NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|392928255|ref|NP_001257279|]
View 

Histone deacetylase 4 [Caenorhabditis elegans]

Protein Classification

histone deacetylase( domain architecture ID 10184833)

class IIa histone deacetylase is Zn-dependent enzyme that catalyzes hydrolysis of N(6)-acetyl-lysine residues of histones (EC 3.5.1.98) to yield deacetylated histones

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 407-781 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: 696.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 407 CTTGLGYDQAMVRHECCCGNNASHVENGGRIQSIWSKLIEHGHVQKCEKVTAKKASLEQLQLVHSQTYTTFFAVSPTACL 486
Cdd:cd11681    1 FTTGLAYDPLMLKHQCICGNNSSHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTLLYGTNPLSRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 487 KIDANSL---PLKRFLQLPCGGIGVDSDTYFNDASTQTAARLAAGTLIELSSQVAEGRLKNGFACIRPPGHHAEHEQAMG 563
Cdd:cd11681   81 KLDPTKLaglPQKSFVRLPCGGIGVDSDTVWNELHTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQAMG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 564 FCFFNNVAVAVKVLQTKYPaqCAKIAIIDWDVHHGNGTQLSFENDPNVLYMSLHRHDKGNFFPGTGSVTEVGKNDAKGLT 643
Cdd:cd11681  161 FCFFNSVAIAAKQLQQKLK--LRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFPGTGAPTEVGSGAGEGFN 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 644 VNVPFSGDV---MRDPEYLAAWRTVIEPVMASFCPDFIIVSAGFDACHGHPNALGGYEVTPEMFGYMTKSLLNYASGKVV 720
Cdd:cd11681  239 VNIAWSGGLdppMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPPPLGGYKVSPACFGYMTRQLMNLAGGKVV 318

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392928255 721 LALEGGYDLKSISEAAQQCVQALIGESDDAgrLSSVALESLPNPSAVETLQKVIAIHKSYW 781
Cdd:cd11681  319 LALEGGYDLTAICDASEACVRALLGDELDP--LSEEELERRPNPNAVTSLEKVIAIQSPYW 377
 
Name Accession Description Interval E-value
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 407-781 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: 696.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 407 CTTGLGYDQAMVRHECCCGNNASHVENGGRIQSIWSKLIEHGHVQKCEKVTAKKASLEQLQLVHSQTYTTFFAVSPTACL 486
Cdd:cd11681    1 FTTGLAYDPLMLKHQCICGNNSSHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTLLYGTNPLSRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 487 KIDANSL---PLKRFLQLPCGGIGVDSDTYFNDASTQTAARLAAGTLIELSSQVAEGRLKNGFACIRPPGHHAEHEQAMG 563
Cdd:cd11681   81 KLDPTKLaglPQKSFVRLPCGGIGVDSDTVWNELHTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQAMG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 564 FCFFNNVAVAVKVLQTKYPaqCAKIAIIDWDVHHGNGTQLSFENDPNVLYMSLHRHDKGNFFPGTGSVTEVGKNDAKGLT 643
Cdd:cd11681  161 FCFFNSVAIAAKQLQQKLK--LRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFPGTGAPTEVGSGAGEGFN 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 644 VNVPFSGDV---MRDPEYLAAWRTVIEPVMASFCPDFIIVSAGFDACHGHPNALGGYEVTPEMFGYMTKSLLNYASGKVV 720
Cdd:cd11681  239 VNIAWSGGLdppMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPPPLGGYKVSPACFGYMTRQLMNLAGGKVV 318

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392928255 721 LALEGGYDLKSISEAAQQCVQALIGESDDAgrLSSVALESLPNPSAVETLQKVIAIHKSYW 781
Cdd:cd11681  319 LALEGGYDLTAICDASEACVRALLGDELDP--LSEEELERRPNPNAVTSLEKVIAIQSPYW 377
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 430-743 3.03e-105

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: 325.73  E-value: 3.03e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255  430 HVENGGRIQSIWSKLIEHGHVQKCEKVTAKKASLEQLQLVHSQTYTTFFAvspTACLKIDAnslplkrflQLPCGGIGVD 509
Cdd:pfam00850   1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLE---EAAPEGGA---------LLLLSYLSGD 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255  510 SDTYFNDASTQtAARLAAGTLIELSSQVAEGRLKNGFACIRPPGHHAEHEQAMGFCFFNNVAVAVKVLQTKYpaQCAKIA 589
Cdd:pfam00850  69 DDTPVSPGSYE-AALLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKY--GLKRVA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255  590 IIDWDVHHGNGTQLSFENDPNVLYMSLHRHDkGNFFPGTGSVTEVGKNDAKGLTVNVPFSGDvMRDPEYLAAWRTVIEPV 669
Cdd:pfam00850 146 IVDFDVHHGNGTQEIFYDDPSVLTLSIHQYP-GGFYPGTGFADETGEGKGKGYTLNVPLPPG-TGDAEYLAAFEEILLPA 223

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392928255  670 MASFCPDFIIVSAGFDACHGHPnaLGGYEVTPEMFGYMTKSLLNYA---SGKVVLALEGGYDLKSISEAAQQCVQAL 743
Cdd:pfam00850 224 LEEFQPDLILVSAGFDAHAGDP--LGGLNLTTEGFAEITRILLELAdplCIRVVSVLEGGYNLDALARSATAVLAAL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 409-745 6.88e-96

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 301.64  E-value: 6.88e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 409 TGLGYDQAMVRHECccgnNASHVENGGRIQSIWSKLIEHGHVQKCEKVTAKKASLEQLQLVHSQTYttffavsptaclkI 488
Cdd:COG0123    1 TALIYHPDYLLHDL----GPGHPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDY-------------V 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 489 DAnslpLKRFLqlPCGGIG-VDSDTYFNDASTQtAARLAAGTLIELSSQVAEGRLKNGFACIRPPGHHAEHEQAMGFCFF 567
Cdd:COG0123   64 DA----LRAAS--LDGGYGqLDPDTPVSPGTWE-AALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGFCLF 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 568 NNVAVAVKVLQTKYpaqCAKIAIIDWDVHHGNGTQLSFENDPNVLYMSLHRHdkgNFFPGTGSVTEVGKNDAKGLTVNVP 647
Cdd:COG0123  137 NNAAIAARYLLAKG---LERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD---PLYPGTGAADETGEGAGEGSNLNVP 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 648 ---FSGdvmrDPEYLAAWRTVIEPVMASFCPDFIIVSAGFDACHGHPnaLGGYEVTPEMFGYMTKSLL---NYASGKVVL 721
Cdd:COG0123  211 lppGTG----DAEYLAALEEALLPALEAFKPDLIVVSAGFDAHADDP--LGRLNLTTEGYAWRTRRVLelaDHCGGPVVS 284

                        330       340
                 ....*....|....*....|....
gi 392928255 722 ALEGGYDLKSISEAAQQCVQALIG 745
Cdd:COG0123  285 VLEGGYNLDALARSVAAHLETLLG 308
PTZ00063 PTZ00063
histone deacetylase; Provisional
 460-700 2.53e-25

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 109.90  E-value: 2.53e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 460 KASLEQLQLVHSQTYTTFFA-VSPTACLKIdanSLPLKRFlqlpcgGIGVDSDTYFNDASTQTAARLAAGTLIelssqvA 538
Cdd:PTZ00063  53 KSVEPELVLFHDEEYVDFLSsISPENYRDF---TYQLKRF------NVGEATDCPVFDGLFEFQQSCAGASID------G 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 539 EGRLKNGFA--CIRPPG--HHAEHEQAMGFCFFNNVAVAVKVLqTKYPAqcaKIAIIDWDVHHGNGTQLSFENDPNVLYM 614
Cdd:PTZ00063 118 AYKLNNHQAdiCVNWSGglHHAKRSEASGFCYINDIVLGILEL-LKYHA---RVMYIDIDVHHGDGVEEAFYVTHRVMTV 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 615 SLHRHdkGNFFPGTGSVTEVGKNDAKGLTVNVPFSgDVMRDPEYLAAWRTVIEPVMASFCPDFIIVSAGFDACHGhpNAL 694
Cdd:PTZ00063 194 SFHKF--GDFFPGTGDVTDIGVAQGKYYSVNVPLN-DGIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTG--DRL 268


                 ....*.
gi 392928255 695 GGYEVT 700
Cdd:PTZ00063 269 GRFNLT 274
 
Name Accession Description Interval E-value
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 407-781 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: 696.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 407 CTTGLGYDQAMVRHECCCGNNASHVENGGRIQSIWSKLIEHGHVQKCEKVTAKKASLEQLQLVHSQTYTTFFAVSPTACL 486
Cdd:cd11681    1 FTTGLAYDPLMLKHQCICGNNSSHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTLLYGTNPLSRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 487 KIDANSL---PLKRFLQLPCGGIGVDSDTYFNDASTQTAARLAAGTLIELSSQVAEGRLKNGFACIRPPGHHAEHEQAMG 563
Cdd:cd11681   81 KLDPTKLaglPQKSFVRLPCGGIGVDSDTVWNELHTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQAMG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 564 FCFFNNVAVAVKVLQTKYPaqCAKIAIIDWDVHHGNGTQLSFENDPNVLYMSLHRHDKGNFFPGTGSVTEVGKNDAKGLT 643
Cdd:cd11681  161 FCFFNSVAIAAKQLQQKLK--LRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFPGTGAPTEVGSGAGEGFN 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 644 VNVPFSGDV---MRDPEYLAAWRTVIEPVMASFCPDFIIVSAGFDACHGHPNALGGYEVTPEMFGYMTKSLLNYASGKVV 720
Cdd:cd11681  239 VNIAWSGGLdppMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPPPLGGYKVSPACFGYMTRQLMNLAGGKVV 318

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392928255 721 LALEGGYDLKSISEAAQQCVQALIGESDDAgrLSSVALESLPNPSAVETLQKVIAIHKSYW 781
Cdd:cd11681  319 LALEGGYDLTAICDASEACVRALLGDELDP--LSEEELERRPNPNAVTSLEKVIAIQSPYW 377
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
 408-781 6.22e-160

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: 469.88  E-value: 6.22e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 408 TTGLGYDQAMVRHECCCGNNASHVENGGRIQSIWSKLIEHGHVQKCEKVTAKKASLEQLQLVHSQTYTTFFAVSPTACLK 487
Cdd:cd10008    2 TTGLVYDSVMLKHQCSCGDNSNHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 488 ID----ANSLPLKRFLQLPCGGIGVDSDTYFNDASTQTAARLAAGTLIELSSQVAEGRLKNGFACIRPPGHHAEHEQAMG 563
Cdd:cd10008   82 LDngklAGLLAQRMFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 564 FCFFNNVAVAVKVLQTKypAQCAKIAIIDWDVHHGNGTQLSFENDPNVLYMSLHRHDKGNFFPGTGSVTEVGKNDAKGLT 643
Cdd:cd10008  162 FCFFNSVAIACRQLQQQ--GKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGAGSGEGFN 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 644 VNVPFSGDV---MRDPEYLAAWRTVIEPVMASFCPDFIIVSAGFDACHGHPNALGGYEVTPEMFGYMTKSLLNYASGKVV 720
Cdd:cd10008  240 VNVAWAGGLdppMGDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVV 319

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392928255 721 LALEGGYDLKSISEAAQQCVQALIGESDDAgrLSSVALESLPNPSAVETLQKVIAIHKSYW 781
Cdd:cd10008  320 LALEGGHDLTAICDASEACVAALLGNEVDP--LSEESWKQKPNLNAIRSLEAVIRVHSKYW 378
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
 404-785 1.81e-159

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: 469.90  E-value: 1.81e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 404 EPTCTTGLGYDQAMVRHECCCGNNASHVENGGRIQSIWSKLIEHGHVQKCEKVTAKKASLEQLQLVHSQTYTTFFAVSPT 483
Cdd:cd10006    1 KPRFTTGLVYDTLMLKHQCTCGNSNSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 484 ACLKIDANSLPLK---RFLQLPCGGIGVDSDTYFNDASTQTAARLAAGTLIELSSQVAEGRLKNGFACIRPPGHHAEHEQ 560
Cdd:cd10006   81 NRQKLDSKKLLGSlasVFVRLPCGGVGVDSDTIWNEVHSSGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEEST 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 561 AMGFCFFNNVAVAVKVLQTKYpaQCAKIAIIDWDVHHGNGTQLSFENDPNVLYMSLHRHDKGNFFPGTGSVTEVGKNDAK 640
Cdd:cd10006  161 PMGFCYFNSVAIAAKLLQQRL--NVSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYDDGNFFPGSGAPDEVGTGPGV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 641 GLTVNVPFSGDV---MRDPEYLAAWRTVIEPVMASFCPDFIIVSAGFDACHGHPNALGGYEVTPEMFGYMTKSLLNYASG 717
Cdd:cd10006  239 GFNVNMAFTGGLdppMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSAKCFGYLTKQLMGLAGG 318

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392928255 718 KVVLALEGGYDLKSISEAAQQCVQALIGESDDAgrLSSVALESLPNPSAVETLQKVIAIHKSYWPALH 785
Cdd:cd10006  319 RIVLALEGGHDLTAICDASEACVSALLGNELDP--LPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQ 384
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
 408-784 5.25e-155

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: 459.07  E-value: 5.25e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 408 TTGLGYDQAMVRHECCCGNNASHVENGGRIQSIWSKLIEHGHVQKCEKVTAKKASLEQLQLVHSQTYTTFFAVSPTACLK 487
Cdd:cd10007    4 TTGLVYDTFMLKHQCTCGNTNVHPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHSEHHTLLYGTSPLNRQK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 488 IDANSL--PL--KRFLQLPCGGIGVDSDTYFNDASTQTAARLAAGTLIELSSQVAEGRLKNGFACIRPPGHHAEHEQAMG 563
Cdd:cd10007   84 LDSKKLlgPLsqKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLIELAFKVAAGELKNGFAVIRPPGHHAEESTAMG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 564 FCFFNNVAVAVKVLQTKYpaQCAKIAIIDWDVHHGNGTQLSFENDPNVLYMSLHRHDKGNFFPGTGSVTEVGKNDAKGLT 643
Cdd:cd10007  164 FCFFNSVAIAAKLLQQKL--NVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGNFFPGSGAPDEVGAGPGVGFN 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 644 VNVPFSGDV---MRDPEYLAAWRTVIEPVMASFCPDFIIVSAGFDACHGHPNALGGYEVTPEMFGYMTKSLLNYASGKVV 720
Cdd:cd10007  242 VNIAWTGGVdppIGDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGHQSPLGGYSVTAKCFGHLTKQLMTLAGGRVV 321

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392928255 721 LALEGGYDLKSISEAAQQCVQALIGesDDAGRLSSVALESLPNPSAVETLQKVIAIHKSYWPAL 784
Cdd:cd10007  322 LALEGGHDLTAICDASEACVSALLG--MELTPLDNTVLQQKPNDNAVATLERVIEIQSKHWSCL 383
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
 408-781 5.78e-134

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: 403.24  E-value: 5.78e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 408 TTGLGYDQAMVRHECCCGNNASHVENGGRIQSIWSKLIEHGHVQKCEKVTAKKASLEQLQLVHSQTYTTFFAVSPTACLK 487
Cdd:cd10009    2 ATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 488 IDANSL----PLKRFLQLPCGGIGVDSDTYFNDASTQTAARLAAGTLIELSSQVAEGRLKNGFACIRPPGHHAEHEQAMG 563
Cdd:cd10009   82 LDPRILlgddSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 564 FCFFNNVAVAVKVLQTKYpaQCAKIAIIDWDVHHGNGTQLSFENDPNVLYMSLHRHDKGNFFPGTGSVTEVGKNDAKGLT 643
Cdd:cd10009  162 FCFFNSVAITAKYLRDQL--NISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYN 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 644 VNVPFSGDV---MRDPEYLAAWRTVIEPVMASFCPDFIIVSAGFDACHGHPNALGGYEVTPEMFGYMTKSLLNYASGKVV 720
Cdd:cd10009  240 INIAWTGGLdppMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVV 319

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392928255 721 LALEGGYDLKSISEAAQQCVQALIGesDDAGRLSSVALESLPNPSAVETLQKVIAIHKSYW 781
Cdd:cd10009  320 LALEGGHDLTAICDASEACVNALLG--NELEPLAEDILHQSPNMNAVISLQKIIEIQSKYW 378
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
 430-743 3.54e-124

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: 374.53  E-value: 3.54e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 430 HVENGGRIQSIWSKLIEHGHVQKCEKVTAKKASLEQLQLVHSQTYttffavsptaclkidanslpLKRFLQLPCGGIGV- 508
Cdd:cd09992    1 HPERPERLLAILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEY--------------------IERVEETCEAGGGYl 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 509 DSDTYFNDASTQtAARLAAGTLIELSSQVAEGRLKNGFACIRPPGHHAEHEQAMGFCFFNNVAVAVKVLQTKYPAQcaKI 588
Cdd:cd09992   61 DPDTYVSPGSYE-AALLAAGAALAAVDAVLSGEAENAFALVRPPGHHAEPDRAMGFCLFNNVAIAARYAQKRYGLK--RV 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 589 AIIDWDVHHGNGTQLSFENDPNVLYMSLHRHDkgnFFPGTGSVTEVGKNDAKGLTVNVPFSGDvMRDPEYLAAWRTVIEP 668
Cdd:cd09992  138 LIVDWDVHHGNGTQDIFYDDPSVLYFSIHQYP---FYPGTGAAEETGGGAGEGFTINVPLPPG-SGDAEYLAAFEEVLLP 213

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392928255 669 VMASFCPDFIIVSAGFDACHGHPnaLGGYEVTPEMFGYMTKSLLN----YASGKVVLALEGGYDLKSISEAAQQCVQAL 743
Cdd:cd09992  214 IAREFQPDLVLVSAGFDAHRGDP--LGGMNLTPEGYARLTRLLKEladeHCGGRLVFVLEGGYNLEALAESVLAVLEAL 290
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
 413-784 1.13e-116

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: 357.42  E-value: 1.13e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 413 YDQAMVRHecCCGNNASHVENGGRIQSIWSKLIEHGHVQKCEKVTAKKASLEQLQLVHSQTYttffavsptacLKIDANS 492
Cdd:cd10003    1 YDQRMMNH--HNLWDPGHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEH-----------LDEMKSL 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 493 LPLK-RFLqlpcGGIGVDSDTYFNDASTQTAARLAAGTLIELSSQVAEGRLKNGFACIRPPGHHAEHEQAMGFCFFNNVA 571
Cdd:cd10003   68 EKMKpREL----NRLGKEYDSIYIHPDSYQCALLAAGCVLQVVEAVLTGESRNGVAIVRPPGHHAEQDTACGFCFFNNVA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 572 VAVKVLQTKYPAQcaKIAIIDWDVHHGNGTQLSFENDPNVLYMSLHRHDKGNFFPGT--GSVTEVGKNDAKGLTVNVPFS 649
Cdd:cd10003  144 IAARYAQKKYGLK--RILIVDWDVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSpeGNYDVVGKGKGEGFNVNIPWN 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 650 GDVMRDPEYLAAWRTVIEPVMASFCPDFIIVSAGFDACHGHPnaLGGYEVTPEMFGYMTKSLLNYASGKVVLALEGGYDL 729
Cdd:cd10003  222 KGGMGDAEYIAAFQQVVLPIAYEFNPELVLVSAGFDAARGDP--LGGCKVTPEGYAHMTHMLMSLAGGRVIVILEGGYNL 299

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 392928255 730 KSISEAAQQCVQALIGESddagrLSSVALESLPNPSAVETLQKVIAIHKSYWPAL 784
Cdd:cd10003  300 TSISESMSMCTKTLLGDP-----PPVLDLPRPPCSSALKSINNVLQVHQKYWKSL 349
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 430-750 1.45e-110

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: 340.09  E-value: 1.45e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 430 HVENGGRIQSIWSKLIEHGHVQKCEKVTAKKASLEQLQLVHSQTYTTFfaVSPTAcLKIDANSLPLKRFLqlpcggiGVD 509
Cdd:cd11600    3 HPEDPSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEHWDR--VEATE-KMSDEQLKDRTEIF-------ERD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 510 SdTYFNDaSTQTAARLAAGTLIELSSQVAEGRLKNGFACIRPPGHHAEHEQAMGFCFFNNVAVAVKVLQTKYPAQCAKIA 589
Cdd:cd11600   73 S-LYVNN-DTAFCARLSCGGAIEACRAVAEGRVKNAFAVVRPPGHHAEPDESMGFCFFNNVAVAAKWLQTEYPDKIKKIL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 590 IIDWDVHHGNGTQLSFENDPNVLYMSLHRHDKGNFFPGT--GSVTEVGKNDAKGLTVNVPFSGDVMRDPEYLAAWRTVIE 667
Cdd:cd11600  151 ILDWDIHHGNGTQRAFYDDPNVLYISLHRFENGGFYPGTpyGDYESVGEGAGLGFNVNIPWPQGGMGDADYIYAFQRIVM 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 668 PVMASFCPDFIIVSAGFDACHGHPnaLGGYEVTPEMFGYMTKSLLNYASGKVVLALEGGYDLKSISEAAQQCVQALIGES 747
Cdd:cd11600  231 PIAYEFDPDLVIISAGFDAADGDE--LGQCHVTPAGYAHMTHMLMSLAGGKLVVALEGGYNLDAISDSALAVAKVLLGEA 308


                 ...
gi 392928255 748 DDA 750
Cdd:cd11600  309 PPK 311
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 430-743 3.03e-105

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: 325.73  E-value: 3.03e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255  430 HVENGGRIQSIWSKLIEHGHVQKCEKVTAKKASLEQLQLVHSQTYTTFFAvspTACLKIDAnslplkrflQLPCGGIGVD 509
Cdd:pfam00850   1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLE---EAAPEGGA---------LLLLSYLSGD 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255  510 SDTYFNDASTQtAARLAAGTLIELSSQVAEGRLKNGFACIRPPGHHAEHEQAMGFCFFNNVAVAVKVLQTKYpaQCAKIA 589
Cdd:pfam00850  69 DDTPVSPGSYE-AALLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKY--GLKRVA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255  590 IIDWDVHHGNGTQLSFENDPNVLYMSLHRHDkGNFFPGTGSVTEVGKNDAKGLTVNVPFSGDvMRDPEYLAAWRTVIEPV 669
Cdd:pfam00850 146 IVDFDVHHGNGTQEIFYDDPSVLTLSIHQYP-GGFYPGTGFADETGEGKGKGYTLNVPLPPG-TGDAEYLAAFEEILLPA 223

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392928255  670 MASFCPDFIIVSAGFDACHGHPnaLGGYEVTPEMFGYMTKSLLNYA---SGKVVLALEGGYDLKSISEAAQQCVQAL 743
Cdd:pfam00850 224 LEEFQPDLILVSAGFDAHAGDP--LGGLNLTTEGFAEITRILLELAdplCIRVVSVLEGGYNLDALARSATAVLAAL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 409-745 6.88e-96

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 301.64  E-value: 6.88e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 409 TGLGYDQAMVRHECccgnNASHVENGGRIQSIWSKLIEHGHVQKCEKVTAKKASLEQLQLVHSQTYttffavsptaclkI 488
Cdd:COG0123    1 TALIYHPDYLLHDL----GPGHPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDY-------------V 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 489 DAnslpLKRFLqlPCGGIG-VDSDTYFNDASTQtAARLAAGTLIELSSQVAEGRLKNGFACIRPPGHHAEHEQAMGFCFF 567
Cdd:COG0123   64 DA----LRAAS--LDGGYGqLDPDTPVSPGTWE-AALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGFCLF 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 568 NNVAVAVKVLQTKYpaqCAKIAIIDWDVHHGNGTQLSFENDPNVLYMSLHRHdkgNFFPGTGSVTEVGKNDAKGLTVNVP 647
Cdd:COG0123  137 NNAAIAARYLLAKG---LERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD---PLYPGTGAADETGEGAGEGSNLNVP 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 648 ---FSGdvmrDPEYLAAWRTVIEPVMASFCPDFIIVSAGFDACHGHPnaLGGYEVTPEMFGYMTKSLL---NYASGKVVL 721
Cdd:COG0123  211 lppGTG----DAEYLAALEEALLPALEAFKPDLIVVSAGFDAHADDP--LGRLNLTTEGYAWRTRRVLelaDHCGGPVVS 284

                        330       340
                 ....*....|....*....|....
gi 392928255 722 ALEGGYDLKSISEAAQQCVQALIG 745
Cdd:COG0123  285 VLEGGYNLDALARSVAAHLETLLG 308
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 429-781 3.48e-88

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: 282.28  E-value: 3.48e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 429 SHVENGGRIQSIWSKLIEHGHVQKCEKVTAKKASLEQLQLVHSQTYTtffavsptACLKiDANSLPLKRFLQLpCGGIgv 508
Cdd:cd10002    6 NHIECPERLEAILERLTQDGLLERCVKIPAREAEEDEILLVHSQEYI--------DLVK-STETMEKEELESL-CSGY-- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 509 dSDTYFNdASTQTAARLAAGTLIELSSQVAEGRLKNGFACIRPPGHHAEHEQAMGFCFFNNVAVAVKVLQTKYPAQcaKI 588
Cdd:cd10002   74 -DSVYLC-PSTYEAARLAAGSTIELVKAVMAGKIQNGFALIRPPGHHAMRNEANGYCIFNNVAIAAKYAIEKLGLK--RI 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 589 AIIDWDVHHGNGTQLSFENDPNVLYMSLHRHDKGNFFPG--TGSVTEVGKNDAKGLTVNVPFSGDVMRDPEYLAAWRTVI 666
Cdd:cd10002  150 LIVDWDVHHGQGTQQGFYEDPRVLYFSIHRYEHGRFWPHlfESDYDYIGVGHGYGFNVNVPLNQTGLGDADYLAIFHHIL 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 667 EPVMASFCPDFIIVSAGFDACHGHPNalGGYEVTPEMFGYMTKSLLNYASGKVVLALEGGYDLKSISEAAQQCVQALIGE 746
Cdd:cd10002  230 LPLALEFQPELVLVSAGFDASIGDPE--GEMAVTPAGYAHLTRLLMGLAGGKLLLVLEGGYLLESLAESVSMTLRGLLGD 307

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 392928255 747 SddagrLSSVALESlPNPSAVETLQKVIAIHKSYW 781
Cdd:cd10002  308 P-----LPPLAPPI-PIRSVLETILNAIAHLSPRW 336
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
 430-744 3.66e-83

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: 267.46  E-value: 3.66e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 430 HVENGGRIQSIWSKLIEHGHVQKCEKVTAKKASLEQLQLVHSQTYttffavsptaclkIDA--NSLPLKRFLQLpcggig 507
Cdd:cd11599    1 HPESPERLEAILDALIASGLDRLLRQLEAPPATREQLLRVHDAAY-------------VDRleAAAPEEGLVQL------ 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 508 vDSDTYFNDASTQtAARLAAGTLIELSSQVAEGRLKNGFACIRPPGHHAEHEQAMGFCFFNNVAVAVKVLQTKYPAQcaK 587
Cdd:cd11599   62 -DPDTAMSPGSLE-AALRAAGAVVAAVDAVMAGEARNAFCAVRPPGHHAERDKAMGFCLFNNVAIAAAHALAHHGLE--R 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 588 IAIIDWDVHHGNGTQLSFENDPNVLYMSLHRHdkgNFFPGTGSVTEVGKNDAkgltVNVPFSGDVMRDpEYLAAWRTVIE 667
Cdd:cd11599  138 VAIVDFDVHHGNGTEDIFRDDPRVLFCSSHQH---PLYPGTGAPDETGHGNI----VNVPLPAGTGGA-EFREAVEDRWL 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 668 PVMASFCPDFIIVSAGFDAchgHPN-ALGGYEVTPEMFGYMTKSLL----NYASGKVVLALEGGYDLKSISEAAQQCVQA 742
Cdd:cd11599  210 PALDAFKPDLILISAGFDA---HRDdPLAQLNLTEEDYAWITEQLMdvadRYCDGRIVSVLEGGYDLSALARSVAAHVRA 286


                 ..
gi 392928255 743 LI 744
Cdd:cd11599  287 LM 288
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
 409-727 7.91e-76

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: 250.56  E-value: 7.91e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 409 TGLGYDQAMVRHECccGNNASHVENGGRIQSIW------------------SKLIEHGHVqkcekVTAKKASLEQLQLVH 470
Cdd:cd09996    1 TGFVWDERYLWHDT--GTGALFLPVGGLLVQPGrhpenpetkrriknllevSGLSDHLVL-----ITPRPATDEELLRVH 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 471 SQTYttffavsptaclkIDAnslpLKRFLQLPCGGIGvdSDTYFNDASTQtAARLAAGTLIELSSQVAEGRLKNGFACIR 550
Cdd:cd09996   74 TPEY-------------IDR----VKAASAAGGGEAG--GGTPFGPGSYE-IALLAAGGAIAAVDAVLDGEVDNAYALVR 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 551 PPGHHAEHEQAMGFCFFNNVAVAVKVLQTKYpaQCAKIAIIDWDVHHGNGTQLSFENDPNVLYMSLHRHdkGNFFPGTGS 630
Cdd:cd09996  134 PPGHHAEPDQGMGFCLFNNVAIAARHALAVG--GVKRVAVVDWDVHHGNGTQAIFYDDPDVLTISLHQD--RCFPPDSGA 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 631 VTEVGKNDAKGLTVNVPF---SGdvmrDPEYLAAWRTVIEPVMASFCPDFIIVSAGFDACHGHPnaLGGYEVTPEMFGYM 707
Cdd:cd09996  210 VEERGEGAGEGYNLNIPLppgSG----DGAYLHAFERIVLPALRAFRPELIIVASGFDASAFDP--LGRMMLTSDGFRAL 283

                        330       340
                 ....*....|....*....|....
gi 392928255 708 TKSLL----NYASGKVVLALEGGY 727
Cdd:cd09996  284 TRKLRdladELCGGRLVMVHEGGY 307
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 431-781 1.64e-75

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: 249.01  E-value: 1.64e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 431 VENGGRIQSIWSKLIEHGHVQKCEKVTAKKASLEQLQLVHSQTYTTFFAVSPTAclkidaNSLPLKRFLQlpcggigvDS 510
Cdd:cd11683    8 IEVPERLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRETQVM------NKEELMAISG--------KY 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 511 DTYFNDASTQTAARLAAGTLIELSSQVAEGRLKNGFACIRPPGHHAEHEQAMGFCFFNNVAVAVKVLQTKYPAQcaKIAI 590
Cdd:cd11683   74 DAVYFHPNTFHCARLAAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYAKKKYGLH--RILI 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 591 IDWDVHHGNGTQLSFENDPNVLYMSLHRHDKGNFFPG--TGSVTEVGKNDAKGLTVNVPFSGDVMRDPEYLAAWRTVIEP 668
Cdd:cd11683  152 VDWDVHHGQGIQYIFEEDPSVLYFSWHRYEHQRFWPFlrESDYDAVGRGKGLGFNINLPWNKVGMGNADYLAAFFHVLLP 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 669 VMASFCPDFIIVSAGFDACHGHPNalGGYEVTPEMFGYMTKSLLNYASGKVVLALEGGYDLKSISEAAQQCVQALIGesD 748
Cdd:cd11683  232 LAFEFDPELVLVSAGFDSAIGDPE--GQMCATPECFAHLTHLLMVLAGGKLCAVLEGGYHLESLAESVCMTVQTLLG--D 307

                        330       340       350
                 ....*....|....*....|....*....|...
gi 392928255 749 DAGRLSSvalESLPNPSAVETLQKVIAIHKSYW 781
Cdd:cd11683  308 PLPRLSG---EMTPCQSALESIQNVRAAQAPYW 337
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
 424-781 1.69e-75

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: 248.61  E-value: 1.69e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 424 CGNNASHVENGGRIQSIWSKLIEHGHVQKCEKVTAKKASLEQLQLVHSQTYTTFfavsptaclkidanslpLKRFLQLPC 503
Cdd:cd11682    1 CLWDESFPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYVAL-----------------MKSTQYMTE 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 504 GGIGVDSDTY---FNDASTQTAARLAAGTLIELSSQVAEGRLKNGFACIRPPGHHAEHEQAMGFCFFNNVAVAVKVLQTK 580
Cdd:cd11682   64 EELRTLADTYdsvYLHPNSYSCACLAVGSVLQLVDKVLGGEIRNGLAIVRPPGHHAQHDKMDGYCMFNNVAIAARYAQQK 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 581 YPAQcaKIAIIDWDVHHGNGTQLSFENDPNVLYMSLHRHDKGNFFP--GTGSVTEVGKNDAKGLTVNVPFSGDVMRDPEY 658
Cdd:cd11682  144 HGVQ--RVLIVDWDVHHGQGTQFIFEQDPSVLYFSIHRYEQGRFWPhlKESDSSAVGFGRGEGYNINVPWNQVGMRDADY 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 659 LAAWRTVIEPVMASFCPDFIIVSAGFDACHGHPNalGGYEVTPEMFGYMTKSLLNYASGKVVLALEGGYDLKSISEAAQQ 738
Cdd:cd11682  222 IAAFLHVLLPVALEFQPQLVLVAAGFDAVIGDPK--GEMAATPACFAHLTHLLMGLAGGKLILSLEGGYNLRSLAEGVCA 299

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 392928255 739 CVQALIGesDDAGRLSSvalESLPNPSAVETLQKVIAIHKSYW 781
Cdd:cd11682  300 SLKALLG--DPCPMLES---PGAPCRSALASVSCTISALEPFW 337
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
 436-743 6.16e-67

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: 223.85  E-value: 6.16e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 436 RIQSIWSKLIEHGHVQKCEKVTAKKASLEQLQLVHSQTYTTFFAVSPtaclkidanslplkRFLQLPCGGIGVDSDTYFN 515
Cdd:cd09301    1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKANF--------------AVATITESKPVIFGPNFPV 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 516 DASTQTAARLAAGTLIELSSQVAEGRLKNGFACIRPPGHHAEHEQAMGFCFFNNVAVAVKVLQTKypaQCAKIAIIDWDV 595
Cdd:cd09301   67 QRHYFRGARLSTGGVVEAAELVAKGELERAFAVVGAGGHHAGKSRAWGFCYFNDVVLAIKFLRER---GISRILIIDTDA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 596 HHGNGTQLSFENDPNVLYMSLHRHDKGNFFPGTGsvtevgkndaKGLTVNVPFsGDVMRDPEYLAAWRTVIEPVMASFCP 675
Cdd:cd09301  144 HHGDGTREAFYDDDRVLHMSFHNYDIYPFGRGKG----------KGYKINVPL-EDGLGDEEYLDAVERVISKVLEEFEP 212

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392928255 676 DFIIVSAGFDACHGHPnaLGGYEVTPEMFGYMTKSLLNYASGK-VVLALEGGYDLKSISEAAQQCVQAL 743
Cdd:cd09301  213 EVVVLQFGHDTHEGDR--LGGFNLSEKGFVKLAEIVKEFARGGpILMVLGGGYNPEAAARIWTAIIKEL 279
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
 418-736 1.40e-65

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: 220.49  E-value: 1.40e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 418 VRHECCCGNNASHVENGGRIQSIWSKLIEHGHVqkcEKVTAKKASLEQLQLVHSQTYTTFfavsptaclkidanslpLKR 497
Cdd:cd10001   13 PKTELSRGKLVPHPENPERAEAILDALKRAGLG---EVLPPRDFGLEPILAVHDPDYVDF-----------------LET 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 498 FlqlpcggigvDSDTYFNdASTQTAARLAAGTLIELSSQVAEGRlKNGFACIRPPGHHAEHEQAMGFCFFNNVAVAVKVL 577
Cdd:cd10001   73 A----------DTDTPIS-EGTWEAALAAADTALTAADLVLEGE-RAAYALCRPPGHHAGRDRAGGFCYFNNAAIAAQYL 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 578 QtkypAQCAKIAIIDWDVHHGNGTQLSFENDPNVLYMSLHRHDKgNFFPGT-GSVTEVGKNDAKGLTVNVPF---SGdvm 653
Cdd:cd10001  141 R----DRAGRVAILDVDVHHGNGTQEIFYERPDVLYVSIHGDPR-TFYPFFlGFADETGEGEGEGYNLNLPLppgTG--- 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 654 rDPEYLAAWRTVIEPVMAsFCPDFIIVSAGFDACHGHPnaLGGYEVTPEMFGYMTKSL--LNYasgKVVLALEGGYDLKS 731
Cdd:cd10001  213 -DDDYLAALDEALAAIAA-FGPDALVVSLGFDTHEGDP--LSDFKLTTEDYARIGRRIaaLGL---PTVFVQEGGYNVDA 285


                 ....*
gi 392928255 732 ISEAA 736
Cdd:cd10001  286 LGRNA 290
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
 456-729 5.73e-49

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: 175.44  E-value: 5.73e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 456 VTAKKASLEQLQLVHSQTYTTFF-AVSPTACLKIDAnslplkRFlqlpcgGIGVDSDTYFndASTQTAARLAAGTLIELS 534
Cdd:cd09994   43 VPPRPATEEELLLFHTPDYIEAVkEASRGQEPEGRG------RL------GLGTEDNPVF--PGMHEAAALVVGGTLLAA 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 535 SQVAEGRLKNGFAcirPPG--HHAEHEQAMGFCFFNNVAVAVKVLQTKYpaqCAKIAIIDWDVHHGNGTQLSFENDPNVL 612
Cdd:cd09994  109 RLVLEGEARRAFN---PAGglHHAMRGRASGFCVYNDAAVAIERLRDKG---GLRVAYVDIDAHHGDGVQAAFYDDPRVL 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 613 YMSLHRHDKGnFFPGTGSVTEVGKNDAKGLTVNVPfsgdVMR---DPEYLAAWRTVIEPVMASFCPDFIIVSAGFDACHG 689
Cdd:cd09994  183 TISLHESGRY-LFPGTGFVDEIGEGEGYGYAVNIP----LPPgtgDDEFLRAFEAVVPPLLRAFRPDVIVSQHGADAHAG 257

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 392928255 690 HPnaLGGYEVTPEMFGYMTKSLLN----YASGKVVLALEGGYDL 729
Cdd:cd09994  258 DP--LTHLNLSNRAYRAAVRRIREladeYCGGRWLALGGGGYNP 299
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 413-733 2.36e-36

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: 140.94  E-value: 2.36e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 413 YDQAMVRhECccgNNASHVENGGriqSIWSKLIE-HGHVQKCEKVTAKKASLEQLQLVHSQTYTTFFAvSPTACLKIDAN 491
Cdd:cd10000    5 HSPEYVN-LC---DRLPKVPNRA---SMVHSLIEaYGLLKQLRVVKPRVATEEELASFHSDEYIQFLK-KASNEGDNDEE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 492 SLPLKRFlqlpcgGIGVD----SDTYFNDASTQTAARLAAGTLIELSSQVAegrlkngfacIRPPG--HHAEHEQAMGFC 565
Cdd:cd10000   77 PSEQQEF------GLGYDcpifEGIYDYAAAVAGATLTAAQLLIDGKCKVA----------INWFGgwHHAQRDEASGFC 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 566 FFNNVAVAVKVLQTKYpaqcAKIAIIDWDVHHGNGTQLSFENDPNVLYMSLHRHDKGnFFPGTGSVTEVGKNDAKGLTVN 645
Cdd:cd10000  141 YVNDIVLGILKLREKF----DRVLYVDLDLHHGDGVEDAFSFTSKVMTVSLHKYSPG-FFPGTGDVSDVGLGKGKYYTVN 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 646 VPFSgDVMRDPEYLAAWRTVIEPVMASFCPDFIIVSAGFDACHGHPnaLGGYEVTPEMFGYMTKSLLNYASGKVVLAlEG 725
Cdd:cd10000  216 VPLR-DGIQDEQYLQIFTAVVPEIVAAFRPEAVVLQCGADTLAGDP--MGAFNLTPVGIGKCLKYVLGWKLPTLILG-GG 291


                 ....*...
gi 392928255 726 GYDLKSIS 733
Cdd:cd10000  292 GYNLANTA 299
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 440-702 1.27e-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: 1.27e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 440 IWSKLIEHGHVQKCEKVTAKKASLEQLQLVHSQTY-TTFF--AVSPTACLKIDansLP-----LKRFLqLPCGGigvdsd 511
Cdd:cd09993   11 LREALLEEGLVLPEDIVEPEPATREDLLRVHDPEYlESLKsgELSREEIRRIG---FPwspelVERTR-LAVGG------ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 512 tyfndasTQTAARLAagtlielssqvaegrLKNGFACiRPPG--HHAEHEQAMGFCFFNNVAVAVKVLQTKYPAQcaKIA 589
Cdd:cd09993   81 -------TILAARLA---------------LEHGLAI-NLAGgtHHAFPDRGEGFCVFNDIAIAARVLLAEGLVR--RVL 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 590 IIDWDVHHGNGTQLSFENDPNVLYMSLHrhdKGNFFPGtgsvtevgknDAKGLTVNVPFsGDVMRDPEYLAAWRTVIEPV 669
Cdd:cd09993  136 IVDLDVHQGNGTAAIFADDPSVFTFSMH---GEKNYPF----------RKEPSDLDVPL-PDGTGDDEYLAALEEALPRL 201

                        250       260       270
                 ....*....|....*....|....*....|...
gi 392928255 670 MASFCPDFIIVSAGFDACHGHPnaLGGYEVTPE 702
Cdd:cd09993  202 LAEFRPDLVFYNAGVDVLAGDR--LGRLSLSLE 232
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
 433-726 5.34e-29

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: 117.75  E-value: 5.34e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 433 NGGRIQSIWSKLIEHG-HVQKCEKVTAKKASLEQLQLVHSQTYTTFFavsptaclkidanslpLKRFlqlpcggiGVDSD 511
Cdd:cd11680   18 NKGRSSLVHSLIRAYGlLQHFDEIIEPERATRKDLTKYHDKDYVDFL----------------LKKY--------GLEDD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 512 TY-FndASTQTAARLAAGTLIELSSQVAEGRlkngfacIRPPG-------HHAEHEQAMGFCFFNNVAVAVKVL-QTKYP 582
Cdd:cd11680   74 CPvF--PFLSMYVQLVAGSSLALAKHLITQV-------ERDIAinwyggrHHAQKSRASGFCYVNDIVLAILRLrRARFR 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 583 aqcaKIAIIDWDVHHGNGTQLSFENDPNVLYMSLHRHDKGnFFPGTGSVtevgKNDAKGLTVNVPFS-GdvMRDPEYLAA 661
Cdd:cd11680  145 ----RVFYLDLDLHHGDGVESAFFFSKNVLTCSIHRYDPG-FFPGTGSL----KNSSDKGMLNIPLKrG--LSDKTLLRI 213

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392928255 662 WRTVIEPVMASFCPDFIIVSAGFDACHGHPnaLGGYEVTPEMFGYMTKSLLNYASGKVVLALEGG 726
Cdd:cd11680  214 IDSIVRPLIEKFEPEVIVIQCGCDGLSGDP--HKEWNLTIRGYGSVIELLLKEFKDKPTLLLGGG 276
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
 458-735 9.56e-27

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: 111.39  E-value: 9.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 458 AKKASLEQLQLVHSQTYTTFFA-VSPTaclkiDANSLPLKRFLQLPCGGIGVDSDTYFNDASTQTAARLAAG-TLIELSS 535
Cdd:cd11598   46 ARAATREELRQFHDADYLDFLSkVSPE-----NANQLRFDKAEPFNIGDDCPVFDGMYDYCQLYAGASLDAArKLCSGQS 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 536 QVA---EGRLkngfacirppgHHAEHEQAMGFCFFNNVAVAVKVLQTKYPaqcaKIAIIDWDVHHGNGTQLSFENDPNVL 612
Cdd:cd11598  121 DIAinwSGGL-----------HHAKKSEASGFCYVNDIVLAILNLLRYFP----RVLYIDIDVHHGDGVEEAFYRTDRVM 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 613 YMSLHRHDkGNFFPGTGSVTEVGKNDAKGLTVNVPFSgDVMRDPEYLAAWRTVIEPVMASFCPDFIIVSAGFDACHGhpN 692
Cdd:cd11598  186 TLSFHKYN-GEFFPGTGDLDDNGGTPGKHFALNVPLE-DGIDDEQYNLLFKSIIGPTIEKFQPSAIVLQCGADSLGG--D 261

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 392928255 693 ALGGYEVTPEMFGYMTKSLLNYASGKVVLAlEGGYDLKSISEA 735
Cdd:cd11598  262 RLGQFNLNIKAHGACVKFVKSFGIPMLVVG-GGGYTPRNVARA 303
PTZ00063 PTZ00063
histone deacetylase; Provisional
 460-700 2.53e-25

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 109.90  E-value: 2.53e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 460 KASLEQLQLVHSQTYTTFFA-VSPTACLKIdanSLPLKRFlqlpcgGIGVDSDTYFNDASTQTAARLAAGTLIelssqvA 538
Cdd:PTZ00063  53 KSVEPELVLFHDEEYVDFLSsISPENYRDF---TYQLKRF------NVGEATDCPVFDGLFEFQQSCAGASID------G 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 539 EGRLKNGFA--CIRPPG--HHAEHEQAMGFCFFNNVAVAVKVLqTKYPAqcaKIAIIDWDVHHGNGTQLSFENDPNVLYM 614
Cdd:PTZ00063 118 AYKLNNHQAdiCVNWSGglHHAKRSEASGFCYINDIVLGILEL-LKYHA---RVMYIDIDVHHGDGVEEAFYVTHRVMTV 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 615 SLHRHdkGNFFPGTGSVTEVGKNDAKGLTVNVPFSgDVMRDPEYLAAWRTVIEPVMASFCPDFIIVSAGFDACHGhpNAL 694
Cdd:PTZ00063 194 SFHKF--GDFFPGTGDVTDIGVAQGKYYSVNVPLN-DGIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTG--DRL 268


                 ....*.
gi 392928255 695 GGYEVT 700
Cdd:PTZ00063 269 GRFNLT 274
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
 444-705 3.72e-25

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


Pssm-ID: 212517 [Multi-domain]  Cd Length: 306  Bit Score: 106.90  E-value: 3.72e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 444 LIEH-GHVQKCEKVTAKKASLEQLQLVHSQTYTTF-FAVSPtACLKidANSLPLKRFlqlpcgGIGVD---SDTYFNDAS 518
Cdd:cd09991   28 LILSyGLYKKMEIYRPRPATAEELTKFHSDDYIDFlRSVSP-DNMK--EFKKQLERF------NVGEDcpvFDGLYEYCQ 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 519 TQTAARLAAGTliELSSQVAEgrlkngfACIRPPG--HHAEHEQAMGFCFFNNVAVAVKVLQtKYpaqCAKIAIIDWDVH 596
Cdd:cd09991   99 LYAGGSIAAAV--KLNRGQAD-------IAINWAGglHHAKKSEASGFCYVNDIVLAILELL-KY---HQRVLYIDIDIH 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 597 HGNGTQLSFENDPNVLYMSLHRHdkGNFFPGTGSVTEVGKNDAKGLTVNVPFSgDVMRDPEYLAAWRTVIEPVMASFCPD 676
Cdd:cd09991  166 HGDGVEEAFYTTDRVMTVSFHKF--GEYFFPGTGLRDIGAGKGKYYAVNVPLK-DGIDDESYLQIFEPVLSKVMEVFQPS 242

                        250       260
                 ....*....|....*....|....*....
gi 392928255 677 FIIVSAGFDACHGHPnaLGGYEVTPEMFG 705
Cdd:cd09991  243 AVVLQCGADSLAGDR--LGCFNLSIKGHA 269
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
 436-733 4.61e-22

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: 98.98  E-value: 4.61e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 436 RIQSIWSKLIEHGHVQKCEKVTAKKASLEQLQLVHSQTYTTFF-AVSPTaclKIDANSLPLKRFlqlpcgGIGVDS---D 511
Cdd:cd10010   31 RIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLrSIRPD---NMSEYSKQMQRF------NVGEDCpvfD 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 512 TYFNDASTQTAARLAAGTLIELSSQVAEGRLKNGFacirppgHHAEHEQAMGFCFFNNVAVAVKVLqTKYPAqcaKIAII 591
Cdd:cd10010  102 GLFEFCQLSAGGSVASAVKLNKQQTDIAVNWAGGL-------HHAKKSEASGFCYVNDIVLAILEL-LKYHQ---RVLYI 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 592 DWDVHHGNGTQLSFENDPNVLYMSLHRHdkGNFFPGTGSVTEVGKNDAKGLTVNVPFSgDVMRDPEYLAAWRTVIEPVMA 671
Cdd:cd10010  171 DIDIHHGDGVEEAFYTTDRVMTVSFHKY--GEYFPGTGDLRDIGAGKGKYYAVNYPLR-DGIDDESYEAIFKPVMSKVME 247

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392928255 672 SFCPDFIIVSAGFDACHGhpNALGGYEVTPEMFGYMTKSLLNYASGKVVLAlEGGYDLKSIS 733
Cdd:cd10010  248 MFQPSAVVLQCGADSLSG--DRLGCFNLTIKGHAKCVEFVKSFNLPMLMLG-GGGYTIRNVA 306
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
 436-686 2.97e-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: 96.70  E-value: 2.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 436 RIQSIWSKLIEHGHVQKCEKVTAKKASLEQLQLVHSQTYTTFFA-VSPTaclKIDANSLPLKRFlqlpcgGIGVDS---D 511
Cdd:cd10005   26 RLALTHSLVLHYGLYKKMQVYKPYRASAHDMCRFHSEDYIDFLQrVTPQ---NIQGFTKSLNQF------NVGDDCpvfP 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 512 TYFNDASTQTAARLAAGTlielssqvaegRLKNGFA--CIRPPG--HHAEHEQAMGFCFFNNVAVAVKVLQTKYPaqcaK 587
Cdd:cd10005   97 GLFDFCSMYTGASLEGAT-----------KLNHKICdiAINWSGglHHAKKFEASGFCYVNDIVIAILELLKYHP----R 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 588 IAIIDWDVHHGNGTQLSFENDPNVLYMSLHRHdkGN-FFPGTGSVTEVGKNDAKGLTVNVPFSgDVMRDPEYLAAWRTVI 666
Cdd:cd10005  162 VLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKY--GNyFFPGTGDMYEVGAESGRYYSVNVPLK-DGIDDQSYLQLFKPVI 238

                        250       260
                 ....*....|....*....|
gi 392928255 667 EPVMASFCPDFIIVSAGFDA 686
Cdd:cd10005  239 QQVIDFYQPTCIVLQCGADS 258
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
 436-689 8.51e-19

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


Pssm-ID: 212528 [Multi-domain]  Cd Length: 375  Bit Score: 89.10  E-value: 8.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 436 RIQSIWSKLIEHGHVQKCEKVTAKKASLEQLQLVHSQTYTTFFA-VSPTACLKIDANSLP------------LKRFLQLP 502
Cdd:cd10004   27 RIRMAHSLVMNYGLYKKMEIYRAKPATKNEMTQFHTDEYIDFLSrVTPDNMEKFQKEQVKynvgddcpvfdgLFEFCSIS 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 503 CGGigvdsdtyfndaSTQTAARLAAGTlIELSSQVAEGRlkngfacirppgHHAEHEQAMGFCFFNNVAVAVKVLQTKYP 582
Cdd:cd10004  107 AGG------------SMEGAARLNRGK-CDIAVNWAGGL------------HHAKKSEASGFCYVNDIVLGILELLRYHQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 583 aqcaKIAIIDWDVHHGNGTQLSFENDPNVLYMSLHRHdkGNFFPGTGSVTEVGKNDAKGLTVNVPFSgDVMRDPEYLAAW 662
Cdd:cd10004  162 ----RVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKY--GEYFPGTGELRDIGIGTGKNYAVNVPLR-DGIDDESYKSIF 234

                        250       260
                 ....*....|....*....|....*..
gi 392928255 663 RTVIEPVMASFCPDFIIVSAGFDACHG 689
Cdd:cd10004  235 EPVIKHVMEWYQPEAVVLQCGGDSLSG 261
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
 522-727 2.09e-17

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: 84.81  E-value: 2.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 522 AARLAAGTLIELSSQVAEGRL---KNGFACIRPPGHHAEHEQAMGFCFFNNVAVAVKVLQTKYpaQCAKIAIIDWDVHHG 598
Cdd:cd09998   85 AIQGALGAVCEAVDSVFKPESpgtKRAFVAIRPPGHHCSESTPSGFCWVNNVHVGAAHAYLTH--GITRVVILDIDLHHG 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 599 NGTQ------------------------LSFENDPNVLYMSLhrHDKGNFFPGTGSVTEVgkNDAK-------GLTV-NV 646
Cdd:cd09998  163 NGTQdiawrinaeankqalesssyddfkPAGAPGLRIFYSSL--HDINSFPCEDGDPAKV--KDASvsidgahGQWIwNV 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 647 ---PFSGDVMRDPEYLAAWRTVIEPVMASFCPD--------FIIVSAGFDACHGHPNALGGYE--VTPEMFGYMTKSLLN 713
Cdd:cd09998  239 hlqPWTTEEDFWELYYPKYRILFEKAAEFLRLTtaatpfktLVFISAGFDASEHEYESMQRHGvnVPTSFYYRFARDAVR 318

                        250
                 ....*....|....*...
gi 392928255 714 ----YASGKVVLALEGGY 727
Cdd:cd09998  319 fadaHAHGRLISVLEGGY 336
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
 436-733 4.70e-17

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: 83.96  E-value: 4.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 436 RIQSIWSKLIEHGHVQKCEKVTAKKASLEQLQLVHSQTYTTFF-AVSPTaclKIDANSLPLKRFlqlpcgGIGVDS---D 511
Cdd:cd10011   27 RIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLrSIRPD---NMSEYSKQMQRF------NVGEDCpvfD 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 512 TYFNDASTQTAARLAAGtlielssqVAEGRLKNGFACIRPPG-HHAEHEQAMGFCFFNNVAVAVKVLqTKYPaqcAKIAI 590
Cdd:cd10011   98 GLFEFCQLSTGGSVAGA--------VKLNRQQTDMAVNWAGGlHHAKKSEASGFCYVNDIVLAILEL-LKYH---QRVLY 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 591 IDWDVHHGNGTQLSFENDPNVlyMSLHRHDKGNFFPGTGSVTEVGKNDAKGLTVNVPFSgDVMRDPEYLAAWRTVIEPVM 670
Cdd:cd10011  166 IDIDIHHGDGVEEAFYTTDRV--MTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMR-DGIDDESYGQIFKPIISKVM 242

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392928255 671 ASFCPDFIIVSAGFDACHGhpNALGGYEVTPEMFGYMTKSLLNYASGKVVLAlEGGYDLKSIS 733
Cdd:cd10011  243 EMYQPSAVVLQCGADSLSG--DRLGCFNLTVKGHAKCVEVVKTFNLPLLMLG-GGGYTIRNVA 302
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 531-743 3.12e-13

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: 69.71  E-value: 3.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 531 IELSSQVAEGRLKNGFACIRPPGHHAEheqamgfcfFNNVAVAVKVLQtkypaqcAKIAIIDWDVHHGNGTQLSF----- 605
Cdd:cd09987   11 HELLAGVVVAVLKDGKVPVVLGGDHSI---------ANGAIRAVAELH-------PDLGVIDVDAHHDVRTPEAFgkgnh 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 606 ---------ENDPNVLYMSLHRHDKGNFFPgtgsvtevGKNDAKGLTVNVpFSGDVMRDPEYLAAWRTVIEPVMasFCPD 676
Cdd:cd09987   75 htprhllcePLISDVHIVSIGIRGVSNGEA--------GGAYARKLGVVY-FSMTEVDKLGLGDVFEEIVSYLG--DKGD 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392928255 677 FIIVSAGFDACHGHP----NALGGYEVTPEMFGYMTKSLLNYAsGKVVLALEGGYDLKS----ISEAAQQCVQAL 743
Cdd:cd09987  144 NVYLSVDVDGLDPSFapgtGTPGPGGLSYREGLYITERIAKTN-LVVGLDIVEVNPLLDetgrTARLAAALTLEL 217
PTZ00346 PTZ00346
histone deacetylase; Provisional
 453-734 9.35e-11

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 64.67  E-value: 9.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 453 CEKVTAKKASLEQLQLVHSQTYTTFFAVSptACLKIDANSLPLKRFLQLPCGGIgvdsdTYFNDASTQTAARLAAGTLIE 532
Cdd:PTZ00346  66 CRTVVPPLVKVEELMAYHTDTYLANLGLH--SCRSWLWNAETSKVFFSGDCPPV-----EGLMEHSIATASGTLMGAVLL 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 533 LSSQVAEGRLKNGFAcirppgHHAEHEQAMGFCFFNNVAVAVKVLqtkypAQCA-KIAIIDWDVHHGNGTQLSFENDPNV 611
Cdd:PTZ00346 139 NSGQVDVAVHWGGGM------HHSKCGECSGFCYVNDIVLGILEL-----LKCHdRVLYVDIDMHHGDGVDEAFCTSDRV 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928255 612 LYMSLHRHDKgNFFPGTGSVTEVGKNDAKGLTVNVPFsGDVMRDPEYLAAWRTVIEPVMASFCPDFIIVSAGFDACHGhp 691
Cdd:PTZ00346 208 FTLSLHKFGE-SFFPGTGHPRDVGYGRGRYYSMNLAV-WDGITDFYYLGLFEHALHSIVRRYSPDAIVLQCGADSLAG-- 283

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 392928255 692 NALGGYEVTPEMFGYMTKSLLNYasGKVVLAL-EGGYDLKSISE 734
Cdd:PTZ00346 284 DRLGLLNLSSFGHGQCVQAVRDL--GIPMLALgGGGYTIRNVAK 325
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH