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Conserved domains on  [gi|324073135|ref|NP_001191205|]
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histone deacetylase 7 isoform 2 [Mus musculus]

Protein Classification

histone deacetylase 7( domain architecture ID 10178055)

histone deacetylase 7 (HD7) 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)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
 515-890 0e+00

Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. Class IIa histone deacetylases are signal-dependent co-repressors, having N-terminal regulatory domain with two or three conserved serine residues; phosphorylation of these residues is important for ability to shuttle between the nucleus and cytoplasm and act as transcriptional co-repressors. HDAC7 is involved in regulation of myocyte migration and differentiation. Known interaction partners of class IIa HDAC7 are myocyte enhancer factors - MEF2A, -2C, and -2D, 14-3-3 proteins, SMRT and N-CoR co-repressors, HDAC3, ETA (endothelin receptor). This enzyme is also involved in the development of the immune system as well as brain and heart development. Multiple alternatively spliced transcript variants encoding several isoforms have been found for this gene.


:

Pssm-ID: 212532 [Multi-domain]  Cd Length: 378  Bit Score: 841.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 515 TGLVYDSVMLKHQCSCGDNSKHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLKL 594
Cdd:cd10008    3 TGLVYDSVMLKHQCSCGDNSNHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLKL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 595 DNGKLTGLLAQRTFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGF 674
Cdd:cd10008   83 DNGKLAGLLAQRMFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGF 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 675 CFFNSVAIACRQLQQHGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGTGSGEGFNVNV 754
Cdd:cd10008  163 CFFNSVAIACRQLQQQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGAGSGEGFNVNV 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 755 AWAGGLDPPMGDPEYLAAFRIVVMPIAREFAPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVLAL 834
Cdd:cd10008  243 AWAGGLDPPMGDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVLAL 322

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 324073135 835 EGGHDLTAICDASEACVAALLGNKVDPLSEESWKQKPNLSAIRSLEAVVRVHRKYW 890
Cdd:cd10008  323 EGGHDLTAICDASEACVAALLGNEVDPLSEESWKQKPNLNAIRSLEAVIRVHSKYW 378
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 100-514 5.57e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 5.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135  100 AALERTVHPSSPSIPYRTLEPLDTEGAARSVLSSFLPPVPSLPTEPP------------EHFPLRKTVSEPNLKLRYKPK 167
Cdd:PHA03247 2581 AVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPppspspaanepdPHPPPTVPPPERPRDDPAPGR 2660

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135  168 KSLERRKNPLLR--KESAPPSLRRRPAetlgdssPSSSSTPASGCSSPNDSEHGPNPAlgSEALLGQRLRLQETSLAPFA 245
Cdd:PHA03247 2661 VSRPRRARRLGRaaQASSPPQRPRRRA-------ARPTVGSLTSLADPPPPPPTPEPA--PHALVSATPLPPGPAAARQA 2731

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135  246 LPTVSLLPAITLGLPAPARADGDRRTHSTLGPRGPVLGNPHAplflhhglEPEAGGTLPSRLQPILLLDPSVSHAPLWTV 325
Cdd:PHA03247 2732 SPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPA--------APAAGPPRRLTRPAVASLSESRESLPSPWD 2803

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135  326 PGLGPLPFHFAQPLLTTERLSGSGLHRPLNRTRSEPLPPSATASPLLAP---LQPRQD--RLKPHVQLIKRPAKPSEKP- 399
Cdd:PHA03247 2804 PADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLggsVAPGGDvrRRPPSRSPAAKPAAPARPPv 2883

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135  400 -RLRQIPSAEDLETDgggvgPMANDGLEHRESGRGPPEGRGSISLQQHQQVPPWEQQH-------LAGRLSQGSPGDSVL 471
Cdd:PHA03247 2884 rRLARPAVSRSTESF-----ALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPprpqpplAPTTDPAGAGEPSGA 2958

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 324073135  472 IPLAQVGHR-----PLSRTQSSPAAPvSLLSPEPTcqTQVLNSSETPA 514
Cdd:PHA03247 2959 VPQPWLGALvpgrvAVPRFRVPQPAP-SREAPASS--TPPLTGHSLSR 3003
 
Name Accession Description Interval E-value
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
 515-890 0e+00

Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. Class IIa histone deacetylases are signal-dependent co-repressors, having N-terminal regulatory domain with two or three conserved serine residues; phosphorylation of these residues is important for ability to shuttle between the nucleus and cytoplasm and act as transcriptional co-repressors. HDAC7 is involved in regulation of myocyte migration and differentiation. Known interaction partners of class IIa HDAC7 are myocyte enhancer factors - MEF2A, -2C, and -2D, 14-3-3 proteins, SMRT and N-CoR co-repressors, HDAC3, ETA (endothelin receptor). This enzyme is also involved in the development of the immune system as well as brain and heart development. Multiple alternatively spliced transcript variants encoding several isoforms have been found for this gene.


Pssm-ID: 212532 [Multi-domain]  Cd Length: 378  Bit Score: 841.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 515 TGLVYDSVMLKHQCSCGDNSKHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLKL 594
Cdd:cd10008    3 TGLVYDSVMLKHQCSCGDNSNHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLKL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 595 DNGKLTGLLAQRTFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGF 674
Cdd:cd10008   83 DNGKLAGLLAQRMFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGF 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 675 CFFNSVAIACRQLQQHGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGTGSGEGFNVNV 754
Cdd:cd10008  163 CFFNSVAIACRQLQQQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGAGSGEGFNVNV 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 755 AWAGGLDPPMGDPEYLAAFRIVVMPIAREFAPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVLAL 834
Cdd:cd10008  243 AWAGGLDPPMGDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVLAL 322

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 324073135 835 EGGHDLTAICDASEACVAALLGNKVDPLSEESWKQKPNLSAIRSLEAVVRVHRKYW 890
Cdd:cd10008  323 EGGHDLTAICDASEACVAALLGNEVDPLSEESWKQKPNLNAIRSLEAVIRVHSKYW 378
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 536-854 4.16e-116

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: 357.32  E-value: 4.16e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135  536 HPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHV-LLYGTNPLSRLKLDNGKLTGllaqrtfvmlpcg 614
Cdd:pfam00850   1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLeFLEEAAPEGGALLLLSYLSG------------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135  615 gvgvDTDTIWNElHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGFCFFNSVAIACRQLQQHGKAS 694
Cdd:pfam00850  68 ----DDDTPVSP-GSYEAALLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLK 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135  695 KILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHdDGNFFPGSGAVDEVGTGSGEGFNVNVAWAGGldppMGDPEYLAAFR 774
Cdd:pfam00850 143 RVAIVDFDVHHGNGTQEIFYDDPSVLTLSIHQY-PGGFYPGTGFADETGEGKGKGYTLNVPLPPG----TGDAEYLAAFE 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135  775 IVVMPIAREFAPDLVLVSAGFDAAEGHpaPLGGYHVSAKCFGYMTQQLMNLA---GGAVVLALEGGHDLTAICDASEACV 851
Cdd:pfam00850 218 EILLPALEEFQPDLILVSAGFDAHAGD--PLGGLNLTTEGFAEITRILLELAdplCIRVVSVLEGGYNLDALARSATAVL 295


                  ...
gi 324073135  852 AAL 854
Cdd:pfam00850 296 AAL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 515-856 1.24e-101

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 319.75  E-value: 1.24e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 515 TGLVYDSVMLKHQCSCGdnskHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVllygtnplSRLKl 594
Cdd:COG0123    1 TALIYHPDYLLHDLGPG----HPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYV--------DALR- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 595 dNGKLTGllaqrtfvmlpcGGVGVDTDTIWNElHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGF 674
Cdd:COG0123   68 -AASLDG------------GYGQLDPDTPVSP-GTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGF 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 675 CFFNSVAIACRQLQQHGkASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHddgNFFPGSGAVDEVGTGSGEGFNVNV 754
Cdd:COG0123  134 CLFNNAAIAARYLLAKG-LERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD---PLYPGTGAADETGEGAGEGSNLNV 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 755 AwaggLDPPMGDPEYLAAFRIVVMPIAREFAPDLVLVSAGFDAAEGHpaPLGGYHVSAKCFGYMTQQLMNLA---GGAVV 831
Cdd:COG0123  210 P----LPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHADD--PLGRLNLTTEGYAWRTRRVLELAdhcGGPVV 283

                        330       340
                 ....*....|....*....|....*
gi 324073135 832 LALEGGHDLTAICDASEACVAALLG 856
Cdd:COG0123  284 SVLEGGYNLDALARSVAAHLETLLG 308
PTZ00063 PTZ00063
histone deacetylase; Provisional
 536-824 3.20e-23

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 103.74  E-value: 3.20e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 536 HPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVllygtNPLSRLKLDNGKLTGLLAQRTfvmlpcgG 615
Cdd:PTZ00063  23 HPMKPQRIRMAHALILSYDLYKHMEIYRPHKSVEPELVLFHDEEYV-----DFLSSISPENYRDFTYQLKRF-------N 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 616 VGVDTDT-IWNELHSSNAArwAAGSVTDLAFKvasreLKNGFA--VVRPPG--HHADHSTAMGFCFFNSVAIACRQLQQH 690
Cdd:PTZ00063  91 VGEATDCpVFDGLFEFQQS--CAGASIDGAYK-----LNNHQAdiCVNWSGglHHAKRSEASGFCYINDIVLGILELLKY 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 691 gkASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHddGNFFPGSGAVDEVGTGSGEGFNVNVAWAGGLDppmgDPEYL 770
Cdd:PTZ00063 164 --HARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFPGTGDVTDIGVAQGKYYSVNVPLNDGID----DDSFV 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 771 AAFRIVVMPIAREFAPDLVLVSAGFDAA------------EGHPA----------PL-----GGYHVS--AKCFGYMTQQ 821
Cdd:PTZ00063 236 DLFKPVISKCVEVYRPGAIVLQCGADSLtgdrlgrfnltiKGHAAcvefvrslniPLlvlggGGYTIRnvARCWAYETGV 315


                 ...
gi 324073135 822 LMN 824
Cdd:PTZ00063 316 ILN 318
PHA03247 PHA03247
large tegument protein UL36; Provisional
 100-514 5.57e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 5.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135  100 AALERTVHPSSPSIPYRTLEPLDTEGAARSVLSSFLPPVPSLPTEPP------------EHFPLRKTVSEPNLKLRYKPK 167
Cdd:PHA03247 2581 AVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPppspspaanepdPHPPPTVPPPERPRDDPAPGR 2660

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135  168 KSLERRKNPLLR--KESAPPSLRRRPAetlgdssPSSSSTPASGCSSPNDSEHGPNPAlgSEALLGQRLRLQETSLAPFA 245
Cdd:PHA03247 2661 VSRPRRARRLGRaaQASSPPQRPRRRA-------ARPTVGSLTSLADPPPPPPTPEPA--PHALVSATPLPPGPAAARQA 2731

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135  246 LPTVSLLPAITLGLPAPARADGDRRTHSTLGPRGPVLGNPHAplflhhglEPEAGGTLPSRLQPILLLDPSVSHAPLWTV 325
Cdd:PHA03247 2732 SPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPA--------APAAGPPRRLTRPAVASLSESRESLPSPWD 2803

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135  326 PGLGPLPFHFAQPLLTTERLSGSGLHRPLNRTRSEPLPPSATASPLLAP---LQPRQD--RLKPHVQLIKRPAKPSEKP- 399
Cdd:PHA03247 2804 PADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLggsVAPGGDvrRRPPSRSPAAKPAAPARPPv 2883

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135  400 -RLRQIPSAEDLETDgggvgPMANDGLEHRESGRGPPEGRGSISLQQHQQVPPWEQQH-------LAGRLSQGSPGDSVL 471
Cdd:PHA03247 2884 rRLARPAVSRSTESF-----ALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPprpqpplAPTTDPAGAGEPSGA 2958

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 324073135  472 IPLAQVGHR-----PLSRTQSSPAAPvSLLSPEPTcqTQVLNSSETPA 514
Cdd:PHA03247 2959 VPQPWLGALvpgrvAVPRFRVPQPAP-SREAPASS--TPPLTGHSLSR 3003
 
Name Accession Description Interval E-value
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
 515-890 0e+00

Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. Class IIa histone deacetylases are signal-dependent co-repressors, having N-terminal regulatory domain with two or three conserved serine residues; phosphorylation of these residues is important for ability to shuttle between the nucleus and cytoplasm and act as transcriptional co-repressors. HDAC7 is involved in regulation of myocyte migration and differentiation. Known interaction partners of class IIa HDAC7 are myocyte enhancer factors - MEF2A, -2C, and -2D, 14-3-3 proteins, SMRT and N-CoR co-repressors, HDAC3, ETA (endothelin receptor). This enzyme is also involved in the development of the immune system as well as brain and heart development. Multiple alternatively spliced transcript variants encoding several isoforms have been found for this gene.


Pssm-ID: 212532 [Multi-domain]  Cd Length: 378  Bit Score: 841.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 515 TGLVYDSVMLKHQCSCGDNSKHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLKL 594
Cdd:cd10008    3 TGLVYDSVMLKHQCSCGDNSNHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLKL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 595 DNGKLTGLLAQRTFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGF 674
Cdd:cd10008   83 DNGKLAGLLAQRMFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGF 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 675 CFFNSVAIACRQLQQHGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGTGSGEGFNVNV 754
Cdd:cd10008  163 CFFNSVAIACRQLQQQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGAGSGEGFNVNV 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 755 AWAGGLDPPMGDPEYLAAFRIVVMPIAREFAPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVLAL 834
Cdd:cd10008  243 AWAGGLDPPMGDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVLAL 322

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 324073135 835 EGGHDLTAICDASEACVAALLGNKVDPLSEESWKQKPNLSAIRSLEAVVRVHRKYW 890
Cdd:cd10008  323 EGGHDLTAICDASEACVAALLGNEVDPLSEESWKQKPNLNAIRSLEAVIRVHSKYW 378
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 515-890 0e+00

Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues of histones (EC 3.5.1.98) to yield deacetylated histones. This subclass includes animal HDAC4, HDAC5, HDAC7, and HDCA9. Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. Class IIa histone deacetylases are signal-dependent co-repressors, they have N-terminal regulatory domain with two or three conserved serine residues, phosphorylation of these residues is important for ability to shuttle between the nucleus and cytoplasm and act as transcriptional co-repressors. HDAC9 is involved in regulation of gene expression and dendritic growth in developing cortical neurons. It also plays a role in hematopoiesis. HDAC7 is involved in regulation of myocyte migration and differentiation. HDAC5 is involved in integration of chronic drug (cocaine) addiction and depression with changes in chromatin structure and gene expression. HDAC4 participates in regulation of chondrocyte hypertrophy and skeletogenesis.


Pssm-ID: 212544 [Multi-domain]  Cd Length: 377  Bit Score: 778.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 515 TGLVYDSVMLKHQCSCGDNSKHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLKL 594
Cdd:cd11681    3 TGLAYDPLMLKHQCICGNNSSHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTLLYGTNPLSRLKL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 595 DNGKLTGLlAQRTFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGF 674
Cdd:cd11681   83 DPTKLAGL-PQKSFVRLPCGGIGVDSDTVWNELHTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQAMGF 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 675 CFFNSVAIACRQLQQHGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGTGSGEGFNVNV 754
Cdd:cd11681  162 CFFNSVAIAAKQLQQKLKLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFPGTGAPTEVGSGAGEGFNVNI 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 755 AWAGGLDPPMGDPEYLAAFRIVVMPIAREFAPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVLAL 834
Cdd:cd11681  242 AWSGGLDPPMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPPPLGGYKVSPACFGYMTRQLMNLAGGKVVLAL 321

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 324073135 835 EGGHDLTAICDASEACVAALLGNKVDPLSEESWKQKPNLSAIRSLEAVVRVHRKYW 890
Cdd:cd11681  322 EGGYDLTAICDASEACVRALLGDELDPLSEEELERRPNPNAVTSLEKVIAIQSPYW 377
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
 515-898 0e+00

Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. Class IIa histone deacetylases are signal-dependent co-repressors, having N-terminal regulatory domain with two or three conserved serine residues; phosphorylation of these residues is important for ability to shuttle between the nucleus and cytoplasm and act as transcriptional co-repressors. HDAC4 participates in regulation of chondrocyte hypertrophy and skeletogenesis. However, biological substrates for HDAC4 have not been identified; only low lysine deacetylation activity has been demonstrated and active site mutant has enhanced activity toward acetylated lysines. HDAC4 does not bind DNA directly, but through transcription factors MEF2C (myocyte enhancer factor-2C) and MEF2D. Other known interaction partners of the protein are 14-3-3 proteins, SMRT and N-CoR co-repressors, BCL6, HP1, SUMO-1 ubiquitin-like protein, and ANKRA2. It appears to interact in a multiprotein complex with RbAp48 and HDAC3. Furthermore, HDAC4 is required for TGFbeta1-induced myofibroblastic differentiation.


Pssm-ID: 212530 [Multi-domain]  Cd Length: 409  Bit Score: 701.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 515 TGLVYDSVMLKHQCSCGDNSKHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLKL 594
Cdd:cd10006    6 TGLVYDTLMLKHQCTCGNSNSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 595 DNGKLTGLLAQrTFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGF 674
Cdd:cd10006   86 DSKKLLGSLAS-VFVRLPCGGVGVDSDTIWNEVHSSGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGF 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 675 CFFNSVAIACRQLQQHGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGTGSGEGFNVNV 754
Cdd:cd10006  165 CYFNSVAIAAKLLQQRLNVSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNM 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 755 AWAGGLDPPMGDPEYLAAFRIVVMPIAREFAPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVLAL 834
Cdd:cd10006  245 AFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSAKCFGYLTKQLMGLAGGRIVLAL 324

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 324073135 835 EGGHDLTAICDASEACVAALLGNKVDPLSEESWKQKPNLSAIRSLEAVVRVHRKYWGCMQRLAS 898
Cdd:cd10006  325 EGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTS 388
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
 515-926 0e+00

Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. Class IIa histone deacetylases are signal-dependent co-repressors, having N-terminal regulatory domain with two or three conserved serine residues; phosphorylation of these residues is important for ability to shuttle between the nucleus and cytoplasm and act as transcriptional co-repressors. HDAC5 is involved in integration of chronic drug (cocaine) addiction and depression with changes in chromatin structure and gene expression; cocaine regulates HDAC5 function to antagonize the rewarding impact of cocaine, possibly by blocking drug-stimulated gene expression that supports drug-induced behavioral change. It is also involved in regulation of angiogenesis and cell cycle as well as immune system development. HDAC5 and HDAC9 have been found to be significantly up-regulated in high-risk medulloblastoma compared with low-risk and may potentially be novel drug targets.


Pssm-ID: 212531 [Multi-domain]  Cd Length: 420  Bit Score: 679.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 515 TGLVYDSVMLKHQCSCGDNSKHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLKL 594
Cdd:cd10007    5 TGLVYDTFMLKHQCTCGNTNVHPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHSEHHTLLYGTSPLNRQKL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 595 DNGKLTGLLAQRTFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGF 674
Cdd:cd10007   85 DSKKLLGPLSQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLIELAFKVAAGELKNGFAVIRPPGHHAEESTAMGF 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 675 CFFNSVAIACRQLQQHGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGTGSGEGFNVNV 754
Cdd:cd10007  165 CFFNSVAIAAKLLQQKLNVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGNFFPGSGAPDEVGAGPGVGFNVNI 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 755 AWAGGLDPPMGDPEYLAAFRIVVMPIAREFAPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVLAL 834
Cdd:cd10007  245 AWTGGVDPPIGDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGHQSPLGGYSVTAKCFGHLTKQLMTLAGGRVVLAL 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 835 EGGHDLTAICDASEACVAALLGNKVDPLSEESWKQKPNLSAIRSLEAVVRVHRKYWGCMQRLAS-CPDSWLPRVPGADAE 913
Cdd:cd10007  325 EGGHDLTAICDASEACVSALLGMELTPLDNTVLQQKPNDNAVATLERVIEIQSKHWSCLKRFAAtLGFSLLEAQRGELEE 404

                        410
                 ....*....|...
gi 324073135 914 VEAVTALASLSVG 926
Cdd:cd10007  405 AETVSAMASLSVD 417
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
 514-890 0e+00

Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. Class IIa histone deacetylases are signal-dependent co-repressors, they have N-terminal regulatory domain with two or three conserved serine residues, phosphorylation of these residues is important for ability to shuttle between the nucleus and cytoplasm and act as transcriptional co-repressors. HDAC9 is involved in regulation of gene expression and dendritic growth in developing cortical neurons. It also plays a role in hematopoiesis. Its deregulated expression may be associated with some human cancers. HDAC5 and HDAC9 have been found to be significantly up-regulated in high-risk medulloblastoma compared with low-risk and may potentially be novel drug targets.


Pssm-ID: 212533 [Multi-domain]  Cd Length: 379  Bit Score: 583.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 514 ATGLVYDSVMLKHQCSCGDNSKHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLK 593
Cdd:cd10009    2 ATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 594 LDNGKLTGLLAQRTFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMG 673
Cdd:cd10009   82 LDPRILLGDDSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 674 FCFFNSVAIACRQLQQHGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGTGSGEGFNVN 753
Cdd:cd10009  162 FCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYNIN 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 754 VAWAGGLDPPMGDPEYLAAFRIVVMPIAREFAPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVLA 833
Cdd:cd10009  242 IAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVLA 321

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 324073135 834 LEGGHDLTAICDASEACVAALLGNKVDPLSEESWKQKPNLSAIRSLEAVVRVHRKYW 890
Cdd:cd10009  322 LEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSKYW 378
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
 536-855 2.42e-136

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: 409.58  E-value: 2.42e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 536 HPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTnplsrlkldngkltgllaqrtfvMLPCGG 615
Cdd:cd09992    1 HPERPERLLAILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYIERVEE-----------------------TCEAGG 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 616 VGVDTDTIWNElHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGFCFFNSVAIACRQLQQHGKASK 695
Cdd:cd09992   58 GYLDPDTYVSP-GSYEAALLAAGAALAAVDAVLSGEAENAFALVRPPGHHAEPDRAMGFCLFNNVAIAARYAQKRYGLKR 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 696 ILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDdgnFFPGSGAVDEVGTGSGEGFNVNVAWAGGldppMGDPEYLAAFRI 775
Cdd:cd09992  137 VLIVDWDVHHGNGTQDIFYDDPSVLYFSIHQYP---FYPGTGAAEETGGGAGEGFTINVPLPPG----SGDAEYLAAFEE 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 776 VVMPIAREFAPDLVLVSAGFDAAEGHpaPLGGYHVSAKCFGYMTQQLMNLA----GGAVVLALEGGHDLTAICDASEACV 851
Cdd:cd09992  210 VLLPIAREFQPDLVLVSAGFDAHRGD--PLGGMNLTPEGYARLTRLLKELAdehcGGRLVFVLEGGYNLEALAESVLAVL 287


                 ....
gi 324073135 852 AALL 855
Cdd:cd09992  288 EALL 291
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
 519-893 4.61e-133

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: 403.64  E-value: 4.61e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 519 YDSVMLKHQCSCgdNSKHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVllygtNPLSRLKldNGK 598
Cdd:cd10003    1 YDQRMMNHHNLW--DPGHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHL-----DEMKSLE--KMK 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 599 LTGLLAQrtfvmlpcggvGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGFCFFN 678
Cdd:cd10003   72 PRELNRL-----------GKEYDSIYIHPDSYQCALLAAGCVLQVVEAVLTGESRNGVAIVRPPGHHAEQDTACGFCFFN 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 679 SVAIACRQLQQHGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGS--GAVDEVGTGSGEGFNVNVAW 756
Cdd:cd10003  141 NVAIAARYAQKKYGLKRILIVDWDVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSpeGNYDVVGKGKGEGFNVNIPW 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 757 AGGldpPMGDPEYLAAFRIVVMPIAREFAPDLVLVSAGFDAAEGHpaPLGGYHVSAKCFGYMTQQLMNLAGGAVVLALEG 836
Cdd:cd10003  221 NKG---GMGDAEYIAAFQQVVLPIAYEFNPELVLVSAGFDAARGD--PLGGCKVTPEGYAHMTHMLMSLAGGRVIVILEG 295

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 324073135 837 GHDLTAICDASEACVAALLGnkvDPLSEESWKQKPNLSAIRSLEAVVRVHRKYWGCM 893
Cdd:cd10003  296 GYNLTSISESMSMCTKTLLG---DPPPVLDLPRPPCSSALKSINNVLQVHQKYWKSL 349
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 536-856 2.77e-118

Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone deacetylase Zn-dependent enzyme that catalyzes hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Clr3 is the homolog of the class-II HDAC HdaI in S. cerevisiae, and is essential for silencing in heterochromatin regions, such as centromeric regions, ribosomal DNA, the mating-type region and telomeric loci. Clr3 has also been implicated in the regulation of stress-related genes; the histone acetyltransferase, Gcn5, in S. cerevisiae, preferentially acetylates global histone H3K14 while Clr3 preferentially deacetylates H3K14ac, and therefore, interplay between Gcn5 and Clr3 is crucial for the regulation of many stress-response genes.


Pssm-ID: 212542 [Multi-domain]  Cd Length: 313  Bit Score: 363.59  E-value: 2.77e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 536 HPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHvllygtnpLSRLKLDNGKLTGLLAQRTFVMlpcgg 615
Cdd:cd11600    3 HPEDPSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEH--------WDRVEATEKMSDEQLKDRTEIF----- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 616 vgvDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGFCFFNSVAIACRQLQ--QHGKA 693
Cdd:cd11600   70 ---ERDSLYVNNDTAFCARLSCGGAIEACRAVAEGRVKNAFAVVRPPGHHAEPDESMGFCFFNNVAVAAKWLQteYPDKI 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 694 SKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGS--GAVDEVGTGSGEGFNVNVAWAgglDPPMGDPEYLA 771
Cdd:cd11600  147 KKILILDWDIHHGNGTQRAFYDDPNVLYISLHRFENGGFYPGTpyGDYESVGEGAGLGFNVNIPWP---QGGMGDADYIY 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 772 AFRIVVMPIAREFAPDLVLVSAGFDAAEGHpaPLGGYHVSAKCFGYMTQQLMNLAGGAVVLALEGGHDLTAICDASEACV 851
Cdd:cd11600  224 AFQRIVMPIAYEFDPDLVIISAGFDAADGD--ELGQCHVTPAGYAHMTHMLMSLAGGKLVVALEGGYNLDAISDSALAVA 301


                 ....*
gi 324073135 852 AALLG 856
Cdd:cd11600  302 KVLLG 306
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 536-854 4.16e-116

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: 357.32  E-value: 4.16e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135  536 HPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHV-LLYGTNPLSRLKLDNGKLTGllaqrtfvmlpcg 614
Cdd:pfam00850   1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLeFLEEAAPEGGALLLLSYLSG------------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135  615 gvgvDTDTIWNElHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGFCFFNSVAIACRQLQQHGKAS 694
Cdd:pfam00850  68 ----DDDTPVSP-GSYEAALLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLK 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135  695 KILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHdDGNFFPGSGAVDEVGTGSGEGFNVNVAWAGGldppMGDPEYLAAFR 774
Cdd:pfam00850 143 RVAIVDFDVHHGNGTQEIFYDDPSVLTLSIHQY-PGGFYPGTGFADETGEGKGKGYTLNVPLPPG----TGDAEYLAAFE 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135  775 IVVMPIAREFAPDLVLVSAGFDAAEGHpaPLGGYHVSAKCFGYMTQQLMNLA---GGAVVLALEGGHDLTAICDASEACV 851
Cdd:pfam00850 218 EILLPALEEFQPDLILVSAGFDAHAGD--PLGGLNLTTEGFAEITRILLELAdplCIRVVSVLEGGYNLDALARSATAVL 295


                  ...
gi 324073135  852 AAL 854
Cdd:pfam00850 296 AAL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 515-856 1.24e-101

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 319.75  E-value: 1.24e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 515 TGLVYDSVMLKHQCSCGdnskHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVllygtnplSRLKl 594
Cdd:COG0123    1 TALIYHPDYLLHDLGPG----HPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYV--------DALR- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 595 dNGKLTGllaqrtfvmlpcGGVGVDTDTIWNElHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGF 674
Cdd:COG0123   68 -AASLDG------------GYGQLDPDTPVSP-GTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGF 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 675 CFFNSVAIACRQLQQHGkASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHddgNFFPGSGAVDEVGTGSGEGFNVNV 754
Cdd:COG0123  134 CLFNNAAIAARYLLAKG-LERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD---PLYPGTGAADETGEGAGEGSNLNV 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 755 AwaggLDPPMGDPEYLAAFRIVVMPIAREFAPDLVLVSAGFDAAEGHpaPLGGYHVSAKCFGYMTQQLMNLA---GGAVV 831
Cdd:COG0123  210 P----LPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHADD--PLGRLNLTTEGYAWRTRRVLELAdhcGGPVV 283

                        330       340
                 ....*....|....*....|....*
gi 324073135 832 LALEGGHDLTAICDASEACVAALLG 856
Cdd:COG0123  284 SVLEGGYNLDALARSVAAHLETLLG 308
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 530-890 1.37e-97

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: 310.01  E-value: 1.37e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 530 CGDNSKHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLygtnpLSRLKLDNGKltgllAQRTFv 609
Cdd:cd10002    1 CNWDSNHIECPERLEAILERLTQDGLLERCVKIPAREAEEDEILLVHSQEYIDL-----VKSTETMEKE-----ELESL- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 610 mlpCGGVgvdtDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGFCFFNSVAIACRQLQQ 689
Cdd:cd10002   70 ---CSGY----DSVYLCPSTYEAARLAAGSTIELVKAVMAGKIQNGFALIRPPGHHAMRNEANGYCIFNNVAIAAKYAIE 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 690 HGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGA--VDEVGTGSGEGFNVNVAWAGGLdppMGDP 767
Cdd:cd10002  143 KLGLKRILIVDWDVHHGQGTQQGFYEDPRVLYFSIHRYEHGRFWPHLFEsdYDYIGVGHGYGFNVNVPLNQTG---LGDA 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 768 EYLAAFRIVVMPIAREFAPDLVLVSAGFDAAEGhpAPLGGYHVSAKCFGYMTQQLMNLAGGAVVLALEGGHDLTAICDAS 847
Cdd:cd10002  220 DYLAIFHHILLPLALEFQPELVLVSAGFDASIG--DPEGEMAVTPAGYAHLTRLLMGLAGGKLLLVLEGGYLLESLAESV 297

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 324073135 848 EACVAALLGNKVDPLSeeswKQKPNLSAIRSLEAVVRVHRKYW 890
Cdd:cd10002  298 SMTLRGLLGDPLPPLA----PPIPIRSVLETILNAIAHLSPRW 336
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
 542-854 1.55e-93

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: 297.04  E-value: 1.55e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 542 RIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLKLDNGKltgllaqrtfvmlpcggvGVDTD 621
Cdd:cd09301    1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKANFAVATITESKP------------------VIFGP 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 622 TIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGFCFFNSVAIACRQLQQHGkASKILIVDW 701
Cdd:cd09301   63 NFPVQRHYFRGARLSTGGVVEAAELVAKGELERAFAVVGAGGHHAGKSRAWGFCYFNDVVLAIKFLRERG-ISRILIIDT 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 702 DVHHGNGTQQTFYQDPSVLYISLHRHDDGNFfpgsgavdevGTGSGEGFNVNVAWAGGldppMGDPEYLAAFRIVVMPIA 781
Cdd:cd09301  142 DAHHGDGTREAFYDDDRVLHMSFHNYDIYPF----------GRGKGKGYKINVPLEDG----LGDEEYLDAVERVISKVL 207

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 324073135 782 REFAPDLVLVSAGFDAAEGHpaPLGGYHVSAKCFGYMTQQLMNLA-GGAVVLALEGGHDLTAICDASEACVAAL 854
Cdd:cd09301  208 EEFEPEVVVLQFGHDTHEGD--RLGGFNLSEKGFVKLAEIVKEFArGGPILMVLGGGYNPEAAARIWTAIIKEL 279
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
 515-865 6.52e-82

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: 269.04  E-value: 6.52e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 515 TGLVYDSVMLKHQ----------CSCGDN-SKHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHvll 583
Cdd:cd09996    1 TGFVWDERYLWHDtgtgalflpvGGLLVQpGRHPENPETKRRIKNLLEVSGLSDHLVLITPRPATDEELLRVHTPEY--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 584 ygtnpLSRLKLDNGKLTGLLAQRTFVmlpcgGVGvdtdtiwnelhSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPG 663
Cdd:cd09996   78 -----IDRVKAASAAGGGEAGGGTPF-----GPG-----------SYEIALLAAGGAIAAVDAVLDGEVDNAYALVRPPG 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 664 HHADHSTAMGFCFFNSVAIACRQLQQHGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRhdDGNFFPGSGAVDEVG 743
Cdd:cd09996  137 HHAEPDQGMGFCLFNNVAIAARHALAVGGVKRVAVVDWDVHHGNGTQAIFYDDPDVLTISLHQ--DRCFPPDSGAVEERG 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 744 TGSGEGFNVNVAwaggLDPPMGDPEYLAAFRIVVMPIAREFAPDLVLVSAGFDAaeGHPAPLGGYHVSAKCFGYMTQQLM 823
Cdd:cd09996  215 EGAGEGYNLNIP----LPPGSGDGAYLHAFERIVLPALRAFRPELIIVASGFDA--SAFDPLGRMMLTSDGFRALTRKLR 288

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 324073135 824 NLA----GGAVVLALEGGHDLT--AICDAseACVAALLG---NKVDPLSEE 865
Cdd:cd09996  289 DLAdelcGGRLVMVHEGGYSEAyvPFCGL--AVLEELSGvrtGIADPLLYY 337
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
 530-890 3.05e-80

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: 263.64  E-value: 3.05e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 530 CGDNSKHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPlsrlKLDNGKLTGLlaqrtfv 609
Cdd:cd11682    1 CLWDESFPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYVALMKSTQ----YMTEEELRTL------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 610 mlpcggvgVDT-DTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGFCFFNSVAIACRQLQ 688
Cdd:cd11682   70 --------ADTyDSVYLHPNSYSCACLAVGSVLQLVDKVLGGEIRNGLAIVRPPGHHAQHDKMDGYCMFNNVAIAARYAQ 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 689 QHGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDE--VGTGSGEGFNVNVAWAgglDPPMGD 766
Cdd:cd11682  142 QKHGVQRVLIVDWDVHHGQGTQFIFEQDPSVLYFSIHRYEQGRFWPHLKESDSsaVGFGRGEGYNINVPWN---QVGMRD 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 767 PEYLAAFRIVVMPIAREFAPDLVLVSAGFDAAEGHPAplGGYHVSAKCFGYMTQQLMNLAGGAVVLALEGGHDLTAICDA 846
Cdd:cd11682  219 ADYIAAFLHVLLPVALEFQPQLVLVAAGFDAVIGDPK--GEMAATPACFAHLTHLLMGLAGGKLILSLEGGYNLRSLAEG 296

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 324073135 847 SEACVAALLGnkvDPLSEESWKQKPNLSAIRSLEAVVRVHRKYW 890
Cdd:cd11682  297 VCASLKALLG---DPCPMLESPGAPCRSALASVSCTISALEPFW 337
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
 536-855 2.81e-78

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: 256.67  E-value: 2.81e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 536 HPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVllygtnplsrlkldngkltgllaQRTFVMLPC-G 614
Cdd:cd11599    1 HPESPERLEAILDALIASGLDRLLRQLEAPPATREQLLRVHDAAYV-----------------------DRLEAAAPEeG 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 615 GVGVDTDTIWNElHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGFCFFNSVAIACRQLQQHGKAS 694
Cdd:cd11599   58 LVQLDPDTAMSP-GSLEAALRAAGAVVAAVDAVMAGEARNAFCAVRPPGHHAERDKAMGFCLFNNVAIAAAHALAHHGLE 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 695 KILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHddgNFFPGSGAVDEVGTGsgegfN-VNVAwaggLDPPMGDPEYLAAF 773
Cdd:cd11599  137 RVAIVDFDVHHGNGTEDIFRDDPRVLFCSSHQH---PLYPGTGAPDETGHG-----NiVNVP----LPAGTGGAEFREAV 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 774 RIVVMPIAREFAPDLVLVSAGFDAaegHPA-PLGGYHVSAKCFGYMTQQLMNLA----GGAVVLALEGGHDLTAICDASE 848
Cdd:cd11599  205 EDRWLPALDAFKPDLILISAGFDA---HRDdPLAQLNLTEEDYAWITEQLMDVAdrycDGRIVSVLEGGYDLSALARSVA 281


                 ....*..
gi 324073135 849 ACVAALL 855
Cdd:cd11599  282 AHVRALM 288
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 542-890 4.54e-74

Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. HDACs usually act via association with DNA binding proteins to target specific chromatin regions. HDAC10 has an N-terminal deacetylase domain and a C-terminal pseudo-repeat that shares significant similarity with its catalytic domain. It is located in the nucleus and cytoplasm, and is involved in regulation of melanogenesis. It transcriptionally down-regulates thioredoxin-interacting protein (TXNIP), leading to altered reactive oxygen species (ROS) signaling in human gastric cancer cells. Known interaction partners of HDAC10 are Pax3, KAP1, hsc70 and HDAC3 proteins.


Pssm-ID: 212546 [Multi-domain]  Cd Length: 337  Bit Score: 247.08  E-value: 4.54e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 542 RIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSrlkldNGKLTGLLAQRTfvmlpcggvgvdtD 621
Cdd:cd11683   13 RLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRETQVM-----NKEELMAISGKY-------------D 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 622 TIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGFCFFNSVAIACRQLQQHGKASKILIVDW 701
Cdd:cd11683   75 AVYFHPNTFHCARLAAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYAKKKYGLHRILIVDW 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 702 DVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPG--SGAVDEVGTGSGEGFNVNVAWAgglDPPMGDPEYLAAFRIVVMP 779
Cdd:cd11683  155 DVHHGQGIQYIFEEDPSVLYFSWHRYEHQRFWPFlrESDYDAVGRGKGLGFNINLPWN---KVGMGNADYLAAFFHVLLP 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 780 IAREFAPDLVLVSAGFDAAEGHPAplGGYHVSAKCFGYMTQQLMNLAGGAVVLALEGGHDLTAICDASEACVAALLGnkv 859
Cdd:cd11683  232 LAFEFDPELVLVSAGFDSAIGDPE--GQMCATPECFAHLTHLLMVLAGGKLCAVLEGGYHLESLAESVCMTVQTLLG--- 306

                        330       340       350
                 ....*....|....*....|....*....|.
gi 324073135 860 DPLSEESWKQKPNLSAIRSLEAVVRVHRKYW 890
Cdd:cd11683  307 DPLPRLSGEMTPCQSALESIQNVRAAQAPYW 337
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
 517-856 9.24e-72

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: 239.36  E-value: 9.24e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 517 LVYDSVMLKHQ----CSCGDNSKHPEHAGRIQSIWSRLQERGLRSQcecLRGRKASLEELQSVHSERHVllygtnplsrl 592
Cdd:cd10001    2 IVYSEDHLLHHpkteLSRGKLVPHPENPERAEAILDALKRAGLGEV---LPPRDFGLEPILAVHDPDYV----------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 593 kldngkltgllaqrTFVMlpcggvGVDTDTIWNElHSSNAARWAAGSVTDLAFKVASRElKNGFAVVRPPGHHADHSTAM 672
Cdd:cd10001   68 --------------DFLE------TADTDTPISE-GTWEAALAAADTALTAADLVLEGE-RAAYALCRPPGHHAGRDRAG 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 673 GFCFFNSVAIACRQLQQHGKasKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRhDDGNFFPG-SGAVDEVGTGSGEGFN 751
Cdd:cd10001  126 GFCYFNNAAIAAQYLRDRAG--RVAILDVDVHHGNGTQEIFYERPDVLYVSIHG-DPRTFYPFfLGFADETGEGEGEGYN 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 752 VNVAwaggLDPPMGDPEYLAAFRIVVMPIaREFAPDLVLVSAGFDAAEGHpaPLGGYHVSAKCFGYMTQQLMNLaGGAVV 831
Cdd:cd10001  203 LNLP----LPPGTGDDDYLAALDEALAAI-AAFGPDALVVSLGFDTHEGD--PLSDFKLTTEDYARIGRRIAAL-GLPTV 274

                        330       340
                 ....*....|....*....|....*
gi 324073135 832 LALEGGHDLTAIcdaSEACVAALLG 856
Cdd:cd10001  275 FVQEGGYNVDAL---GRNAVAFLAG 296
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
 517-840 3.20e-46

Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin utilization protein) is a class I deacetylase found only in bacteria and is involved in post-translational control of the acetyl-coenzyme A synthetase (AcsA). Deacetylase AcuC works in coordination with deacetylase SrtN (class III), possibly to maintain AcsA in active (deacetylated) form and let the cell grow under low concentration of acetate. B. subtilis AcuC is a member of operon acuABC; this operon is repressed by the presence of glucose and does not show induction by acetoin; acetoin is a bacterial fermentation product that can be converted to acetate via the butanediol cycle in absence of other carbon sources. Inactivation of AcuC leads to slower growth and lower cell yield under low-acetate conditions in Bacillus subtilis. In general, Class I histone deacetylases (HDACs) are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues in histone amino termini to yield a deacetylated histone (EC 3.5.1.98). Enzymes belonging to this group participate in regulation of a number of processes through protein (mostly different histones) modification (deacetylation). Class I histone deacetylases in general act via the formation of large multiprotein complexes. Members of this class are involved in cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and in posttranslational control of the acetyl coenzyme A synthetase.


Pssm-ID: 212520 [Multi-domain]  Cd Length: 313  Bit Score: 168.51  E-value: 3.20e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 517 LVYDSVMLKHqcSCGDNskHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVllygtnplSRLKLdn 596
Cdd:cd09994    2 FIYSEEYLRY--SFGPN--HPFNPPRLSLTKDLLRALGLLPPVDLVPPRPATEEELLLFHTPDYI--------EAVKE-- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 597 gkltgllAQRTFVMLPCGGVGVDT-DT-IWNELHSsnAARWAAGSVTDLAFKVASRElknGFAVVRPPG--HHADHSTAM 672
Cdd:cd09994   68 -------ASRGQEPEGRGRLGLGTeDNpVFPGMHE--AAALVVGGTLLAARLVLEGE---ARRAFNPAGglHHAMRGRAS 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 673 GFCFFNSVAIACRQLQQHGkASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRhDDGNFFPGSGAVDEVGTGSGEGFNV 752
Cdd:cd09994  136 GFCVYNDAAVAIERLRDKG-GLRVAYVDIDAHHGDGVQAAFYDDPRVLTISLHE-SGRYLFPGTGFVDEIGEGEGYGYAV 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 753 NVAwaggLDPPMGDPEYLAAFRIVVMPIAREFAPDLVLVSAGFDAAEGHpaPLGGYHVSAKCFGYMTQQLMNLA----GG 828
Cdd:cd09994  214 NIP----LPPGTGDDEFLRAFEAVVPPLLRAFRPDVIVSQHGADAHAGD--PLTHLNLSNRAYRAAVRRIRELAdeycGG 287

                        330
                 ....*....|..
gi 324073135 829 AVVLALEGGHDL 840
Cdd:cd09994  288 RWLALGGGGYNP 299
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 530-824 1.81e-32

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: 129.77  E-value: 1.81e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 530 CGDNSKHPEHAGRIQSIwsrLQERGLRSQCECLRGRKASLEELQSVHSERHV--LLYGTNPLsrlklDNGKLTGLLAQrt 607
Cdd:cd10000   13 CDRLPKVPNRASMVHSL---IEAYGLLKQLRVVKPRVATEEELASFHSDEYIqfLKKASNEG-----DNDEEPSEQQE-- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 608 fvmlpcggVGVDTDTIWNELHSSNAARWAAGSVTdlafkvASRELKNGFA--VVRPPG--HHADHSTAMGFCFFNSVAIA 683
Cdd:cd10000   83 --------FGLGYDCPIFEGIYDYAAAVAGATLT------AAQLLIDGKCkvAINWFGgwHHAQRDEASGFCYVNDIVLG 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 684 CRQLQQhgKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGnFFPGSGAVDEVGTGSGEGFNVNVAWAGGLDpp 763
Cdd:cd10000  149 ILKLRE--KFDRVLYVDLDLHHGDGVEDAFSFTSKVMTVSLHKYSPG-FFPGTGDVSDVGLGKGKYYTVNVPLRDGIQ-- 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 764 mgDPEYLAAFRIVVMPIAREFAPDLVLVSAGFDAAEGHPA----------------------PL-----GGYHVS--AKC 814
Cdd:cd10000  224 --DEQYLQIFTAVVPEIVAAFRPEAVVLQCGADTLAGDPMgafnltpvgigkclkyvlgwklPTlilggGGYNLAntARC 301

                        330
                 ....*....|
gi 324073135 815 FGYMTQQLMN 824
Cdd:cd10000  302 WTYLTGLILG 311
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 546-812 1.57e-30

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: 121.84  E-value: 1.57e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 546 IWSRLQERGLRSQCECLRGRKASLEELQSVHSERHV--LLYGTnpLSRLKLdngKLTGL-----LAQRTFVMlpCGGvgv 618
Cdd:cd09993   11 LREALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLesLKSGE--LSREEI---RRIGFpwspeLVERTRLA--VGG--- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 619 dtdTIwnelhssNAARWAagsvtdlafkvasreLKNGFAVvRPPG--HHADHSTAMGFCFFNSVAIACRQLQQHGKASKI 696
Cdd:cd09993   81 ---TI-------LAARLA---------------LEHGLAI-NLAGgtHHAFPDRGEGFCVFNDIAIAARVLLAEGLVRRV 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 697 LIVDWDVHHGNGTQQTFYQDPSVLYISLHrhdDGNFFPGSGAVDevgtgsgegfNVNVawagGLDPPMGDPEYLAAFRIV 776
Cdd:cd09993  135 LIVDLDVHQGNGTAAIFADDPSVFTFSMH---GEKNYPFRKEPS----------DLDV----PLPDGTGDDEYLAALEEA 197

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 324073135 777 VMPIAREFAPDLVLVSAGFDAAEGHpaPLGGYHVSA 812
Cdd:cd09993  198 LPRLLAEFRPDLVFYNAGVDVLAGD--RLGRLSLSL 231
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
 535-828 4.14e-29

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: 118.45  E-value: 4.14e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 535 KHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVllygtNPLSRLKLDNGKLTGLLAQRtfvmlpcg 614
Cdd:cd09991   14 GHPMKPHRIRMTHSLILSYGLYKKMEIYRPRPATAEELTKFHSDDYI-----DFLRSVSPDNMKEFKKQLER-------- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 615 gVGVDTD-TIWNELHSSnAARWAAGSVTdlafkvASRELKNGFA--VVRPPG--HHADHSTAMGFCFFNSVAIACRQLQQ 689
Cdd:cd09991   81 -FNVGEDcPVFDGLYEY-CQLYAGGSIA------AAVKLNRGQAdiAINWAGglHHAKKSEASGFCYVNDIVLAILELLK 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 690 HGKasKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHddGNFFPGSGAVDEVGTGSGEGFNVNVAwaggLDPPMGDPEY 769
Cdd:cd09991  153 YHQ--RVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKF--GEYFFPGTGLRDIGAGKGKYYAVNVP----LKDGIDDESY 224

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 324073135 770 LAAFRIVVMPIAREFAPDLVLVSAGFDAAEGHpaPLGGYHVS----AKCFGYMTQ---QLMNLAGG 828
Cdd:cd09991  225 LQIFEPVLSKVMEVFQPSAVVLQCGADSLAGD--RLGCFNLSikghAKCVKFVKSfniPLLVLGGG 288
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
 537-844 1.45e-27

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: 113.90  E-value: 1.45e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 537 PEHAGRIQSIWSRLQERGL-RSQCECLRGRKASLEELQSVHSERHVllygtnplsrlkldngklTGLLAQrtfvmlpcgg 615
Cdd:cd11680   16 PSNKGRSSLVHSLIRAYGLlQHFDEIIEPERATRKDLTKYHDKDYV------------------DFLLKK---------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 616 VGVDTDT-IWNELHssNAARWAAGSVTDLAfKVASRELKNGFAVVRPPG-HHADHSTAMGFCFFNSVAIACRQLQQHGKa 693
Cdd:cd11680   68 YGLEDDCpVFPFLS--MYVQLVAGSSLALA-KHLITQVERDIAINWYGGrHHAQKSRASGFCYVNDIVLAILRLRRARF- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 694 SKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGnFFPGSGAVDEvgtgSGEGFNVNVAWAGGLDppmgDPEYLAAF 773
Cdd:cd11680  144 RRVFYLDLDLHHGDGVESAFFFSKNVLTCSIHRYDPG-FFPGTGSLKN----SSDKGMLNIPLKRGLS----DKTLLRII 214

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 324073135 774 RIVVMPIAREFAPDLVLVSAGFDAAEGHpaPLGGYHVSAKCFGYMTQQLMNLAGGAVVLALEGG---HDLTAIC 844
Cdd:cd11680  215 DSIVRPLIEKFEPEVIVIQCGCDGLSGD--PHKEWNLTIRGYGSVIELLLKEFKDKPTLLLGGGgynHTEAARA 286
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
 535-816 1.76e-25

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: 107.93  E-value: 1.76e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 535 KHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVllygtNPLSRLKLDNGKLtglLAQRTFVMLPCG 614
Cdd:cd11598   17 THPMKPFRLTLTKHLVMGYGLHKAMDTYEARAATREELRQFHDADYL-----DFLSKVSPENANQ---LRFDKAEPFNIG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 615 gvgvDTDTIWNELhSSNAARWAAGSVTdlafkvASRELKNG---FAVVRPPG-HHADHSTAMGFCFFNSVAIACRQLQQH 690
Cdd:cd11598   89 ----DDCPVFDGM-YDYCQLYAGASLD------AARKLCSGqsdIAINWSGGlHHAKKSEASGFCYVNDIVLAILNLLRY 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 691 gkASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHdDGNFFPGSGAVDEVGTGSGEGFNVNVAWAGGLDppmgDPEYL 770
Cdd:cd11598  158 --FPRVLYIDIDVHHGDGVEEAFYRTDRVMTLSFHKY-NGEFFPGTGDLDDNGGTPGKHFALNVPLEDGID----DEQYN 230

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 324073135 771 AAFRIVVMPIAREFAPDLVLVSAGFDAAEGHpaPLGGYHVSAKCFG 816
Cdd:cd11598  231 LLFKSIIGPTIEKFQPSAIVLQCGADSLGGD--RLGQFNLNIKAHG 274
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
 536-832 3.56e-25

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: 108.61  E-value: 3.56e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 536 HPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLygtnpLSRLKLDNGKLTGLLAQR--------- 606
Cdd:cd10010   25 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKF-----LRSIRPDNMSEYSKQMQRfnvgedcpv 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 607 -----TFVMLPCGGvGVDTDTIWNELHSSNAARWAAGSvtdlafkvasrelkngfavvrppgHHADHSTAMGFCFFNSVA 681
Cdd:cd10010  100 fdglfEFCQLSAGG-SVASAVKLNKQQTDIAVNWAGGL------------------------HHAKKSEASGFCYVNDIV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 682 IACRQLQQHGKasKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHddGNFFPGSGAVDEVGTGSGEGFNVNVAWAGGLD 761
Cdd:cd10010  155 LAILELLKYHQ--RVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKY--GEYFPGTGDLRDIGAGKGKYYAVNYPLRDGID 230

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 324073135 762 ppmgDPEYLAAFRIVVMPIAREFAPDLVLVSAGFDAAEGHpaPLGGYHVS----AKCFGYMTQ---QLMNLAGGAVVL 832
Cdd:cd10010  231 ----DESYEAIFKPVMSKVMEMFQPSAVVLQCGADSLSGD--RLGCFNLTikghAKCVEFVKSfnlPMLMLGGGGYTI 302
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 627-854 2.87e-24

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: 102.07  E-value: 2.87e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 627 LHSSNAARWAAGSVTDLAFKVasrelKNGFAVVrppGHHAdhstamgfcFFNSVAIACRQLQQhgkasKILIVDWDVHHG 706
Cdd:cd09987    5 IRKAEAHELLAGVVVAVLKDG-----KVPVVLG---GDHS---------IANGAIRAVAELHP-----DLGVIDVDAHHD 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 707 NGTQQTFY--------------QDPSVLYISLHRHDDGNFFPGsgavdevGTGSGEGFNVNVAWAGGLdppmgDPEYLAA 772
Cdd:cd09987   63 VRTPEAFGkgnhhtprhllcepLISDVHIVSIGIRGVSNGEAG-------GAYARKLGVVYFSMTEVD-----KLGLGDV 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 773 FRIVVMPIarEFAPDLVLVSAGFDAAEGHPAP----LGGYHVSAKCFGYMTQQLMNLaGGAVVLALEGGHDL----TAIC 844
Cdd:cd09987  131 FEEIVSYL--GDKGDNVYLSVDVDGLDPSFAPgtgtPGPGGLSYREGLYITERIAKT-NLVVGLDIVEVNPLldetGRTA 207

                        250
                 ....*....|
gi 324073135 845 DASEACVAAL 854
Cdd:cd09987  208 RLAAALTLEL 217
PTZ00063 PTZ00063
histone deacetylase; Provisional
 536-824 3.20e-23

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 103.74  E-value: 3.20e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 536 HPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVllygtNPLSRLKLDNGKLTGLLAQRTfvmlpcgG 615
Cdd:PTZ00063  23 HPMKPQRIRMAHALILSYDLYKHMEIYRPHKSVEPELVLFHDEEYV-----DFLSSISPENYRDFTYQLKRF-------N 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 616 VGVDTDT-IWNELHSSNAArwAAGSVTDLAFKvasreLKNGFA--VVRPPG--HHADHSTAMGFCFFNSVAIACRQLQQH 690
Cdd:PTZ00063  91 VGEATDCpVFDGLFEFQQS--CAGASIDGAYK-----LNNHQAdiCVNWSGglHHAKRSEASGFCYINDIVLGILELLKY 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 691 gkASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHddGNFFPGSGAVDEVGTGSGEGFNVNVAWAGGLDppmgDPEYL 770
Cdd:PTZ00063 164 --HARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFPGTGDVTDIGVAQGKYYSVNVPLNDGID----DDSFV 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 771 AAFRIVVMPIAREFAPDLVLVSAGFDAA------------EGHPA----------PL-----GGYHVS--AKCFGYMTQQ 821
Cdd:PTZ00063 236 DLFKPVISKCVEVYRPGAIVLQCGADSLtgdrlgrfnltiKGHAAcvefvrslniPLlvlggGGYTIRnvARCWAYETGV 315


                 ...
gi 324073135 822 LMN 824
Cdd:PTZ00063 316 ILN 318
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
 629-854 1.93e-22

Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from Saccharomyces cerevisiae is a Zn-dependent enzyme belonging to HDAC class II. It catalyzes hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. Hos3 deacetylase is homodimer, in vitro it shows specificity to H4, H3 and H2A.


Pssm-ID: 212522 [Multi-domain]  Cd Length: 353  Bit Score: 99.83  E-value: 1.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 629 SSNAARWAAGSVT---DLAFKVASRELKNGFAVVRPPGHHADHSTAMGFCFFNSVAIACRQ-LQQHGkASKILIVDWDVH 704
Cdd:cd09998   82 SLDAIQGALGAVCeavDSVFKPESPGTKRAFVAIRPPGHHCSESTPSGFCWVNNVHVGAAHaYLTHG-ITRVVILDIDLH 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 705 HGNGTQQTFYQ------------------------DPSVLYISLHrhdDGNFFP-GSGAVDEVGTGSgegfnVNVAWAGG 759
Cdd:cd09998  161 HGNGTQDIAWRinaeankqalesssyddfkpagapGLRIFYSSLH---DINSFPcEDGDPAKVKDAS-----VSIDGAHG 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 760 -------LDPPMGDPE----YLAAFRIVVMPIAREFAPD--------LVLVSAGFDAAE---------GHPAPLGGYHVS 811
Cdd:cd09998  233 qwiwnvhLQPWTTEEDfwelYYPKYRILFEKAAEFLRLTtaatpfktLVFISAGFDASEheyesmqrhGVNVPTSFYYRF 312

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 324073135 812 AKCFGYMTQQlmnLAGGAVVLALEGGHDLTAICDASEACVAAL 854
Cdd:cd09998  313 ARDAVRFADA---HAHGRLISVLEGGYSDRALCSGVLAHLTGL 352
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
 534-828 5.46e-22

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: 99.11  E-value: 5.46e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 534 SKHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHV-LLYGTNP--LSRLKLDNGKLT---------G 601
Cdd:cd10004   19 PGHPMKPHRIRMAHSLVMNYGLYKKMEIYRAKPATKNEMTQFHTDEYIdFLSRVTPdnMEKFQKEQVKYNvgddcpvfdG 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 602 LLAqrtFVMLPCGGvGVDTDTIWNELHSSNAARWAAGSvtdlafkvasrelkngfavvrppgHHADHSTAMGFCFFNSVA 681
Cdd:cd10004   99 LFE---FCSISAGG-SMEGAARLNRGKCDIAVNWAGGL------------------------HHAKKSEASGFCYVNDIV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 682 IACRQLQQHGKasKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHddGNFFPGSGAVDEVGTGSGEGFNVNVAWAGGLD 761
Cdd:cd10004  151 LGILELLRYHQ--RVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKY--GEYFPGTGELRDIGIGTGKNYAVNVPLRDGID 226

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 324073135 762 ppmgDPEYLAAFRIVVMPIAREFAPDLVLVSAGFDAAEGHpaPLGGYHVS----AKCFGYMTQ---QLMNLAGG 828
Cdd:cd10004  227 ----DESYKSIFEPVIKHVMEWYQPEAVVLQCGGDSLSGD--RLGCFNLSmkghANCVNFVKSfnlPMLVLGGG 294
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
 664-824 8.27e-21

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: 95.54  E-value: 8.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 664 HHADHSTAMGFCFFNSVAIACRQ-LQQHgkaSKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHddGN-FFPGSGAVDE 741
Cdd:cd10005  132 HHAKKFEASGFCYVNDIVIAILElLKYH---PRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKY--GNyFFPGTGDMYE 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 742 VGTGSGEGFNVNVAWAGGLDppmgDPEYLAAFRIVVMPIAREFAPDLVLVSAGFDA------------AEGHPA------ 803
Cdd:cd10005  207 VGAESGRYYSVNVPLKDGID----DQSYLQLFKPVIQQVIDFYQPTCIVLQCGADSlgcdrlgcfnlsIKGHGEcvefvk 282

                        170       180       190
                 ....*....|....*....|....*....|..
gi 324073135 804 ----PL-----GGYHVS--AKCFGYMTQQLMN 824
Cdd:cd10005  283 sfniPLlvlggGGYTVRnvARCWTYETSLLVD 314
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
 536-813 2.03e-20

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


Pssm-ID: 212535 [Multi-domain]  Cd Length: 366  Bit Score: 94.36  E-value: 2.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 536 HPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLygtnpLSRLKLDNGKLTGLLAQR--------- 606
Cdd:cd10011   21 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKF-----LRSIRPDNMSEYSKQMQRfnvgedcpv 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 607 -----TFVMLPCGGvGVDTDTIWNELHSSNAARWAAGSvtdlafkvasrelkngfavvrppgHHADHSTAMGFCFFNSVA 681
Cdd:cd10011   96 fdglfEFCQLSTGG-SVAGAVKLNRQQTDMAVNWAGGL------------------------HHAKKSEASGFCYVNDIV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 682 IACRQLQQHGKasKILIVDWDVHHGNGTQQTFYQDPSVLYISlhRHDDGNFFPGSGAVDEVGTGSGEGFNVNVAWAGGLD 761
Cdd:cd10011  151 LAILELLKYHQ--RVLYIDIDIHHGDGVEEAFYTTDRVMTVS--FHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGID 226

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 324073135 762 ppmgDPEYLAAFRIVVMPIAREFAPDLVLVSAGFDAAEGHpaPLGGYHVSAK 813
Cdd:cd10011  227 ----DESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGD--RLGCFNLTVK 272
PTZ00346 PTZ00346
histone deacetylase; Provisional
 664-837 2.91e-15

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 79.30  E-value: 2.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 664 HHADHSTAMGFCFFNSVAIACRQLQQHgkASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDgNFFPGSGAVDEVG 743
Cdd:PTZ00346 154 HHSKCGECSGFCYVNDIVLGILELLKC--HDRVLYVDIDMHHGDGVDEAFCTSDRVFTLSLHKFGE-SFFPGTGHPRDVG 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135 744 TGSGEGFNVNVA-WAGgldppMGDPEYLAAFRIVVMPIAREFAPDLVLVSAGFDAAEGHpaPLGGYHVSAKCFGYMTQQL 822
Cdd:PTZ00346 231 YGRGRYYSMNLAvWDG-----ITDFYYLGLFEHALHSIVRRYSPDAIVLQCGADSLAGD--RLGLLNLSSFGHGQCVQAV 303

                        170
                 ....*....|....*
gi 324073135 823 MNLagGAVVLALEGG 837
Cdd:PTZ00346 304 RDL--GIPMLALGGG 316
PHA03247 PHA03247
large tegument protein UL36; Provisional
 100-514 5.57e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 5.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135  100 AALERTVHPSSPSIPYRTLEPLDTEGAARSVLSSFLPPVPSLPTEPP------------EHFPLRKTVSEPNLKLRYKPK 167
Cdd:PHA03247 2581 AVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPppspspaanepdPHPPPTVPPPERPRDDPAPGR 2660

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135  168 KSLERRKNPLLR--KESAPPSLRRRPAetlgdssPSSSSTPASGCSSPNDSEHGPNPAlgSEALLGQRLRLQETSLAPFA 245
Cdd:PHA03247 2661 VSRPRRARRLGRaaQASSPPQRPRRRA-------ARPTVGSLTSLADPPPPPPTPEPA--PHALVSATPLPPGPAAARQA 2731

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135  246 LPTVSLLPAITLGLPAPARADGDRRTHSTLGPRGPVLGNPHAplflhhglEPEAGGTLPSRLQPILLLDPSVSHAPLWTV 325
Cdd:PHA03247 2732 SPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPA--------APAAGPPRRLTRPAVASLSESRESLPSPWD 2803

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135  326 PGLGPLPFHFAQPLLTTERLSGSGLHRPLNRTRSEPLPPSATASPLLAP---LQPRQD--RLKPHVQLIKRPAKPSEKP- 399
Cdd:PHA03247 2804 PADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLggsVAPGGDvrRRPPSRSPAAKPAAPARPPv 2883

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135  400 -RLRQIPSAEDLETDgggvgPMANDGLEHRESGRGPPEGRGSISLQQHQQVPPWEQQH-------LAGRLSQGSPGDSVL 471
Cdd:PHA03247 2884 rRLARPAVSRSTESF-----ALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPprpqpplAPTTDPAGAGEPSGA 2958

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 324073135  472 IPLAQVGHR-----PLSRTQSSPAAPvSLLSPEPTcqTQVLNSSETPA 514
Cdd:PHA03247 2959 VPQPWLGALvpgrvAVPRFRVPQPAP-SREAPASS--TPPLTGHSLSR 3003
PHA03247 PHA03247
large tegument protein UL36; Provisional
 43-401 4.68e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 4.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135   43 SAEPMRLSMDPPMPELQGGQQEQELRQLLNKDKSKRSAVASSVvkqklAEVILKKQQAALERTVHPSSPSIPYRTLEPLD 122
Cdd:PHA03247 2616 PLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAP-----GRVSRPRRARRLGRAAQASSPPQRPRRRAARP 2690

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135  123 TEGaarSVLSSFLPPVPSLPTEPPEHfPLRKTVSEPnlklrykPKKSLERRKNPLLRKESAPPSLRRRPAETLGDSSPSS 202
Cdd:PHA03247 2691 TVG---SLTSLADPPPPPPTPEPAPH-ALVSATPLP-------PGPAAARQASPALPAAPAPPAVPAGPATPGGPARPAR 2759

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135  203 SSTPASGCSS--PNDSEHGPNPALGSEALLGQRLRLQETSLAPFALPTVSLLPAITLGLPAPARADGDRRTHSTLGPRGP 280
Cdd:PHA03247 2760 PPTTAGPPAPapPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAP 2839

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324073135  281 VLGNPHAPLFLHHGLEPEAGGTL----PSRLQPILLLDPSVSHAPLWTVPGLGPLPFHFAQPLLTTERLSGSGLHRPLNR 356
Cdd:PHA03247 2840 PPPPGPPPPSLPLGGSVAPGGDVrrrpPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQP 2919

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 324073135  357 TRSEPLPPSATASPLLAPLQPRQDRLKPHVQLIKRPAKPSEKPRL 401
Cdd:PHA03247 2920 QPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWL 2964
 
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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