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Conserved domains on  [gi|2519023616|pdb|7YI2|B]
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Chain B, Histone deacetylase RPD3

Protein Classification

RPD3/Clr6 family histone deacetylase( domain architecture ID 10178012)

RPD3/Clr6 family histone deacetylase similar to Saccharomyces cerevisiae histone deacetylase RPD3 and Schizosaccharomyces pombe cryptic loci regulator 6 (Clr6), both of which 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)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
 18-392 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: 762.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       18 KRRVAYFYDADVGNYAYGAGHPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDNLEMF 97
Cdd:cd10004   1 KKKVAYFYDSDVGNYAYGPGHPMKPHRIRMAHSLVMNYGLYKKMEIYRAKPATKNEMTQFHTDEYIDFLSRVTPDNMEKF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       98 KRESVKFNVGDDCPVFDGLYEYCSISGGGSMEGAARLNRGKCDVAVNYAGGLHHAKKSEASGFCYLNDIVLGIIELLRYH 177
Cdd:cd10004  81 QKEQVKYNVGDDCPVFDGLFEFCSISAGGSMEGAARLNRGKCDIAVNWAGGLHHAKKSEASGFCYVNDIVLGILELLRYH 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      178 PRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYGEFFPGTGELRDIGVGAGKNYAVNVPLRDGIDDATYRSVFEPVIKK 257
Cdd:cd10004 161 QRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYGEYFPGTGELRDIGIGTGKNYAVNVPLRDGIDDESYKSIFEPVIKH 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      258 IMEWYQPSAVVLQCGGDSLSGDRLGCFNLSMEGHANCVNYVKSFGIPMMVVGGGGYTMRNVARTWCFETGLLNNVVLDKD 337
Cdd:cd10004 241 VMEWYQPEAVVLQCGGDSLSGDRLGCFNLSMKGHANCVNFVKSFNLPMLVLGGGGYTMRNVARTWAFETGLLAGEELDKD 320

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
7YI2_B      338 LPYNEYYEYYGPDYKLSVRPSNMFNVNTPEYLDKVMTNIFANLENTKYAPSVQLN 392
Cdd:cd10004 321 LPYNEYYEYYGPDYELNVRPSNMENHNTPEYLDKITTAVIENLRNTSFAPSVQMQ 375
 
Name Accession Description Interval E-value
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
 18-392 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: 762.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       18 KRRVAYFYDADVGNYAYGAGHPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDNLEMF 97
Cdd:cd10004   1 KKKVAYFYDSDVGNYAYGPGHPMKPHRIRMAHSLVMNYGLYKKMEIYRAKPATKNEMTQFHTDEYIDFLSRVTPDNMEKF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       98 KRESVKFNVGDDCPVFDGLYEYCSISGGGSMEGAARLNRGKCDVAVNYAGGLHHAKKSEASGFCYLNDIVLGIIELLRYH 177
Cdd:cd10004  81 QKEQVKYNVGDDCPVFDGLFEFCSISAGGSMEGAARLNRGKCDIAVNWAGGLHHAKKSEASGFCYVNDIVLGILELLRYH 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      178 PRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYGEFFPGTGELRDIGVGAGKNYAVNVPLRDGIDDATYRSVFEPVIKK 257
Cdd:cd10004 161 QRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYGEYFPGTGELRDIGIGTGKNYAVNVPLRDGIDDESYKSIFEPVIKH 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      258 IMEWYQPSAVVLQCGGDSLSGDRLGCFNLSMEGHANCVNYVKSFGIPMMVVGGGGYTMRNVARTWCFETGLLNNVVLDKD 337
Cdd:cd10004 241 VMEWYQPEAVVLQCGGDSLSGDRLGCFNLSMKGHANCVNFVKSFNLPMLVLGGGGYTMRNVARTWAFETGLLAGEELDKD 320

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
7YI2_B      338 LPYNEYYEYYGPDYKLSVRPSNMFNVNTPEYLDKVMTNIFANLENTKYAPSVQLN 392
Cdd:cd10004 321 LPYNEYYEYYGPDYELNVRPSNMENHNTPEYLDKITTAVIENLRNTSFAPSVQMQ 375
PTZ00063 PTZ00063
histone deacetylase; Provisional
 16-433 0e+00

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 559.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B        16 SDKRRVAYFYDADVGNYAYGAGHPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDNLE 95
Cdd:PTZ00063   1 SMRKRVSYFYDPDIGSYYYGPGHPMKPQRIRMAHALILSYDLYKHMEIYRPHKSVEPELVLFHDEEYVDFLSSISPENYR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B        96 MFKRESVKFNVGD--DCPVFDGLYEYCSISGGGSMEGAARLNRGKCDVAVNYAGGLHHAKKSEASGFCYLNDIVLGIIEL 173
Cdd:PTZ00063  81 DFTYQLKRFNVGEatDCPVFDGLFEFQQSCAGASIDGAYKLNNHQADICVNWSGGLHHAKRSEASGFCYINDIVLGILEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       174 LRYHPRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYGEFFPGTGELRDIGVGAGKNYAVNVPLRDGIDDATYRSVFEP 253
Cdd:PTZ00063 161 LKYHARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKFGDFFPGTGDVTDIGVAQGKYYSVNVPLNDGIDDDSFVDLFKP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       254 VIKKIMEWYQPSAVVLQCGGDSLSGDRLGCFNLSMEGHANCVNYVKSFGIPMMVVGGGGYTMRNVARTWCFETGllnnVV 333
Cdd:PTZ00063 241 VISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAACVEFVRSLNIPLLVLGGGGYTIRNVARCWAYETG----VI 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       334 LDK------DLPYNEYYEYYGPDYKLSVRPSNMFNVNTPEYLDKVMTNIFANLENTKYAPSVQLNHTPRD--AEDLGDVE 405
Cdd:PTZ00063 317 LNKhdemsdQISLNDYYDYYAPDFQLHLQPSNIPNYNSPEHLEKIKVKILENLRYLEHAPGVQFAYVPPDffDRDIDDED 396

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
7YI2_B       406 EDSAEAKDTKGGSQYA------------RDLHVEHDNEFY 433
Cdd:PTZ00063 397 EKNQYELSDEGGGRAAgstakrhstnshRLRRKDYADDFY 436
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 38-329 6.84e-113

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: 333.43  E-value: 6.84e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B         38 HPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDNLEMFKRESVKFnvGDDCPVFDGLY 117
Cdd:pfam00850   1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAAPEGGALLLLSYLSG--DDDTPVSPGSY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B        118 EYCSISGGGSMEGAARLNRGKCDVAVNYA-GGLHHAKKSEASGFCYLNDIVLGIIELLRYH--PRVLYIDIDVHHGDGVE 194
Cdd:pfam00850  79 EAALLAAGGTLAAADAVLSGEARNAFALVrPPGHHAERDRASGFCIFNNVAIAAKYLREKYglKRVAIVDFDVHHGNGTQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B        195 EAFYTTDRVMTCSFHKYGE-FFPGTGELRDIGVGAGKNYAVNVPLRDGIDDATYRSVFEPVIKKIMEWYQPSAVVLQCGG 273
Cdd:pfam00850 159 EIFYDDPSVLTLSIHQYPGgFYPGTGFADETGEGKGKGYTLNVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAGF 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B        274 DSLSGDRLGCFNLSMEGHANCVNYVKSF----GIPMMVVGGGGYTMRNVARTWCFETGLL 329
Cdd:pfam00850 239 DAHAGDPLGGLNLTTEGFAEITRILLELadplCIRVVSVLEGGYNLDALARSATAVLAAL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 21-322 3.04e-89

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 273.14  E-value: 3.04e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       21 VAYFYDADVGNYAYGAGHPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDN-LEMFkr 99
Cdd:COG0123   1 TALIYHPDYLLHDLGPGHPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAASLDGgYGQL-- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      100 esvkfnvGDDCPVFDGLYEYCSISGGGSMEGAARLNRGKCDVA-VNYAGGLHHAKKSEASGFCYLNDIVLGIIELL-RYH 177
Cdd:COG0123  79 -------DPDTPVSPGTWEAALLAAGGALAAADAVLEGEARNAfALVRPPGHHAERDRAMGFCLFNNAAIAARYLLaKGL 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      178 PRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYGeFFPGTGELRDIGVGAGKNYAVNVPLRDGIDDATYRSVFEPVIKK 257
Cdd:COG0123 152 ERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQDP-LYPGTGAADETGEGAGEGSNLNVPLPPGTGDAEYLAALEEALLP 230

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
7YI2_B      258 IMEWYQPSAVVLQCGGDSLSGDRLGCFNLSMEGHANCVNYVKSF----GIPMMVVGGGGYTMRNVARTW 322
Cdd:COG0123 231 ALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELadhcGGPVVSVLEGGYNLDALARSV 299
 
Name Accession Description Interval E-value
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
 18-392 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: 762.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       18 KRRVAYFYDADVGNYAYGAGHPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDNLEMF 97
Cdd:cd10004   1 KKKVAYFYDSDVGNYAYGPGHPMKPHRIRMAHSLVMNYGLYKKMEIYRAKPATKNEMTQFHTDEYIDFLSRVTPDNMEKF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       98 KRESVKFNVGDDCPVFDGLYEYCSISGGGSMEGAARLNRGKCDVAVNYAGGLHHAKKSEASGFCYLNDIVLGIIELLRYH 177
Cdd:cd10004  81 QKEQVKYNVGDDCPVFDGLFEFCSISAGGSMEGAARLNRGKCDIAVNWAGGLHHAKKSEASGFCYVNDIVLGILELLRYH 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      178 PRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYGEFFPGTGELRDIGVGAGKNYAVNVPLRDGIDDATYRSVFEPVIKK 257
Cdd:cd10004 161 QRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYGEYFPGTGELRDIGIGTGKNYAVNVPLRDGIDDESYKSIFEPVIKH 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      258 IMEWYQPSAVVLQCGGDSLSGDRLGCFNLSMEGHANCVNYVKSFGIPMMVVGGGGYTMRNVARTWCFETGLLNNVVLDKD 337
Cdd:cd10004 241 VMEWYQPEAVVLQCGGDSLSGDRLGCFNLSMKGHANCVNFVKSFNLPMLVLGGGGYTMRNVARTWAFETGLLAGEELDKD 320

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
7YI2_B      338 LPYNEYYEYYGPDYKLSVRPSNMFNVNTPEYLDKVMTNIFANLENTKYAPSVQLN 392
Cdd:cd10004 321 LPYNEYYEYYGPDYELNVRPSNMENHNTPEYLDKITTAVIENLRNTSFAPSVQMQ 375
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
 24-329 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: 621.52  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       24 FYDADVGNYAYGAGHPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDNLEMFKRESVK 103
Cdd:cd09991   1 FYDPDVGNYYYGQGHPMKPHRIRMTHSLILSYGLYKKMEIYRPRPATAEELTKFHSDDYIDFLRSVSPDNMKEFKKQLER 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      104 FNVGDDCPVFDGLYEYCSISGGGSMEGAARLNRGKCDVAVNYAGGLHHAKKSEASGFCYLNDIVLGIIELLRYHPRVLYI 183
Cdd:cd09991  81 FNVGEDCPVFDGLYEYCQLYAGGSIAAAVKLNRGQADIAINWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      184 DIDVHHGDGVEEAFYTTDRVMTCSFHKYGEFFPGTGELRDIGVGAGKNYAVNVPLRDGIDDATYRSVFEPVIKKIMEWYQ 263
Cdd:cd09991 161 DIDIHHGDGVEEAFYTTDRVMTVSFHKFGEYFFPGTGLRDIGAGKGKYYAVNVPLKDGIDDESYLQIFEPVLSKVMEVFQ 240

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
7YI2_B      264 PSAVVLQCGGDSLSGDRLGCFNLSMEGHANCVNYVKSFGIPMMVVGGGGYTMRNVARTWCFETGLL 329
Cdd:cd09991 241 PSAVVLQCGADSLAGDRLGCFNLSIKGHAKCVKFVKSFNIPLLVLGGGGYTLRNVARCWTYETAVL 306
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
 19-397 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: 612.86  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       19 RRVAYFYDADVGNYAYGAGHPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDNLEMFK 98
Cdd:cd10005   1 KRVAYFYDPDVGNFHYGPGHPMKPHRLALTHSLVLHYGLYKKMQVYKPYRASAHDMCRFHSEDYIDFLQRVTPQNIQGFT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       99 RESVKFNVGDDCPVFDGLYEYCSISGGGSMEGAARLNRGKCDVAVNYAGGLHHAKKSEASGFCYLNDIVLGIIELLRYHP 178
Cdd:cd10005  81 KSLNQFNVGDDCPVFPGLFDFCSMYTGASLEGATKLNHKICDIAINWSGGLHHAKKFEASGFCYVNDIVIAILELLKYHP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      179 RVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYG-EFFPGTGELRDIGVGAGKNYAVNVPLRDGIDDATYRSVFEPVIKK 257
Cdd:cd10005 161 RVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGnYFFPGTGDMYEVGAESGRYYSVNVPLKDGIDDQSYLQLFKPVIQQ 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      258 IMEWYQPSAVVLQCGGDSLSGDRLGCFNLSMEGHANCVNYVKSFGIPMMVVGGGGYTMRNVARTWCFETGLLNNVVLDKD 337
Cdd:cd10005 241 VIDFYQPTCIVLQCGADSLGCDRLGCFNLSIKGHGECVEFVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVDEEISNE 320

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
7YI2_B      338 LPYNEYYEYYGPDYKLsvRPSNMF---NVNTPEYLDKVMTNIFANLENTKYAPSVQLNHTPRD 397
Cdd:cd10005 321 LPYNEYFEYFAPDFTL--HPDVSTrieNQNSKQYLDQIRQTVFENLKMLNHAPSVQMQDVPPD 381
PTZ00063 PTZ00063
histone deacetylase; Provisional
 16-433 0e+00

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 559.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B        16 SDKRRVAYFYDADVGNYAYGAGHPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDNLE 95
Cdd:PTZ00063   1 SMRKRVSYFYDPDIGSYYYGPGHPMKPQRIRMAHALILSYDLYKHMEIYRPHKSVEPELVLFHDEEYVDFLSSISPENYR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B        96 MFKRESVKFNVGD--DCPVFDGLYEYCSISGGGSMEGAARLNRGKCDVAVNYAGGLHHAKKSEASGFCYLNDIVLGIIEL 173
Cdd:PTZ00063  81 DFTYQLKRFNVGEatDCPVFDGLFEFQQSCAGASIDGAYKLNNHQADICVNWSGGLHHAKRSEASGFCYINDIVLGILEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       174 LRYHPRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYGEFFPGTGELRDIGVGAGKNYAVNVPLRDGIDDATYRSVFEP 253
Cdd:PTZ00063 161 LKYHARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKFGDFFPGTGDVTDIGVAQGKYYSVNVPLNDGIDDDSFVDLFKP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       254 VIKKIMEWYQPSAVVLQCGGDSLSGDRLGCFNLSMEGHANCVNYVKSFGIPMMVVGGGGYTMRNVARTWCFETGllnnVV 333
Cdd:PTZ00063 241 VISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAACVEFVRSLNIPLLVLGGGGYTIRNVARCWAYETG----VI 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       334 LDK------DLPYNEYYEYYGPDYKLSVRPSNMFNVNTPEYLDKVMTNIFANLENTKYAPSVQLNHTPRD--AEDLGDVE 405
Cdd:PTZ00063 317 LNKhdemsdQISLNDYYDYYAPDFQLHLQPSNIPNYNSPEHLEKIKVKILENLRYLEHAPGVQFAYVPPDffDRDIDDED 396

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
7YI2_B       406 EDSAEAKDTKGGSQYA------------RDLHVEHDNEFY 433
Cdd:PTZ00063 397 EKNQYELSDEGGGRAAgstakrhstnshRLRRKDYADDFY 436
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
 18-380 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: 539.65  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       18 KRRVAYFYDADVGNYAYGAGHPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDNLEMF 97
Cdd:cd10010   5 KKKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEY 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       98 KRESVKFNVGDDCPVFDGLYEYCSISGGGSMEGAARLNRGKCDVAVNYAGGLHHAKKSEASGFCYLNDIVLGIIELLRYH 177
Cdd:cd10010  85 SKQMQRFNVGEDCPVFDGLFEFCQLSAGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYH 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      178 PRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYGEFFPGTGELRDIGVGAGKNYAVNVPLRDGIDDATYRSVFEPVIKK 257
Cdd:cd10010 165 QRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSK 244

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      258 IMEWYQPSAVVLQCGGDSLSGDRLGCFNLSMEGHANCVNYVKSFGIPMMVVGGGGYTMRNVARTWCFETGLLNNVVLDKD 337
Cdd:cd10010 245 VMEMFQPSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDSEIPNE 324

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
7YI2_B      338 LPYNEYYEYYGPDYKLSVRPSNMFNVNTPEYLDKVMTNIFANL 380
Cdd:cd10010 325 LPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENL 367
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
 18-380 0e+00

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: 530.02  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       18 KRRVAYFYDADVGNYAYGAGHPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDNLEMF 97
Cdd:cd10011   1 KKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       98 KRESVKFNVGDDCPVFDGLYEYCSISGGGSMEGAARLNRGKCDVAVNYAGGLHHAKKSEASGFCYLNDIVLGIIELLRYH 177
Cdd:cd10011  81 SKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYH 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      178 PRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYGEFFPGTGELRDIGVGAGKNYAVNVPLRDGIDDATYRSVFEPVIKK 257
Cdd:cd10011 161 QRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQIFKPIISK 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      258 IMEWYQPSAVVLQCGGDSLSGDRLGCFNLSMEGHANCVNYVKSFGIPMMVVGGGGYTMRNVARTWCFETGLLNNVVLDKD 337
Cdd:cd10011 241 VMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLGGGGYTIRNVARCWTYETAVALDCEIPNE 320

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
7YI2_B      338 LPYNEYYEYYGPDYKLSVRPSNMFNVNTPEYLDKVMTNIFANL 380
Cdd:cd10011 321 LPYNDYFEYFGPDFKLHISPSNMTNQNTPEYMEKIKQRLFENL 363
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
 21-329 9.88e-175

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: 490.81  E-value: 9.88e-175
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       21 VAYFYDADVGNYAYGAGHPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDNLEMFKRE 100
Cdd:cd11598   1 VSYHFNSRVEDYHFGRTHPMKPFRLTLTKHLVMGYGLHKAMDTYEARAATREELRQFHDADYLDFLSKVSPENANQLRFD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      101 SV-KFNVGDDCPVFDGLYEYCSISGGGSMEGAARLNRGKCDVAVNYAGGLHHAKKSEASGFCYLNDIVLGIIELLRYHPR 179
Cdd:cd11598  81 KAePFNIGDDCPVFDGMYDYCQLYAGASLDAARKLCSGQSDIAINWSGGLHHAKKSEASGFCYVNDIVLAILNLLRYFPR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      180 VLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKY-GEFFPGTGELRDIGVGAGKNYAVNVPLRDGIDDATYRSVFEPVIKKI 258
Cdd:cd11598 161 VLYIDIDVHHGDGVEEAFYRTDRVMTLSFHKYnGEFFPGTGDLDDNGGTPGKHFALNVPLEDGIDDEQYNLLFKSIIGPT 240

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
7YI2_B      259 MEWYQPSAVVLQCGGDSLSGDRLGCFNLSMEGHANCVNYVKSFGIPMMVVGGGGYTMRNVARTWCFETGLL 329
Cdd:cd11598 241 IEKFQPSAIVLQCGADSLGGDRLGQFNLNIKAHGACVKFVKSFGIPMLVVGGGGYTPRNVARAWCYETAVA 311
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 39-383 9.57e-147

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: 421.75  E-value: 9.57e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       39 PMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTP--DNLEMFKrESVKFNVGDDCPVFDGL 116
Cdd:cd10000  17 PKVPNRASMVHSLIEAYGLLKQLRVVKPRVATEEELASFHSDEYIQFLKKASNegDNDEEPS-EQQEFGLGYDCPIFEGI 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      117 YEYCSISGGGSMEGAARLNRGKCDVAVNYAGGLHHAKKSEASGFCYLNDIVLGIIELLRYHPRVLYIDIDVHHGDGVEEA 196
Cdd:cd10000  96 YDYAAAVAGATLTAAQLLIDGKCKVAINWFGGWHHAQRDEASGFCYVNDIVLGILKLREKFDRVLYVDLDLHHGDGVEDA 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      197 FYTTDRVMTCSFHKYGE-FFPGTGELRDIGVGAGKNYAVNVPLRDGIDDATYRSVFEPVIKKIMEWYQPSAVVLQCGGDS 275
Cdd:cd10000 176 FSFTSKVMTVSLHKYSPgFFPGTGDVSDVGLGKGKYYTVNVPLRDGIQDEQYLQIFTAVVPEIVAAFRPEAVVLQCGADT 255

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      276 LSGDRLGCFNLSMEGHANCVNYVKSFGIPMMVVGGGGYTMRNVARTWCFETGLLNNVVLDKDLPYNEYYEYYGPDYKLSV 355
Cdd:cd10000 256 LAGDPMGAFNLTPVGIGKCLKYVLGWKLPTLILGGGGYNLANTARCWTYLTGLILGEPLSSDIPDHEFFTSYGPDYELEI 335

                       330       340
                ....*....|....*....|....*...
7YI2_B      356 RPSNMFNVNTPEYLDKVMTNIFANLENT 383
Cdd:cd10000 336 SPSLRPDLNEDQYIEKILETIKGNLKNV 363
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 38-329 6.84e-113

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: 333.43  E-value: 6.84e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B         38 HPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDNLEMFKRESVKFnvGDDCPVFDGLY 117
Cdd:pfam00850   1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAAPEGGALLLLSYLSG--DDDTPVSPGSY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B        118 EYCSISGGGSMEGAARLNRGKCDVAVNYA-GGLHHAKKSEASGFCYLNDIVLGIIELLRYH--PRVLYIDIDVHHGDGVE 194
Cdd:pfam00850  79 EAALLAAGGTLAAADAVLSGEARNAFALVrPPGHHAERDRASGFCIFNNVAIAAKYLREKYglKRVAIVDFDVHHGNGTQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B        195 EAFYTTDRVMTCSFHKYGE-FFPGTGELRDIGVGAGKNYAVNVPLRDGIDDATYRSVFEPVIKKIMEWYQPSAVVLQCGG 273
Cdd:pfam00850 159 EIFYDDPSVLTLSIHQYPGgFYPGTGFADETGEGKGKGYTLNVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAGF 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B        274 DSLSGDRLGCFNLSMEGHANCVNYVKSF----GIPMMVVGGGGYTMRNVARTWCFETGLL 329
Cdd:pfam00850 239 DAHAGDPLGGLNLTTEGFAEITRILLELadplCIRVVSVLEGGYNLDALARSATAVLAAL 298
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
 22-323 7.56e-109

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: 323.36  E-value: 7.56e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       22 AYFYDADVGNYAYGAGHPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDNLEmfkRES 101
Cdd:cd09994   1 AFIYSEEYLRYSFGPNHPFNPPRLSLTKDLLRALGLLPPVDLVPPRPATEEELLLFHTPDYIEAVKEASRGQEP---EGR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      102 VKFNVG-DDCPVFDGLYEYCSISGGGSMEGAARLNRGKCDVAVNYAGGLHHAKKSEASGFCYLNDIVLGIIELLR-YHPR 179
Cdd:cd09994  78 GRLGLGtEDNPVFPGMHEAAALVVGGTLLAARLVLEGEARRAFNPAGGLHHAMRGRASGFCVYNDAAVAIERLRDkGGLR 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      180 VLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYGE-FFPGTGELRDIGVGAGKNYAVNVPLRDGIDDATYRSVFEPVIKKI 258
Cdd:cd09994 158 VAYVDIDAHHGDGVQAAFYDDPRVLTISLHESGRyLFPGTGFVDEIGEGEGYGYAVNIPLPPGTGDDEFLRAFEAVVPPL 237

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      259 MEWYQPSAVVLQCGGDSLSGDRLGCFNLSMEGHANCVNYVK-----SFGIPMMVVGGGGYTMRNVARTWC 323
Cdd:cd09994 238 LRAFRPDVIVSQHGADAHAGDPLTHLNLSNRAYRAAVRRIReladeYCGGRWLALGGGGYNPDVVARAWA 307
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
 44-322 5.09e-96

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: 289.72  E-value: 5.09e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       44 RIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDNLemfKRESVKFNVGDDCPVFDGLYEYCSIS 123
Cdd:cd09301   1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKANFAVAT---ITESKPVIFGPNFPVQRHYFRGARLS 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      124 GGGSMEGAARLNRGKCDVAVNYA-GGLHHAKKSEASGFCYLNDIVLGIIELLRY-HPRVLYIDIDVHHGDGVEEAFYTTD 201
Cdd:cd09301  78 TGGVVEAAELVAKGELERAFAVVgAGGHHAGKSRAWGFCYFNDVVLAIKFLRERgISRILIIDTDAHHGDGTREAFYDDD 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      202 RVMTCSFHKYGEFFPGTGElrdigvgaGKNYAVNVPLRDGIDDATYRSVFEPVIKKIMEWYQPSAVVLQCGGDSLSGDRL 281
Cdd:cd09301 158 RVLHMSFHNYDIYPFGRGK--------GKGYKINVPLEDGLGDEEYLDAVERVISKVLEEFEPEVVVLQFGHDTHEGDRL 229

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
7YI2_B      282 GCFNLSMEGHANCVNYVKSF--GIPMMVVGGGGYTMRNVARTW 322
Cdd:cd09301 230 GGFNLSEKGFVKLAEIVKEFarGGPILMVLGGGYNPEAAARIW 272
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
 44-329 2.51e-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: 2.51e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       44 RIRMAHSLIMNYGL-YKKMEIYRAKPATKQEMCQFHTDEYIDFLSRvtpdnlemfkresvKFNVGDDCPVFDGLYEYCSI 122
Cdd:cd11680  21 RSSLVHSLIRAYGLlQHFDEIIEPERATRKDLTKYHDKDYVDFLLK--------------KYGLEDDCPVFPFLSMYVQL 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      123 SGGGSMEGAARLNRG-KCDVAVNYAGGLHHAKKSEASGFCYLNDIVLGIIELLRYH-PRVLYIDIDVHHGDGVEEAFYTT 200
Cdd:cd11680  87 VAGSSLALAKHLITQvERDIAINWYGGRHHAQKSRASGFCYVNDIVLAILRLRRARfRRVFYLDLDLHHGDGVESAFFFS 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      201 DRVMTCSFHKYGE-FFPGTGELRDigvgAGKNYAVNVPLRDGIDDATYRSVFEPVIKKIMEWYQPSAVVLQCGGDSLSGD 279
Cdd:cd11680 167 KNVLTCSIHRYDPgFFPGTGSLKN----SSDKGMLNIPLKRGLSDKTLLRIIDSIVRPLIEKFEPEVIVIQCGCDGLSGD 242

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
7YI2_B      280 RLGCFNLSMEGHANCVNYVKSF--GIPMMVVGGGGYTMRNVARTWCFETGLL 329
Cdd:cd11680 243 PHKEWNLTIRGYGSVIELLLKEfkDKPTLLLGGGGYNHTEAARAWTYLTSMV 294
PTZ00346 PTZ00346
histone deacetylase; Provisional
 25-329 6.72e-94

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 289.62  E-value: 6.72e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B        25 YDADVGNYAYGAGHPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSrVTPDNLEMFKRESVKF 104
Cdd:PTZ00346  30 YASDMNISAFVPQHAMKPYRVLAAMEIVRSLKIDAHCRTVVPPLVKVEELMAYHTDTYLANLG-LHSCRSWLWNAETSKV 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       105 NVGDDCPVFDGLYEYCSISGGGSMEGAARLNRGKCDVAVNYAGGLHHAKKSEASGFCYLNDIVLGIIELLRYHPRVLYID 184
Cdd:PTZ00346 109 FFSGDCPPVEGLMEHSIATASGTLMGAVLLNSGQVDVAVHWGGGMHHSKCGECSGFCYVNDIVLGILELLKCHDRVLYVD 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       185 IDVHHGDGVEEAFYTTDRVMTCSFHKYGE-FFPGTGELRDIGVGAGKNYAVNVPLRDGIDDATYRSVFEPVIKKIMEWYQ 263
Cdd:PTZ00346 189 IDMHHGDGVDEAFCTSDRVFTLSLHKFGEsFFPGTGHPRDVGYGRGRYYSMNLAVWDGITDFYYLGLFEHALHSIVRRYS 268

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
7YI2_B       264 PSAVVLQCGGDSLSGDRLGCFNLSMEGHANCVNYVKSFGIPMMVVGGGGYTMRNVARTWCFETGLL 329
Cdd:PTZ00346 269 PDAIVLQCGADSLAGDRLGLLNLSSFGHGQCVQAVRDLGIPMLALGGGGYTIRNVAKLWAYETSIL 334
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 21-322 3.04e-89

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 273.14  E-value: 3.04e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       21 VAYFYDADVGNYAYGAGHPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDN-LEMFkr 99
Cdd:COG0123   1 TALIYHPDYLLHDLGPGHPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAASLDGgYGQL-- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      100 esvkfnvGDDCPVFDGLYEYCSISGGGSMEGAARLNRGKCDVA-VNYAGGLHHAKKSEASGFCYLNDIVLGIIELL-RYH 177
Cdd:COG0123  79 -------DPDTPVSPGTWEAALLAAGGALAAADAVLEGEARNAfALVRPPGHHAERDRAMGFCLFNNAAIAARYLLaKGL 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      178 PRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYGeFFPGTGELRDIGVGAGKNYAVNVPLRDGIDDATYRSVFEPVIKK 257
Cdd:COG0123 152 ERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQDP-LYPGTGAADETGEGAGEGSNLNVPLPPGTGDAEYLAALEEALLP 230

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
7YI2_B      258 IMEWYQPSAVVLQCGGDSLSGDRLGCFNLSMEGHANCVNYVKSF----GIPMMVVGGGGYTMRNVARTW 322
Cdd:COG0123 231 ALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELadhcGGPVVSVLEGGYNLDALARSV 299
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
 38-320 3.70e-53

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: 179.23  E-value: 3.70e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       38 HPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDNLEMFkresvkfnvGDDCPVFDGLY 117
Cdd:cd09992   1 HPERPERLLAILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYIERVEETCEAGGGYL---------DPDTYVSPGSY 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      118 EYCSISGGGSMEGAARLNRGKCDVAvnYA-----GglHHAKKSEASGFCYLNDIVLGIIELLRYH--PRVLYIDIDVHHG 190
Cdd:cd09992  72 EAALLAAGAALAAVDAVLSGEAENA--FAlvrppG--HHAEPDRAMGFCLFNNVAIAARYAQKRYglKRVLIVDWDVHHG 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      191 DGVEEAFYTTDRVMTCSFHKYGeFFPGTGELRDIGVGAGKNYAVNVPLRDGIDDATYRSVFEPVIKKIMEWYQPSAVVLQ 270
Cdd:cd09992 148 NGTQDIFYDDPSVLYFSIHQYP-FYPGTGAAEETGGGAGEGFTINVPLPPGSGDAEYLAAFEEVLLPIAREFQPDLVLVS 226

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
7YI2_B      271 CGGDSLSGDRLGCFNLSMEGHANCVNYVKSF-----GIPMMVVGGGGYTMRNVAR 320
Cdd:cd09992 227 AGFDAHRGDPLGGMNLTPEGYARLTRLLKELadehcGGRLVFVLEGGYNLEALAE 281
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
 21-290 9.39e-46

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: 161.96  E-value: 9.39e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       21 VAYFYD-----ADVGNYAY----------GAGHPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDf 85
Cdd:cd09996   1 TGFVWDerylwHDTGTGALflpvggllvqPGRHPENPETKRRIKNLLEVSGLSDHLVLITPRPATDEELLRVHTPEYID- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       86 lsrvtpdnleMFKRESvKFNVGDDC---PVFDGLYEYCSISGGGSMEGAARLNRGKCDVAvnYA-----GglHHAKKSEA 157
Cdd:cd09996  80 ----------RVKAAS-AAGGGEAGggtPFGPGSYEIALLAAGGAIAAVDAVLDGEVDNA--YAlvrppG--HHAEPDQG 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      158 SGFCYLNDIVLGIIELLRYHP--RVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYGEFFPGTGELRDIGVGAGKNYAVN 235
Cdd:cd09996 145 MGFCLFNNVAIAARHALAVGGvkRVAVVDWDVHHGNGTQAIFYDDPDVLTISLHQDRCFPPDSGAVEERGEGAGEGYNLN 224

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
7YI2_B      236 VPLRDGIDDATYRSVFEPVIKKIMEWYQPSAVVLQCGGDSLSGDRLGCFNLSMEG 290
Cdd:cd09996 225 IPLPPGSGDGAYLHAFERIVLPALRAFRPELIIVASGFDASAFDPLGRMMLTSDG 279
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 38-321 7.50e-43

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: 151.88  E-value: 7.50e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       38 HPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDNLEMFKresVKFnvgddcPVFDGLY 117
Cdd:cd09993   1 HRFPMRKYGLLREALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLESLKSGELSREEIRR---IGF------PWSPELV 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      118 EYCSISGGGSMEgAAR--LNRGkcdVAVNYAGGLHHAKKSEASGFCYLNDIVLGIIELLRYHP--RVLYIDIDVHHGDGV 193
Cdd:cd09993  72 ERTRLAVGGTIL-AARlaLEHG---LAINLAGGTHHAFPDRGEGFCVFNDIAIAARVLLAEGLvrRVLIVDLDVHQGNGT 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      194 EEAFYTTDRVMTCSFHkyGE-FFPGTGELRDIgvgagknyavNVPLRDGIDDATYRSVFEPVIKKIMEWYQPSAVVLQCG 272
Cdd:cd09993 148 AAIFADDPSVFTFSMH--GEkNYPFRKEPSDL----------DVPLPDGTGDDEYLAALEEALPRLLAEFRPDLVFYNAG 215

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
7YI2_B      273 GDSLSGDRLGCFNLSMEGHANCVNYV----KSFGIPMMVVGGGGYtMRNVART 321
Cdd:cd09993 216 VDVLAGDRLGRLSLSLEGLRERDRLVlrfaRARGIPVAMVLGGGY-SRDIARL 267
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 37-330 1.71e-41

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: 149.77  E-value: 1.71e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       37 GHPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDNLEMFKRESVKFnvgDDCPVFDGL 116
Cdd:cd10002   6 NHIECPERLEAILERLTQDGLLERCVKIPAREAEEDEILLVHSQEYIDLVKSTETMEKEELESLCSGY---DSVYLCPST 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      117 YEYCSISGGGSMEGAARLNRGKCdvavnyAGGL-------HHAKKSEASGFCYLNDIVLG---IIELLRYHpRVLYIDID 186
Cdd:cd10002  83 YEAARLAAGSTIELVKAVMAGKI------QNGFalirppgHHAMRNEANGYCIFNNVAIAakyAIEKLGLK-RILIVDWD 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      187 VHHGDGVEEAFYTTDRVMTCSFHKY--GEFFPGTGE--LRDIGVGAGKNYAVNVPLRD-GIDDATYRSVFEPVIKKIMEW 261
Cdd:cd10002 156 VHHGQGTQQGFYEDPRVLYFSIHRYehGRFWPHLFEsdYDYIGVGHGYGFNVNVPLNQtGLGDADYLAIFHHILLPLALE 235

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
7YI2_B      262 YQPSAVVLQCGGDSLSGDRLGCFNLSMEGHANCVNYVKSFGIPMMVVG-GGGYTMRNVARTWCFET-GLLN 330
Cdd:cd10002 236 FQPELVLVSAGFDASIGDPEGEMAVTPAGYAHLTRLLMGLAGGKLLLVlEGGYLLESLAESVSMTLrGLLG 306
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 37-321 6.11e-41

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: 147.88  E-value: 6.11e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       37 GHPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDF---LSRVTPDNL----EMFKRESVKFNvgdd 109
Cdd:cd11600   2 PHPEDPSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEHWDRveaTEKMSDEQLkdrtEIFERDSLYVN---- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      110 cpvfdGLYEYCS-ISGGGSMEGAARLNRG--KCDVAVNYAGGlHHAKKSEASGFCYLNDIVLGIIELL-RYHP---RVLY 182
Cdd:cd11600  78 -----NDTAFCArLSCGGAIEACRAVAEGrvKNAFAVVRPPG-HHAEPDESMGFCFFNNVAVAAKWLQtEYPDkikKILI 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      183 IDIDVHHGDGVEEAFYTTDRVMTCSFHKY--GEFFPGT--GELRDIGVGAGKNYAVNVPLRD-GIDDATYRSVFEPVIKK 257
Cdd:cd11600 152 LDWDIHHGNGTQRAFYDDPNVLYISLHRFenGGFYPGTpyGDYESVGEGAGLGFNVNIPWPQgGMGDADYIYAFQRIVMP 231

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
7YI2_B      258 IMEWYQPSAVVLQCGGDSLSGDRLGCFNLSMEGHANCVNYVKSF-GIPMMVVGGGGYTMRNVART 321
Cdd:cd11600 232 IAYEFDPDLVIISAGFDAADGDELGQCHVTPAGYAHMTHMLMSLaGGKLVVALEGGYNLDAISDS 296
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
 37-329 1.59e-38

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: 140.75  E-value: 1.59e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       37 GHPMKPHRIRMAHSLIMNYGLYKKMEiyrAKPATKQEMCQFHTDEYIDFLSRVTPDnlemfkresvkfnvgddCPVFDGL 116
Cdd:cd10001  24 PHPENPERAEAILDALKRAGLGEVLP---PRDFGLEPILAVHDPDYVDFLETADTD-----------------TPISEGT 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      117 YEYCSISGGGSMEGAARLNRGkCDVAvnYA-----GglHHAKKSEASGFCYLNDIVLGIIELLRYHPRVLYIDIDVHHGD 191
Cdd:cd10001  84 WEAALAAADTALTAADLVLEG-ERAA--YAlcrppG--HHAGRDRAGGFCYFNNAAIAAQYLRDRAGRVAILDVDVHHGN 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      192 GVEEAFYTTDRVMTCSFHKYGE-FFPGT-GELRDIGVGAGKNYAVNVPLRDGIDDATYRSVFEPVIKKIMEwYQPSAVVL 269
Cdd:cd10001 159 GTQEIFYERPDVLYVSIHGDPRtFYPFFlGFADETGEGEGEGYNLNLPLPPGTGDDDYLAALDEALAAIAA-FGPDALVV 237

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
7YI2_B      270 QCGGDSLSGDRLGCFNLSMEGHANCVNYVKSFGIPMMVVGGGGYT----MRNVARtwcFETGLL 329
Cdd:cd10001 238 SLGFDTHEGDPLSDFKLTTEDYARIGRRIAALGLPTVFVQEGGYNvdalGRNAVA---FLAGFE 298
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
 37-319 4.32e-38

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: 141.32  E-value: 4.32e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       37 GHPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDNLEMFKRESVKFNVGDDCPvfdGL 116
Cdd:cd10003  15 GHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHLDEMKSLEKMKPRELNRLGKEYDSIYIHP---DS 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      117 YEYCSISGGGSMEGAARLNRGKCD--VAVNYAGGlHHAKKSEASGFCYLNDIVLGI-IELLRYHP-RVLYIDIDVHHGDG 192
Cdd:cd10003  92 YQCALLAAGCVLQVVEAVLTGESRngVAIVRPPG-HHAEQDTACGFCFFNNVAIAArYAQKKYGLkRILIVDWDVHHGNG 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      193 VEEAFYTTDRVMTCSFHKY--GEFFPGT--GELRDIGVGAGKNYAVNVPL-RDGIDDATYRSVFEPVIKKIMEWYQPSAV 267
Cdd:cd10003 171 TQHMFESDPSVLYISLHRYdnGSFFPNSpeGNYDVVGKGKGEGFNVNIPWnKGGMGDAEYIAAFQQVVLPIAYEFNPELV 250

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
7YI2_B      268 VLQCGGDSLSGDRLGCFNLSMEGHANCVNYVKSF-GIPMMVVGGGGYTMRNVA 319
Cdd:cd10003 251 LVSAGFDAARGDPLGGCKVTPEGYAHMTHMLMSLaGGRVIVILEGGYNLTSIS 303
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 30-297 1.92e-32

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: 126.31  E-value: 1.92e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       30 GNYAYgagHPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIdFLSRVTPdnLEMFKRESVKFNVgdd 109
Cdd:cd11681  19 GNNSS---HPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHT-LLYGTNP--LSRLKLDPTKLAG--- 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      110 cpvfDGLYEYCSISGGG------------SMEGAARLNRGkC--DVAVNYAGGL------------HHAKKSEASGFCYL 163
Cdd:cd11681  90 ----LPQKSFVRLPCGGigvdsdtvwnelHTSNAARMAVG-CviDLAFKVATGElkngfavvrppgHHAEPSQAMGFCFF 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      164 NDIVLGIIELLRYHP--RVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKY--GEFFPGTGELRDIGVGAGKNYAVNVPLR 239
Cdd:cd11681 165 NSVAIAAKQLQQKLKlrKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYddGNFFPGTGAPTEVGSGAGEGFNVNIAWS 244

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
7YI2_B      240 DGID----DATYRSVFEPVIKKIMEWYQPSAVVLQCGGDSLSG--DRLGCFNLSmeghANCVNY 297
Cdd:cd11681 245 GGLDppmgDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGhpPPLGGYKVS----PACFGY 304
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
 38-311 3.35e-31

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: 123.61  E-value: 3.35e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       38 HPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIdFLSRVTPDNLEmfKRESVKFnVGDDCPVFDGLY 117
Cdd:cd10006  27 HPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHT-LLYGTNPLNRQ--KLDSKKL-LGSLASVFVRLP 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      118 eyCSISGGGS--------MEGAARLNRGKC-DVAVNYAGGL------------HHAKKSEASGFCYLNDIVLGIiELLRY 176
Cdd:cd10006 103 --CGGVGVDSdtiwnevhSSGAARLAVGCVvELVFKVATGElkngfavvrppgHHAEESTPMGFCYFNSVAIAA-KLLQQ 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      177 H---PRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKY--GEFFPGTGELRDIGVGAGKNYAVNVPLRDGID----DATY 247
Cdd:cd10006 180 RlnvSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYddGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDppmgDAEY 259

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
7YI2_B      248 RSVFEPVIKKIMEWYQPSAVVLQCGGDSLSGD--RLGCFNLSmeghANCVNYVKSfgiPMMVVGGG 311
Cdd:cd10006 260 LAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHptPLGGYNLS----AKCFGYLTK---QLMGLAGG 318
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
 38-311 1.78e-29

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: 118.94  E-value: 1.78e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       38 HPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTdEYIDFLSRVTPDNLEmfKRESVKFnVGddcPVFDGLY 117
Cdd:cd10007  26 HPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHS-EHHTLLYGTSPLNRQ--KLDSKKL-LG---PLSQKMY 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      118 EYCSISGGG----------SMEGAARLNRGkCDVAVNY---AGGL-----------HHAKKSEASGFCYLNDIVLGIiEL 173
Cdd:cd10007  99 AVLPCGGIGvdsdtvwnemHSSSAVRMAVG-CLIELAFkvaAGELkngfavirppgHHAEESTAMGFCFFNSVAIAA-KL 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      174 LRYH---PRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKY--GEFFPGTGELRDIGVGAGKNYAVNVPLRDGID----D 244
Cdd:cd10007 177 LQQKlnvGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYddGNFFPGSGAPDEVGAGPGVGFNVNIAWTGGVDppigD 256

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
7YI2_B      245 ATYRSVFEPVIKKIMEWYQPSAVVLQCGGDSLSGDR--LGCFNLSmeghANCVNYVKSfgiPMMVVGGG 311
Cdd:cd10007 257 VEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGHQspLGGYSVT----AKCFGHLTK---QLMTLAGG 318
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
 38-287 3.53e-29

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: 115.30  E-value: 3.53e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       38 HPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDNLEMFkresvkfnVGDDCPVFDGLY 117
Cdd:cd11599   1 HPESPERLEAILDALIASGLDRLLRQLEAPPATREQLLRVHDAAYVDRLEAAAPEEGLVQ--------LDPDTAMSPGSL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      118 EYCSISGGGSMEGAARLNRGKCD---VAVNYAGglHHAKKSEASGFCYLNDIVLGIIELLRYHP--RVLYIDIDVHHGDG 192
Cdd:cd11599  73 EAALRAAGAVVAAVDAVMAGEARnafCAVRPPG--HHAERDKAMGFCLFNNVAIAAAHALAHHGleRVAIVDFDVHHGNG 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      193 VEEAFYTTDRVMTCSFHKYgEFFPGTGELRDIGVGagknYAVNVPLRDGIDDATYRSVFEPVIKKIMEWYQPSAVVLQCG 272
Cdd:cd11599 151 TEDIFRDDPRVLFCSSHQH-PLYPGTGAPDETGHG----NIVNVPLPAGTGGAEFREAVEDRWLPALDAFKPDLILISAG 225

                       250
                ....*....|....*
7YI2_B      273 GDSLSGDRLGCFNLS 287
Cdd:cd11599 226 FDAHRDDPLAQLNLT 240
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
 38-311 3.75e-28

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: 114.34  E-value: 3.75e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       38 HPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYI-----DFLSRVTPDNLEMF----KRESVKFNVG- 107
Cdd:cd10008  24 HPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVllygtNPLSRLKLDNGKLAgllaQRMFVMLPCGg 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      108 ---DDCPVFDGLYEycsisgggsmEGAARLNRGKC-DVAVNYAG-----GL-------HHAKKSEASGFCYLNDIVLGI- 170
Cdd:cd10008 104 vgvDTDTIWNELHS----------SNAARWAAGSVtDLAFKVASrelknGFavvrppgHHADHSTAMGFCFFNSVAIACr 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      171 -IELLRYHPRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKY--GEFFPGTGELRDIGVGAGKNYAVNVPLRDGID---- 243
Cdd:cd10008 174 qLQQQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHddGNFFPGSGAVDEVGAGSGEGFNVNVAWAGGLDppmg 253

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      244 DATYRSVFEPVIKKIMEWYQPSAVVLQCGGDSLSGD--RLGCFNLSmeghANCVNYVKSfgiPMMVVGGG 311
Cdd:cd10008 254 DPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHpaPLGGYHVS----AKCFGYMTQ---QLMNLAGG 316
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
 30-278 1.12e-26

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: 110.49  E-value: 1.12e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       30 GNYAygaGHPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEY-----IDFLSRVTPDNLEMFKRESVKF 104
Cdd:cd10009  19 GNST---THPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHsllygTNPLDGQKLDPRILLGDDSQKF 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      105 NVGDDCPVF----DGLYEYCSISGGGSM------EGAARLNRG--KCDVAVNYAGGlHHAKKSEASGFCYLNDIVLgIIE 172
Cdd:cd10009  96 FSSLPCGGLgvdsDTIWNELHSSGAARMavgcviELASKVASGelKNGFAVVRPPG-HHAEESTAMGFCFFNSVAI-TAK 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      173 LLRYH---PRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKY--GEFFPGTGELRDIGVGAGKNYAVNVPLRDGID---- 243
Cdd:cd10009 174 YLRDQlniSKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdeGNFFPGSGAPNEVGTGLGEGYNINIAWTGGLDppmg 253

                       250       260       270
                ....*....|....*....|....*....|....*
7YI2_B      244 DATYRSVFEPVIKKIMEWYQPSAVVLQCGGDSLSG 278
Cdd:cd10009 254 DVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEG 288
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 129-326 1.71e-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: 103.22  E-value: 1.71e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      129 EGAARLNRGKCDVAVNYAGglHHAKKseasgfcylNDIVLGIIELlryHPRVLYIDIDVHHGDGVEEAFY---------- 198
Cdd:cd09987  15 AGVVVAVLKDGKVPVVLGG--DHSIA---------NGAIRAVAEL---HPDLGVIDVDAHHDVRTPEAFGkgnhhtprhl 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      199 ----TTDRVMTCSFHKYGEFFPGTGelrdiGVGAGKNYAVNVPLRDGiDDATYRSVFEPVIKKIMewYQPSAVVLQCGGD 274
Cdd:cd09987  81 lcepLISDVHIVSIGIRGVSNGEAG-----GAYARKLGVVYFSMTEV-DKLGLGDVFEEIVSYLG--DKGDNVYLSVDVD 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
7YI2_B      275 SLSGD------RLGCFNLSMEGHANCVNYVKSFGIPMMVVGGGGYTM----RNVARTWCFET 326
Cdd:cd09987 153 GLDPSfapgtgTPGPGGLSYREGLYITERIAKTNLVVGLDIVEVNPLldetGRTARLAAALT 214
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
 36-323 3.09e-23

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: 99.93  E-value: 3.09e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       36 AGHPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDNLEMFKRESVKFnvgDDCPVFDG 115
Cdd:cd11682   5 ESFPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYVALMKSTQYMTEEELRTLADTY---DSVYLHPN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      116 LYEYCSISGGGSMEGAARLNRGKC--DVAVNYAGGlHHAKKSEASGFCYLNDIVLGIIELLRYH--PRVLYIDIDVHHGD 191
Cdd:cd11682  82 SYSCACLAVGSVLQLVDKVLGGEIrnGLAIVRPPG-HHAQHDKMDGYCMFNNVAIAARYAQQKHgvQRVLIVDWDVHHGQ 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      192 GVEEAFYTTDRVMTCSFHKY--GEFFPGTGE--LRDIGVGAGKNYAVNVPL-RDGIDDATYRSVFEPVIKKIMEWYQPSA 266
Cdd:cd11682 161 GTQFIFEQDPSVLYFSIHRYeqGRFWPHLKEsdSSAVGFGRGEGYNINVPWnQVGMRDADYIAAFLHVLLPVALEFQPQL 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
7YI2_B      267 VVLQCGGDSLSGDRLGCFNLSMEGHANCVNYVKSFGIPMMVVG-GGGYTMRNVARTWC 323
Cdd:cd11682 241 VLVAAGFDAVIGDPKGEMAATPACFAHLTHLLMGLAGGKLILSlEGGYNLRSLAEGVC 298
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 42-323 3.67e-21

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: 93.77  E-value: 3.67e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B       42 PHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDNLEMFKRESVKFnvgDDCPVFDGLYEYCS 121
Cdd:cd11683  11 PERLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRETQVMNKEELMAISGKY---DAVYFHPNTFHCAR 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      122 ISGGGSMEGA-ARLNRGKCD-VAVNYAGGlHHAKKSEASGFCYLNDIVLGIIELLRYH--PRVLYIDIDVHHGDGVEEAF 197
Cdd:cd11683  88 LAAGATLQLVdAVLTGEVQNgMALVRPPG-HHSQRNAANGFCVFNNVAIAAEYAKKKYglHRILIVDWDVHHGQGIQYIF 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7YI2_B      198 YTTDRVMTCSFHKY--GEFFPGTGE--LRDIGVGAGKNYAVNVPLRD-GIDDATYRSVFEPVIKKIMEWYQPSAVVLQCG 272
Cdd:cd11683 167 EEDPSVLYFSWHRYehQRFWPFLREsdYDAVGRGKGLGFNINLPWNKvGMGNADYLAAFFHVLLPLAFEFDPELVLVSAG 246

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
7YI2_B      273 GDSLSGDRLGCFNLSMEGHANCVNYVKSF-GIPMMVVGGGGYTMRNVARTWC 323
Cdd:cd11683 247 FDSAIGDPEGQMCATPECFAHLTHLLMVLaGGKLCAVLEGGYHLESLAESVC 298
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
 150-195 8.05e-07

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: 50.91  E-value: 8.05e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
7YI2_B      150 HHAKKSEASGFCYLNDIVLGIIELLRYH--PRVLYIDIDVHHGDGVEE 195
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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