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Conserved domains on  [gi|164662747|ref|XP_001732495|]
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hypothetical protein MGL_0270 [Malassezia globosa CBS 7966]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Arginase_HDAC super family cl17011
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 1-282 1.91e-162

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.


The actual alignment was detected with superfamily member cd11600:

Pssm-ID: 450134 [Multi-domain]  Cd Length: 313  Bit Score: 467.21  E-value: 1.91e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747   1 MHQIYSREATRAEIELIHDSALWDQYEANMTLPLAQLKTLSHDLElSSSLYLNHASTFCARLSCGSVVEMCSAVASGRVH 80
Cdd:cd11600   26 MLRIPIREATKEEILLVHSEEHWDRVEATEKMSDEQLKDRTEIFE-RDSLYVNNDTAFCARLSCGGAIEACRAVAEGRVK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  81 NGFAIVRPPGHHAEPGAGFGFCLYNNVAVSTRVLLDRplgAPDRVERVMILDWDVHHGNGTQRAFWDNKQVLYISLHRYE 160
Cdd:cd11600  105 NAFAVVRPPGHHAEPDESMGFCFFNNVAVAAKWLQTE---YPDKIKKILILDWDIHHGNGTQRAFYDDPNVLYISLHRFE 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 161 NGTFYPGTSFGNYDQVGGESARGTSVNVPWPCSGMDDGDYLHAFQHCIMPIAYEFAPDLVIVSAGFDAAQDDMLGGCLVS 240
Cdd:cd11600  182 NGGFYPGTPYGDYESVGEGAGLGFNVNIPWPQGGMGDADYIYAFQRIVMPIAYEFDPDLVIISAGFDAADGDELGQCHVT 261

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 164662747 241 PAGYAHMTHQLMALAQGNLVVALEGGYTLDAISRSALAVVRT 282
Cdd:cd11600  262 PAGYAHMTHMLMSLAGGKLVVALEGGYNLDAISDSALAVAKV 303
Arb2 super family cl10738
Arb2 domain; This domain is found at the C-terminal of Clr3 (Cryptic loci regulator 3) also ...
 390-603 1.95e-26

Arb2 domain; This domain is found at the C-terminal of Clr3 (Cryptic loci regulator 3) also known as histone deacetylase clr3 (EC:3.5.1.98). Structure analysis reveals that the Arb2 domain has clear homology to alpha/beta-hydrolases but that it is lacking the catalytic triad of these enzymes. Functional studies show that the Arb2 domain is necessary for centromeric heterochromatin silencing suggesting a model where the Arb2 domain, through residues N562 and Y563, acts as an anchor that connects the HDAC activity of Clr3 to the SHREC complex. SHREC (Snf2/Hdac Repressive) complex in fission yeast drives transcriptional gene silencing in heterochromatin.


The actual alignment was detected with superfamily member pfam09757:

Pssm-ID: 401634  Cd Length: 252  Bit Score: 108.43  E-value: 1.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  390 AARLWKRHQLLPIP-THAGLQR---NQALCSSSLMlpTTQTLVIFVHDLAnlhkDVQGAP------------YVADSADA 453
Cdd:pfam09757  10 AKQLFEKYGMVPLPiQRDKLSKsfeNQVLATPNIY--KARTLLVIVHDPP----ELWAQPdpitnkldphnsWLVDSVLD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  454 LVQWAMERNYALMDlctmVPLPLQTVRNHSHgkalAYPDDP--TPSALNEQIQHIWDVYcaISPVP---KVFLVGLGTGC 528
Cdd:pfam09757  84 YIDWAVKQGYGVID----VNIPQHITETPES----LEEDDEynRISESQELLLYLWDNY--IELFDsatKIFFIGVGDAY 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164662747  529 EVLMHLITTRAIQSRVHGMVQVMGMNSI-PLVPKAQRELKSWYLKHARVICPPTHPYFAWNEQASSGKRLGTVQRA 603
Cdd:pfam09757 154 SGIVHLLGHRDCRSRVKGVINFVGGNPLrPVKSLTDESLSDWYFKNSLVFVSSDHSCWGDEENKKPRKRYGRVLRS 229
 
Name Accession Description Interval E-value
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 1-282 1.91e-162

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: 467.21  E-value: 1.91e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747   1 MHQIYSREATRAEIELIHDSALWDQYEANMTLPLAQLKTLSHDLElSSSLYLNHASTFCARLSCGSVVEMCSAVASGRVH 80
Cdd:cd11600   26 MLRIPIREATKEEILLVHSEEHWDRVEATEKMSDEQLKDRTEIFE-RDSLYVNNDTAFCARLSCGGAIEACRAVAEGRVK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  81 NGFAIVRPPGHHAEPGAGFGFCLYNNVAVSTRVLLDRplgAPDRVERVMILDWDVHHGNGTQRAFWDNKQVLYISLHRYE 160
Cdd:cd11600  105 NAFAVVRPPGHHAEPDESMGFCFFNNVAVAAKWLQTE---YPDKIKKILILDWDIHHGNGTQRAFYDDPNVLYISLHRFE 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 161 NGTFYPGTSFGNYDQVGGESARGTSVNVPWPCSGMDDGDYLHAFQHCIMPIAYEFAPDLVIVSAGFDAAQDDMLGGCLVS 240
Cdd:cd11600  182 NGGFYPGTPYGDYESVGEGAGLGFNVNIPWPQGGMGDADYIYAFQRIVMPIAYEFDPDLVIISAGFDAADGDELGQCHVT 261

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 164662747 241 PAGYAHMTHQLMALAQGNLVVALEGGYTLDAISRSALAVVRT 282
Cdd:cd11600  262 PAGYAHMTHMLMSLAGGKLVVALEGGYNLDAISDSALAVAKV 303
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 2-282 4.88e-103

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: 314.56  E-value: 4.88e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747    2 HQIYSREATRAEIELIHDSALWDQYEANmtlplaqlkTLSHDLELSSSLYLNHASTF-------CARLSCGSVVEMCSAV 74
Cdd:pfam00850  25 EIIAPRPATEEELLLVHSPEYLEFLEEA---------APEGGALLLLSYLSGDDDTPvspgsyeAALLAAGGTLAAADAV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747   75 ASGRVHNGFAIVRPPGHHAEPGAGFGFCLYNNVAVSTRVLLDRplgapDRVERVMILDWDVHHGNGTQRAFWDNKQVLYI 154
Cdd:pfam00850  96 LSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREK-----YGLKRVAIVDFDVHHGNGTQEIFYDDPSVLTL 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  155 SLHRYEnGTFYPGTsfGNYDQVGGESARGTSVNVPWPcSGMDDGDYLHAFQHCIMPIAYEFAPDLVIVSAGFDAAQDDML 234
Cdd:pfam00850 171 SIHQYP-GGFYPGT--GFADETGEGKGKGYTLNVPLP-PGTGDAEYLAAFEEILLPALEEFQPDLILVSAGFDAHAGDPL 246

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 164662747  235 GGCLVSPAGYAHMTHQLMALAQ---GNLVVALEGGYTLDAISRSALAVVRT 282
Cdd:pfam00850 247 GGLNLTTEGFAEITRILLELADplcIRVVSVLEGGYNLDALARSATAVLAA 297
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 7-282 3.73e-89

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 278.91  E-value: 3.73e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747   7 REATRAEIELIHDSAlwdqYeanmtlpLAQLKTLSHD---LELSSSLYLNHASTFCARLSCGSVVEMCSAVASGRVHNGF 83
Cdd:COG0123   47 PPATEEDLLRVHTPD----Y-------VDALRAASLDggyGQLDPDTPVSPGTWEAALLAAGGALAAADAVLEGEARNAF 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  84 AIVRPPGHHAEPGAGFGFCLYNNVAVSTRVLLDRplgapdRVERVMILDWDVHHGNGTQRAFWDNKQVLYISLHRYengT 163
Cdd:COG0123  116 ALVRPPGHHAERDRAMGFCLFNNAAIAARYLLAK------GLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD---P 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 164 FYPGTsfGNYDQVGGESARGTSVNVPWPcSGMDDGDYLHAFQHCIMPIAYEFAPDLVIVSAGFDAAQDDMLGGCLVSPAG 243
Cdd:COG0123  187 LYPGT--GAADETGEGAGEGSNLNVPLP-PGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEG 263

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 164662747 244 YAHMTHQLMALA---QGNLVVALEGGYTLDAISRSALAVVRT 282
Cdd:COG0123  264 YAWRTRRVLELAdhcGGPVVSVLEGGYNLDALARSVAAHLET 305
Arb2 pfam09757
Arb2 domain; This domain is found at the C-terminal of Clr3 (Cryptic loci regulator 3) also ...
 390-603 1.95e-26

Arb2 domain; This domain is found at the C-terminal of Clr3 (Cryptic loci regulator 3) also known as histone deacetylase clr3 (EC:3.5.1.98). Structure analysis reveals that the Arb2 domain has clear homology to alpha/beta-hydrolases but that it is lacking the catalytic triad of these enzymes. Functional studies show that the Arb2 domain is necessary for centromeric heterochromatin silencing suggesting a model where the Arb2 domain, through residues N562 and Y563, acts as an anchor that connects the HDAC activity of Clr3 to the SHREC complex. SHREC (Snf2/Hdac Repressive) complex in fission yeast drives transcriptional gene silencing in heterochromatin.


Pssm-ID: 401634  Cd Length: 252  Bit Score: 108.43  E-value: 1.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  390 AARLWKRHQLLPIP-THAGLQR---NQALCSSSLMlpTTQTLVIFVHDLAnlhkDVQGAP------------YVADSADA 453
Cdd:pfam09757  10 AKQLFEKYGMVPLPiQRDKLSKsfeNQVLATPNIY--KARTLLVIVHDPP----ELWAQPdpitnkldphnsWLVDSVLD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  454 LVQWAMERNYALMDlctmVPLPLQTVRNHSHgkalAYPDDP--TPSALNEQIQHIWDVYcaISPVP---KVFLVGLGTGC 528
Cdd:pfam09757  84 YIDWAVKQGYGVID----VNIPQHITETPES----LEEDDEynRISESQELLLYLWDNY--IELFDsatKIFFIGVGDAY 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164662747  529 EVLMHLITTRAIQSRVHGMVQVMGMNSI-PLVPKAQRELKSWYLKHARVICPPTHPYFAWNEQASSGKRLGTVQRA 603
Cdd:pfam09757 154 SGIVHLLGHRDCRSRVKGVINFVGGNPLrPVKSLTDESLSDWYFKNSLVFVSSDHSCWGDEENKKPRKRYGRVLRS 229
PTZ00063 PTZ00063
histone deacetylase; Provisional
 91-274 6.32e-20

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 92.95  E-value: 6.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  91 HHAEPGAGFGFCLYNNVAVSTRVLLDRPlgapdrvERVMILDWDVHHGNGTQRAFWDNKQVLYISLHRYenGTFYPGTsf 170
Cdd:PTZ00063 137 HHAKRSEASGFCYINDIVLGILELLKYH-------ARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFPGT-- 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 171 GNYDQVGGESARGTSVNVPWPcSGMDDGDYLHAFQHCIMPIAYEFAPDLVIVSAGFDAAQDDMLGGCLVSPAGYAHMTHQ 250
Cdd:PTZ00063 206 GDVTDIGVAQGKYYSVNVPLN-DGIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAACVEF 284

                        170       180
                 ....*....|....*....|....
gi 164662747 251 LMALAQGNLVVAlEGGYTLDAISR 274
Cdd:PTZ00063 285 VRSLNIPLLVLG-GGGYTIRNVAR 307
 
Name Accession Description Interval E-value
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 1-282 1.91e-162

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: 467.21  E-value: 1.91e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747   1 MHQIYSREATRAEIELIHDSALWDQYEANMTLPLAQLKTLSHDLElSSSLYLNHASTFCARLSCGSVVEMCSAVASGRVH 80
Cdd:cd11600   26 MLRIPIREATKEEILLVHSEEHWDRVEATEKMSDEQLKDRTEIFE-RDSLYVNNDTAFCARLSCGGAIEACRAVAEGRVK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  81 NGFAIVRPPGHHAEPGAGFGFCLYNNVAVSTRVLLDRplgAPDRVERVMILDWDVHHGNGTQRAFWDNKQVLYISLHRYE 160
Cdd:cd11600  105 NAFAVVRPPGHHAEPDESMGFCFFNNVAVAAKWLQTE---YPDKIKKILILDWDIHHGNGTQRAFYDDPNVLYISLHRFE 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 161 NGTFYPGTSFGNYDQVGGESARGTSVNVPWPCSGMDDGDYLHAFQHCIMPIAYEFAPDLVIVSAGFDAAQDDMLGGCLVS 240
Cdd:cd11600  182 NGGFYPGTPYGDYESVGEGAGLGFNVNIPWPQGGMGDADYIYAFQRIVMPIAYEFDPDLVIISAGFDAADGDELGQCHVT 261

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 164662747 241 PAGYAHMTHQLMALAQGNLVVALEGGYTLDAISRSALAVVRT 282
Cdd:cd11600  262 PAGYAHMTHMLMSLAGGKLVVALEGGYNLDAISDSALAVAKV 303
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
 1-320 4.63e-125

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: 373.21  E-value: 4.63e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747   1 MHQIYSREATRAEIELIHDSALWDQYEANMTLPLAQLKTLSHDLElssSLYLNHASTFCARLSCGSVVEMCSAVASGRVH 80
Cdd:cd10003   39 CLRLPSRLATEDELLLCHSEEHLDEMKSLEKMKPRELNRLGKEYD---SIYIHPDSYQCALLAAGCVLQVVEAVLTGESR 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  81 NGFAIVRPPGHHAEPGAGFGFCLYNNVAVSTRVLLDRpLGapdrVERVMILDWDVHHGNGTQRAFWDNKQVLYISLHRYE 160
Cdd:cd10003  116 NGVAIVRPPGHHAEQDTACGFCFFNNVAIAARYAQKK-YG----LKRILIVDWDVHHGNGTQHMFESDPSVLYISLHRYD 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 161 NGTFYPGTSFGNYDQVGGESARGTSVNVPWPCSGMDDGDYLHAFQHCIMPIAYEFAPDLVIVSAGFDAAQDDMLGGCLVS 240
Cdd:cd10003  191 NGSFFPNSPEGNYDVVGKGKGEGFNVNIPWNKGGMGDAEYIAAFQQVVLPIAYEFNPELVLVSAGFDAARGDPLGGCKVT 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 241 PAGYAHMTHQLMALAQGNLVVALEGGYTLDAISRSALAVVRTLLGDPLPPLPRGTACSLAAADTVRRVIRAQAPYWVSLR 320
Cdd:cd10003  271 PEGYAHMTHMLMSLAGGRVIVILEGGYNLTSISESMSMCTKTLLGDPPPVLDLPRPPCSSALKSINNVLQVHQKYWKSLR 350
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
 7-282 1.27e-114

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: 344.10  E-value: 1.27e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747   7 REATRAEIELIHDSALWDQYEANMtlplaqlktLSHDLELSSSLYLNHASTFCARLSCGSVVEMCSAVASGRVHNGFAIV 86
Cdd:cd09992   30 RPATEEELLRVHTPEYIERVEETC---------EAGGGYLDPDTYVSPGSYEAALLAAGAALAAVDAVLSGEAENAFALV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  87 RPPGHHAEPGAGFGFCLYNNVAVSTRVLLDRPLgapdrVERVMILDWDVHHGNGTQRAFWDNKQVLYISLHRYEngtFYP 166
Cdd:cd09992  101 RPPGHHAEPDRAMGFCLFNNVAIAARYAQKRYG-----LKRVLIVDWDVHHGNGTQDIFYDDPSVLYFSIHQYP---FYP 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 167 GTsfGNYDQVGGESARGTSVNVPWPCsGMDDGDYLHAFQHCIMPIAYEFAPDLVIVSAGFDAAQDDMLGGCLVSPAGYAH 246
Cdd:cd09992  173 GT--GAAEETGGGAGEGFTINVPLPP-GSGDAEYLAAFEEVLLPIAREFQPDLVLVSAGFDAHRGDPLGGMNLTPEGYAR 249

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 164662747 247 MTHQLMALA----QGNLVVALEGGYTLDAISRSALAVVRT 282
Cdd:cd09992  250 LTRLLKELAdehcGGRLVFVLEGGYNLEALAESVLAVLEA 289
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 2-282 4.88e-103

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: 314.56  E-value: 4.88e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747    2 HQIYSREATRAEIELIHDSALWDQYEANmtlplaqlkTLSHDLELSSSLYLNHASTF-------CARLSCGSVVEMCSAV 74
Cdd:pfam00850  25 EIIAPRPATEEELLLVHSPEYLEFLEEA---------APEGGALLLLSYLSGDDDTPvspgsyeAALLAAGGTLAAADAV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747   75 ASGRVHNGFAIVRPPGHHAEPGAGFGFCLYNNVAVSTRVLLDRplgapDRVERVMILDWDVHHGNGTQRAFWDNKQVLYI 154
Cdd:pfam00850  96 LSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREK-----YGLKRVAIVDFDVHHGNGTQEIFYDDPSVLTL 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  155 SLHRYEnGTFYPGTsfGNYDQVGGESARGTSVNVPWPcSGMDDGDYLHAFQHCIMPIAYEFAPDLVIVSAGFDAAQDDML 234
Cdd:pfam00850 171 SIHQYP-GGFYPGT--GFADETGEGKGKGYTLNVPLP-PGTGDAEYLAAFEEILLPALEEFQPDLILVSAGFDAHAGDPL 246

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 164662747  235 GGCLVSPAGYAHMTHQLMALAQ---GNLVVALEGGYTLDAISRSALAVVRT 282
Cdd:pfam00850 247 GGLNLTTEGFAEITRILLELADplcIRVVSVLEGGYNLDALARSATAVLAA 297
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 4-316 1.18e-99

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: 307.31  E-value: 1.18e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747   4 IYSREATRAEIELIHDSALWDQYEANMTLPLAQLKTLSHDLElssSLYLNHASTFCARLSCGSVVEMCSAVASGRVHNGF 83
Cdd:cd10002   33 IPAREAEEDEILLVHSQEYIDLVKSTETMEKEELESLCSGYD---SVYLCPSTYEAARLAAGSTIELVKAVMAGKIQNGF 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  84 AIVRPPGHHAEPGAGFGFCLYNNVAVSTRVLLDRPlgapdRVERVMILDWDVHHGNGTQRAFWDNKQVLYISLHRYENGT 163
Cdd:cd10002  110 ALIRPPGHHAMRNEANGYCIFNNVAIAAKYAIEKL-----GLKRILIVDWDVHHGQGTQQGFYEDPRVLYFSIHRYEHGR 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 164 FYPGTSFGNYDQVGGESARGTSVNVPWPCSGMDDGDYLHAFQHCIMPIAYEFAPDLVIVSAGFDAAQDDMLGGCLVSPAG 243
Cdd:cd10002  185 FWPHLFESDYDYIGVGHGYGFNVNVPLNQTGLGDADYLAIFHHILLPLALEFQPELVLVSAGFDASIGDPEGEMAVTPAG 264

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164662747 244 YAHMTHQLMALAQGNLVVALEGGYTLDAISRSALAVVRTLLGDPLPPLPRGTACSlAAADTVRRVIRAQAPYW 316
Cdd:cd10002  265 YAHLTRLLMGLAGGKLLLVLEGGYLLESLAESVSMTLRGLLGDPLPPLAPPIPIR-SVLETILNAIAHLSPRW 336
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 2-316 6.56e-99

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: 306.96  E-value: 6.56e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747   2 HQIYSREATRAEIELIHDSALWDQYEANmtlPLAQLKTLSHDLELSSSL----------------YLNHAST-FCARLSC 64
Cdd:cd11681   48 ERLRGRKATLEELQLVHSEVHTLLYGTN---PLSRLKLDPTKLAGLPQKsfvrlpcggigvdsdtVWNELHTsNAARMAV 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  65 GSVVEMCSAVASGRVHNGFAIVRPPGHHAEPGAGFGFCLYNNVAVSTRVLLDRplgapDRVERVMILDWDVHHGNGTQRA 144
Cdd:cd11681  125 GCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQAMGFCFFNSVAIAAKQLQQK-----LKLRKILIVDWDVHHGNGTQQI 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 145 FWDNKQVLYISLHRYENGTFYPGTsfGNYDQVGGESARGTSVNVPWPcSG----MDDGDYLHAFQHCIMPIAYEFAPDLV 220
Cdd:cd11681  200 FYEDPNVLYISLHRYDDGNFFPGT--GAPTEVGSGAGEGFNVNIAWS-GGldppMGDAEYLAAFRTVVMPIAREFSPDIV 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 221 IVSAGFDAA--QDDMLGGCLVSPAGYAHMTHQLMALAQGNLVVALEGGYTLDAISRSALAVVRT---LLGDPLPPLPRGT 295
Cdd:cd11681  277 LVSAGFDAAegHPPPLGGYKVSPACFGYMTRQLMNLAGGKVVLALEGGYDLTAICDASEACVRAllgDELDPLSEEELER 356

                        330       340
                 ....*....|....*....|.
gi 164662747 296 ACSLAAADTVRRVIRAQAPYW 316
Cdd:cd11681  357 RPNPNAVTSLEKVIAIQSPYW 377
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 7-282 3.73e-89

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 278.91  E-value: 3.73e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747   7 REATRAEIELIHDSAlwdqYeanmtlpLAQLKTLSHD---LELSSSLYLNHASTFCARLSCGSVVEMCSAVASGRVHNGF 83
Cdd:COG0123   47 PPATEEDLLRVHTPD----Y-------VDALRAASLDggyGQLDPDTPVSPGTWEAALLAAGGALAAADAVLEGEARNAF 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  84 AIVRPPGHHAEPGAGFGFCLYNNVAVSTRVLLDRplgapdRVERVMILDWDVHHGNGTQRAFWDNKQVLYISLHRYengT 163
Cdd:COG0123  116 ALVRPPGHHAERDRAMGFCLFNNAAIAARYLLAK------GLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD---P 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 164 FYPGTsfGNYDQVGGESARGTSVNVPWPcSGMDDGDYLHAFQHCIMPIAYEFAPDLVIVSAGFDAAQDDMLGGCLVSPAG 243
Cdd:COG0123  187 LYPGT--GAADETGEGAGEGSNLNVPLP-PGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEG 263

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 164662747 244 YAHMTHQLMALA---QGNLVVALEGGYTLDAISRSALAVVRT 282
Cdd:COG0123  264 YAWRTRRVLELAdhcGGPVVSVLEGGYNLDALARSVAAHLET 305
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
 3-316 4.76e-85

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: 269.41  E-value: 4.76e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747   3 QIYSREATRAEIELIHDSALWDQYEANMTLPLAQLKTLShdlELSSSLYLNHASTFCARLSCGSVVEMCSAVASGRVHNG 82
Cdd:cd11682   32 SVQAREASEEELLLVHSPEYVALMKSTQYMTEEELRTLA---DTYDSVYLHPNSYSCACLAVGSVLQLVDKVLGGEIRNG 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  83 FAIVRPPGHHAEPGAGFGFCLYNNVAVSTRVLLDRplgapDRVERVMILDWDVHHGNGTQRAFWDNKQVLYISLHRYENG 162
Cdd:cd11682  109 LAIVRPPGHHAQHDKMDGYCMFNNVAIAARYAQQK-----HGVQRVLIVDWDVHHGQGTQFIFEQDPSVLYFSIHRYEQG 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 163 TFYPGTSFGNYDQVGGESARGTSVNVPWPCSGMDDGDYLHAFQHCIMPIAYEFAPDLVIVSAGFDAAQDDMLGGCLVSPA 242
Cdd:cd11682  184 RFWPHLKESDSSAVGFGRGEGYNINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDAVIGDPKGEMAATPA 263

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164662747 243 GYAHMTHQLMALAQGNLVVALEGGYTLDAISRSALAVVRTLLGDPLPPLPRGTACSLAAADTVRRVIRAQAPYW 316
Cdd:cd11682  264 CFAHLTHLLMGLAGGKLILSLEGGYNLRSLAEGVCASLKALLGDPCPMLESPGAPCRSALASVSCTISALEPFW 337
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
 4-316 6.74e-78

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: 252.24  E-value: 6.74e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747   4 IYSREATRAEIELIHDSALWDQYEANmtlPLAQLKTLSHDLE--LSSSLYLN-----------------HASTfCARLSC 64
Cdd:cd10008   50 LRGRKASLEELQSVHSERHVLLYGTN---PLSRLKLDNGKLAglLAQRMFVMlpcggvgvdtdtiwnelHSSN-AARWAA 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  65 GSVVEMCSAVASGRVHNGFAIVRPPGHHAEPGAGFGFCLYNNVAVSTRVLLDRplgapDRVERVMILDWDVHHGNGTQRA 144
Cdd:cd10008  126 GSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGFCFFNSVAIACRQLQQQ-----GKASKILIVDWDVHHGNGTQQT 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 145 FWDNKQVLYISLHRYENGTFYPGTsfGNYDQVGGESARGTSVNVPWpCSGMD----DGDYLHAFQHCIMPIAYEFAPDLV 220
Cdd:cd10008  201 FYQDPSVLYISLHRHDDGNFFPGS--GAVDEVGAGSGEGFNVNVAW-AGGLDppmgDPEYLAAFRIVVMPIAREFSPDLV 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 221 IVSAGFDAAQDD--MLGGCLVSPAGYAHMTHQLMALAQGNLVVALEGGYTLDAISRSALAVVRTLLGDPLPPLPRGTACS 298
Cdd:cd10008  278 LVSAGFDAAEGHpaPLGGYHVSAKCFGYMTQQLMNLAGGAVVLALEGGHDLTAICDASEACVAALLGNEVDPLSEESWKQ 357

                        330       340
                 ....*....|....*....|.
gi 164662747 299 LAAADTVRR---VIRAQAPYW 316
Cdd:cd10008  358 KPNLNAIRSleaVIRVHSKYW 378
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 3-316 8.38e-78

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: 250.55  E-value: 8.38e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747   3 QIYSREATRAEIELIHDSALWDQYEANMTLPLAQLKTLSHDLElssSLYLNHASTFCARLSCGSVVEMCSAVASGRVHNG 82
Cdd:cd11683   32 RLPAREASEEEILLVHSPEYLSLVRETQVMNKEELMAISGKYD---AVYFHPNTFHCARLAAGATLQLVDAVLTGEVQNG 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  83 FAIVRPPGHHAEPGAGFGFCLYNNVAVSTRVLLDRplgapDRVERVMILDWDVHHGNGTQRAFWDNKQVLYISLHRYENG 162
Cdd:cd11683  109 MALVRPPGHHSQRNAANGFCVFNNVAIAAEYAKKK-----YGLHRILIVDWDVHHGQGIQYIFEEDPSVLYFSWHRYEHQ 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 163 TFYPGTSFGNYDQVGGESARGTSVNVPWPCSGMDDGDYLHAFQHCIMPIAYEFAPDLVIVSAGFDAAQDDMLGGCLVSPA 242
Cdd:cd11683  184 RFWPFLRESDYDAVGRGKGLGFNINLPWNKVGMGNADYLAAFFHVLLPLAFEFDPELVLVSAGFDSAIGDPEGQMCATPE 263

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164662747 243 GYAHMTHQLMALAQGNLVVALEGGYTLDAISRSALAVVRTLLGDPLPPLPRGTACSLAAADTVRRVIRAQAPYW 316
Cdd:cd11683  264 CFAHLTHLLMVLAGGKLCAVLEGGYHLESLAESVCMTVQTLLGDPLPRLSGEMTPCQSALESIQNVRAAQAPYW 337
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
 4-330 4.11e-77

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: 251.11  E-value: 4.11e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747   4 IYSREATRAEIELIHDSALWDQYEANmtlPLAQLKTLSHDLELS-SSLYLN-----------------HASTfCARLSCG 65
Cdd:cd10006   53 IRGRKATLEELQTVHSEAHTLLYGTN---PLNRQKLDSKKLLGSlASVFVRlpcggvgvdsdtiwnevHSSG-AARLAVG 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  66 SVVEMCSAVASGRVHNGFAIVRPPGHHAEPGAGFGFCLYNNVAVSTRVLLDRPlgapdRVERVMILDWDVHHGNGTQRAF 145
Cdd:cd10006  129 CVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAIAAKLLQQRL-----NVSKILIVDWDVHHGNGTQQAF 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 146 WDNKQVLYISLHRYENGTFYPGTsfGNYDQVGGESARGTSVNVPWpCSGMD----DGDYLHAFQHCIMPIAYEFAPDLVI 221
Cdd:cd10006  204 YSDPNVLYMSLHRYDDGNFFPGS--GAPDEVGTGPGVGFNVNMAF-TGGLDppmgDAEYLAAFRTVVMPIASEFAPDVVL 280

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 222 VSAGFDAAQDD--MLGGCLVSPAGYAHMTHQLMALAQGNLVVALEGGYTLDAISRSALAVVRTLLGDPLPPLPRGTACSL 299
Cdd:cd10006  281 VSSGFDAVEGHptPLGGYNLSAKCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQR 360

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 164662747 300 AAADTVR---RVIRAQAPYWVSL-RTALEYGPSAV 330
Cdd:cd10006  361 PNANAVRsmeKVMEIHSKYWRCLqRTTSTAGYSLI 395
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
 3-320 4.93e-76

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: 248.75  E-value: 4.93e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747   3 QIYSREATRAEIELIHDsalwdQYEANM--TLPLAQLKTLSHDL--ELSSSLYL-----------------NHASTfCAR 61
Cdd:cd10007   51 RVRGRKATLDEIQTVHS-----EHHTLLygTSPLNRQKLDSKKLlgPLSQKMYAvlpcggigvdsdtvwneMHSSS-AVR 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  62 LSCGSVVEMCSAVASGRVHNGFAIVRPPGHHAEPGAGFGFCLYNNVAVSTRvLLDRPLGapdrVERVMILDWDVHHGNGT 141
Cdd:cd10007  125 MAVGCLIELAFKVAAGELKNGFAVIRPPGHHAEESTAMGFCFFNSVAIAAK-LLQQKLN----VGKILIVDWDIHHGNGT 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 142 QRAFWDNKQVLYISLHRYENGTFYPGTsfGNYDQVGGESARGTSVNVPWpCSGMD----DGDYLHAFQHCIMPIAYEFAP 217
Cdd:cd10007  200 QQAFYNDPNVLYISLHRYDDGNFFPGS--GAPDEVGAGPGVGFNVNIAW-TGGVDppigDVEYLTAFRTVVMPIANEFSP 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 218 DLVIVSAGFDAAQDDM--LGGCLVSPAGYAHMTHQLMALAQGNLVVALEGGYTLDAISRSALAVVRTLLGDPL----PPL 291
Cdd:cd10007  277 DVVLVSAGFDAVEGHQspLGGYSVTAKCFGHLTKQLMTLAGGRVVLALEGGHDLTAICDASEACVSALLGMELtpldNTV 356

                        330       340
                 ....*....|....*....|....*....
gi 164662747 292 PRGTACSLAAAdTVRRVIRAQAPYWVSLR 320
Cdd:cd10007  357 LQQKPNDNAVA-TLERVIEIQSKHWSCLK 384
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
 2-282 7.33e-74

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: 238.57  E-value: 7.33e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747   2 HQIYSREATRAEIELIHDSALWDQYEANmtLPLAQLKTLSHDLelssslYLNHASTFCARLSCGSVVEMCSAVASGRVHN 81
Cdd:cd11599   25 RQLEAPPATREQLLRVHDAAYVDRLEAA--APEEGLVQLDPDT------AMSPGSLEAALRAAGAVVAAVDAVMAGEARN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  82 GFAIVRPPGHHAEPGAGFGFCLYNNVAVSTRVLLDRPlgapdRVERVMILDWDVHHGNGTQRAFWDNKQVLYISLHRYEn 161
Cdd:cd11599   97 AFCAVRPPGHHAERDKAMGFCLFNNVAIAAAHALAHH-----GLERVAIVDFDVHHGNGTEDIFRDDPRVLFCSSHQHP- 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 162 gtFYPGTsfGNYDQVGgesaRGTSVNVPWPcSGMDDGDYLHAFQHCIMPIAYEFAPDLVIVSAGFDAAQDDMLGGCLVSP 241
Cdd:cd11599  171 --LYPGT--GAPDETG----HGNIVNVPLP-AGTGGAEFREAVEDRWLPALDAFKPDLILISAGFDAHRDDPLAQLNLTE 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 164662747 242 AGYAHMTHQLMALA----QGNLVVALEGGYTLDAISRSALAVVRT 282
Cdd:cd11599  242 EDYAWITEQLMDVAdrycDGRIVSVLEGGYDLSALARSVAAHVRA 286
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
 1-267 1.28e-72

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: 237.84  E-value: 1.28e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747   1 MHQIYSREATRAEIELIHDSALWDQyeanmtlplaqLKTLSHD--LELSSSLYLNHASTFCARLSCGSVVEMCSAVASGR 78
Cdd:cd09996   56 LVLITPRPATDEELLRVHTPEYIDR-----------VKAASAAggGEAGGGTPFGPGSYEIALLAAGGAIAAVDAVLDGE 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  79 VHNGFAIVRPPGHHAEPGAGFGFCLYNNVAVSTRVLLDRplgapDRVERVMILDWDVHHGNGTQRAFWDNKQVLYISLHr 158
Cdd:cd09996  125 VDNAYALVRPPGHHAEPDQGMGFCLFNNVAIAARHALAV-----GGVKRVAVVDWDVHHGNGTQAIFYDDPDVLTISLH- 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 159 yENGTFYPGTSFgnYDQVGGESARGTSVNVPWPcSGMDDGDYLHAFQHCIMPIAYEFAPDLVIVSAGFDAAQDDMLGGCL 238
Cdd:cd09996  199 -QDRCFPPDSGA--VEERGEGAGEGYNLNIPLP-PGSGDGAYLHAFERIVLPALRAFRPELIIVASGFDASAFDPLGRMM 274

                        250       260       270
                 ....*....|....*....|....*....|...
gi 164662747 239 VSPAGYAHMTHQLMALA----QGNLVVALEGGY 267
Cdd:cd09996  275 LTSDGFRALTRKLRDLAdelcGGRLVMVHEGGY 307
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
 56-280 1.36e-63

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: 214.50  E-value: 1.36e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  56 STFCARLSCGSVVEMCSAVASGRVHNGFAIVRPPGHHAEPGAGFGFCLYNNVAVSTRVLLDRPlgapdRVERVMILDWDV 135
Cdd:cd10009  117 SSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQL-----NISKILIVDLDV 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 136 HHGNGTQRAFWDNKQVLYISLHRYENGTFYPGTsfGNYDQVGGESARGTSVNVPWpCSGMD----DGDYLHAFQHCIMPI 211
Cdd:cd10009  192 HHGNGTQQAFYADPSILYISLHRYDEGNFFPGS--GAPNEVGTGLGEGYNINIAW-TGGLDppmgDVEYLEAFRTIVKPV 268

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164662747 212 AYEFAPDLVIVSAGFDAAQ--DDMLGGCLVSPAGYAHMTHQLMALAQGNLVVALEGGYTLDAISRSALAVV 280
Cdd:cd10009  269 AKEFDPDMVLVSAGFDALEghTPPLGGYKVTAKCFGHLTKQLMTLADGRVVLALEGGHDLTAICDASEACV 339
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
 51-281 4.32e-63

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: 210.47  E-value: 4.32e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  51 YLNHASTFC---------ARLSCGSVVEMCSAVASGRVHNgFAIVRPPGHHAEPGAGFGFCLYNNVAVSTRVLLDRplga 121
Cdd:cd10001   69 FLETADTDTpisegtweaALAAADTALTAADLVLEGERAA-YALCRPPGHHAGRDRAGGFCYFNNAAIAAQYLRDR---- 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 122 pdrVERVMILDWDVHHGNGTQRAFWDNKQVLYISLHRYENgTFYPGTSfGNYDQVGGESARGTSVNVPWPcSGMDDGDYL 201
Cdd:cd10001  144 ---AGRVAILDVDVHHGNGTQEIFYERPDVLYVSIHGDPR-TFYPFFL-GFADETGEGEGEGYNLNLPLP-PGTGDDDYL 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 202 HAFQHCIMPIAyEFAPDLVIVSAGFDAAQDDMLGGCLVSPAGYAHMTHQLMALAQGNLVVaLEGGYTLDAISRSALAVVR 281
Cdd:cd10001  218 AALDEALAAIA-AFGPDALVVSLGFDTHEGDPLSDFKLTTEDYARIGRRIAALGLPTVFV-QEGGYNVDALGRNAVAFLA 295
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
 4-282 3.32e-57

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: 194.19  E-value: 3.32e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747   4 IYSREATRAEIELIHDSALWDQYEANmtlPLAQLKTLSHDLELSSSLYLNHASTFCARLSCGSVVEMCSAVASGRVHNGF 83
Cdd:cd09301   21 IECREATEELLLKVHTEEYLNELKAN---FAVATITESKPVIFGPNFPVQRHYFRGARLSTGGVVEAAELVAKGELERAF 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  84 AIVRPPGHHAEPGAGFGFCLYNNVAVSTRVLLDRPLgapdrvERVMILDWDVHHGNGTQRAFWDNKQVLYISLHRYengt 163
Cdd:cd09301   98 AVVGAGGHHAGKSRAWGFCYFNDVVLAIKFLRERGI------SRILIIDTDAHHGDGTREAFYDDDRVLHMSFHNY---- 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 164 fypgtsfgNYDQVGGESARGTSVNVPWPcSGMDDGDYLHAFQHCIMPIAYEFAPDLVIVSAGFDAAQDDMLGGCLVSPAG 243
Cdd:cd09301  168 --------DIYPFGRGKGKGYKINVPLE-DGLGDEEYLDAVERVISKVLEEFEPEVVVLQFGHDTHEGDRLGGFNLSEKG 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 164662747 244 YAHMTHQLMALAQ-GNLVVALEGGYTLDAISRSALAVVRT 282
Cdd:cd09301  239 FVKLAEIVKEFARgGPILMVLGGGYNPEAAARIWTAIIKE 278
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
 6-275 1.56e-46

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: 166.58  E-value: 1.56e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747   6 SREATRAEIELIHDSALwdqyeanmtlpLAQLKTLSHDLELSSSLYLN------------HAStfcARLSCGSVVEMCSA 73
Cdd:cd09994   45 PRPATEEELLLFHTPDY-----------IEAVKEASRGQEPEGRGRLGlgtednpvfpgmHEA---AALVVGGTLLAARL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  74 VASGRVHNGFAivrPPG--HHAEPGAGFGFCLYNNVAVSTRVLLDRplgapdRVERVMILDWDVHHGNGTQRAFWDNKQV 151
Cdd:cd09994  111 VLEGEARRAFN---PAGglHHAMRGRASGFCVYNDAAVAIERLRDK------GGLRVAYVDIDAHHGDGVQAAFYDDPRV 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 152 LYISLHryENG-TFYPGTsfGNYDQVGGESARGTSVNVPWPcSGMDDGDYLHAFQHCIMPIAYEFAPDLVIVSAGFDAAQ 230
Cdd:cd09994  182 LTISLH--ESGrYLFPGT--GFVDEIGEGEGYGYAVNIPLP-PGTGDDEFLRAFEAVVPPLLRAFRPDVIVSQHGADAHA 256

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 164662747 231 DDMLGGCLVSPAGYAHMTHQLMALA----QGNLVVALEGGYTLDAISRS 275
Cdd:cd09994  257 GDPLTHLNLSNRAYRAAVRRIRELAdeycGGRWLALGGGGYNPDVVARA 305
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 6-243 3.33e-33

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: 128.38  E-value: 3.33e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747   6 SREATRAEIELIHDSALWDQYEANMTLPLAQLKT---LSHDLeLSSSLYLNHASTFCARLscgsvvemcsAVASGRVHN- 81
Cdd:cd09993   29 PEPATREDLLRVHDPEYLESLKSGELSREEIRRIgfpWSPEL-VERTRLAVGGTILAARL----------ALEHGLAINl 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  82 --GFaivrppgHHAEPGAGFGFCLYNNVAVSTRVLLDRPlgapdRVERVMILDWDVHHGNGTQRAFWDNKQVLYISLHry 159
Cdd:cd09993   98 agGT-------HHAFPDRGEGFCVFNDIAIAARVLLAEG-----LVRRVLIVDLDVHQGNGTAAIFADDPSVFTFSMH-- 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 160 eNGTFYPGtsfgnydqvggeSARGTSVNVPWPcSGMDDGDYLHAFQHCIMPIAYEFAPDLVIVSAGFDAAQDDMLGGCLV 239
Cdd:cd09993  164 -GEKNYPF------------RKEPSDLDVPLP-DGTGDDEYLAALEEALPRLLAEFRPDLVFYNAGVDVLAGDRLGRLSL 229


                 ....
gi 164662747 240 SPAG 243
Cdd:cd09993  230 SLEG 233
Arb2 pfam09757
Arb2 domain; This domain is found at the C-terminal of Clr3 (Cryptic loci regulator 3) also ...
 390-603 1.95e-26

Arb2 domain; This domain is found at the C-terminal of Clr3 (Cryptic loci regulator 3) also known as histone deacetylase clr3 (EC:3.5.1.98). Structure analysis reveals that the Arb2 domain has clear homology to alpha/beta-hydrolases but that it is lacking the catalytic triad of these enzymes. Functional studies show that the Arb2 domain is necessary for centromeric heterochromatin silencing suggesting a model where the Arb2 domain, through residues N562 and Y563, acts as an anchor that connects the HDAC activity of Clr3 to the SHREC complex. SHREC (Snf2/Hdac Repressive) complex in fission yeast drives transcriptional gene silencing in heterochromatin.


Pssm-ID: 401634  Cd Length: 252  Bit Score: 108.43  E-value: 1.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  390 AARLWKRHQLLPIP-THAGLQR---NQALCSSSLMlpTTQTLVIFVHDLAnlhkDVQGAP------------YVADSADA 453
Cdd:pfam09757  10 AKQLFEKYGMVPLPiQRDKLSKsfeNQVLATPNIY--KARTLLVIVHDPP----ELWAQPdpitnkldphnsWLVDSVLD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  454 LVQWAMERNYALMDlctmVPLPLQTVRNHSHgkalAYPDDP--TPSALNEQIQHIWDVYcaISPVP---KVFLVGLGTGC 528
Cdd:pfam09757  84 YIDWAVKQGYGVID----VNIPQHITETPES----LEEDDEynRISESQELLLYLWDNY--IELFDsatKIFFIGVGDAY 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164662747  529 EVLMHLITTRAIQSRVHGMVQVMGMNSI-PLVPKAQRELKSWYLKHARVICPPTHPYFAWNEQASSGKRLGTVQRA 603
Cdd:pfam09757 154 SGIVHLLGHRDCRSRVKGVINFVGGNPLrPVKSLTDESLSDWYFKNSLVFVSSDHSCWGDEENKKPRKRYGRVLRS 229
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
 1-274 2.09e-26

Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I histone deacetylase (HDAC) Hos2 from Saccharomyces cerevisiae as well as a histone deacetylase Phd1 from Schizosaccharomyces pombe. Hos2 binds to the coding regions of genes during gene activation, specifically it deacetylates the lysines in H3 and H4 histone tails. It is preferentially associated with genes of high activity genome-wide and is shown to be necessary for efficient transcription. Thus, Hos2 is directly required for gene activation in contrast to other class I histone deacetylases. Protein encoded by phd1 is inhibited by trichostatin A (TSA), a specific inhibitor of histone deacetylase, and is involved in the meiotic cell cycle in S. pombe. Class 1 HDACs are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues in histone amino termini to yield a deacetylated histone (EC 3.5.1.98).


Pssm-ID: 212540 [Multi-domain]  Cd Length: 311  Bit Score: 109.85  E-value: 2.09e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747   1 MHQIYSREATRAEIELIHDSALWDqYEANMT------LPLAQLKTLSH--DLELSSSLYlnhasTFCaRLSCGSVVEMCS 72
Cdd:cd11598   41 MDTYEARAATREELRQFHDADYLD-FLSKVSpenanqLRFDKAEPFNIgdDCPVFDGMY-----DYC-QLYAGASLDAAR 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  73 AVASGRvhNGFAIVRPPG-HHAEPGAGFGFCLYNNVAVSTRVLLdrplgapdRV-ERVMILDWDVHHGNGTQRAFWDNKQ 150
Cdd:cd11598  114 KLCSGQ--SDIAINWSGGlHHAKKSEASGFCYVNDIVLAILNLL--------RYfPRVLYIDIDVHHGDGVEEAFYRTDR 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 151 VLYISLHRYeNGTFYPGTsfGNYDQVGGESARGTSVNVPWPcSGMDDGDYLHAFQHCIMPIAYEFAPDLVIVSAGFDAAQ 230
Cdd:cd11598  184 VMTLSFHKY-NGEFFPGT--GDLDDNGGTPGKHFALNVPLE-DGIDDEQYNLLFKSIIGPTIEKFQPSAIVLQCGADSLG 259

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 164662747 231 DDMLGGCLVSPAGYAHMTHQLMALAQGNLVVAlEGGYTLDAISR 274
Cdd:cd11598  260 GDRLGQFNLNIKAHGACVKFVKSFGIPMLVVG-GGGYTPRNVAR 302
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 91-274 2.55e-26

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: 110.89  E-value: 2.55e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  91 HHAEPGAGFGFCLYNNVAVSTRVLLDRplgapdrVERVMILDWDVHHGNGTQRAFWDNKQVLYISLHRYENGtFYPGTsf 170
Cdd:cd10000  129 HHAQRDEASGFCYVNDIVLGILKLREK-------FDRVLYVDLDLHHGDGVEDAFSFTSKVMTVSLHKYSPG-FFPGT-- 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 171 GNYDQVGGESARGTSVNVPWPcSGMDDGDYLHAFQHCIMPIAYEFAPDLVIVSAGFDAAQDDMLGGCLVSPAGYAHMTHQ 250
Cdd:cd10000  199 GDVSDVGLGKGKYYTVNVPLR-DGIQDEQYLQIFTAVVPEIVAAFRPEAVVLQCGADTLAGDPMGAFNLTPVGIGKCLKY 277

                        170       180
                 ....*....|....*....|....
gi 164662747 251 LMALAQGNLVVAlEGGYTLDAISR 274
Cdd:cd10000  278 VLGWKLPTLILG-GGGYNLANTAR 300
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
 6-274 6.58e-25

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: 105.36  E-value: 6.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747   6 SREATRAEIELIHDsalwDQY--------EANMTLPLAQLK--TLSHDLELSSSLYlnhasTFCArLSCGSVVEMCSAVA 75
Cdd:cd09991   43 PRPATAEELTKFHS----DDYidflrsvsPDNMKEFKKQLErfNVGEDCPVFDGLY-----EYCQ-LYAGGSIAAAVKLN 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  76 SGRVHngFAIvRPPG--HHAEPGAGFGFCLYNNVAVSTRVLLDRplgapdrVERVMILDWDVHHGNGTQRAFWDNKQVLY 153
Cdd:cd09991  113 RGQAD--IAI-NWAGglHHAKKSEASGFCYVNDIVLAILELLKY-------HQRVLYIDIDIHHGDGVEEAFYTTDRVMT 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 154 ISLHRYenGTFYPGTSFGNYdqVGGESARGTSVNVPWPcSGMDDGDYLHAFQHCIMPIAYEFAPDLVIVSAGFDAAQDDM 233
Cdd:cd09991  183 VSFHKF--GEYFFPGTGLRD--IGAGKGKYYAVNVPLK-DGIDDESYLQIFEPVLSKVMEVFQPSAVVLQCGADSLAGDR 257

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 164662747 234 LGGCLVSPAGYAHMThQLMALAQGNLVVALEGGYTLDAISR 274
Cdd:cd09991  258 LGCFNLSIKGHAKCV-KFVKSFNIPLLVLGGGGYTLRNVAR 297
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
 91-274 8.67e-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: 97.85  E-value: 8.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  91 HHAEPGAGFGFCLYNNVAVSTRVLLD-RPlgapdrveRVMILDWDVHHGNGTQRAFWDNKQVLYISLHRYENgTFYPGTs 169
Cdd:cd10005  132 HHAKKFEASGFCYVNDIVIAILELLKyHP--------RVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGN-YFFPGT- 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 170 fGNYDQVGGESARGTSVNVPWPcSGMDDGDYLHAFQHCIMPIAYEFAPDLVIVSAGFDAAQDDMLGGCLVSPAGYAHMTH 249
Cdd:cd10005  202 -GDMYEVGAESGRYYSVNVPLK-DGIDDQSYLQLFKPVIQQVIDFYQPTCIVLQCGADSLGCDRLGCFNLSIKGHGECVE 279

                        170       180
                 ....*....|....*....|....*
gi 164662747 250 QLMALAQGNLVVAlEGGYTLDAISR 274
Cdd:cd10005  280 FVKSFNIPLLVLG-GGGYTVRNVAR 303
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
 91-266 1.39e-20

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: 92.33  E-value: 1.39e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  91 HHAEPGAGFGFCLYNNVAVSTRVLldRPLGAPdrveRVMILDWDVHHGNGTQRAFWDNKQVLYISLHRYENGtFYPGTsf 170
Cdd:cd11680  115 HHAQKSRASGFCYVNDIVLAILRL--RRARFR----RVFYLDLDLHHGDGVESAFFFSKNVLTCSIHRYDPG-FFPGT-- 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 171 GNYDqvggESARGTSVNVPWPcSGMDDGDYLHAFQHCIMPIAYEFAPDLVIVSAGFDAAQDDMLGGCLVSPAGYAHMTHQ 250
Cdd:cd11680  186 GSLK----NSSDKGMLNIPLK-RGLSDKTLLRIIDSIVRPLIEKFEPEVIVIQCGCDGLSGDPHKEWNLTIRGYGSVIEL 260

                        170
                 ....*....|....*.
gi 164662747 251 LMALAQGNLVVALEGG 266
Cdd:cd11680  261 LLKEFKDKPTLLLGGG 276
PTZ00063 PTZ00063
histone deacetylase; Provisional
 91-274 6.32e-20

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 92.95  E-value: 6.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  91 HHAEPGAGFGFCLYNNVAVSTRVLLDRPlgapdrvERVMILDWDVHHGNGTQRAFWDNKQVLYISLHRYenGTFYPGTsf 170
Cdd:PTZ00063 137 HHAKRSEASGFCYINDIVLGILELLKYH-------ARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFPGT-- 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 171 GNYDQVGGESARGTSVNVPWPcSGMDDGDYLHAFQHCIMPIAYEFAPDLVIVSAGFDAAQDDMLGGCLVSPAGYAHMTHQ 250
Cdd:PTZ00063 206 GDVTDIGVAQGKYYSVNVPLN-DGIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAACVEF 284

                        170       180
                 ....*....|....*....|....
gi 164662747 251 LMALAQGNLVVAlEGGYTLDAISR 274
Cdd:PTZ00063 285 VRSLNIPLLVLG-GGGYTIRNVAR 307
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
 58-274 3.22e-19

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: 89.74  E-value: 3.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  58 FCARLSCGSVVemcSAVASGRVHNGFAIVRPPG-HHAEPGAGFGFCLYNNVAVSTRVLLDRPlgapdrvERVMILDWDVH 136
Cdd:cd10010  106 FCQLSAGGSVA---SAVKLNKQQTDIAVNWAGGlHHAKKSEASGFCYVNDIVLAILELLKYH-------QRVLYIDIDIH 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 137 HGNGTQRAFWDNKQVLYISLHRYenGTFYPGTsfGNYDQVGGESARGTSVNVPWPcSGMDDGDYLHAFQHCIMPIAYEFA 216
Cdd:cd10010  176 HGDGVEEAFYTTDRVMTVSFHKY--GEYFPGT--GDLRDIGAGKGKYYAVNYPLR-DGIDDESYEAIFKPVMSKVMEMFQ 250

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 164662747 217 PDLVIVSAGFDAAQDDMLGGCLVSPAGYAHMTHQLMALAQGNLVVAlEGGYTLDAISR 274
Cdd:cd10010  251 PSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLG-GGGYTIRNVAR 307
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
 91-275 4.13e-19

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: 89.48  E-value: 4.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  91 HHAEPGAGFGFCLYNNVAVSTRVLLDRPlgapdrvERVMILDWDVHHGNGTQRAFWDNKQVLYISLHRYenGTFYPGTsf 170
Cdd:cd10004  133 HHAKKSEASGFCYVNDIVLGILELLRYH-------QRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKY--GEYFPGT-- 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 171 GNYDQVGGESARGTSVNVPWPcSGMDDGDYLHAFQHCIMPIAYEFAPDLVIVSAGFDAAQDDMLGGCLVSPAGYAHMTHQ 250
Cdd:cd10004  202 GELRDIGIGTGKNYAVNVPLR-DGIDDESYKSIFEPVIKHVMEWYQPEAVVLQCGGDSLSGDRLGCFNLSMKGHANCVNF 280

                        170       180
                 ....*....|....*....|....*
gi 164662747 251 LMALAQGNLVVAlEGGYTLDAISRS 275
Cdd:cd10004  281 VKSFNLPMLVLG-GGGYTMRNVART 304
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
 58-274 1.66e-15

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: 78.57  E-value: 1.66e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  58 FCARLSCGSVVemcSAVASGRVHNGFAIVRPPG-HHAEPGAGFGFCLYNNVAVSTRVLLDRPlgapdrvERVMILDWDVH 136
Cdd:cd10011  102 FCQLSTGGSVA---GAVKLNRQQTDMAVNWAGGlHHAKKSEASGFCYVNDIVLAILELLKYH-------QRVLYIDIDIH 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 137 HGNGTQRAFWDNKQVLYISLHRYENGtfYPGTsfGNYDQVGGESARGTSVNVPWPcSGMDDGDYLHAFQHCIMPIAYEFA 216
Cdd:cd10011  172 HGDGVEEAFYTTDRVMTVSFHKYGEY--FPGT--GDLRDIGAGKGKYYAVNFPMR-DGIDDESYGQIFKPIISKVMEMYQ 246

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 164662747 217 PDLVIVSAGFDAAQDDMLGGCLVSPAGYAHMTHQLMALAQGNLVVAlEGGYTLDAISR 274
Cdd:cd10011  247 PSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLG-GGGYTIRNVAR 303
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
 50-278 6.59e-15

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: 76.34  E-value: 6.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  50 LYLNHASTFCARLSCGSVVEMCSAVASGRVH---NGFAIVRPPGHHAEPGAGFGFCLYNNVAVSTRVLLDRplgapDRVE 126
Cdd:cd09998   76 LYLCPESLDAIQGALGAVCEAVDSVFKPESPgtkRAFVAIRPPGHHCSESTPSGFCWVNNVHVGAAHAYLT-----HGIT 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 127 RVMILDWDVHHGNGTQ------------------------RAFWDNKQVLYISLHRYENgtfYPgTSFGNYDQVGGES-- 180
Cdd:cd09998  151 RVVILDIDLHHGNGTQdiawrinaeankqalesssyddfkPAGAPGLRIFYSSLHDINS---FP-CEDGDPAKVKDASvs 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 181 ---ARGTSV-NV---PWpcsgMDDGDYLHAFQHC---IMPIAYEF------APD---LVIVSAGFDAAQ---DDMLGGCL 238
Cdd:cd09998  227 idgAHGQWIwNVhlqPW----TTEEDFWELYYPKyriLFEKAAEFlrlttaATPfktLVFISAGFDASEheyESMQRHGV 302

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 164662747 239 VSPAG-YAHMTHQLMALAQ----GNLVVALEGGYTLDAISRSALA 278
Cdd:cd09998  303 NVPTSfYYRFARDAVRFADahahGRLISVLEGGYSDRALCSGVLA 347
PTZ00346 PTZ00346
histone deacetylase; Provisional
 91-274 1.73e-14

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 75.84  E-value: 1.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747  91 HHAEPGAGFGFCLYNNVAVSTRVLLDRPlgapdrvERVMILDWDVHHGNGTQRAFWDNKQVLYISLHRYENgTFYPGTsf 170
Cdd:PTZ00346 154 HHSKCGECSGFCYVNDIVLGILELLKCH-------DRVLYVDIDMHHGDGVDEAFCTSDRVFTLSLHKFGE-SFFPGT-- 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 171 GNYDQVGGESARGTSVNVP-WpcSGMDDGDYLHAFQHCIMPIAYEFAPDLVIVSAGFDAAQDDMLGGCLVSPAGYAHMTH 249
Cdd:PTZ00346 224 GHPRDVGYGRGRYYSMNLAvW--DGITDFYYLGLFEHALHSIVRRYSPDAIVLQCGADSLAGDRLGLLNLSSFGHGQCVQ 301

                        170       180
                 ....*....|....*....|....*
gi 164662747 250 QLMALAQGNLVVAlEGGYTLDAISR 274
Cdd:PTZ00346 302 AVRDLGIPMLALG-GGGYTIRNVAK 325
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 119-281 1.19e-04

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: 43.90  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 119 LGAPDRVERVMILDWDVHHGNGTQRAFwdNKQVLYISLHRYENGTFYPG--TSFGNYD----QVGGESARGTSVNVPWpc 192
Cdd:cd09987   43 RAVAELHPDLGVIDVDAHHDVRTPEAF--GKGNHHTPRHLLCEPLISDVhiVSIGIRGvsngEAGGAYARKLGVVYFS-- 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164662747 193 sgMDDGD---YLHAFQHCIMPIayEFAPDLVIVSAGFDA-AQDDMLG-GCL----VSPAGYAHMTHQLMALaqGNLVVAL 263
Cdd:cd09987  119 --MTEVDklgLGDVFEEIVSYL--GDKGDNVYLSVDVDGlDPSFAPGtGTPgpggLSYREGLYITERIAKT--NLVVGLD 192

                        170       180
                 ....*....|....*....|
gi 164662747 264 --EGGYTLDAISRSALAVVR 281
Cdd:cd09987  193 ivEVNPLLDETGRTARLAAA 212
 
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.
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