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Conserved domains on  [gi|30692236|ref|NP_190054|]
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histone deacetylase 9 [Arabidopsis thaliana]

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 ...
6-384 0e+00

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 cd10005:

Pssm-ID: 450134  Cd Length: 381  Bit Score: 637.13  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236   6 KISYFYDGDVGSVYFGPNHPMKPHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVEFLQRINPENQNLFPN 85
Cdd:cd10005   2 RVAYFYDPDVGNFHYGPGHPMKPHRLALTHSLVLHYGLYKKMQVYKPYRASAHDMCRFHSEDYIDFLQRVTPQNIQGFTK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  86 EMARYNLGEDCPVFEDLFEFCQLYAGGTIDAARRLNNKLCDIAINWAGGLHHAKKCDASGFCYINDLVLGILELLKHHPR 165
Cdd:cd10005  82 SLNQFNVGDDCPVFPGLFDFCSMYTGASLEGATKLNHKICDIAINWSGGLHHAKKFEASGFCYVNDIVIAILELLKYHPR 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 166 VLYIDIDVHHGDGVEEAFYFTDRVMTVSFHKFGDKFFPGTGDVKEIGEREGKFYAINVPLKDGIDDSSFNRLFRTIISKV 245
Cdd:cd10005 162 VLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYSVNVPLKDGIDDQSYLQLFKPVIQQV 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 246 VEIYQPGAIVLQCGADSLARDRLGCFNLSIDGHAECVKFVKKFNLPLLVTGGGGYTKENVARCWTVETGILLDTELPNEI 325
Cdd:cd10005 242 IDFYQPTCIVLQCGADSLGCDRLGCFNLSIKGHGECVEFVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVDEEISNEL 321
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30692236 326 PENDYIKYFAPDFSLkIP--GGHIENLNTKSYISSIKVQILENLRYIQHAPSVQMQEVPPD 384
Cdd:cd10005 322 PYNEYFEYFAPDFTL-HPdvSTRIENQNSKQYLDQIRQTVFENLKMLNHAPSVQMQDVPPD 381
 
Name Accession Description Interval E-value
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
6-384 0e+00

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: 637.13  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236   6 KISYFYDGDVGSVYFGPNHPMKPHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVEFLQRINPENQNLFPN 85
Cdd:cd10005   2 RVAYFYDPDVGNFHYGPGHPMKPHRLALTHSLVLHYGLYKKMQVYKPYRASAHDMCRFHSEDYIDFLQRVTPQNIQGFTK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  86 EMARYNLGEDCPVFEDLFEFCQLYAGGTIDAARRLNNKLCDIAINWAGGLHHAKKCDASGFCYINDLVLGILELLKHHPR 165
Cdd:cd10005  82 SLNQFNVGDDCPVFPGLFDFCSMYTGASLEGATKLNHKICDIAINWSGGLHHAKKFEASGFCYVNDIVIAILELLKYHPR 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 166 VLYIDIDVHHGDGVEEAFYFTDRVMTVSFHKFGDKFFPGTGDVKEIGEREGKFYAINVPLKDGIDDSSFNRLFRTIISKV 245
Cdd:cd10005 162 VLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYSVNVPLKDGIDDQSYLQLFKPVIQQV 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 246 VEIYQPGAIVLQCGADSLARDRLGCFNLSIDGHAECVKFVKKFNLPLLVTGGGGYTKENVARCWTVETGILLDTELPNEI 325
Cdd:cd10005 242 IDFYQPTCIVLQCGADSLGCDRLGCFNLSIKGHGECVEFVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVDEEISNEL 321
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30692236 326 PENDYIKYFAPDFSLkIP--GGHIENLNTKSYISSIKVQILENLRYIQHAPSVQMQEVPPD 384
Cdd:cd10005 322 PYNEYFEYFAPDFTL-HPdvSTRIENQNSKQYLDQIRQTVFENLKMLNHAPSVQMQDVPPD 381
PTZ00063 PTZ00063
histone deacetylase; Provisional
6-396 0e+00

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 585.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236    6 KISYFYDGDVGSVYFGPNHPMKPHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVEFLQRINPENQNLFPN 85
Cdd:PTZ00063   5 RVSYFYDPDIGSYYYGPGHPMKPQRIRMAHALILSYDLYKHMEIYRPHKSVEPELVLFHDEEYVDFLSSISPENYRDFTY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236   86 EMARYNLGE--DCPVFEDLFEFCQLYAGGTIDAARRLNNKLCDIAINWAGGLHHAKKCDASGFCYINDLVLGILELLKHH 163
Cdd:PTZ00063  85 QLKRFNVGEatDCPVFDGLFEFQQSCAGASIDGAYKLNNHQADICVNWSGGLHHAKRSEASGFCYINDIVLGILELLKYH 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  164 PRVLYIDIDVHHGDGVEEAFYFTDRVMTVSFHKFGDkFFPGTGDVKEIGEREGKFYAINVPLKDGIDDSSFNRLFRTIIS 243
Cdd:PTZ00063 165 ARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKFGD-FFPGTGDVTDIGVAQGKYYSVNVPLNDGIDDDSFVDLFKPVIS 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  244 KVVEIYQPGAIVLQCGADSLARDRLGCFNLSIDGHAECVKFVKKFNLPLLVTGGGGYTKENVARCWTVETGILLD--TEL 321
Cdd:PTZ00063 244 KCVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAACVEFVRSLNIPLLVLGGGGYTIRNVARCWAYETGVILNkhDEM 323
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30692236  322 PNEIPENDYIKYFAPDFSLKIPGGHIENLNTKSYISSIKVQILENLRYIQHAPSVQMQEVPPDFYIPDFD-EDEQN 396
Cdd:PTZ00063 324 SDQISLNDYYDYYAPDFQLHLQPSNIPNYNSPEHLEKIKVKILENLRYLEHAPGVQFAYVPPDFFDRDIDdEDEKN 399
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
24-316 2.57e-111

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: 328.81  E-value: 2.57e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236    24 HPMKPHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVEFLQRINPENQNLfpNEMARYNLGEDCPVFEDLF 103
Cdd:pfam00850   1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAAPEGGAL--LLLSYLSGDDDTPVSPGSY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236   104 EFCQLYAGGTIDAARRLNNK--LCDIAINWaGGLHHAKKCDASGFCYINDLVLGILELLKHH--PRVLYIDIDVHHGDGV 179
Cdd:pfam00850  79 EAALLAAGGTLAAADAVLSGeaRNAFALVR-PPGHHAERDRASGFCIFNNVAIAAKYLREKYglKRVAIVDFDVHHGNGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236   180 EEAFYFTDRVMTVSFHKFGDKFFPGTGDVKEIGEREGKFYAINVPLKDGIDDSSFNRLFRTIISKVVEIYQPGAIVLQCG 259
Cdd:pfam00850 158 QEIFYDDPSVLTLSIHQYPGGFYPGTGFADETGEGKGKGYTLNVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAG 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30692236   260 ADSLARDRLGCFNLSIDGHAECVKFVKKFNL----PLLVTGGGGYTKENVARCWTVETGIL 316
Cdd:pfam00850 238 FDAHAGDPLGGLNLTTEGFAEITRILLELADplciRVVSVLEGGYNLDALARSATAVLAAL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
20-310 1.05e-90

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 276.60  E-value: 1.05e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  20 FGPNHPMKPHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVEFLQRINPENqnlfpnemARYNLGEDCPVF 99
Cdd:COG0123  14 LGPGHPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAASLDG--------GYGQLDPDTPVS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 100 EDLFEFCQLYAGGTIDAARRLNNKLCDIA-INWAGGLHHAKKCDASGFCYINDLVLGILELLKH-HPRVLYIDIDVHHGD 177
Cdd:COG0123  86 PGTWEAALLAAGGALAAADAVLEGEARNAfALVRPPGHHAERDRAMGFCLFNNAAIAARYLLAKgLERVAIVDFDVHHGN 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 178 GVEEAFYFTDRVMTVSFHkfGDKFFPGTGDVKEIGEREGKFYAINVPLKDGIDDSSFNRLFRTIISKVVEIYQPGAIVLQ 257
Cdd:COG0123 166 GTQDIFYDDPDVLTISIH--QDPLYPGTGAADETGEGAGEGSNLNVPLPPGTGDAEYLAALEEALLPALEAFKPDLIVVS 243
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 30692236 258 CGADSLARDRLGCFNLSIDGHAECVKFVKKF----NLPLLVTGGGGYTKENVARCWT 310
Cdd:COG0123 244 AGFDAHADDPLGRLNLTTEGYAWRTRRVLELadhcGGPVVSVLEGGYNLDALARSVA 300
 
Name Accession Description Interval E-value
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
6-384 0e+00

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: 637.13  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236   6 KISYFYDGDVGSVYFGPNHPMKPHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVEFLQRINPENQNLFPN 85
Cdd:cd10005   2 RVAYFYDPDVGNFHYGPGHPMKPHRLALTHSLVLHYGLYKKMQVYKPYRASAHDMCRFHSEDYIDFLQRVTPQNIQGFTK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  86 EMARYNLGEDCPVFEDLFEFCQLYAGGTIDAARRLNNKLCDIAINWAGGLHHAKKCDASGFCYINDLVLGILELLKHHPR 165
Cdd:cd10005  82 SLNQFNVGDDCPVFPGLFDFCSMYTGASLEGATKLNHKICDIAINWSGGLHHAKKFEASGFCYVNDIVIAILELLKYHPR 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 166 VLYIDIDVHHGDGVEEAFYFTDRVMTVSFHKFGDKFFPGTGDVKEIGEREGKFYAINVPLKDGIDDSSFNRLFRTIISKV 245
Cdd:cd10005 162 VLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYSVNVPLKDGIDDQSYLQLFKPVIQQV 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 246 VEIYQPGAIVLQCGADSLARDRLGCFNLSIDGHAECVKFVKKFNLPLLVTGGGGYTKENVARCWTVETGILLDTELPNEI 325
Cdd:cd10005 242 IDFYQPTCIVLQCGADSLGCDRLGCFNLSIKGHGECVEFVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVDEEISNEL 321
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30692236 326 PENDYIKYFAPDFSLkIP--GGHIENLNTKSYISSIKVQILENLRYIQHAPSVQMQEVPPD 384
Cdd:cd10005 322 PYNEYFEYFAPDFTL-HPdvSTRIENQNSKQYLDQIRQTVFENLKMLNHAPSVQMQDVPPD 381
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
10-316 0e+00

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: 599.95  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  10 FYDGDVGSVYFGPNHPMKPHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVEFLQRINPENQNLFPNEMAR 89
Cdd:cd09991   1 FYDPDVGNYYYGQGHPMKPHRIRMTHSLILSYGLYKKMEIYRPRPATAEELTKFHSDDYIDFLRSVSPDNMKEFKKQLER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  90 YNLGEDCPVFEDLFEFCQLYAGGTIDAARRLNNKLCDIAINWAGGLHHAKKCDASGFCYINDLVLGILELLKHHPRVLYI 169
Cdd:cd09991  81 FNVGEDCPVFDGLYEYCQLYAGGSIAAAVKLNRGQADIAINWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 170 DIDVHHGDGVEEAFYFTDRVMTVSFHKFGDKFFPGTGDvKEIGEREGKFYAINVPLKDGIDDSSFNRLFRTIISKVVEIY 249
Cdd:cd09991 161 DIDIHHGDGVEEAFYTTDRVMTVSFHKFGEYFFPGTGL-RDIGAGKGKYYAVNVPLKDGIDDESYLQIFEPVLSKVMEVF 239
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30692236 250 QPGAIVLQCGADSLARDRLGCFNLSIDGHAECVKFVKKFNLPLLVTGGGGYTKENVARCWTVETGIL 316
Cdd:cd09991 240 QPSAVVLQCGADSLAGDRLGCFNLSIKGHAKCVKFVKSFNIPLLVLGGGGYTLRNVARCWTYETAVL 306
PTZ00063 PTZ00063
histone deacetylase; Provisional
6-396 0e+00

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 585.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236    6 KISYFYDGDVGSVYFGPNHPMKPHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVEFLQRINPENQNLFPN 85
Cdd:PTZ00063   5 RVSYFYDPDIGSYYYGPGHPMKPQRIRMAHALILSYDLYKHMEIYRPHKSVEPELVLFHDEEYVDFLSSISPENYRDFTY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236   86 EMARYNLGE--DCPVFEDLFEFCQLYAGGTIDAARRLNNKLCDIAINWAGGLHHAKKCDASGFCYINDLVLGILELLKHH 163
Cdd:PTZ00063  85 QLKRFNVGEatDCPVFDGLFEFQQSCAGASIDGAYKLNNHQADICVNWSGGLHHAKRSEASGFCYINDIVLGILELLKYH 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  164 PRVLYIDIDVHHGDGVEEAFYFTDRVMTVSFHKFGDkFFPGTGDVKEIGEREGKFYAINVPLKDGIDDSSFNRLFRTIIS 243
Cdd:PTZ00063 165 ARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKFGD-FFPGTGDVTDIGVAQGKYYSVNVPLNDGIDDDSFVDLFKPVIS 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  244 KVVEIYQPGAIVLQCGADSLARDRLGCFNLSIDGHAECVKFVKKFNLPLLVTGGGGYTKENVARCWTVETGILLD--TEL 321
Cdd:PTZ00063 244 KCVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAACVEFVRSLNIPLLVLGGGGYTIRNVARCWAYETGVILNkhDEM 323
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30692236  322 PNEIPENDYIKYFAPDFSLKIPGGHIENLNTKSYISSIKVQILENLRYIQHAPSVQMQEVPPDFYIPDFD-EDEQN 396
Cdd:PTZ00063 324 SDQISLNDYYDYYAPDFQLHLQPSNIPNYNSPEHLEKIKVKILENLRYLEHAPGVQFAYVPPDFFDRDIDdEDEKN 399
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
4-379 0e+00

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: 543.25  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236   4 KDKISYFYDGDVGSVYFGPNHPMKPHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVEFLQRINPENQNLF 83
Cdd:cd10004   1 KKKVAYFYDSDVGNYAYGPGHPMKPHRIRMAHSLVMNYGLYKKMEIYRAKPATKNEMTQFHTDEYIDFLSRVTPDNMEKF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  84 PNEMARYNLGEDCPVFEDLFEFCQLYAGGTIDAARRLNNKLCDIAINWAGGLHHAKKCDASGFCYINDLVLGILELLKHH 163
Cdd:cd10004  81 QKEQVKYNVGDDCPVFDGLFEFCSISAGGSMEGAARLNRGKCDIAVNWAGGLHHAKKSEASGFCYVNDIVLGILELLRYH 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 164 PRVLYIDIDVHHGDGVEEAFYFTDRVMTVSFHKFGDkFFPGTGDVKEIGEREGKFYAINVPLKDGIDDSSFNRLFRTIIS 243
Cdd:cd10004 161 QRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYGE-YFPGTGELRDIGIGTGKNYAVNVPLRDGIDDESYKSIFEPVIK 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 244 KVVEIYQPGAIVLQCGADSLARDRLGCFNLSIDGHAECVKFVKKFNLPLLVTGGGGYTKENVARCWTVETGILLDTELPN 323
Cdd:cd10004 240 HVMEWYQPEAVVLQCGGDSLSGDRLGCFNLSMKGHANCVNFVKSFNLPMLVLGGGGYTMRNVARTWAFETGLLAGEELDK 319
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 30692236 324 EIPENDYIKYFAPDFSLKIPGGHIENLNTKSYISSIKVQILENLRYIQHAPSVQMQ 379
Cdd:cd10004 320 DLPYNEYYEYYGPDYELNVRPSNMENHNTPEYLDKITTAVIENLRNTSFAPSVQMQ 375
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
3-370 0e+00

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: 521.93  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236   3 SKDKISYFYDGDVGSVYFGPNHPMKPHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVEFLQRINPENQNL 82
Cdd:cd10010   4 TKKKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  83 FPNEMARYNLGEDCPVFEDLFEFCQLYAGGTIDAARRLNNKLCDIAINWAGGLHHAKKCDASGFCYINDLVLGILELLKH 162
Cdd:cd10010  84 YSKQMQRFNVGEDCPVFDGLFEFCQLSAGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 163 HPRVLYIDIDVHHGDGVEEAFYFTDRVMTVSFHKFGDkFFPGTGDVKEIGEREGKFYAINVPLKDGIDDSSFNRLFRTII 242
Cdd:cd10010 164 HQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGE-YFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVM 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 243 SKVVEIYQPGAIVLQCGADSLARDRLGCFNLSIDGHAECVKFVKKFNLPLLVTGGGGYTKENVARCWTVETGILLDTELP 322
Cdd:cd10010 243 SKVMEMFQPSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDSEIP 322
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 30692236 323 NEIPENDYIKYFAPDFSLKIPGGHIENLNTKSYISSIKVQILENLRYI 370
Cdd:cd10010 323 NELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRML 370
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
4-370 1.56e-180

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: 507.68  E-value: 1.56e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236   4 KDKISYFYDGDVGSVYFGPNHPMKPHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVEFLQRINPENQNLF 83
Cdd:cd10011   1 KKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  84 PNEMARYNLGEDCPVFEDLFEFCQLYAGGTIDAARRLNNKLCDIAINWAGGLHHAKKCDASGFCYINDLVLGILELLKHH 163
Cdd:cd10011  81 SKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYH 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 164 PRVLYIDIDVHHGDGVEEAFYFTDRVMTVSFHKFGDKfFPGTGDVKEIGEREGKFYAINVPLKDGIDDSSFNRLFRTIIS 243
Cdd:cd10011 161 QRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEY-FPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQIFKPIIS 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 244 KVVEIYQPGAIVLQCGADSLARDRLGCFNLSIDGHAECVKFVKKFNLPLLVTGGGGYTKENVARCWTVETGILLDTELPN 323
Cdd:cd10011 240 KVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLGGGGYTIRNVARCWTYETAVALDCEIPN 319
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 30692236 324 EIPENDYIKYFAPDFSLKIPGGHIENLNTKSYISSIKVQILENLRYI 370
Cdd:cd10011 320 ELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYMEKIKQRLFENLRML 366
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
7-316 5.33e-172

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: 483.50  E-value: 5.33e-172
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236   7 ISYFYDGDVGSVYFGPNHPMKPHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVEFLQRINPENQN-LFPN 85
Cdd:cd11598   1 VSYHFNSRVEDYHFGRTHPMKPFRLTLTKHLVMGYGLHKAMDTYEARAATREELRQFHDADYLDFLSKVSPENANqLRFD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  86 EMARYNLGEDCPVFEDLFEFCQLYAGGTIDAARRLNNKLCDIAINWAGGLHHAKKCDASGFCYINDLVLGILELLKHHPR 165
Cdd:cd11598  81 KAEPFNIGDDCPVFDGMYDYCQLYAGASLDAARKLCSGQSDIAINWSGGLHHAKKSEASGFCYVNDIVLAILNLLRYFPR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 166 VLYIDIDVHHGDGVEEAFYFTDRVMTVSFHKFGDKFFPGTGDVKEIGEREGKFYAINVPLKDGIDDSSFNRLFRTIISKV 245
Cdd:cd11598 161 VLYIDIDVHHGDGVEEAFYRTDRVMTLSFHKYNGEFFPGTGDLDDNGGTPGKHFALNVPLEDGIDDEQYNLLFKSIIGPT 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30692236 246 VEIYQPGAIVLQCGADSLARDRLGCFNLSIDGHAECVKFVKKFNLPLLVTGGGGYTKENVARCWTVETGIL 316
Cdd:cd11598 241 IEKFQPSAIVLQCGADSLGGDRLGQFNLNIKAHGACVKFVKSFGIPMLVVGGGGYTPRNVARAWCYETAVA 311
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
23-371 1.19e-150

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: 431.38  E-value: 1.19e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  23 NHPMKPHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVEFLQRINPENQNLFP-NEMARYNLGEDCPVFED 101
Cdd:cd10000  15 RLPKVPNRASMVHSLIEAYGLLKQLRVVKPRVATEEELASFHSDEYIQFLKKASNEGDNDEEpSEQQEFGLGYDCPIFEG 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 102 LFEFCQLYAGGTIDAARRLNNKLCDIAINWAGGLHHAKKCDASGFCYINDLVLGILELLKHHPRVLYIDIDVHHGDGVEE 181
Cdd:cd10000  95 IYDYAAAVAGATLTAAQLLIDGKCKVAINWFGGWHHAQRDEASGFCYVNDIVLGILKLREKFDRVLYVDLDLHHGDGVED 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 182 AFYFTDRVMTVSFHKFGDKFFPGTGDVKEIGEREGKFYAINVPLKDGIDDSSFNRLFRTIISKVVEIYQPGAIVLQCGAD 261
Cdd:cd10000 175 AFSFTSKVMTVSLHKYSPGFFPGTGDVSDVGLGKGKYYTVNVPLRDGIQDEQYLQIFTAVVPEIVAAFRPEAVVLQCGAD 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 262 SLARDRLGCFNLSIDGHAECVKFVKKFNLPLLVTGGGGYTKENVARCWTVETGILLDTELPNEIPENDYIKYFAPDFSLK 341
Cdd:cd10000 255 TLAGDPMGAFNLTPVGIGKCLKYVLGWKLPTLILGGGGYNLANTARCWTYLTGLILGEPLSSDIPDHEFFTSYGPDYELE 334
                       330       340       350
                ....*....|....*....|....*....|
gi 30692236 342 IPGGHIENLNTKSYISSIKVQILENLRYIQ 371
Cdd:cd10000 335 ISPSLRPDLNEDQYIEKILETIKGNLKNVV 364
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
9-310 6.64e-115

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: 338.77  E-value: 6.64e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236   9 YFYDGDVGSVYFGPNHPMKPHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVEFLQRINPENQnlfPNEMA 88
Cdd:cd09994   2 FIYSEEYLRYSFGPNHPFNPPRLSLTKDLLRALGLLPPVDLVPPRPATEEELLLFHTPDYIEAVKEASRGQE---PEGRG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  89 RYNLG-EDCPVFEDLFEFCQLYAGGTIDAARRLNNKLCDIAINWAGGLHHAKKCDASGFCYINDLVLGILELLKHH-PRV 166
Cdd:cd09994  79 RLGLGtEDNPVFPGMHEAAALVVGGTLLAARLVLEGEARRAFNPAGGLHHAMRGRASGFCVYNDAAVAIERLRDKGgLRV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 167 LYIDIDVHHGDGVEEAFYFTDRVMTVSFHKFGDKFFPGTGDVKEIGEREGKFYAINVPLKDGIDDSSFNRLFRTIISKVV 246
Cdd:cd09994 159 AYVDIDAHHGDGVQAAFYDDPRVLTISLHESGRYLFPGTGFVDEIGEGEGYGYAVNIPLPPGTGDDEFLRAFEAVVPPLL 238
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30692236 247 EIYQPGAIVLQCGADSLARDRLGCFNLSIDGHAECVKFVK-----KFNLPLLVTGGGGYTKENVARCWT 310
Cdd:cd09994 239 RAFRPDVIVSQHGADAHAGDPLTHLNLSNRAYRAAVRRIReladeYCGGRWLALGGGGYNPDVVARAWA 307
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
24-316 2.57e-111

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: 328.81  E-value: 2.57e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236    24 HPMKPHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVEFLQRINPENQNLfpNEMARYNLGEDCPVFEDLF 103
Cdd:pfam00850   1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAAPEGGAL--LLLSYLSGDDDTPVSPGSY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236   104 EFCQLYAGGTIDAARRLNNK--LCDIAINWaGGLHHAKKCDASGFCYINDLVLGILELLKHH--PRVLYIDIDVHHGDGV 179
Cdd:pfam00850  79 EAALLAAGGTLAAADAVLSGeaRNAFALVR-PPGHHAERDRASGFCIFNNVAIAAKYLREKYglKRVAIVDFDVHHGNGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236   180 EEAFYFTDRVMTVSFHKFGDKFFPGTGDVKEIGEREGKFYAINVPLKDGIDDSSFNRLFRTIISKVVEIYQPGAIVLQCG 259
Cdd:pfam00850 158 QEIFYDDPSVLTLSIHQYPGGFYPGTGFADETGEGKGKGYTLNVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAG 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30692236   260 ADSLARDRLGCFNLSIDGHAECVKFVKKFNL----PLLVTGGGGYTKENVARCWTVETGIL 316
Cdd:pfam00850 238 FDAHAGDPLGGLNLTTEGFAEITRILLELADplciRVVSVLEGGYNLDALARSATAVLAAL 298
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
30-316 2.12e-94

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: 285.70  E-value: 2.12e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  30 RLCMTHHLILAYGLH-SKMEVYRPHKAYPIEMAQFHSPDYVEFLQRinpenqnlfpnemaRYNLGEDCPVFEDLFEFCQL 108
Cdd:cd11680  21 RSSLVHSLIRAYGLLqHFDEIIEPERATRKDLTKYHDKDYVDFLLK--------------KYGLEDDCPVFPFLSMYVQL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 109 YAGGTIDAARRLNNKL-CDIAINWAGGLHHAKKCDASGFCYINDLVLGILELLKHH-PRVLYIDIDVHHGDGVEEAFYFT 186
Cdd:cd11680  87 VAGSSLALAKHLITQVeRDIAINWYGGRHHAQKSRASGFCYVNDIVLAILRLRRARfRRVFYLDLDLHHGDGVESAFFFS 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 187 DRVMTVSFHKFGDKFFPGTGDVKEigerEGKFYAINVPLKDGIDDSSFNRLFRTIISKVVEIYQPGAIVLQCGADSLARD 266
Cdd:cd11680 167 KNVLTCSIHRYDPGFFPGTGSLKN----SSDKGMLNIPLKRGLSDKTLLRIIDSIVRPLIEKFEPEVIVIQCGCDGLSGD 242
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 30692236 267 RLGCFNLSIDGHAECVKFVKKF--NLPLLVTGGGGYTKENVARCWTVETGIL 316
Cdd:cd11680 243 PHKEWNLTIRGYGSVIELLLKEfkDKPTLLLGGGGYNHTEAARAWTYLTSMV 294
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
20-310 1.05e-90

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 276.60  E-value: 1.05e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  20 FGPNHPMKPHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVEFLQRINPENqnlfpnemARYNLGEDCPVF 99
Cdd:COG0123  14 LGPGHPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAASLDG--------GYGQLDPDTPVS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 100 EDLFEFCQLYAGGTIDAARRLNNKLCDIA-INWAGGLHHAKKCDASGFCYINDLVLGILELLKH-HPRVLYIDIDVHHGD 177
Cdd:COG0123  86 PGTWEAALLAAGGALAAADAVLEGEARNAfALVRPPGHHAERDRAMGFCLFNNAAIAARYLLAKgLERVAIVDFDVHHGN 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 178 GVEEAFYFTDRVMTVSFHkfGDKFFPGTGDVKEIGEREGKFYAINVPLKDGIDDSSFNRLFRTIISKVVEIYQPGAIVLQ 257
Cdd:COG0123 166 GTQDIFYDDPDVLTISIH--QDPLYPGTGAADETGEGAGEGSNLNVPLPPGTGDAEYLAALEEALLPALEAFKPDLIVVS 243
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 30692236 258 CGADSLARDRLGCFNLSIDGHAECVKFVKKF----NLPLLVTGGGGYTKENVARCWT 310
Cdd:COG0123 244 AGFDAHADDPLGRLNLTTEGYAWRTRRVLELadhcGGPVVSVLEGGYNLDALARSVA 300
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
30-316 3.75e-87

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: 266.61  E-value: 3.75e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  30 RLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVEFLQRINPENQNLfpnEMARYNLGEDCPVFEDLFEFCQLY 109
Cdd:cd09301   1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKANFAVATIT---ESKPVIFGPNFPVQRHYFRGARLS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 110 AGGTIDAARRLNNKLCDIAINWA-GGLHHAKKCDASGFCYINDLVLGILELLKH-HPRVLYIDIDVHHGDGVEEAFYFTD 187
Cdd:cd09301  78 TGGVVEAAELVAKGELERAFAVVgAGGHHAGKSRAWGFCYFNDVVLAIKFLRERgISRILIIDTDAHHGDGTREAFYDDD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 188 RVMTVSFHKFGDKFFpgtgdvkeiGEREGKFYAINVPLKDGIDDSSFNRLFRTIISKVVEIYQPGAIVLQCGADSLARDR 267
Cdd:cd09301 158 RVLHMSFHNYDIYPF---------GRGKGKGYKINVPLEDGLGDEEYLDAVERVISKVLEEFEPEVVVLQFGHDTHEGDR 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 30692236 268 LGCFNLSIDGHAECVKFVKKFN--LPLLVTGGGGYTKENVARCWTVETGIL 316
Cdd:cd09301 229 LGGFNLSEKGFVKLAEIVKEFArgGPILMVLGGGYNPEAAARIWTAIIKEL 279
PTZ00346 PTZ00346
histone deacetylase; Provisional
11-322 4.08e-87

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 271.90  E-value: 4.08e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236   11 YDGDVGSVYFGPNHPMKPHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVEFLQrINPENQNLFPNEMARY 90
Cdd:PTZ00346  30 YASDMNISAFVPQHAMKPYRVLAAMEIVRSLKIDAHCRTVVPPLVKVEELMAYHTDTYLANLG-LHSCRSWLWNAETSKV 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236   91 NLGEDCPVFEDLFEFCQLYAGGTIDAARRLNNKLCDIAINWAGGLHHAKKCDASGFCYINDLVLGILELLKHHPRVLYID 170
Cdd:PTZ00346 109 FFSGDCPPVEGLMEHSIATASGTLMGAVLLNSGQVDVAVHWGGGMHHSKCGECSGFCYVNDIVLGILELLKCHDRVLYVD 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  171 IDVHHGDGVEEAFYFTDRVMTVSFHKFGDKFFPGTGDVKEIGEREGKFYAINVPLKDGIDDSSFNRLFRTIISKVVEIYQ 250
Cdd:PTZ00346 189 IDMHHGDGVDEAFCTSDRVFTLSLHKFGESFFPGTGHPRDVGYGRGRYYSMNLAVWDGITDFYYLGLFEHALHSIVRRYS 268
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30692236  251 PGAIVLQCGADSLARDRLGCFNLSIDGHAECVKFVKKFNLPLLVTGGGGYTKENVARCWTVETGILLDTELP 322
Cdd:PTZ00346 269 PDAIVLQCGADSLAGDRLGLLNLSSFGHGQCVQAVRDLGIPMLALGGGGYTIRNVAKLWAYETSILTGHPLP 340
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
24-303 4.23e-47

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: 162.67  E-value: 4.23e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  24 HPMKPHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVEFLqrinpENQNLFPNEMARYNLgedcPVFEDLF 103
Cdd:cd09993   1 HRFPMRKYGLLREALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLESL-----KSGELSREEIRRIGF----PWSPELV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 104 EFCQLYAGGTIDAARR-LNnklCDIAINWAGGLHHAKKCDASGFCYINDLVLGILELLKHHP--RVLYIDIDVHHGDGVE 180
Cdd:cd09993  72 ERTRLAVGGTILAARLaLE---HGLAINLAGGTHHAFPDRGEGFCVFNDIAIAARVLLAEGLvrRVLIVDLDVHQGNGTA 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 181 EAFYFTDRVMTVSFHkfGDKFFPGtgdVKEIGEregkfyaINVPLKDGIDDSSFNRLFRTIISKVVEIYQPGAIVLQCGA 260
Cdd:cd09993 149 AIFADDPSVFTFSMH--GEKNYPF---RKEPSD-------LDVPLPDGTGDDEYLAALEEALPRLLAEFRPDLVFYNAGV 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 30692236 261 DSLARDRLGCFNLSIDGHAE----CVKFVKKFNLPLLVTGGGGYTKE 303
Cdd:cd09993 217 DVLAGDRLGRLSLSLEGLRErdrlVLRFARARGIPVAMVLGGGYSRD 263
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
24-308 1.28e-44

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: 156.89  E-value: 1.28e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  24 HPMKPHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVEFLQRINPENQNLfpnemarynLGEDCPVFEDLF 103
Cdd:cd09992   1 HPERPERLLAILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYIERVEETCEAGGGY---------LDPDTYVSPGSY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 104 EFCQLYAGGTIDAARRLNNKLCDIAinWA-----GglHHAKKCDASGFCYINDLVLGILELLKHH--PRVLYIDIDVHHG 176
Cdd:cd09992  72 EAALLAAGAALAAVDAVLSGEAENA--FAlvrppG--HHAEPDRAMGFCLFNNVAIAARYAQKRYglKRVLIVDWDVHHG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 177 DGVEEAFYFTDRVMTVSFHKFGdkFFPGTGDVKEIGEREGKFYAINVPLKDGIDDSSFNRLFRTIISKVVEIYQPGAIVL 256
Cdd:cd09992 148 NGTQDIFYDDPSVLYFSIHQYP--FYPGTGAAEETGGGAGEGFTINVPLPPGSGDAEYLAAFEEVLLPIAREFQPDLVLV 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 30692236 257 QCGADSLARDRLGCFNLSIDGHAECVKFVKKF-----NLPLLVTGGGGYTKENVARC 308
Cdd:cd09992 226 SAGFDAHRGDPLGGMNLTPEGYARLTRLLKELadehcGGRLVFVLEGGYNLEALAES 282
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
22-308 2.42e-41

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: 148.45  E-value: 2.42e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  22 PNHPMKPHRLcmthHLILAyGLHS-KMEVYRPHKAYPIE-MAQFHSPDYVEFLQRINPenqnlfpnemarynlgeDCPVF 99
Cdd:cd10001  23 VPHPENPERA----EAILD-ALKRaGLGEVLPPRDFGLEpILAVHDPDYVDFLETADT-----------------DTPIS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 100 EDLFEFCQLYAGGTIDAARRLNNklcdiAINWAGGL-----HHAKKCDASGFCYINDLVLGILELLKHHPRVLYIDIDVH 174
Cdd:cd10001  81 EGTWEAALAAADTALTAADLVLE-----GERAAYALcrppgHHAGRDRAGGFCYFNNAAIAAQYLRDRAGRVAILDVDVH 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 175 HGDGVEEAFYFTDRVMTVSFHKFGDKFFPGT-GDVKEIGEREGKFYAINVPLKDGIDDSSFNRLFRTIISKVVEiYQPGA 253
Cdd:cd10001 156 HGNGTQEIFYERPDVLYVSIHGDPRTFYPFFlGFADETGEGEGEGYNLNLPLPPGTGDDDYLAALDEALAAIAA-FGPDA 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 30692236 254 IVLQCGADSLARDRLGCFNLSIDGHAECVKFVKKFNLPLLVTGGGGYTKENVARC 308
Cdd:cd10001 235 LVVSLGFDTHEGDPLSDFKLTTEDYARIGRRIAALGLPTVFVQEGGYNVDALGRN 289
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
7-269 3.04e-34

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: 130.76  E-value: 3.04e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236   7 ISYFYDGDVGSVYFGPnHPMKPHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVEFLQRINPENQNlfpne 86
Cdd:cd09996  17 GALFLPVGGLLVQPGR-HPENPETKRRIKNLLEVSGLSDHLVLITPRPATDEELLRVHTPEYIDRVKAASAAGGG----- 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  87 maryNLGEDCPVFEDLFEFCQLYAGGTIDAARRLNNKLCDIA---INWAGglHHAKKCDASGFCYINDLVLGILELLKHH 163
Cdd:cd09996  91 ----EAGGGTPFGPGSYEIALLAAGGAIAAVDAVLDGEVDNAyalVRPPG--HHAEPDQGMGFCLFNNVAIAARHALAVG 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 164 P--RVLYIDIDVHHGDGVEEAFYFTDRVMTVSFHKfgDKFFP-GTGDVKEIGEREGKFYAINVPLKDGIDDSSFNRLFRT 240
Cdd:cd09996 165 GvkRVAVVDWDVHHGNGTQAIFYDDPDVLTISLHQ--DRCFPpDSGAVEERGEGAGEGYNLNIPLPPGSGDGAYLHAFER 242
                       250       260
                ....*....|....*....|....*....
gi 30692236 241 IISKVVEIYQPGAIVLQCGADSLARDRLG 269
Cdd:cd09996 243 IVLPALRAFRPELIIVASGFDASAFDPLG 271
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
24-274 1.14e-28

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: 113.76  E-value: 1.14e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  24 HPMKPHRLCMTHHLILAYGLhskMEVYRPHKAYPIEMAQF---HSPDYVEFLQRINPENQNLFpnemarynLGEDCPVFE 100
Cdd:cd11599   1 HPESPERLEAILDALIASGL---DRLLRQLEAPPATREQLlrvHDAAYVDRLEAAAPEEGLVQ--------LDPDTAMSP 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 101 DLFEFCQLYAGGTIDA-----ARRLNNKLCdiAINWAGglHHAKKCDASGFCYINDLVLGILELLKHHP--RVLYIDIDV 173
Cdd:cd11599  70 GSLEAALRAAGAVVAAvdavmAGEARNAFC--AVRPPG--HHAERDKAMGFCLFNNVAIAAAHALAHHGleRVAIVDFDV 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 174 HHGDGVEEAFYFTDRVMTVSFHKFGdkFFPGTGDVKEIGERegkfYAINVPLKDGIDDSSFNRLFRTIISKVVEIYQPGA 253
Cdd:cd11599 146 HHGNGTEDIFRDDPRVLFCSSHQHP--LYPGTGAPDETGHG----NIVNVPLPAGTGGAEFREAVEDRWLPALDAFKPDL 219
                       250       260
                ....*....|....*....|.
gi 30692236 254 IVLQCGADSLARDRLGCFNLS 274
Cdd:cd11599 220 ILISAGFDAHRDDPLAQLNLT 240
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
22-279 3.91e-27

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: 110.13  E-value: 3.91e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  22 PNHPMKPHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVEFLQRINPENQNLFPNEMARYNlGEDCPVFED 101
Cdd:cd11600   1 DPHPEDPSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEHWDRVEATEKMSDEQLKDRTEIFE-RDSLYVNND 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 102 LFEFCQLYAGGTIDAAR-----RLNNKlcdIAINWAGGlHHAKKCDASGFCYINDLVLGILELLKHHP----RVLYIDID 172
Cdd:cd11600  80 TAFCARLSCGGAIEACRavaegRVKNA---FAVVRPPG-HHAEPDESMGFCFFNNVAVAAKWLQTEYPdkikKILILDWD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 173 VHHGDGVEEAFYFTDRVMTVSFHKF-GDKFFPGT--GDVKEIGEREGKFYAINVPLKD-GIDDSSFNRLFRTIISKVVEI 248
Cdd:cd11600 156 IHHGNGTQRAFYDDPNVLYISLHRFeNGGFYPGTpyGDYESVGEGAGLGFNVNIPWPQgGMGDADYIYAFQRIVMPIAYE 235
                       250       260       270
                ....*....|....*....|....*....|.
gi 30692236 249 YQPGAIVLQCGADSLARDRLGCFNLSIDGHA 279
Cdd:cd11600 236 FDPDLVIISAGFDAADGDELGQCHVTPAGYA 266
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
22-328 4.53e-27

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: 110.48  E-value: 4.53e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  22 PNHPMKPHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVEFLQRINpenqnlfpnEMARYNLGEDCPVFED 101
Cdd:cd10002   5 SNHIECPERLEAILERLTQDGLLERCVKIPAREAEEDEILLVHSQEYIDLVKSTE---------TMEKEELESLCSGYDS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 102 L------FEFCQLYAGGTIDA-----ARRLNNKLCdiAINWAGglHHAKKCDASGFCYINDLVLGILELL-KHHP-RVLY 168
Cdd:cd10002  76 VylcpstYEAARLAAGSTIELvkavmAGKIQNGFA--LIRPPG--HHAMRNEANGYCIFNNVAIAAKYAIeKLGLkRILI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 169 IDIDVHHGDGVEEAFYFTDRVMTVSFHKFGD-KFFPG--TGDVKEIGEREGKFYAINVPLKD-GIDDSSFNRLFRTIISK 244
Cdd:cd10002 152 VDWDVHHGQGTQQGFYEDPRVLYFSIHRYEHgRFWPHlfESDYDYIGVGHGYGFNVNVPLNQtGLGDADYLAIFHHILLP 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 245 VVEIYQPGAIVLQCGADSLARDRLGCFNLSIDGHAECVKFVKKFNLP-LLVTGGGGYTKENVARC--WTVETgiLLDTEL 321
Cdd:cd10002 232 LALEFQPELVLVSAGFDASIGDPEGEMAVTPAGYAHLTRLLMGLAGGkLLLVLEGGYLLESLAESvsMTLRG--LLGDPL 309
                       330
                ....*....|
gi 30692236 322 PN---EIPEN 328
Cdd:cd10002 310 PPlapPIPIR 319
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
103-316 5.40e-25

Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily includes metal-dependent enzymes that belong to Arginase-like amidino hydrolase family and histone/histone-like deacetylase class I, II, IV family, respectively. These enzymes catalyze hydrolysis of amide bond. Arginases are known to be involved in control of cellular levels of arginine and ornithine, in histidine and arginine degradation and in clavulanic acid biosynthesis. Deacetylases play a role in signal transduction through histone and/or other protein modification and can repress/activate transcription of a number of different genes. They participate in different cellular processes including cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and post-translational control of the acetyl coenzyme A synthetase. Mammalian histone deacetyases are known to be involved in progression of different tumors. Specific inhibitors of mammalian histone deacetylases are an emerging class of promising novel anticancer drugs.


Pssm-ID: 212513  Cd Length: 217  Bit Score: 101.68  E-value: 5.40e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 103 FEFCQLYAGGTIDAARRlnnklCDIAINWAGglHHAKkcdasgfcyINDLVLGILEllkHHPRVLYIDIDVHHGDGVEEA 182
Cdd:cd09987   8 AEAHELLAGVVVAVLKD-----GKVPVVLGG--DHSI---------ANGAIRAVAE---LHPDLGVIDVDAHHDVRTPEA 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 183 FYF--------------TDRVMTVSFHKFGDKFFPgtgdvkEIGEREGKFYAINVPLKDGiDDSSFNRLFRTIISKVVei 248
Cdd:cd09987  69 FGKgnhhtprhllceplISDVHIVSIGIRGVSNGE------AGGAYARKLGVVYFSMTEV-DKLGLGDVFEEIVSYLG-- 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30692236 249 YQPGAIVLQCGADSL------ARDRLGCFNLSIDGHAECVKFVKKFNLPLLVTGGGGYT----KENVARCWTVETGIL 316
Cdd:cd09987 140 DKGDNVYLSVDVDGLdpsfapGTGTPGPGGLSYREGLYITERIAKTNLVVGLDIVEVNPlldeTGRTARLAAALTLEL 217
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
23-264 2.43e-23

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: 100.50  E-value: 2.43e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  23 NHPMKPHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVeFLQRINPEN-QNLFPNEMARYNLGEdcpvfed 101
Cdd:cd11681  23 SHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHT-LLYGTNPLSrLKLDPTKLAGLPQKS------- 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 102 lfeFCQLYAGG-------------TIDAARRLNNKLCDIAINWAGGL------------HHAKKCDASGFCYINDLVLG- 155
Cdd:cd11681  95 ---FVRLPCGGigvdsdtvwnelhTSNAARMAVGCVIDLAFKVATGElkngfavvrppgHHAEPSQAMGFCFFNSVAIAa 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 156 -ILELLKHHPRVLYIDIDVHHGDGVEEAFYFTDRVMTVSFHKFGD-KFFPGTGDVKEIGEREGKFYAINVPLKDGID--- 230
Cdd:cd11681 172 kQLQQKLKLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDgNFFPGTGAPTEVGSGAGEGFNVNIAWSGGLDppm 251
                       250       260       270
                ....*....|....*....|....*....|....*
gi 30692236 231 -DSSFNRLFRTIISKVVEIYQPGAIVLQCGADSLA 264
Cdd:cd11681 252 gDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAE 286
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
22-322 9.67e-23

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: 98.56  E-value: 9.67e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  22 PNHPMKPHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVEFLQRInpenQNLFPNEMAR----YNLGEDCP 97
Cdd:cd10003  14 PGHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHLDEMKSL----EKMKPRELNRlgkeYDSIYIHP 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  98 vfeDLFEFCQLYAGGTIDAARRL--NNKLCDIAINWAGGlHHAKKCDASGFCYINDLVLGI-LELLKHHP-RVLYIDIDV 173
Cdd:cd10003  90 ---DSYQCALLAAGCVLQVVEAVltGESRNGVAIVRPPG-HHAEQDTACGFCFFNNVAIAArYAQKKYGLkRILIVDWDV 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 174 HHGDGVEEAFYFTDRVMTVSFHKFGD-KFFPGT--GDVKEIGEREGKFYAINVPL-KDGIDDSSFNRLFRTIISKVVEIY 249
Cdd:cd10003 166 HHGNGTQHMFESDPSVLYISLHRYDNgSFFPNSpeGNYDVVGKGKGEGFNVNIPWnKGGMGDAEYIAAFQQVVLPIAYEF 245
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30692236 250 QPGAIVLQCGADSLARDRLGCFNLSIDGHAECVKFVKKF-NLPLLVTGGGGYTKENVARCWTVETGILLDTELP 322
Cdd:cd10003 246 NPELVLVSAGFDAARGDPLGGCKVTPEGYAHMTHMLMSLaGGRVIVILEGGYNLTSISESMSMCTKTLLGDPPP 319
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
23-262 1.07e-22

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: 98.93  E-value: 1.07e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  23 NHPMKPHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVeFLQRINPENQNLFPNEMARYNLGEDCpvfedl 102
Cdd:cd10008  23 NHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHV-LLYGTNPLSRLKLDNGKLAGLLAQRM------ 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 103 feFCQLYAGGT-IDAARRLNNKLCDIAINWAGGL------------------------HHAKKCDASGFCYINDLVLGI- 156
Cdd:cd10008  96 --FVMLPCGGVgVDTDTIWNELHSSNAARWAAGSvtdlafkvasrelkngfavvrppgHHADHSTAMGFCFFNSVAIACr 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 157 -LELLKHHPRVLYIDIDVHHGDGVEEAFYFTDRVMTVSFHKFGD-KFFPGTGDVKEIGEREGKFYAINVPLKDGID---- 230
Cdd:cd10008 174 qLQQQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDgNFFPGSGAVDEVGAGSGEGFNVNVAWAGGLDppmg 253
                       250       260       270
                ....*....|....*....|....*....|..
gi 30692236 231 DSSFNRLFRTIISKVVEIYQPGAIVLQCGADS 262
Cdd:cd10008 254 DPEYLAAFRIVVMPIAREFSPDLVLVSAGFDA 285
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
24-287 1.55e-22

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: 98.96  E-value: 1.55e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  24 HPMKPHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVeFLQRINPENQNLFPnemARYNLGEDCPVFedlf 103
Cdd:cd10006  27 HPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHT-LLYGTNPLNRQKLD---SKKLLGSLASVF---- 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 104 efCQLYAGG------TI-------DAARRLNNKLCDIAINWAGGL------------HHAKKCDASGFCYINDLVLG--I 156
Cdd:cd10006  99 --VRLPCGGvgvdsdTIwnevhssGAARLAVGCVVELVFKVATGElkngfavvrppgHHAEESTPMGFCYFNSVAIAakL 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 157 LELLKHHPRVLYIDIDVHHGDGVEEAFYFTDRVMTVSFHKFGD-KFFPGTGDVKEIGEREGKFYAINVPLKDGID----D 231
Cdd:cd10006 177 LQQRLNVSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYDDgNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDppmgD 256
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 30692236 232 SSFNRLFRTIISKVVEIYQPGAIVLQCGADSLA--RDRLGCFNLSidghAECVKFVKK 287
Cdd:cd10006 257 AEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEghPTPLGGYNLS----AKCFGYLTK 310
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
136-263 2.87e-20

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: 92.36  E-value: 2.87e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 136 HHAKKCDASGFCYINDLVLGIlELLKHH---PRVLYIDIDVHHGDGVEEAFYFTDRVMTVSFHKFGD-KFFPGTGDVKEI 211
Cdd:cd10007 154 HHAEESTAMGFCFFNSVAIAA-KLLQQKlnvGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDgNFFPGSGAPDEV 232
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 30692236 212 GEREGKFYAINVPLKDGID----DSSFNRLFRTIISKVVEIYQPGAIVLQCGADSL 263
Cdd:cd10007 233 GAGPGVGFNVNIAWTGGVDppigDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAV 288
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
23-263 3.57e-20

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: 91.62  E-value: 3.57e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  23 NHPMKPHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSpDYVEFLQRINPEN-QNLFPNEMarynLGEDCPVFed 101
Cdd:cd10009  23 THPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHS-EHHSLLYGTNPLDgQKLDPRIL----LGDDSQKF-- 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 102 lfeFCQLYAGG-------------TIDAARRLNNKLCDIAINWAGGL------------HHAKKCDASGFCYINDLVLGI 156
Cdd:cd10009  96 ---FSSLPCGGlgvdsdtiwnelhSSGAARMAVGCVIELASKVASGElkngfavvrppgHHAEESTAMGFCFFNSVAITA 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 157 LELLK--HHPRVLYIDIDVHHGDGVEEAFYFTDRVMTVSFHKFGD-KFFPGTGDVKEIGEREGKFYAINVPLKDGID--- 230
Cdd:cd10009 173 KYLRDqlNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEgNFFPGSGAPNEVGTGLGEGYNINIAWTGGLDppm 252
                       250       260       270
                ....*....|....*....|....*....|....
gi 30692236 231 -DSSFNRLFRTIISKVVEIYQPGAIVLQCGADSL 263
Cdd:cd10009 253 gDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDAL 286
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
23-269 4.57e-14

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: 72.96  E-value: 4.57e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  23 NHPMKPHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVEFLQrinpENQNLFPNEMARYNLGEDCPVFEDL 102
Cdd:cd11682   6 SFPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYVALMK----STQYMTEEELRTLADTYDSVYLHPN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 103 FEFCQLYAGGTI--DAARRLNNKLCD-IAINWAGGlHHAKKCDASGFCYINDLVLGILELLKHH--PRVLYIDIDVHHGD 177
Cdd:cd11682  82 SYSCACLAVGSVlqLVDKVLGGEIRNgLAIVRPPG-HHAQHDKMDGYCMFNNVAIAARYAQQKHgvQRVLIVDWDVHHGQ 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 178 GVEEAFYFTDRVMTVSFHKFGD-KFFP--GTGDVKEIGEREGKFYAINVPL-KDGIDDSSFNRLFRTIISKVVEIYQPGA 253
Cdd:cd11682 161 GTQFIFEQDPSVLYFSIHRYEQgRFWPhlKESDSSAVGFGRGEGYNINVPWnQVGMRDADYIAAFLHVLLPVALEFQPQL 240
                       250
                ....*....|....*.
gi 30692236 254 IVLQCGADSLARDRLG 269
Cdd:cd11682 241 VLVAAGFDAVIGDPKG 256
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
28-322 5.25e-14

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: 72.59  E-value: 5.25e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236  28 PHRLCMTHHLILAYGLHSKMEVYRPHKAYPIEMAQFHSPDYVEFLQrinpENQNLFPNEMARYNLGEDCPVF-EDLFEFC 106
Cdd:cd11683  11 PERLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVR----ETQVMNKEELMAISGKYDAVYFhPNTFHCA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 107 QLYAGGT---IDAArrLNNKLCD-IAINWAGGlHHAKKCDASGFCYINDLVLGILELLKHH--PRVLYIDIDVHHGDGVE 180
Cdd:cd11683  87 RLAAGATlqlVDAV--LTGEVQNgMALVRPPG-HHSQRNAANGFCVFNNVAIAAEYAKKKYglHRILIVDWDVHHGQGIQ 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692236 181 EAFYFTDRVMTVSFHKFGDK-FFPG--TGDVKEIGEREGKFYAINVPL-KDGIDDSSFNRLFRTIISKVVEIYQPGAIVL 256
Cdd:cd11683 164 YIFEEDPSVLYFSWHRYEHQrFWPFlrESDYDAVGRGKGLGFNINLPWnKVGMGNADYLAAFFHVLLPLAFEFDPELVLV 243
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30692236 257 QCGADSLARDRLGCFNLSidghAECVKFVKKFNLPLlvTGG-------GGYTKENVAR--CWTVETgiLLDTELP 322
Cdd:cd11683 244 SAGFDSAIGDPEGQMCAT----PECFAHLTHLLMVL--AGGklcavleGGYHLESLAEsvCMTVQT--LLGDPLP 310
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
136-181 7.88e-06

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: 47.45  E-value: 7.88e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 30692236 136 HHAKKCDASGFCYINDLVLGILE-LLKHH-PRVLYIDIDVHHGDGVEE 181
Cdd:cd09998 120 HHCSESTPSGFCWVNNVHVGAAHaYLTHGiTRVVILDIDLHHGNGTQD 167
 
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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