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Conserved domains on  [gi|731425430|ref|XP_010663245|]
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histone deacetylase 5 isoform X2 [Vitis vinifera]

Protein Classification

arginase family protein( domain architecture ID 98571)

arginase family protein is a metal-dependent enzyme that catalyzes the hydrolysis of an amide bond, such as arginase-like amidino hydrolases and histone/histone-like deacetylases

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 ...
 18-369 1.76e-148

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 cd10003:

Pssm-ID: 450134 [Multi-domain]  Cd Length: 350  Bit Score: 433.69  E-value: 1.76e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  18 YDDRMCEHATADGDPHPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNLIKNISSKQfDSRRNRIA 97
Cdd:cd10003    1 YDQRMMNHHNLWDPGHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHLDEMKSLEKMK-PRELNRLG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  98 SKFNSIYMNEGSSEAAYLAAGSVIEVAERVAKGELSSAFAIVRPPGHHAEQNEPMGFCLYNNVAIATSFLLNeRPDIKKI 177
Cdd:cd10003   80 KEYDSIYIHPDSYQCALLAAGCVLQVVEAVLTGESRNGVAIVRPPGHHAEQDTACGFCFFNNVAIAARYAQK-KYGLKRI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 178 LIVDWDVHHGNGTQKMFWKDPRVLFFSVHRHEFGSFYPANDEGFYAMTGEGPGAGYNINVPWENGRCGDADYLAVWDHIL 257
Cdd:cd10003  159 LIVDWDVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSPEGNYDVVGKGKGEGFNVNIPWNKGGMGDAEYIAAFQQVV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 258 IPVAKDFNPDIVIISAGFDAAIGDPLGGCHVTPYGYSVMLKKLMEFSEGKIIMALEGGYNLVSLANSVLACVEVLLEDKP 337
Cdd:cd10003  239 LPIAYEFNPELVLVSAGFDAARGDPLGGCKVTPEGYAHMTHMLMSLAGGRVIVILEGGYNLTSISESMSMCTKTLLGDPP 318

                        330       340       350
                 ....*....|....*....|....*....|..
gi 731425430 338 IAGSSEAYPFESTWRVIQAVRQELSAFWPTLA 369
Cdd:cd10003  319 PVLDLPRPPCSSALKSINNVLQVHQKYWKSLR 350
 
Name Accession Description Interval E-value
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
 18-369 1.76e-148

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: 433.69  E-value: 1.76e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  18 YDDRMCEHATADGDPHPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNLIKNISSKQfDSRRNRIA 97
Cdd:cd10003    1 YDQRMMNHHNLWDPGHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHLDEMKSLEKMK-PRELNRLG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  98 SKFNSIYMNEGSSEAAYLAAGSVIEVAERVAKGELSSAFAIVRPPGHHAEQNEPMGFCLYNNVAIATSFLLNeRPDIKKI 177
Cdd:cd10003   80 KEYDSIYIHPDSYQCALLAAGCVLQVVEAVLTGESRNGVAIVRPPGHHAEQDTACGFCFFNNVAIAARYAQK-KYGLKRI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 178 LIVDWDVHHGNGTQKMFWKDPRVLFFSVHRHEFGSFYPANDEGFYAMTGEGPGAGYNINVPWENGRCGDADYLAVWDHIL 257
Cdd:cd10003  159 LIVDWDVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSPEGNYDVVGKGKGEGFNVNIPWNKGGMGDAEYIAAFQQVV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 258 IPVAKDFNPDIVIISAGFDAAIGDPLGGCHVTPYGYSVMLKKLMEFSEGKIIMALEGGYNLVSLANSVLACVEVLLEDKP 337
Cdd:cd10003  239 LPIAYEFNPELVLVSAGFDAARGDPLGGCKVTPEGYAHMTHMLMSLAGGRVIVILEGGYNLTSISESMSMCTKTLLGDPP 318

                        330       340       350
                 ....*....|....*....|....*....|..
gi 731425430 338 IAGSSEAYPFESTWRVIQAVRQELSAFWPTLA 369
Cdd:cd10003  319 PVLDLPRPPCSSALKSINNVLQVHQKYWKSLR 350
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 33-332 1.82e-127

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: 378.12  E-value: 1.82e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430   33 HPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNLIKNISSKQFDSRRNRIASKFNSIYMNEGSSEA 112
Cdd:pfam00850   1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAAPEGGALLLLSYLSGDDDTPVSPGSYEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  113 AYLAAGSVIEVAERVAKGELSSAFAIVRPPGHHAEQNEPMGFCLYNNVAIATSFLLnERPDIKKILIVDWDVHHGNGTQK 192
Cdd:pfam00850  81 ALLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLR-EKYGLKRVAIVDFDVHHGNGTQE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  193 MFWKDPRVLFFSVHRHEFGsFYPAndEGFYAMTGEGPGAGYNINVPWENGrCGDADYLAVWDHILIPVAKDFNPDIVIIS 272
Cdd:pfam00850 160 IFYDDPSVLTLSIHQYPGG-FYPG--TGFADETGEGKGKGYTLNVPLPPG-TGDAEYLAAFEEILLPALEEFQPDLILVS 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 731425430  273 AGFDAAIGDPLGGCHVTPYGYSVMLKKLMEFSE---GKIIMALEGGYNLVSLANSVLACVEVL 332
Cdd:pfam00850 236 AGFDAHAGDPLGGLNLTTEGFAEITRILLELADplcIRVVSVLEGGYNLDALARSATAVLAAL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 14-334 6.82e-118

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 354.03  E-value: 6.82e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  14 VGLVYDDRMCEHATadGDPHPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNLIKNISSkqfDSRR 93
Cdd:COG0123    1 TALIYHPDYLLHDL--GPGHPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAASL---DGGY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  94 NRIASKFnsiYMNEGSSEAAYLAAGSVIEVAERVAKGELSSAFAIVRPPGHHAEQNEPMGFCLYNNVAIATSFLLNERpd 173
Cdd:COG0123   76 GQLDPDT---PVSPGTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGFCLFNNAAIAARYLLAKG-- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 174 IKKILIVDWDVHHGNGTQKMFWKDPRVLFFSVHRHefgSFYPanDEGFYAMTGEGPGAGYNINVPWENGrCGDADYLAVW 253
Cdd:COG0123  151 LERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD---PLYP--GTGAADETGEGAGEGSNLNVPLPPG-TGDAEYLAAL 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 254 DHILIPVAKDFNPDIVIISAGFDAAIGDPLGGCHVTPYGYSVMLKKLMEFSE---GKIIMALEGGYNLVSLANSVLACVE 330
Cdd:COG0123  225 EEALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELADhcgGPVVSVLEGGYNLDALARSVAAHLE 304


                 ....
gi 731425430 331 VLLE 334
Cdd:COG0123  305 TLLG 308
PTZ00063 PTZ00063
histone deacetylase; Provisional
 11-322 1.71e-18

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 88.33  E-value: 1.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  11 RRRVGLVYDDRMCEHATADGdpHPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNLIKNIS---SK 87
Cdd:PTZ00063   3 RKRVSYFYDPDIGSYYYGPG--HPMKPQRIRMAHALILSYDLYKHMEIYRPHKSVEPELVLFHDEEYVDFLSSISpenYR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  88 QFDSRRNRiaskFN-----SIYMNEGSSEAAYLAAGSVIEVAERVAKGElsSAFAIVRPPG-HHAEQNEPMGFCLYNNVA 161
Cdd:PTZ00063  81 DFTYQLKR----FNvgeatDCPVFDGLFEFQQSCAGASIDGAYKLNNHQ--ADICVNWSGGlHHAKRSEASGFCYINDIV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 162 IATSFLLNERpdiKKILIVDWDVHHGNGTQKMFWKDPRVLFFSVHRheFGSFYPANdeGFYAMTGEGPGAGYNINVPWEN 241
Cdd:PTZ00063 155 LGILELLKYH---ARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHK--FGDFFPGT--GDVTDIGVAQGKYYSVNVPLND 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 242 GrCGDADYLAVWDHILIPVAKDFNPDIVIISAGFDAAIGDPLGGCHVTPYGYSVMLKKLMEFSEGKIIMAlEGGYNLVSL 321
Cdd:PTZ00063 228 G-IDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAACVEFVRSLNIPLLVLG-GGGYTIRNV 305


                 .
gi 731425430 322 A 322
Cdd:PTZ00063 306 A 306
 
Name Accession Description Interval E-value
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
 18-369 1.76e-148

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: 433.69  E-value: 1.76e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  18 YDDRMCEHATADGDPHPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNLIKNISSKQfDSRRNRIA 97
Cdd:cd10003    1 YDQRMMNHHNLWDPGHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHLDEMKSLEKMK-PRELNRLG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  98 SKFNSIYMNEGSSEAAYLAAGSVIEVAERVAKGELSSAFAIVRPPGHHAEQNEPMGFCLYNNVAIATSFLLNeRPDIKKI 177
Cdd:cd10003   80 KEYDSIYIHPDSYQCALLAAGCVLQVVEAVLTGESRNGVAIVRPPGHHAEQDTACGFCFFNNVAIAARYAQK-KYGLKRI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 178 LIVDWDVHHGNGTQKMFWKDPRVLFFSVHRHEFGSFYPANDEGFYAMTGEGPGAGYNINVPWENGRCGDADYLAVWDHIL 257
Cdd:cd10003  159 LIVDWDVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSPEGNYDVVGKGKGEGFNVNIPWNKGGMGDAEYIAAFQQVV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 258 IPVAKDFNPDIVIISAGFDAAIGDPLGGCHVTPYGYSVMLKKLMEFSEGKIIMALEGGYNLVSLANSVLACVEVLLEDKP 337
Cdd:cd10003  239 LPIAYEFNPELVLVSAGFDAARGDPLGGCKVTPEGYAHMTHMLMSLAGGRVIVILEGGYNLTSISESMSMCTKTLLGDPP 318

                        330       340       350
                 ....*....|....*....|....*....|..
gi 731425430 338 IAGSSEAYPFESTWRVIQAVRQELSAFWPTLA 369
Cdd:cd10003  319 PVLDLPRPPCSSALKSINNVLQVHQKYWKSLR 350
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
 33-333 6.64e-143

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: 417.28  E-value: 6.64e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  33 HPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNLIKNISskqfdsrRNRIASKFNSIYMNEGSSEA 112
Cdd:cd09992    1 HPERPERLLAILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYIERVEETC-------EAGGGYLDPDTYVSPGSYEA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 113 AYLAAGSVIEVAERVAKGELSSAFAIVRPPGHHAEQNEPMGFCLYNNVAIATSFLLnERPDIKKILIVDWDVHHGNGTQK 192
Cdd:cd09992   74 ALLAAGAALAAVDAVLSGEAENAFALVRPPGHHAEPDRAMGFCLFNNVAIAARYAQ-KRYGLKRVLIVDWDVHHGNGTQD 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 193 MFWKDPRVLFFSVHRHEfgsFYPAndEGFYAMTGEGPGAGYNINVPWENGrCGDADYLAVWDHILIPVAKDFNPDIVIIS 272
Cdd:cd09992  153 IFYDDPSVLYFSIHQYP---FYPG--TGAAEETGGGAGEGFTINVPLPPG-SGDAEYLAAFEEVLLPIAREFQPDLVLVS 226

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 731425430 273 AGFDAAIGDPLGGCHVTPYGYSVMLKKLME----FSEGKIIMALEGGYNLVSLANSVLACVEVLL 333
Cdd:cd09992  227 AGFDAHRGDPLGGMNLTPEGYARLTRLLKEladeHCGGRLVFVLEGGYNLEALAESVLAVLEALL 291
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 31-337 8.49e-137

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: 402.49  E-value: 8.49e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  31 DPHPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNLIKN---ISSKQFDSRRNRIASkfNSIYMNE 107
Cdd:cd11600    1 DPHPEDPSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEHWDRVEAtekMSDEQLKDRTEIFER--DSLYVNN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 108 GSSEAAYLAAGSVIEVAERVAKGELSSAFAIVRPPGHHAEQNEPMGFCLYNNVAIATSFLLNERPD-IKKILIVDWDVHH 186
Cdd:cd11600   79 DTAFCARLSCGGAIEACRAVAEGRVKNAFAVVRPPGHHAEPDESMGFCFFNNVAVAAKWLQTEYPDkIKKILILDWDIHH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 187 GNGTQKMFWKDPRVLFFSVHRHEFGSFYPANDEGFYAMTGEGPGAGYNINVPWENGRCGDADYLAVWDHILIPVAKDFNP 266
Cdd:cd11600  159 GNGTQRAFYDDPNVLYISLHRFENGGFYPGTPYGDYESVGEGAGLGFNVNIPWPQGGMGDADYIYAFQRIVMPIAYEFDP 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 731425430 267 DIVIISAGFDAAIGDPLGGCHVTPYGYSVMLKKLMEFSEGKIIMALEGGYNLVSLANSVLACVEVLLEDKP 337
Cdd:cd11600  239 DLVIISAGFDAADGDELGQCHVTPAGYAHMTHMLMSLAGGKLVVALEGGYNLDAISDSALAVAKVLLGEAP 309
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 33-332 1.82e-127

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: 378.12  E-value: 1.82e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430   33 HPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNLIKNISSKQFDSRRNRIASKFNSIYMNEGSSEA 112
Cdd:pfam00850   1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAAPEGGALLLLSYLSGDDDTPVSPGSYEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  113 AYLAAGSVIEVAERVAKGELSSAFAIVRPPGHHAEQNEPMGFCLYNNVAIATSFLLnERPDIKKILIVDWDVHHGNGTQK 192
Cdd:pfam00850  81 ALLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLR-EKYGLKRVAIVDFDVHHGNGTQE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  193 MFWKDPRVLFFSVHRHEFGsFYPAndEGFYAMTGEGPGAGYNINVPWENGrCGDADYLAVWDHILIPVAKDFNPDIVIIS 272
Cdd:pfam00850 160 IFYDDPSVLTLSIHQYPGG-FYPG--TGFADETGEGKGKGYTLNVPLPPG-TGDAEYLAAFEEILLPALEEFQPDLILVS 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 731425430  273 AGFDAAIGDPLGGCHVTPYGYSVMLKKLMEFSE---GKIIMALEGGYNLVSLANSVLACVEVL 332
Cdd:pfam00850 236 AGFDAHAGDPLGGLNLTTEGFAEITRILLELADplcIRVVSVLEGGYNLDALARSATAVLAAL 298
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 15-365 4.04e-121

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: 364.74  E-value: 4.04e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  15 GLVYDDRMCEHATADGDP--HPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNL--IKNISSKQFD 90
Cdd:cd11681    4 GLAYDPLMLKHQCICGNNssHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTLLygTNPLSRLKLD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  91 SRRNRIASKFNSIYM-------------NEG-SSEAAYLAAGSVIEVAERVAKGELSSAFAIVRPPGHHAEQNEPMGFCL 156
Cdd:cd11681   84 PTKLAGLPQKSFVRLpcggigvdsdtvwNELhTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQAMGFCF 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 157 YNNVAIATSfLLNERPDIKKILIVDWDVHHGNGTQKMFWKDPRVLFFSVHRHEFGSFYP---ANDEgfyamTGEGPGAGY 233
Cdd:cd11681  164 FNSVAIAAK-QLQQKLKLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFPgtgAPTE-----VGSGAGEGF 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 234 NINVPWENG---RCGDADYLAVWDHILIPVAKDFNPDIVIISAGFDAAIGDP--LGGCHVTPYGYSVMLKKLMEFSEGKI 308
Cdd:cd11681  238 NVNIAWSGGldpPMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPppLGGYKVSPACFGYMTRQLMNLAGGKV 317

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 309 IMALEGGYNLVSLANSVLACVEVLLEDKPIAGSSEAY---PFESTWRVIQAVRQELSAFW 365
Cdd:cd11681  318 VLALEGGYDLTAICDASEACVRALLGDELDPLSEEELerrPNPNAVTSLEKVIAIQSPYW 377
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 14-334 6.82e-118

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 354.03  E-value: 6.82e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  14 VGLVYDDRMCEHATadGDPHPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNLIKNISSkqfDSRR 93
Cdd:COG0123    1 TALIYHPDYLLHDL--GPGHPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAASL---DGGY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  94 NRIASKFnsiYMNEGSSEAAYLAAGSVIEVAERVAKGELSSAFAIVRPPGHHAEQNEPMGFCLYNNVAIATSFLLNERpd 173
Cdd:COG0123   76 GQLDPDT---PVSPGTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGFCLFNNAAIAARYLLAKG-- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 174 IKKILIVDWDVHHGNGTQKMFWKDPRVLFFSVHRHefgSFYPanDEGFYAMTGEGPGAGYNINVPWENGrCGDADYLAVW 253
Cdd:COG0123  151 LERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD---PLYP--GTGAADETGEGAGEGSNLNVPLPPG-TGDAEYLAAL 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 254 DHILIPVAKDFNPDIVIISAGFDAAIGDPLGGCHVTPYGYSVMLKKLMEFSE---GKIIMALEGGYNLVSLANSVLACVE 330
Cdd:COG0123  225 EEALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELADhcgGPVVSVLEGGYNLDALARSVAAHLE 304


                 ....
gi 731425430 331 VLLE 334
Cdd:COG0123  305 TLLG 308
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 33-365 1.43e-117

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: 354.31  E-value: 1.43e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  33 HPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNLIKNISSKQFDSRRnRIASKFNSIYMNEGSSEA 112
Cdd:cd10002    7 HIECPERLEAILERLTQDGLLERCVKIPAREAEEDEILLVHSQEYIDLVKSTETMEKEELE-SLCSGYDSVYLCPSTYEA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 113 AYLAAGSVIEVAERVAKGELSSAFAIVRPPGHHAEQNEPMGFCLYNNVAIATSFLLNERpDIKKILIVDWDVHHGNGTQK 192
Cdd:cd10002   86 ARLAAGSTIELVKAVMAGKIQNGFALIRPPGHHAMRNEANGYCIFNNVAIAAKYAIEKL-GLKRILIVDWDVHHGQGTQQ 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 193 MFWKDPRVLFFSVHRHEFGSFYPANDEGFYAMTGEGPGAGYNINVPWENGRCGDADYLAVWDHILIPVAKDFNPDIVIIS 272
Cdd:cd10002  165 GFYEDPRVLYFSIHRYEHGRFWPHLFESDYDYIGVGHGYGFNVNVPLNQTGLGDADYLAIFHHILLPLALEFQPELVLVS 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 273 AGFDAAIGDPLGGCHVTPYGYSVMLKKLMEFSEGKIIMALEGGYNLVSLANSVLACVEVLLEDkPIAGSSEAYPFESTWR 352
Cdd:cd10002  245 AGFDASIGDPEGEMAVTPAGYAHLTRLLMGLAGGKLLLVLEGGYLLESLAESVSMTLRGLLGD-PLPPLAPPIPIRSVLE 323

                        330
                 ....*....|...
gi 731425430 353 VIQAVRQELSAFW 365
Cdd:cd10002  324 TILNAIAHLSPRW 336
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
 31-365 2.58e-102

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: 314.87  E-value: 2.58e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  31 DPHPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNLIKNISSKQFDSRRNrIASKFNSIYMNEGSS 110
Cdd:cd11682    5 ESFPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYVALMKSTQYMTEEELRT-LADTYDSVYLHPNSY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 111 EAAYLAAGSVIEVAERVAKGELSSAFAIVRPPGHHAEQNEPMGFCLYNNVAIATSFLlNERPDIKKILIVDWDVHHGNGT 190
Cdd:cd11682   84 SCACLAVGSVLQLVDKVLGGEIRNGLAIVRPPGHHAQHDKMDGYCMFNNVAIAARYA-QQKHGVQRVLIVDWDVHHGQGT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 191 QKMFWKDPRVLFFSVHRHEFGSFYPANDEGFYAMTGEGPGAGYNINVPWENGRCGDADYLAVWDHILIPVAKDFNPDIVI 270
Cdd:cd11682  163 QFIFEQDPSVLYFSIHRYEQGRFWPHLKESDSSAVGFGRGEGYNINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVL 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 271 ISAGFDAAIGDPLGGCHVTPYGYSVMLKKLMEFSEGKIIMALEGGYNLVSLANSVLACVEVLLEDK-PIAGSSEAyPFES 349
Cdd:cd11682  243 VAAGFDAVIGDPKGEMAATPACFAHLTHLLMGLAGGKLILSLEGGYNLRSLAEGVCASLKALLGDPcPMLESPGA-PCRS 321

                        330
                 ....*....|....*.
gi 731425430 350 TWRVIQAVRQELSAFW 365
Cdd:cd11682  322 ALASVSCTISALEPFW 337
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
 15-365 1.57e-99

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: 309.25  E-value: 1.57e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  15 GLVYDDRMCEHATADGDP--HPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNLIKN--ISSKQFD 90
Cdd:cd10008    4 GLVYDSVMLKHQCSCGDNsnHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTnpLSRLKLD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  91 SRR---------------NRIASKFNSIYMNEGSSEAAYLAAGSVIEVAERVAKGELSSAFAIVRPPGHHAEQNEPMGFC 155
Cdd:cd10008   84 NGKlagllaqrmfvmlpcGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGFC 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 156 LYNNVAIATSfLLNERPDIKKILIVDWDVHHGNGTQKMFWKDPRVLFFSVHRHEFGSFYP---ANDEgfyamTGEGPGAG 232
Cdd:cd10008  164 FFNSVAIACR-QLQQQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPgsgAVDE-----VGAGSGEG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 233 YNINVPWENG---RCGDADYLAVWDHILIPVAKDFNPDIVIISAGFDAAIGD--PLGGCHVTPYGYSVMLKKLMEFSEGK 307
Cdd:cd10008  238 FNVNVAWAGGldpPMGDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHpaPLGGYHVSAKCFGYMTQQLMNLAGGA 317

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 731425430 308 IIMALEGGYNLVSLANSVLACVEVLLEDKPIAGSSEAY---PFESTWRVIQAVRQELSAFW 365
Cdd:cd10008  318 VVLALEGGHDLTAICDASEACVAALLGNEVDPLSEESWkqkPNLNAIRSLEAVIRVHSKYW 378
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
 11-368 7.51e-99

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: 308.50  E-value: 7.51e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  11 RRRVGLVYDDRMCEHATADGDP--HPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNL--IKNISS 86
Cdd:cd10006    3 RFTTGLVYDTLMLKHQCTCGNSnsHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLygTNPLNR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  87 KQFDSRR--NRIASKF------------NSIYMNEGSSEAAYLAAGSVIEVAERVAKGELSSAFAIVRPPGHHAEQNEPM 152
Cdd:cd10006   83 QKLDSKKllGSLASVFvrlpcggvgvdsDTIWNEVHSSGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPM 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 153 GFCLYNNVAIATSfLLNERPDIKKILIVDWDVHHGNGTQKMFWKDPRVLFFSVHRHEFGSFYP---ANDEgfyamTGEGP 229
Cdd:cd10006  163 GFCYFNSVAIAAK-LLQQRLNVSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYDDGNFFPgsgAPDE-----VGTGP 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 230 GAGYNINVPWENG---RCGDADYLAVWDHILIPVAKDFNPDIVIISAGFDAAIGD--PLGGCHVTPYGYSVMLKKLMEFS 304
Cdd:cd10006  237 GVGFNVNMAFTGGldpPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHptPLGGYNLSAKCFGYLTKQLMGLA 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 731425430 305 EGKIIMALEGGYNLVSLANSVLACVEVLLEDK--PIAGSS-EAYPFESTWRVIQAVRQELSAFWPTL 368
Cdd:cd10006  317 GGRIVLALEGGHDLTAICDASEACVSALLGNEldPLPEKVlQQRPNANAVRSMEKVMEIHSKYWRCL 383
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
 14-359 1.02e-95

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: 298.71  E-value: 1.02e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  14 VGLVYDDRMCEHATADG-------------DPHPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNL 80
Cdd:cd09996    1 TGFVWDERYLWHDTGTGalflpvggllvqpGRHPENPETKRRIKNLLEVSGLSDHLVLITPRPATDEELLRVHTPEYIDR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  81 IKNISskqfDSRRNRIASKfnsIYMNEGSSEAAYLAAGSVIEVAERVAKGELSSAFAIVRPPGHHAEQNEPMGFCLYNNV 160
Cdd:cd09996   81 VKAAS----AAGGGEAGGG---TPFGPGSYEIALLAAGGAIAAVDAVLDGEVDNAYALVRPPGHHAEPDQGMGFCLFNNV 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 161 AIATSFLLNERpDIKKILIVDWDVHHGNGTQKMFWKDPRVLFFSVHRHefGSFYPanDEGFYAMTGEGPGAGYNINVPWE 240
Cdd:cd09996  154 AIAARHALAVG-GVKRVAVVDWDVHHGNGTQAIFYDDPDVLTISLHQD--RCFPP--DSGAVEERGEGAGEGYNLNIPLP 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 241 NGrCGDADYLAVWDHILIPVAKDFNPDIVIISAGFDAAIGDPLGGCHVTPYGYSVMLKKLM----EFSEGKIIMALEGGY 316
Cdd:cd09996  229 PG-SGDGAYLHAFERIVLPALRAFRPELIIVASGFDASAFDPLGRMMLTSDGFRALTRKLRdladELCGGRLVMVHEGGY 307

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 731425430 317 NLVSLANSVLACVEVLLE-----DKPIAGSSEAY------PFEStwRVIQAVRQ 359
Cdd:cd09996  308 SEAYVPFCGLAVLEELSGvrtgiADPLLYYPEAQggqelqPHQR--AAIDAAAA 359
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
 15-337 2.73e-94

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: 297.28  E-value: 2.73e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  15 GLVYDDRMCEHATADGDP--HPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNLIKN--ISSKQFD 90
Cdd:cd10007    6 GLVYDTFMLKHQCTCGNTnvHPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHSEHHTLLYGTspLNRQKLD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  91 SRR--NRIASKF-------------NSIYMNEGSSEAAYLAAGSVIEVAERVAKGELSSAFAIVRPPGHHAEQNEPMGFC 155
Cdd:cd10007   86 SKKllGPLSQKMyavlpcggigvdsDTVWNEMHSSSAVRMAVGCLIELAFKVAAGELKNGFAVIRPPGHHAEESTAMGFC 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 156 LYNNVAIATSfLLNERPDIKKILIVDWDVHHGNGTQKMFWKDPRVLFFSVHRHEFGSFYP---ANDEgfyamTGEGPGAG 232
Cdd:cd10007  166 FFNSVAIAAK-LLQQKLNVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGNFFPgsgAPDE-----VGAGPGVG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 233 YNINVPWENG---RCGDADYLAVWDHILIPVAKDFNPDIVIISAGFDAAIG--DPLGGCHVTPYGYSVMLKKLMEFSEGK 307
Cdd:cd10007  240 FNVNIAWTGGvdpPIGDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGhqSPLGGYSVTAKCFGHLTKQLMTLAGGR 319

                        330       340       350
                 ....*....|....*....|....*....|
gi 731425430 308 IIMALEGGYNLVSLANSVLACVEVLLEDKP 337
Cdd:cd10007  320 VVLALEGGHDLTAICDASEACVSALLGMEL 349
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 18-365 3.22e-93

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: 291.38  E-value: 3.22e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  18 YDDRMCEhatadgdphPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNLIKNISSKQfDSRRNRIA 97
Cdd:cd11683    1 WDDPECE---------IEVPERLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRETQVMN-KEELMAIS 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  98 SKFNSIYMNEGSSEAAYLAAGSVIEVAERVAKGELSSAFAIVRPPGHHAEQNEPMGFCLYNNVAIATSFLlNERPDIKKI 177
Cdd:cd11683   71 GKYDAVYFHPNTFHCARLAAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYA-KKKYGLHRI 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 178 LIVDWDVHHGNGTQKMFWKDPRVLFFSVHRHEFGSFYPANDEGFYAMTGEGPGAGYNINVPWENGRCGDADYLAVWDHIL 257
Cdd:cd11683  150 LIVDWDVHHGQGIQYIFEEDPSVLYFSWHRYEHQRFWPFLRESDYDAVGRGKGLGFNINLPWNKVGMGNADYLAAFFHVL 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 258 IPVAKDFNPDIVIISAGFDAAIGDPLGGCHVTPYGYSVMLKKLMEFSEGKIIMALEGGYNLVSLANSVLACVEVLLEDKP 337
Cdd:cd11683  230 LPLAFEFDPELVLVSAGFDSAIGDPEGQMCATPECFAHLTHLLMVLAGGKLCAVLEGGYHLESLAESVCMTVQTLLGDPL 309

                        330       340
                 ....*....|....*....|....*...
gi 731425430 338 IAGSSEAYPFESTWRVIQAVRQELSAFW 365
Cdd:cd11683  310 PRLSGEMTPCQSALESIQNVRAAQAPYW 337
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
 33-333 1.12e-92

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: 288.26  E-value: 1.12e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  33 HPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNLIKNISSKQfdsrrnriasKFNSI----YMNEG 108
Cdd:cd11599    1 HPESPERLEAILDALIASGLDRLLRQLEAPPATREQLLRVHDAAYVDRLEAAAPEE----------GLVQLdpdtAMSPG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 109 SSEAAYLAAGSVIEVAERVAKGELSSAFAIVRPPGHHAEQNEPMGFCLYNNVAIATSFLLnERPDIKKILIVDWDVHHGN 188
Cdd:cd11599   71 SLEAALRAAGAVVAAVDAVMAGEARNAFCAVRPPGHHAERDKAMGFCLFNNVAIAAAHAL-AHHGLERVAIVDFDVHHGN 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 189 GTQKMFWKDPRVLFFSVHRHEfgsFYPandegfYAMTGEGPGAGYNINVPWENGrCGDADYLAVWDHILIPVAKDFNPDI 268
Cdd:cd11599  150 GTEDIFRDDPRVLFCSSHQHP---LYP------GTGAPDETGHGNIVNVPLPAG-TGGAEFREAVEDRWLPALDAFKPDL 219

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 731425430 269 VIISAGFDAAIGDPLGGCHVTPYGYSVMLKKLM----EFSEGKIIMALEGGYNLVSLANSVLACVEVLL 333
Cdd:cd11599  220 ILISAGFDAHRDDPLAQLNLTEEDYAWITEQLMdvadRYCDGRIVSVLEGGYDLSALARSVAAHVRALM 288
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
 32-327 1.12e-85

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: 270.18  E-value: 1.12e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  32 PHPENPDRIRAIWKKLESAGIPqrcVVFNAKEAEDKHILSVHSNNHVNLIKNisskqFDSrrnriaskfnSIYMNEGSSE 111
Cdd:cd10001   24 PHPENPERAEAILDALKRAGLG---EVLPPRDFGLEPILAVHDPDYVDFLET-----ADT----------DTPISEGTWE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 112 AAYLAAGSVIEVAERVAKGElSSAFAIVRPPGHHAEQNEPMGFCLYNNVAIATSFLLNERpdiKKILIVDWDVHHGNGTQ 191
Cdd:cd10001   86 AALAAADTALTAADLVLEGE-RAAYALCRPPGHHAGRDRAGGFCYFNNAAIAAQYLRDRA---GRVAILDVDVHHGNGTQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 192 KMFWKDPRVLFFSVHRHeFGSFYPandeGF--YA-MTGEGPGAGYNINVPWENGrCGDADYLAVWDHILIPVAkDFNPDI 268
Cdd:cd10001  162 EIFYERPDVLYVSIHGD-PRTFYP----FFlgFAdETGEGEGEGYNLNLPLPPG-TGDDDYLAALDEALAAIA-AFGPDA 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 731425430 269 VIISAGFDAAIGDPLGGCHVTPYGYSVMLKKLMEFSEGKIIMaLEGGYNLVSLANSVLA 327
Cdd:cd10001  235 LVVSLGFDTHEGDPLSDFKLTTEDYARIGRRIAALGLPTVFV-QEGGYNVDALGRNAVA 292
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
 15-339 3.80e-85

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: 271.89  E-value: 3.80e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  15 GLVYDDRMCEHATADGD--PHPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNLIKN--ISSKQFD 90
Cdd:cd10009    4 GIAYDPLMLKHQCVCGNstTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTnpLDGQKLD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  91 SRR--NRIASKF-------------NSIYMNEGSSEAAYLAAGSVIEVAERVAKGELSSAFAIVRPPGHHAEQNEPMGFC 155
Cdd:cd10009   84 PRIllGDDSQKFfsslpcgglgvdsDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFC 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 156 LYNNVAIATSFlLNERPDIKKILIVDWDVHHGNGTQKMFWKDPRVLFFSVHRHEFGSFYPANdeGFYAMTGEGPGAGYNI 235
Cdd:cd10009  164 FFNSVAITAKY-LRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGS--GAPNEVGTGLGEGYNI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 236 NVPWENG---RCGDADYLAVWDHILIPVAKDFNPDIVIISAGFDAAIGD--PLGGCHVTPYGYSVMLKKLMEFSEGKIIM 310
Cdd:cd10009  241 NIAWTGGldpPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLADGRVVL 320

                        330       340       350
                 ....*....|....*....|....*....|.
gi 731425430 311 ALEGGYNLVSLANSVLACVEVLL--EDKPIA 339
Cdd:cd10009  321 ALEGGHDLTAICDASEACVNALLgnELEPLA 351
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
 39-332 1.59e-66

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: 219.61  E-value: 1.59e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  39 RIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNLIKNISSKQFDSRRNRIASKFNsIYMNEGSSEAAYLAAG 118
Cdd:cd09301    1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKANFAVATITESKPVIFGPN-FPVQRHYFRGARLSTG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 119 SVIEVAERVAKGELSSAFAIVRPPGHHAEQNEPMGFCLYNNVAIATSFLLnERpDIKKILIVDWDVHHGNGTQKMFWKDP 198
Cdd:cd09301   80 GVVEAAELVAKGELERAFAVVGAGGHHAGKSRAWGFCYFNDVVLAIKFLR-ER-GISRILIIDTDAHHGDGTREAFYDDD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 199 RVLFFSVHRhefgsfypaNDEGFYamtGEGPGAGYNINVPWENGrCGDADYLAVWDHILIPVAKDFNPDIVIISAGFDAA 278
Cdd:cd09301  158 RVLHMSFHN---------YDIYPF---GRGKGKGYKINVPLEDG-LGDEEYLDAVERVISKVLEEFEPEVVVLQFGHDTH 224

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 731425430 279 IGDPLGGCHVTPYGYSVMLKKLMEFSEGK-IIMALEGGYNLVSLANSVLACVEVL 332
Cdd:cd09301  225 EGDRLGGFNLSEKGFVKLAEIVKEFARGGpILMVLGGGYNPEAAARIWTAIIKEL 279
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
 16-322 4.27e-57

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: 195.47  E-value: 4.27e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  16 LVYDDRMCEHATadGDPHPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNLIKNISSKQFDSRRNR 95
Cdd:cd09994    2 FIYSEEYLRYSF--GPNHPFNPPRLSLTKDLLRALGLLPPVDLVPPRPATEEELLLFHTPDYIEAVKEASRGQEPEGRGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  96 --IASKFNSIYmnEGSSEAAYLAAGSVIEVAERVAKGELSSAFAivrPPG--HHAEQNEPMGFCLYNNVAIATSFLLNER 171
Cdd:cd09994   80 lgLGTEDNPVF--PGMHEAAALVVGGTLLAARLVLEGEARRAFN---PAGglHHAMRGRASGFCVYNDAAVAIERLRDKG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 172 pdIKKILIVDWDVHHGNGTQKMFWKDPRVLFFSVhrHEFGS-FYPAndEGFYAMTGEGPGAGYNINVPWENGrCGDADYL 250
Cdd:cd09994  155 --GLRVAYVDIDAHHGDGVQAAFYDDPRVLTISL--HESGRyLFPG--TGFVDEIGEGEGYGYAVNIPLPPG-TGDDEFL 227

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 731425430 251 AVWDHILIPVAKDFNPDIVIISAGFDAAIGDPLGGCHVTPYGYSVMLKKLME----FSEGKIIMALEGGYNLVSLA 322
Cdd:cd09994  228 RAFEAVVPPLLRAFRPDVIVSQHGADAHAGDPLTHLNLSNRAYRAAVRRIREladeYCGGRWLALGGGGYNPDVVA 303
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 14-322 1.43e-38

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: 146.33  E-value: 1.43e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  14 VGLVYDD---RMCehatadgDPHPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNLIKNISSKQFD 90
Cdd:cd10000    1 VVYIHSPeyvNLC-------DRLPKVPNRASMVHSLIEAYGLLKQLRVVKPRVATEEELASFHSDEYIQFLKKASNEGDN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  91 SRRNRIASKFNSIY---MNEGSSEAAYLAAGSVIEVAERVAKGElsSAFAIVRPPG-HHAEQNEPMGFCLYNNVAIAtsf 166
Cdd:cd10000   74 DEEPSEQQEFGLGYdcpIFEGIYDYAAAVAGATLTAAQLLIDGK--CKVAINWFGGwHHAQRDEASGFCYVNDIVLG--- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 167 LLNERPDIKKILIVDWDVHHGNGTQKMFWKDPRVLFFSVHRHEFGsFYPANdeGFYAMTGEGPGAGYNINVPWENGrCGD 246
Cdd:cd10000  149 ILKLREKFDRVLYVDLDLHHGDGVEDAFSFTSKVMTVSLHKYSPG-FFPGT--GDVSDVGLGKGKYYTVNVPLRDG-IQD 224

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 731425430 247 ADYLAVWDHILIPVAKDFNPDIVIISAGFDAAIGDPLGGCHVTPYGYSVMLKKLMEFSEGKIIMAlEGGYNLVSLA 322
Cdd:cd10000  225 EQYLQIFTAVVPEIVAAFRPEAVVLQCGADTLAGDPMGAFNLTPVGIGKCLKYVLGWKLPTLILG-GGGYNLANTA 299
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 33-317 1.08e-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: 129.93  E-value: 1.08e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  33 HPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNLIKNISSKQFDSRRnriaSKFNsiyMNEGSSEA 112
Cdd:cd09993    1 HRFPMRKYGLLREALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLESLKSGELSREEIRR----IGFP---WSPELVER 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 113 AYLAAGSVIEVAERVakgeLSSAFAIvRPPG--HHAEQNEPMGFCLYNNVAIATSFLLNERPdIKKILIVDWDVHHGNGT 190
Cdd:cd09993   74 TRLAVGGTILAARLA----LEHGLAI-NLAGgtHHAFPDRGEGFCVFNDIAIAARVLLAEGL-VRRVLIVDLDVHQGNGT 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 191 QKMFWKDPRVLFFSVHRhefGSFYPANDEgfyamtgegPGagyNINVPWENGrCGDADYLAVWDHILIPVAKDFNPDIVI 270
Cdd:cd09993  148 AAIFADDPSVFTFSMHG---EKNYPFRKE---------PS---DLDVPLPDG-TGDDEYLAALEEALPRLLAEFRPDLVF 211

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 731425430 271 ISAGFDAAIGDPLGGCHVTPYGysVMLKKLMEFSEGK-----IIMALEGGYN 317
Cdd:cd09993  212 YNAGVDVLAGDRLGRLSLSLEG--LRERDRLVLRFARargipVAMVLGGGYS 261
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
 115-317 5.01e-31

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: 123.14  E-value: 5.01e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 115 LAAGSVIEVAERVAKgELSSAFAIVRPPG-HHAEQNEPMGFCLYNNVAIATSFLlnERPDIKKILIVDWDVHHGNGTQKM 193
Cdd:cd11680   86 LVAGSSLALAKHLIT-QVERDIAINWYGGrHHAQKSRASGFCYVNDIVLAILRL--RRARFRRVFYLDLDLHHGDGVESA 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 194 FWKDPRVLFFSVHRHefgsfypanDEGFYAMTG--EGPGAGYNINVPWENGrCGDADYLAVWDHILIPVAKDFNPDIVII 271
Cdd:cd11680  163 FFFSKNVLTCSIHRY---------DPGFFPGTGslKNSSDKGMLNIPLKRG-LSDKTLLRIIDSIVRPLIEKFEPEVIVI 232

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 731425430 272 SAGFDAAIGDPLGGCHVTPYGYSVMLKKLMEFSEGKIIMAL-EGGYN 317
Cdd:cd11680  233 QCGCDGLSGDPHKEWNLTIRGYGSVIELLLKEFKDKPTLLLgGGGYN 279
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
 26-322 1.91e-30

Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues in histone amino termini to yield a deacetylated histone (EC 3.5.1.98). Enzymes belonging to this group participate in regulation of a number of processes through protein (mostly different histones) modification (deacetylation). Class I histone deacetylases in general act via the formation of large multiprotein complexes. This group includes animal HDAC1, HDAC2, HDAC3, HDAC8, fungal RPD3, HOS1 and HOS2, plant HDA9, protist, archaeal and bacterial (AcuC) deacetylases. Members of this class are involved in cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and in posttranslational control of the acetyl coenzyme A synthetase. In mammals, they are known to be involved in progression of various tumors. Specific inhibitors of mammalian histone deacetylases are an emerging class of promising novel anticancer drugs.


Pssm-ID: 212517 [Multi-domain]  Cd Length: 306  Bit Score: 121.54  E-value: 1.91e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  26 ATADGDPHPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNLIKNISSKQfDSRRNRIASKFNSIYM 105
Cdd:cd09991    8 NYYYGQGHPMKPHRIRMTHSLILSYGLYKKMEIYRPRPATAEELTKFHSDDYIDFLRSVSPDN-MKEFKKQLERFNVGED 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 106 N---EGSSEAAYLAAGSVIEVAERVAKGELSSAfaiVRPPG--HHAEQNEPMGFCLYNNVAIATSFLL--NERpdikkIL 178
Cdd:cd09991   87 CpvfDGLYEYCQLYAGGSIAAAVKLNRGQADIA---INWAGglHHAKKSEASGFCYVNDIVLAILELLkyHQR-----VL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 179 IVDWDVHHGNGTQKMFWKDPRVLFFSVHRheFGSFYPANDEGFYamTGEGPGAGYNINVPWENGrCGDADYLAVWDHILI 258
Cdd:cd09991  159 YIDIDIHHGDGVEEAFYTTDRVMTVSFHK--FGEYFFPGTGLRD--IGAGKGKYYAVNVPLKDG-IDDESYLQIFEPVLS 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 731425430 259 PVAKDFNPDIVIISAGFDAAIGDPLGGCHVTPYGYSVMLKKLMEFsEGKIIMALEGGYNLVSLA 322
Cdd:cd09991  234 KVMEVFQPSAVVLQCGADSLAGDRLGCFNLSIKGHAKCVKFVKSF-NIPLLVLGGGGYTLRNVA 296
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
 30-284 8.50e-30

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: 119.87  E-value: 8.50e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  30 GDPHPENPDRIrAIWKKLESA-GIPQRCVVFNAKEAEDKHILSVHSNNHVNLIKNISSKQFDSRRNRIASKFN-----SI 103
Cdd:cd11598   15 GRTHPMKPFRL-TLTKHLVMGyGLHKAMDTYEARAATREELRQFHDADYLDFLSKVSPENANQLRFDKAEPFNigddcPV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 104 YmnEGSSEAAYLAAGSVIEVAERVAKGelSSAFAIVRPPG-HHAEQNEPMGFCLYNNVAIATSFLLNERPdikKILIVDW 182
Cdd:cd11598   94 F--DGMYDYCQLYAGASLDAARKLCSG--QSDIAINWSGGlHHAKKSEASGFCYVNDIVLAILNLLRYFP---RVLYIDI 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 183 DVHHGNGTQKMFWKDPRVLFFSVHRHEfGSFYPANdeGFYAMTGEGPGAGYNINVPWENGrCGDADYLAVWDHILIPVAK 262
Cdd:cd11598  167 DVHHGDGVEEAFYRTDRVMTLSFHKYN-GEFFPGT--GDLDDNGGTPGKHFALNVPLEDG-IDDEQYNLLFKSIIGPTIE 242

                        250       260
                 ....*....|....*....|..
gi 731425430 263 DFNPDIVIISAGFDAAIGDPLG 284
Cdd:cd11598  243 KFQPSAIVLQCGADSLGGDRLG 264
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
 11-322 1.04e-26

reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I Zn-dependent Histone deacetylases that catalyze hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). RPD3 is the yeast homolog of class I HDACs. The main function of RPD3-like group members is regulation of a number of different processes through protein (mostly different histones) modification (deacetylation). This group includes fungal RPD3 and acts via the formation of large multiprotein complexes. Members of this group are involved in cell cycle regulation, DNA damage response, embryonic development and cytokine signaling important for immune response. Histone deacetylation by yeast RPD3 represses genes regulated by the Ash1 and Ume6 DNA-binding proteins. In mammals, they are known to be involved in progression of various tumors. Specific inhibitors of mammalian histone deacetylases could be a therapeutic drug option.


Pssm-ID: 212528 [Multi-domain]  Cd Length: 375  Bit Score: 112.21  E-value: 1.04e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  11 RRRVGLVYDDRMCEHATADGdpHPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNLIKNISSKQFD 90
Cdd:cd10004    1 KKKVAYFYDSDVGNYAYGPG--HPMKPHRIRMAHSLVMNYGLYKKMEIYRAKPATKNEMTQFHTDEYIDFLSRVTPDNME 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  91 SRRnRIASKFN---SIYMNEGSSEAAYLAAGSVIEVAERVAKGELSSAfaiVRPPG--HHAEQNEPMGFCLYNNVAIATS 165
Cdd:cd10004   79 KFQ-KEQVKYNvgdDCPVFDGLFEFCSISAGGSMEGAARLNRGKCDIA---VNWAGglHHAKKSEASGFCYVNDIVLGIL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 166 FLLNERPdikKILIVDWDVHHGNGTQKMFWKDPRVLFFSVHRheFGSFYPANDEgfYAMTGEGPGAGYNINVPWENGrCG 245
Cdd:cd10004  155 ELLRYHQ---RVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHK--YGEYFPGTGE--LRDIGIGTGKNYAVNVPLRDG-ID 226

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 731425430 246 DADYLAVWDHILIPVAKDFNPDIVIISAGFDAAIGDPLGGCHVTPYGYSVMLKKLMEFSEGKIIMAlEGGYNLVSLA 322
Cdd:cd10004  227 DESYKSIFEPVIKHVMEWYQPEAVVLQCGGDSLSGDRLGCFNLSMKGHANCVNFVKSFNLPMLVLG-GGGYTMRNVA 302
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
 11-322 1.94e-26

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: 111.31  E-value: 1.94e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  11 RRRVGLVYDDRMCEHATADGdpHPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNLIKNISSKQFd 90
Cdd:cd10010    5 KKKVCYYYDGDVGNYYYGQG--HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNM- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  91 SRRNRIASKFN---SIYMNEGSSEAAYLAAGSVIEVAERVAKGElsSAFAIVRPPG-HHAEQNEPMGFCLYNNVAIATSF 166
Cdd:cd10010   82 SEYSKQMQRFNvgeDCPVFDGLFEFCQLSAGGSVASAVKLNKQQ--TDIAVNWAGGlHHAKKSEASGFCYVNDIVLAILE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 167 LLNERpdiKKILIVDWDVHHGNGTQKMFWKDPRVLffSVHRHEFGSFYPANdeGFYAMTGEGPGAGYNINVPWENGrCGD 246
Cdd:cd10010  160 LLKYH---QRVLYIDIDIHHGDGVEEAFYTTDRVM--TVSFHKYGEYFPGT--GDLRDIGAGKGKYYAVNYPLRDG-IDD 231

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 731425430 247 ADYLAVWDHILIPVAKDFNPDIVIISAGFDAAIGDPLGGCHVTPYGYSVMLKKLMEFSEgKIIMALEGGYNLVSLA 322
Cdd:cd10010  232 ESYEAIFKPVMSKVMEMFQPSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEFVKSFNL-PMLMLGGGGYTIRNVA 306
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
 101-327 5.75e-26

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: 109.85  E-value: 5.75e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 101 NSIYMNEGSSEAAYLAAGSVIEVAERVAKGELS---SAFAIVRPPGHHAEQNEPMGFCLYNNV--AIATSFLlneRPDIK 175
Cdd:cd09998   74 GDLYLCPESLDAIQGALGAVCEAVDSVFKPESPgtkRAFVAIRPPGHHCSESTPSGFCWVNNVhvGAAHAYL---THGIT 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 176 KILIVDWDVHHGNGTQ------------------------KMFWKDPRVLFFSVhrHEFGSfYPANDeGFYAM------T 225
Cdd:cd09998  151 RVVILDIDLHHGNGTQdiawrinaeankqalesssyddfkPAGAPGLRIFYSSL--HDINS-FPCED-GDPAKvkdasvS 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 226 GEGPgAGYNI-NV---PWENgrcgDADYLAVWD---HILIPVAKDF-------NPD--IVIISAGFDAAIGDPLG----G 285
Cdd:cd09998  227 IDGA-HGQWIwNVhlqPWTT----EEDFWELYYpkyRILFEKAAEFlrlttaaTPFktLVFISAGFDASEHEYESmqrhG 301

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 731425430 286 CHVTPYGYSVMLKKLMEFSE----GKIIMALEGGYNLVSLANSVLA 327
Cdd:cd09998  302 VNVPTSFYYRFARDAVRFADahahGRLISVLEGGYSDRALCSGVLA 347
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
 11-322 2.03e-21

Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme that catalyzes hydrolysis of N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. HDAC2 is involved in regulation through association with DNA binding proteins to target specific chromatin regions. It forms transcriptional repressor complexes by associating with several proteins, including the mammalian zinc-finger transcription factor YY1, thus playing an important role in transcriptional regulation, cell cycle progression and developmental events. Additionally, a few non-histone HDAC2 substrates have been found. HDAC2 plays a role in embryonic development and cytokine signaling important for immune response, and is over-expressed in several solid tumors including oral, prostate, ovarian, endometrial and gastric cancer. It participates in DNA-damage response, along with HDAC1; together, they can promote DNA non-homologous end-joining. HDAC2 is considered an important cancer prognostic marker. Inhibitors specifically targeting HDAC2 could be a therapeutic drug option.


Pssm-ID: 212535 [Multi-domain]  Cd Length: 366  Bit Score: 96.29  E-value: 2.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  11 RRRVGLVYDDRMCEHATADGdpHPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNLIKNISSKQFd 90
Cdd:cd10011    1 KKKVCYYYDGDIGNYYYGQG--HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNM- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  91 SRRNRIASKFN---SIYMNEGSSEAAYLAAGSVIEVAERVAKGELSSAfaiVRPPG--HHAEQNEPMGFCLYNNVAIATS 165
Cdd:cd10011   78 SEYSKQMQRFNvgeDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMA---VNWAGglHHAKKSEASGFCYVNDIVLAIL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 166 FLLNERpdiKKILIVDWDVHHGNGTQKMFWKDPRVLffSVHRHEFGSFYPANdeGFYAMTGEGPGAGYNINVPWENGrCG 245
Cdd:cd10011  155 ELLKYH---QRVLYIDIDIHHGDGVEEAFYTTDRVM--TVSFHKYGEYFPGT--GDLRDIGAGKGKYYAVNFPMRDG-ID 226

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 731425430 246 DADYLAVWDHILIPVAKDFNPDIVIISAGFDAAIGDPLGGCHVTPYGYSVMLKKLMEFSEgKIIMALEGGYNLVSLA 322
Cdd:cd10011  227 DESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNL-PLLMLGGGGYTIRNVA 302
PTZ00063 PTZ00063
histone deacetylase; Provisional
 11-322 1.71e-18

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 88.33  E-value: 1.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  11 RRRVGLVYDDRMCEHATADGdpHPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNLIKNIS---SK 87
Cdd:PTZ00063   3 RKRVSYFYDPDIGSYYYGPG--HPMKPQRIRMAHALILSYDLYKHMEIYRPHKSVEPELVLFHDEEYVDFLSSISpenYR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  88 QFDSRRNRiaskFN-----SIYMNEGSSEAAYLAAGSVIEVAERVAKGElsSAFAIVRPPG-HHAEQNEPMGFCLYNNVA 161
Cdd:PTZ00063  81 DFTYQLKR----FNvgeatDCPVFDGLFEFQQSCAGASIDGAYKLNNHQ--ADICVNWSGGlHHAKRSEASGFCYINDIV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 162 IATSFLLNERpdiKKILIVDWDVHHGNGTQKMFWKDPRVLFFSVHRheFGSFYPANdeGFYAMTGEGPGAGYNINVPWEN 241
Cdd:PTZ00063 155 LGILELLKYH---ARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHK--FGDFFPGT--GDVTDIGVAQGKYYSVNVPLND 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 242 GrCGDADYLAVWDHILIPVAKDFNPDIVIISAGFDAAIGDPLGGCHVTPYGYSVMLKKLMEFSEGKIIMAlEGGYNLVSL 321
Cdd:PTZ00063 228 G-IDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAACVEFVRSLNIPLLVLG-GGGYTIRNV 305


                 .
gi 731425430 322 A 322
Cdd:PTZ00063 306 A 306
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
 30-322 4.84e-17

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: 83.60  E-value: 4.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430  30 GDPHPENPDRIRAIWKKLESAGIPQRCVVFNAKEAEDKHILSVHSNNHVNLIKNISSKQFDSRRNRIaSKFN---SIYMN 106
Cdd:cd10005   17 GPGHPMKPHRLALTHSLVLHYGLYKKMQVYKPYRASAHDMCRFHSEDYIDFLQRVTPQNIQGFTKSL-NQFNvgdDCPVF 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 107 EGSSEAAYLAAGSVIEVAERVAKGElsSAFAIVRPPG-HHAEQNEPMGFCLYNNVAIATSFLLNERPdikKILIVDWDVH 185
Cdd:cd10005   96 PGLFDFCSMYTGASLEGATKLNHKI--CDIAINWSGGlHHAKKFEASGFCYVNDIVIAILELLKYHP---RVLYIDIDIH 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 186 HGNGTQKMFWKDPRVLFFSVHRHEfGSFYPANdeGFYAMTGEGPGAGYNINVPWENGrCGDADYLAVWDHILIPVAKDFN 265
Cdd:cd10005  171 HGDGVQEAFYLTDRVMTVSFHKYG-NYFFPGT--GDMYEVGAESGRYYSVNVPLKDG-IDDQSYLQLFKPVIQQVIDFYQ 246

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 731425430 266 PDIVIISAGFDAAIGDPLGGCHVTPYGYSVMLKKLMEFSEGKIIMAlEGGYNLVSLA 322
Cdd:cd10005  247 PTCIVLQCGADSLGCDRLGCFNLSIKGHGECVEFVKSFNIPLLVLG-GGGYTVRNVA 302
PTZ00346 PTZ00346
histone deacetylase; Provisional
 144-315 1.25e-15

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 79.69  E-value: 1.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 144 HHAEQNEPMGFCLYNNVAIATSFLLNERpdiKKILIVDWDVHHGNGTQKMFWKDPRVlfFSVHRHEFG-SFYPANdeGFY 222
Cdd:PTZ00346 154 HHSKCGECSGFCYVNDIVLGILELLKCH---DRVLYVDIDMHHGDGVDEAFCTSDRV--FTLSLHKFGeSFFPGT--GHP 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 223 AMTGEGPGAGYNINVPWENGrCGDADYLAVWDHILIPVAKDFNPDIVIISAGFDAAIGDPLGGCHVTPYGYSVMLKKLME 302
Cdd:PTZ00346 227 RDVGYGRGRYYSMNLAVWDG-ITDFYYLGLFEHALHSIVRRYSPDAIVLQCGADSLAGDRLGLLNLSSFGHGQCVQAVRD 305

                        170
                 ....*....|...
gi 731425430 303 FseGKIIMALEGG 315
Cdd:PTZ00346 306 L--GIPMLALGGG 316
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 109-334 3.99e-07

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: 51.22  E-value: 3.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 109 SSEAAYLAAGSVIEVAERVAkgelsSAFAIVrppGHHAEQNEpmgfclyNNVAIAtsfLLNERpdikkILIVDWDVHHGN 188
Cdd:cd09987    7 KAEAHELLAGVVVAVLKDGK-----VPVVLG---GDHSIANG-------AIRAVA---ELHPD-----LGVIDVDAHHDV 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 189 GTQKMFWK--------------DPRVLFFSVHRHEFGSFYPAndegfyamtGEGPGAGYNINVPWENGRcgDADYLAVWD 254
Cdd:cd09987   64 RTPEAFGKgnhhtprhllceplISDVHIVSIGIRGVSNGEAG---------GAYARKLGVVYFSMTEVD--KLGLGDVFE 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731425430 255 HILIPVakDFNPDIVIISAGFDAAIGDPLGGCHvTPYGYSVMLKKLMEFSE------GKIIMALEGGYNLVSLA-NSVLA 327
Cdd:cd09987  133 EIVSYL--GDKGDNVYLSVDVDGLDPSFAPGTG-TPGPGGLSYREGLYITEriaktnLVVGLDIVEVNPLLDETgRTARL 209


                 ....*..
gi 731425430 328 CVEVLLE 334
Cdd:cd09987  210 AAALTLE 216
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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