55  E-value: 1.91e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  656 HPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAH-TLLYGTNPLNRQKLdsKKLLgslasvfVRLpcgG 734
Cdd:cd09991    15 HPMKPHRIRMTHSLILSYGLYKKMEIYRPRPATAEELTKFHSDDYiDFLRSVSPDNMKEF--KKQL-------ERF---N 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  735 VGVD---SDTIWNEVHSAGAArlAVGCVVELVFKVATgelkngfAVVRPPG--HHAEESTPMGFCYFNSVAVAA-KLLQ- 807
Cdd:cd09991    83 VGEDcpvFDGLYEYCQLYAGG--SIAAAVKLNRGQAD-------IAINWAGglHHAKKSEASGFCYVNDIVLAIlELLKy 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  808 -QRlsvskILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYddGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDppmgDA 886
Cdd:cd09991   154 hQR-----VLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKF--GEYFFPGTGLRDIGAGKGKYYAVNVPLKDGID----DE 222

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767920762  887 EYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGhpTPLGGYNLS----ARCFGYLTK---QLMGLAGG 947
Cdd:cd09991   223 SYLQIFEPVLSKVMEVFQPSAVVLQCGADSLAG--DRLGCFNLSikghAKCVKFVKSfniPLLVLGGG 288
ClassIIa_HDAC4_Gln-rich-N cd10162
Glutamine-rich N-terminal helical domain of HDAC4, a Class IIa histone deacetylase; This ...
 67-128 1.98e-32

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: 121.07  E-value: 1.98e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920762   67 AEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKL 128
Cdd:cd10162    29 AEFQRQHEQLSRQHEAQLHEHIKQQQELLAMKHQQELLEHQRKLERHRQEQEMEKQQREQKL 90
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 666-931 3.20e-31

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: 124.15  E-value: 3.20e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  666 IWSRLQETGLRGKCECIRGRKATLEELQTVHSEA--HTLLYGTNPLNRQKL----DSKKLLGSlasvfVRLPCGGvgvds 739
Cdd:cd09993    11 LREALLEEGLVLPEDIVEPEPATREDLLRVHDPEylESLKSGELSREEIRRigfpWSPELVER-----TRLAVGG----- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  740 dTIwnevhsaGAARLAvgcvvelvfkvatgeLKNGFAVvRPPG--HHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILI 817
Cdd:cd09993    81 -TI-------LAARLA---------------LEHGLAI-NLAGgtHHAFPDRGEGFCVFNDIAIAARVLLAEGLVRRVLI 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  818 VDWDVHHGNGTQQAFYSDPSVLYMSLHrydDGNFFPGSGAPDevgtgpgvGFNVnmaftgGLDPPMGDAEYLAAFRTVVM 897
Cdd:cd09993   137 VDLDVHQGNGTAAIFADDPSVFTFSMH---GEKNYPFRKEPS--------DLDV------PLPDGTGDDEYLAALEEALP 199

                         250       260       270
                  ....*....|....*....|....*....|....
gi 767920762  898 PIASEFAPDVVLVSSGFDAVEGhpTPLGGYNLSA 931
Cdd:cd09993   200 RLLAEFRPDLVFYNAGVDVLAG--DRLGRLSLSL 231
ClassIIa_HDAC_Gln-rich-N cd10149
Glutamine-rich N-terminal helical domain of various Class IIa histone deacetylases (HDAC4, ...
 67-128 2.79e-29

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: 112.09  E-value: 2.79e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920762   67 AEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKL 128
Cdd:cd10149    29 AEFQKQHENLTRQHEAQLQEHIKQQQEMLAIKQQQELLEKQRKLEQQRQEQELEKQRREQQL 90
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
 783-963 7.03e-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: 117.75  E-value: 7.03e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  783 HHAEESTPMGFCYFNSVAVAAKLLQqRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGnFFPGSGAPDEvg 862
Cdd:cd11680   115 HHAQKSRASGFCYVNDIVLAILRLR-RARFRRVFYLDLDLHHGDGVESAFFFSKNVLTCSIHRYDPG-FFPGTGSLKN-- 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  863 tgPGVGFNVNMAFTGGLDppmgDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGhpTPLGGYNLSARCFGYLTKQLM 942
Cdd:cd11680   191 --SSDKGMLNIPLKRGLS----DKTLLRIIDSIVRPLIEKFEPEVIVIQCGCDGLSG--DPHKEWNLTIRGYGSVIELLL 262

                         170       180
                  ....*....|....*....|....
gi 767920762  943 GLAGGRIVLALEGG---HDLTAIC 963
Cdd:cd11680   263 KEFKDKPTLLLGGGgynHTEAARA 286
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
 783-935 2.88e-28

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: 116.40  E-value: 2.88e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  783 HHAEESTPMGFCYFNSVAVAakLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYdDGNFFPGSGAPDEVG 862
Cdd:cd11598   131 HHAKKSEASGFCYVNDIVLA--ILNLLRYFPRVLYIDIDVHHGDGVEEAFYRTDRVMTLSFHKY-NGEFFPGTGDLDDNG 207

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767920762  863 TGPGVGFNVNMAFTGGLDppmgDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGhpTPLGGYNLSARCFG 935
Cdd:cd11598   208 GTPGKHFALNVPLEDGID----DEQYNLLFKSIIGPTIEKFQPSAIVLQCGADSLGG--DRLGQFNLNIKAHG 274
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
 654-947 1.40e-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: 112.98  E-value: 1.40e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  654 SSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHT-LLYGTNPLNR---QKLDSKKLLGSLASVFVR 729
Cdd:cd10004    19 PGHPMKPHRIRMAHSLVMNYGLYKKMEIYRAKPATKNEMTQFHTDEYIdFLSRVTPDNMekfQKEQVKYNVGDDCPVFDG 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  730 LP--CGGVGVDSdtiwnevhSAGAARLAVGcvvelvfkvatgelKNGFAVVRPPG-HHAEESTPMGFCYFNSVAVAA-KL 805
Cdd:cd10004    99 LFefCSISAGGS--------MEGAARLNRG--------------KCDIAVNWAGGlHHAKKSEASGFCYVNDIVLGIlEL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  806 LQQRlsvSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYddGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDppmgD 885
Cdd:cd10004   157 LRYH---QRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKY--GEYFPGTGELRDIGIGTGKNYAVNVPLRDGID----D 227

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920762  886 AEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGhpTPLGGYNLS----ARCFGYLTK---QLMGLAGG 947
Cdd:cd10004   228 ESYKSIFEPVIKHVMEWYQPEAVVLQCGGDSLSG--DRLGCFNLSmkghANCVNFVKSfnlPMLVLGGG 294
HDAC4_Gln pfam12203
Glutamine rich N terminal domain of histone deacetylase 4; This domain is found in eukaryotes, ...
 67-128 8.31e-25

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: 99.16  E-value: 8.31e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920762    67 AEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKL 128
Cdd:pfam12203   30 AEFQKQHELLTRQHEAQLQEHIKQQQELLAMKQQQELLEQQRKLEQQRQEEELEKHRREQQL 91
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
 656-947 2.13e-24

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: 106.30  E-value: 2.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  656 HPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAH-TLLYGTNPLNRQKLdSKKL----LGSLASVFvrl 730
Cdd:cd10010    25 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYiKFLRSIRPDNMSEY-SKQMqrfnVGEDCPVF--- 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  731 pcggvgvDSDTIWNEVHSAGAARLAVgcvvelvfkvATGELKNGFAVVRPPG-HHAEESTPMGFCYFNSVAVAakLLQQR 809
Cdd:cd10010   101 -------DGLFEFCQLSAGGSVASAV----------KLNKQQTDIAVNWAGGlHHAKKSEASGFCYVNDIVLA--ILELL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  810 LSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYddGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDppmgDAEYL 889
Cdd:cd10010   162 KYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKY--GEYFPGTGDLRDIGAGKGKYYAVNYPLRDGID----DESYE 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767920762  890 AAFRTVVMPIASEFAPDVVLVSSGFDAVEGhpTPLGGYNLS----ARCFGYLTK---QLMGLAGG 947
Cdd:cd10010   236 AIFKPVMSKVMEMFQPSAVVLQCGADSLSG--DRLGCFNLTikghAKCVEFVKSfnlPMLMLGGG 298
PTZ00063 PTZ00063
histone deacetylase; Provisional
 783-947 2.03e-22

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 101.43  E-value: 2.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  783 HHAEESTPMGFCYFNSVAVAA-KLLQQRlsvSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYddGNFFPGSGAPDEV 861
Cdd:PTZ00063  137 HHAKRSEASGFCYINDIVLGIlELLKYH---ARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFPGTGDVTDI 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  862 GTGPGVGFNVNMAFTGGLDppmgDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGhpTPLGGYNLS----ARCFGYL 937
Cdd:PTZ00063  212 GVAQGKYYSVNVPLNDGID----DDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTG--DRLGRFNLTikghAACVEFV 285

                         170
                  ....*....|...
gi 767920762  938 TK---QLMGLAGG 947
Cdd:PTZ00063  286 RSlniPLLVLGGG 298
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
 748-973 3.50e-22

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: 99.45  E-value: 3.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  748 SAGAARLAVGCV---VELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHH 824
Cdd:cd09998    82 SLDAIQGALGAVceaVDSVFKPESPGTKRAFVAIRPPGHHCSESTPSGFCWVNNVHVGAAHAYLTHGITRVVILDIDLHH 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  825 GNGTQ------------------------QAFYSDPSVLYMSLHrydDGNFFP-GSGAPDEVGTGpgvgfNVNMAFTGG- 878
Cdd:cd09998   162 GNGTQdiawrinaeankqalesssyddfkPAGAPGLRIFYSSLH---DINSFPcEDGDPAKVKDA-----SVSIDGAHGq 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  879 ------LDPPMGDAEYLAAFR---TVVMPIASEF------APD---VVLVSSGFDAVEGHPTPLG--GYNLSARCFGYLT 938
Cdd:cd09998   234 wiwnvhLQPWTTEEDFWELYYpkyRILFEKAAEFlrlttaATPfktLVFISAGFDASEHEYESMQrhGVNVPTSFYYRFA 313

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767920762  939 KQLMGLA----GGRIVLALEGGHDLTAICDASEACVSAL 973
Cdd:cd09998   314 RDAVRFAdahaHGRLISVLEGGYSDRALCSGVLAHLTGL 352
ClassIIa_HDAC9_Gln-rich-N cd10163
Glutamine-rich N-terminal helical domain of HDAC9, a Class IIa histone deacetylase; This ...
 67-128 5.60e-22

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: 91.35  E-value: 5.60e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920762   67 AEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKL 128
Cdd:cd10163    29 AEFQKQHENLTRQHQAQLQEHLKLQQELLAMKQQQELLEKEQKLEQQRQEQELERHRREQQL 90
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
 783-935 5.78e-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: 99.39  E-value: 5.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  783 HHAEESTPMGFCYFNSVAVAA-KLLQQRlsvSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYddGN-FFPGSGAPDE 860
Cdd:cd10005   132 HHAKKFEASGFCYVNDIVIAIlELLKYH---PRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKY--GNyFFPGTGDMYE 206

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767920762  861 VGTGPGVGFNVNMAFTGGLDppmgDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGhpTPLGGYNLSARCFG 935
Cdd:cd10005   207 VGAESGRYYSVNVPLKDGID----DQSYLQLFKPVIQQVIDFYQPTCIVLQCGADSLGC--DRLGCFNLSIKGHG 275
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
 656-932 1.69e-20

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: 94.74  E-value: 1.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  656 HPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAH-TLLYGTNPLNRQKLdSKKL----LGSLASVF--- 727
Cdd:cd10011    21 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYiKFLRSIRPDNMSEY-SKQMqrfnVGEDCPVFdgl 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  728 ---VRLPCGGvgvdsdtiwnevHSAGAARLavgcvvelvfkvatGELKNGFAVVRPPG-HHAEESTPMGFCYFNSVAVAa 803
Cdd:cd10011   100 fefCQLSTGG------------SVAGAVKL--------------NRQQTDMAVNWAGGlHHAKKSEASGFCYVNDIVLA- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  804 kLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVlyMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDppm 883
Cdd:cd10011   153 -ILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRV--MTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGID--- 226

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767920762  884 gDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGhpTPLGGYNLSAR 932
Cdd:cd10011   227 -DESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSG--DRLGCFNLTVK 272
PTZ00346 PTZ00346
histone deacetylase; Provisional
 783-956 6.68e-18

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 87.78  E-value: 6.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  783 HHAEESTPMGFCYFNSVAVAakLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDgNFFPGSGAPDEVG 862
Cdd:PTZ00346  154 HHSKCGECSGFCYVNDIVLG--ILELLKCHDRVLYVDIDMHHGDGVDEAFCTSDRVFTLSLHKFGE-SFFPGTGHPRDVG 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762  863 TGPGVGFNVNMAFTGGLDppmgDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGhpTPLGGYNLSARCFGYLTKQLM 942
Cdd:PTZ00346  231 YGRGRYYSMNLAVWDGIT----DFYYLGLFEHALHSIVRRYSPDAIVLQCGADSLAG--DRLGLLNLSSFGHGQCVQAVR 304

                         170
                  ....*....|....
gi 767920762  943 GLagGRIVLALEGG 956
Cdd:PTZ00346  305 DL--GIPMLALGGG 316
ClassIIa_HDAC5_Gln-rich-N cd10164
Glutamine-rich N-terminal helical domain of HDAC5, a Class IIa histone deacetylase; This ...
 39-128 1.02e-14

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: 70.62  E-value: 1.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762   39 EPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIK---------QQQEMLAMKHQQElLEHQRK 109
Cdd:cd10164     1 DPSLREQQLQQELLLLKQQQQLQKQLLFAEFQKQHEHLTRQHEVQLQKHLKvraelfseqQQQEILAAKRQQE-LEQQRK 79

                          90
                  ....*....|....*....
gi 767920762  110 LERHRQEqELEKQHREQKL 128
Cdd:cd10164    80 REQQRQE-ELEKQRLEQQL 97
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 67-132 1.85e-06

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 51.13  E-value: 1.85e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920762    67 AEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQEL--------EKQHREQKLQQLK 132
Cdd:pfam02841  224 REKQKEEEQMMEAQERSYQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEEllkegfktEAESLQKEIQDLK 297
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 70-134 1.53e-05

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 47.96  E-value: 1.53e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767920762   70 QRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQE-LEKQHREQKLQQLKNK 134
Cdd:cd16269   221 QRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLKEQEaLLEEGFKEQAELLQEE 286
fliH PRK06800
flagellar assembly protein H; Validated
 68-173 6.59e-05

flagellar assembly protein H; Validated


Pssm-ID: 180700  Cd Length: 228  Bit Score: 45.63  E-value: 6.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762   68 EFQRQHEQLsRQHEAQLHEH---IKQQQEMLAMKHQQeLLEHQRKLERHRQEQELEKQHREQKLQQLKnkekgkesavas 144
Cdd:PRK06800   35 EIQKDHEEL-LAQQKSLHKElnqLRQEQQKLERERQQ-LLADREQFQEHVQQQMKEIEAARQQFQKEQ------------ 100

                          90       100
                  ....*....|....*....|....*....
gi 767920762  145 TEVKMKLQEFVLNKKKALAHRNLNHCISS 173
Cdd:PRK06800  101 QETAYEWTELLWDQSFQLAEKIVNQAVDT 129
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 68-163 3.11e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 44.41  E-value: 3.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762   68 EFQRQHEQLSRQHEAQ-LHEHIKQQQEMLAMKHQQELLEHQRKLERHR-QEQELEKQHREQ-KLQQLKNKEKGKESAVAS 144
Cdd:PRK09510   63 QYNRQQQQQKSAKRAEeQRKKKEQQQAEELQQKQAAEQERLKQLEKERlAAQEQKKQAEEAaKQAALKQKQAEEAAAKAA 142

                          90
                  ....*....|....*....
gi 767920762  145 TEVKMKLQEfvlnKKKALA 163
Cdd:PRK09510  143 AAAKAKAEA----EAKRAA 157
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 70-167 5.35e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 43.37  E-value: 5.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762    70 QRQHEQLSRQHEAQLhEHIKQQQEMLAMKHQQE---LLEHQRKLERHRQEQ-----ELEKQHREQKLQQLKNKEKGKEsa 141
Cdd:pfam13868  231 ARQRQELQQAREEQI-ELKERRLAEEAEREEEEferMLRKQAEDEEIEQEEaekrrMKRLEHRRELEKQIEEREEQRA-- 307

                           90       100
                   ....*....|....*....|....*.
gi 767920762   142 vasTEVKMKLQEFVLNKKKALAHRNL 167
Cdd:pfam13868  308 ---AEREEELEEGERLREEEAERRER 330
FliJ COG2882
Flagellar biosynthesis chaperone FliJ [Cell motility];
82-129 6.99e-04

Flagellar biosynthesis chaperone FliJ [Cell motility];


Pssm-ID: 442129 [Multi-domain]  Cd Length: 142  Bit Score: 41.04  E-value: 6.99e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920762   82 AQLHEHIKQQQEMLAM------KHQQELLEHQRKL-------ERHRQEQELEKQHREQKLQ 129
Cdd:COG2882    74 ARLDEAIEQQQQQVAQaeqqveQARQAWLEARQERkaleklkERRREEERQEENRREQKEL 134
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
67-158 9.57e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.59  E-value: 9.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762   67 AEFQRQHEQLSRQHEaqlhEHIKQQQEMLAMKHQ-QELLEHQRKLERHRQEQELEKQhREQKLQQLKNKEKgkesavAST 145
Cdd:COG1340   216 KEIVEAQEKADELHE----EIIELQKELRELRKElKKLRKKQRALKREKEKEELEEK-AEEIFEKLKKGEK------LTT 284

                          90
                  ....*....|...
gi 767920762  146 EVKMKLQEFVLNK 158
Cdd:COG1340   285 EELKLLQKSGLLE 297
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 70-163 1.15e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 42.49  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762   70 QRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGK--ESAVASTEV 147
Cdd:PRK09510   86 QQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKraAAAAKKAAA 165

                          90
                  ....*....|....*.
gi 767920762  148 KMKLQEFVLNKKKALA 163
Cdd:PRK09510  166 EAKKKAEAEAAKKAAA 181
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
 68-164 2.41e-03

Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.


Pssm-ID: 405647 [Multi-domain]  Cd Length: 206  Bit Score: 40.52  E-value: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762    68 EFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQ-----ELLEHQRKLER--HRQEQELE-----KQHREQKLQQLKNKE 135
Cdd:pfam14988   15 EKQKKIEKLWNQYVQECEEIERRRQELASRYTQQtaelqTQLLQKEKEQAslKKELQALRpfaklKESQEREIQDLEEEK 94

                           90       100
                   ....*....|....*....|....*....
gi 767920762   136 KGKESAVASTEVKMKLQefVLNKKKALAH 164
Cdd:pfam14988   95 EKVRAETAEKDREAHLQ--FLKEKALLEK 121
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 70-130 3.49e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 3.49e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920762    70 QRQHEQLSRQHEAqlHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQ 130
Cdd:pfam13868   72 KRYRQELEEQIEE--REQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLRE 130
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 68-153 3.71e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.26  E-value: 3.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762    68 EFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQ-RKLERHRQEqELEKQHREQKLQQLKNKEKGKESAVASTE 146
Cdd:pfam17380  405 KILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERaREMERVRLE-EQERQQQVERLRQQEEERKRKKLELEKEK 483


                   ....*..
gi 767920762   147 VKMKLQE 153
Cdd:pfam17380  484 RDRKRAE 490
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 67-153 4.91e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 40.25  E-value: 4.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762   67 AEFQRQHEQLSRQHEAQLhehikqQQEMLAMKHQQEllEHQRKLERhRQEQELEKQHREQ-KLQQLKNKEKGKESAVAST 145
Cdd:cd16269   207 AEAAEQERKLLEEQQREL------EQKLEDQERSYE--EHLRQLKE-KMEEERENLLKEQeRALESKLKEQEALLEEGFK 277


                  ....*...
gi 767920762  146 EVKMKLQE 153
Cdd:cd16269   278 EQAELLQE 285
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
67-153 8.62e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 8.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762   67 AEFQRQHEQLSRQHEaQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQeqelEKQHREQKLQQLKNKEKGKESAVASTE 146
Cdd:COG4717   159 RELEEELEELEAELA-ELQEELEELLEQLSLATEEELQDLAEELEELQQ----RLAELEEELEEAQEELEELEEELEQLE 233


                  ....*..
gi 767920762  147 VKMKLQE 153
Cdd:COG4717   234 NELEAAA 240
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 68-153 9.14e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.11  E-value: 9.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762    68 EFQRQHEQL--SRQHEAQLHEHIKQQQEMLAMKHQQEL-----LEHQRKLERHRQEQ---ELEKQHREQKLQ---QLKNK 134
Cdd:pfam17380  313 ERRRKLEEAekARQAEMDRQAAIYAEQERMAMERERELerirqEERKRELERIRQEEiamEISRMRELERLQmerQQKNE 392

                           90
                   ....*....|....*....
gi 767920762   135 EKGKESAVAStevKMKLQE 153
Cdd:pfam17380  393 RVRQELEAAR---KVKILE 408
MAT1 pfam06391
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ...
 67-167 9.84e-03

CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.


Pssm-ID: 461894 [Multi-domain]  Cd Length: 202  Bit Score: 38.76  E-value: 9.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920762    67 AEFQRQHEQL---SRQHEAQLHEHIKQQQEMLAMKHQQellehQRKLERHRQEQELEKQHREQK--LQQLKNKEKGKESA 141
Cdd:pfam06391   71 EQYEKENKDLilkNKMKLSQEEEELEELLELEKREKEE-----RRKEEKQEEEEEKEKKEKAKQelIDELMTSNKDAEEI 145

                           90       100
                   ....*....|....*....|....*.
gi 767920762   142 VASTEVKMKLQEFVLNKKKALAHRNL 167
Cdd:pfam06391  146 IAQHKKTAKKRKSERRRKLEELNRVL 171
PRK12704 PRK12704
phosphodiesterase; Provisional
 68-136 9.87e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 9.87e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767920762   68 EFQRQHEQLsRQHEAQLhehiKQQQEMLAmKHQQELLEHQRKLErhRQEQELEKqhREQKLQQLKNKEK 136
Cdd:PRK12704   83 ELQKLEKRL-LQKEENL----DRKLELLE-KREEELEKKEKELE--QKQQELEK--KEEELEELIEEQL 141
 
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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