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Conserved domains on  [gi|1720373353|ref|XP_030102852|]
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histone deacetylase 9 isoform X15 [Mus musculus]

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

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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 ...
 314-691 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: 768.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 314 SATGIAYDPLMLKHQCICGSSTTHPEHAGRIQSIWSRLQETGLLSKCERIQGRKASLEEIQLVHSEHHSLLYGTSPLDGQ 393
Cdd:cd11681     1 FTTGLAYDPLMLKHQCICGNNSSHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTLLYGTNPLSRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 394 KLDPRTLLGDdSRKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESAAM 473
Cdd:cd11681    81 KLDPTKLAGL-PQKSFVRLPCGGIGVDSDTVWNELHTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQAM 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 474 GFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGVGLGEGYNV 553
Cdd:cd11681   160 GFCFFNSVAIAAKQLQQKLKLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFPGTGAPTEVGSGAGEGFNV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 554 NIAWTGGLDPPMGDVEYLEAFRTVVMPVAREFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLANGRVAL 633
Cdd:cd11681   240 NIAWSGGLDPPMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPPPLGGYKVSPACFGYMTRQLMNLAGGKVVL 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720373353 634 ALEGGHDLTAICDASEACINALLGNEPGPLEEDALHQSVNTNAAASLQKTIDIQSKYW 691
Cdd:cd11681   320 ALEGGYDLTAICDASEACVRALLGDELDPLSEEELERRPNPNAVTSLEKVIAIQSPYW 377
 
Name Accession Description Interval E-value
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 314-691 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: 768.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 314 SATGIAYDPLMLKHQCICGSSTTHPEHAGRIQSIWSRLQETGLLSKCERIQGRKASLEEIQLVHSEHHSLLYGTSPLDGQ 393
Cdd:cd11681     1 FTTGLAYDPLMLKHQCICGNNSSHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTLLYGTNPLSRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 394 KLDPRTLLGDdSRKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESAAM 473
Cdd:cd11681    81 KLDPTKLAGL-PQKSFVRLPCGGIGVDSDTVWNELHTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQAM 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 474 GFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGVGLGEGYNV 553
Cdd:cd11681   160 GFCFFNSVAIAAKQLQQKLKLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFPGTGAPTEVGSGAGEGFNV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 554 NIAWTGGLDPPMGDVEYLEAFRTVVMPVAREFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLANGRVAL 633
Cdd:cd11681   240 NIAWSGGLDPPMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPPPLGGYKVSPACFGYMTRQLMNLAGGKVVL 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720373353 634 ALEGGHDLTAICDASEACINALLGNEPGPLEEDALHQSVNTNAAASLQKTIDIQSKYW 691
Cdd:cd11681   320 ALEGGYDLTAICDASEACVRALLGDELDPLSEEELERRPNPNAVTSLEKVIAIQSPYW 377
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 337-655 1.49e-125

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: 376.19  E-value: 1.49e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 337 HPEHAGRIQSIWSRLQETGLLSKCERIQGRKASLEEIQLVHSEHHSLLYGTSPLDGQKLDPRTLLGDDsrkffsslpcgg 416
Cdd:pfam00850   1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAAPEGGALLLLSYLSGD------------ 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 417 lgvdsDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESAAMGFCFFNSVAITAKYLRDQLNISK 496
Cdd:pfam00850  69 -----DDTPVSPGSYEAALLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLKR 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 497 ILIVDLDVHHGNGTQQAFYADPSILYISLHRYDeGNFFPGSGAPNEVGVGLGEGYNVNIAWTGGldppMGDVEYLEAFRT 576
Cdd:pfam00850 144 VAIVDFDVHHGNGTQEIFYDDPSVLTLSIHQYP-GGFYPGTGFADETGEGKGKGYTLNVPLPPG----TGDAEYLAAFEE 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 577 VVMPVAREFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLA---NGRVALALEGGHDLTAICDASEACIN 653
Cdd:pfam00850 219 ILLPALEEFQPDLILVSAGFDAHAGD--PLGGLNLTTEGFAEITRILLELAdplCIRVVSVLEGGYNLDALARSATAVLA 296


                  ..
gi 1720373353 654 AL 655
Cdd:pfam00850 297 AL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 316-657 1.92e-109

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 335.15  E-value: 1.92e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 316 TGIAYDPLMLKHQCicgsSTTHPEHAGRIQSIWSRLQETGLLSKCERIQGRKASLEEIQLVHSEHHsllygtspldgqkL 395
Cdd:COG0123     1 TALIYHPDYLLHDL----GPGHPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDY-------------V 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 396 DprtllgddsrKFFSSLPCGGLG-VDSDTIWNElHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESAAMG 474
Cdd:COG0123    64 D----------ALRAASLDGGYGqLDPDTPVSP-GTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMG 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 475 FCFFNSVAITAKYLRDQlNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdegNFFPGSGAPNEVGVGLGEGYNVN 554
Cdd:COG0123   133 FCLFNNAAIAARYLLAK-GLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD---PLYPGTGAADETGEGAGEGSNLN 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 555 IAwtggLDPPMGDVEYLEAFRTVVMPVAREFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLA---NGRV 631
Cdd:COG0123   209 VP----LPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHADD--PLGRLNLTTEGYAWRTRRVLELAdhcGGPV 282

                         330       340
                  ....*....|....*....|....*.
gi 1720373353 632 ALALEGGHDLTAICDASEACINALLG 657
Cdd:COG0123   283 VSVLEGGYNLDALARSVAAHLETLLG 308
PTZ00063 PTZ00063
histone deacetylase; Provisional
 465-618 1.01e-22

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 101.81  E-value: 1.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 465 HHAEESAAMGFCFFNSVAITA----KYLrdqlniSKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdeGNFFPGSGAP 540
Cdd:PTZ00063  137 HHAKRSEASGFCYINDIVLGIlellKYH------ARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFPGTGDV 208

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720373353 541 NEVGVGLGEGYNVNIAWTGGLDppmgDVEYLEAFRTVVMPVAREFDPDMVLVSAGFDALEGHTppLGGYKVTAKcfGH 618
Cdd:PTZ00063  209 TDIGVAQGKYYSVNVPLNDGID----DDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDR--LGRFNLTIK--GH 278
 
Name Accession Description Interval E-value
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 314-691 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: 768.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 314 SATGIAYDPLMLKHQCICGSSTTHPEHAGRIQSIWSRLQETGLLSKCERIQGRKASLEEIQLVHSEHHSLLYGTSPLDGQ 393
Cdd:cd11681     1 FTTGLAYDPLMLKHQCICGNNSSHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTLLYGTNPLSRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 394 KLDPRTLLGDdSRKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESAAM 473
Cdd:cd11681    81 KLDPTKLAGL-PQKSFVRLPCGGIGVDSDTVWNELHTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQAM 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 474 GFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGVGLGEGYNV 553
Cdd:cd11681   160 GFCFFNSVAIAAKQLQQKLKLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFPGTGAPTEVGSGAGEGFNV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 554 NIAWTGGLDPPMGDVEYLEAFRTVVMPVAREFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLANGRVAL 633
Cdd:cd11681   240 NIAWSGGLDPPMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPPPLGGYKVSPACFGYMTRQLMNLAGGKVVL 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720373353 634 ALEGGHDLTAICDASEACINALLGNEPGPLEEDALHQSVNTNAAASLQKTIDIQSKYW 691
Cdd:cd11681   320 ALEGGYDLTAICDASEACVRALLGDELDPLSEEELERRPNPNAVTSLEKVIAIQSPYW 377
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
 314-692 0e+00

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


Pssm-ID: 212533 [Multi-domain]  Cd Length: 379  Bit Score: 749.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 314 SATGIAYDPLMLKHQCICGSSTTHPEHAGRIQSIWSRLQETGLLSKCERIQGRKASLEEIQLVHSEHHSLLYGTSPLDGQ 393
Cdd:cd10009     1 SATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 394 KLDPRTLLGDDSRKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESAAM 473
Cdd:cd10009    81 KLDPRILLGDDSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 474 GFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGVGLGEGYNV 553
Cdd:cd10009   161 GFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYNI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 554 NIAWTGGLDPPMGDVEYLEAFRTVVMPVAREFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLANGRVAL 633
Cdd:cd10009   241 NIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVL 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720373353 634 ALEGGHDLTAICDASEACINALLGNEPGPLEEDALHQSVNTNAAASLQKTIDIQSKYWK 692
Cdd:cd10009   321 ALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSKYWK 379
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
 314-729 0e+00

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


Pssm-ID: 212531 [Multi-domain]  Cd Length: 420  Bit Score: 737.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 314 SATGIAYDPLMLKHQCICGSSTTHPEHAGRIQSIWSRLQETGLLSKCERIQGRKASLEEIQLVHSEHHSLLYGTSPLDGQ 393
Cdd:cd10007     3 FTTGLVYDTFMLKHQCTCGNTNVHPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHSEHHTLLYGTSPLNRQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 394 KLDPRTLLGDDSRKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESAAM 473
Cdd:cd10007    83 KLDSKKLLGPLSQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLIELAFKVAAGELKNGFAVIRPPGHHAEESTAM 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 474 GFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGVGLGEGYNV 553
Cdd:cd10007   163 GFCFFNSVAIAAKLLQQKLNVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGNFFPGSGAPDEVGAGPGVGFNV 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 554 NIAWTGGLDPPMGDVEYLEAFRTVVMPVAREFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLANGRVAL 633
Cdd:cd10007   243 NIAWTGGVDPPIGDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGHQSPLGGYSVTAKCFGHLTKQLMTLAGGRVVL 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 634 ALEGGHDLTAICDASEACINALLGNEPGPLEEDALHQSVNTNAAASLQKTIDIQSKYWKSIKMVAAARGGALPASQLQE- 712
Cdd:cd10007   323 ALEGGHDLTAICDASEACVSALLGMELTPLDNTVLQQKPNDNAVATLERVIEIQSKHWSCLKRFAATLGFSLLEAQRGEl 402

                         410
                  ....*....|....*...
gi 1720373353 713 -ETETVSALASLTVDVEQ 729
Cdd:cd10007   403 eEAETVSAMASLSVDTEQ 420
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
 311-718 0e+00

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


Pssm-ID: 212530 [Multi-domain]  Cd Length: 409  Bit Score: 697.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 311 QPSSATGIAYDPLMLKHQCICGSSTTHPEHAGRIQSIWSRLQETGLLSKCERIQGRKASLEEIQLVHSEHHSLLYGTSPL 390
Cdd:cd10006     1 KPRFTTGLVYDTLMLKHQCTCGNSNSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 391 DGQKLDPRTLLGDDSrKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEES 470
Cdd:cd10006    81 NRQKLDSKKLLGSLA-SVFVRLPCGGVGVDSDTIWNEVHSSGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEES 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 471 AAMGFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGVGLGEG 550
Cdd:cd10006   160 TPMGFCYFNSVAIAAKLLQQRLNVSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 551 YNVNIAWTGGLDPPMGDVEYLEAFRTVVMPVAREFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLANGR 630
Cdd:cd10006   240 FNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSAKCFGYLTKQLMGLAGGR 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 631 VALALEGGHDLTAICDASEACINALLGNEPGPLEEDALHQSVNTNAAASLQKTIDIQSKYWKSIKMVAAARGGALPASQL 710
Cdd:cd10006   320 IVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGYSLIEAQT 399

                         410
                  ....*....|
gi 1720373353 711 --QEETETVS 718
Cdd:cd10006   400 ceNEEAETVT 409
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
 316-691 0e+00

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


Pssm-ID: 212532 [Multi-domain]  Cd Length: 378  Bit Score: 657.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 316 TGIAYDPLMLKHQCICGSSTTHPEHAGRIQSIWSRLQETGLLSKCERIQGRKASLEEIQLVHSEHHSLLYGTSPLDGQKL 395
Cdd:cd10008     3 TGLVYDSVMLKHQCSCGDNSNHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLKL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 396 DPRTLLGDDSRKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESAAMGF 475
Cdd:cd10008    83 DNGKLAGLLAQRMFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGF 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 476 CFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGVGLGEGYNVNI 555
Cdd:cd10008   163 CFFNSVAIACRQLQQQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGAGSGEGFNVNV 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 556 AWTGGLDPPMGDVEYLEAFRTVVMPVAREFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLANGRVALAL 635
Cdd:cd10008   243 AWAGGLDPPMGDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVLAL 322

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720373353 636 EGGHDLTAICDASEACINALLGNEPGPLEEDALHQSVNTNAAASLQKTIDIQSKYW 691
Cdd:cd10008   323 EGGHDLTAICDASEACVAALLGNEVDPLSEESWKQKPNLNAIRSLEAVIRVHSKYW 378
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
 320-695 9.89e-142

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: 419.82  E-value: 9.89e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 320 YDPLMLKHQCICGSSttHPEHAGRIQSIWSRLQETGLLSKCERIQGRKASLEEIQLVHSEHH-SLLYGTSpldgqKLDPR 398
Cdd:cd10003     1 YDQRMMNHHNLWDPG--HPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHlDEMKSLE-----KMKPR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 399 TLlgddsrkffsslpcGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESAAMGFCFF 478
Cdd:cd10003    74 EL--------------NRLGKEYDSIYIHPDSYQCALLAAGCVLQVVEAVLTGESRNGVAIVRPPGHHAEQDTACGFCFF 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 479 NSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGS--GAPNEVGVGLGEGYNVNIA 556
Cdd:cd10003   140 NNVAIAARYAQKKYGLKRILIVDWDVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSpeGNYDVVGKGKGEGFNVNIP 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 557 WTGGldpPMGDVEYLEAFRTVVMPVAREFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLANGRVALALE 636
Cdd:cd10003   220 WNKG---GMGDAEYIAAFQQVVLPIAYEFNPELVLVSAGFDAARGD--PLGGCKVTPEGYAHMTHMLMSLAGGRVIVILE 294

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720373353 637 GGHDLTAICDASEACINALLGNEPGPLEedaLHQSVNTNAAASLQKTIDIQSKYWKSIK 695
Cdd:cd10003   295 GGYNLTSISESMSMCTKTLLGDPPPVLD---LPRPPCSSALKSINNVLQVHQKYWKSLR 350
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
 337-656 4.65e-141

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: 415.74  E-value: 4.65e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 337 HPEHAGRIQSIWSRLQETGLLSKCERIQGRKASLEEIQLVHSEHH-SLLYGTSPLDGQKLDPrtllgddsrkffsslpcg 415
Cdd:cd09992     1 HPERPERLLAILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYiERVEETCEAGGGYLDP------------------ 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 416 glgvdsDTIWNElHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESAAMGFCFFNSVAITAKYLRDQLNIS 495
Cdd:cd09992    63 ------DTYVSP-GSYEAALLAAGAALAAVDAVLSGEAENAFALVRPPGHHAEPDRAMGFCLFNNVAIAARYAQKRYGLK 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 496 KILIVDLDVHHGNGTQQAFYADPSILYISLHRYDegnFFPGSGAPNEVGVGLGEGYNVNIAWTGGldppMGDVEYLEAFR 575
Cdd:cd09992   136 RVLIVDWDVHHGNGTQDIFYDDPSVLYFSIHQYP---FYPGTGAAEETGGGAGEGFTINVPLPPG----SGDAEYLAAFE 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 576 TVVMPVAREFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLA----NGRVALALEGGHDLTAICDASEAC 651
Cdd:cd09992   209 EVLLPIAREFQPDLVLVSAGFDAHRGD--PLGGMNLTPEGYARLTRLLKELAdehcGGRLVFVLEGGYNLEALAESVLAV 286


                  ....*
gi 1720373353 652 INALL 656
Cdd:cd09992   287 LEALL 291
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 337-663 4.01e-128

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: 383.62  E-value: 4.01e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 337 HPEHAGRIQSIWSRLQETGLLSKCERIQGRKASLEEIQLVHSEHH-SLLYGTSPLDGQKLDprtllgdDSRKFFSSLpcg 415
Cdd:cd11600     3 HPEDPSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEHwDRVEATEKMSDEQLK-------DRTEIFERD--- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 416 GLGVDSdtiwnelHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESAAMGFCFFNSVAITAKYLRDQL--N 493
Cdd:cd11600    73 SLYVNN-------DTAFCARLSCGGAIEACRAVAEGRVKNAFAVVRPPGHHAEPDESMGFCFFNNVAVAAKWLQTEYpdK 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 494 ISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGS--GAPNEVGVGLGEGYNVNIAWTgglDPPMGDVEYL 571
Cdd:cd11600   146 IKKILILDWDIHHGNGTQRAFYDDPNVLYISLHRFENGGFYPGTpyGDYESVGEGAGLGFNVNIPWP---QGGMGDADYI 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 572 EAFRTVVMPVAREFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLANGRVALALEGGHDLTAICDASEAC 651
Cdd:cd11600   223 YAFQRIVMPIAYEFDPDLVIISAGFDAADGD--ELGQCHVTPAGYAHMTHMLMSLAGGKLVVALEGGYNLDAISDSALAV 300

                         330
                  ....*....|..
gi 1720373353 652 INALLGNEPGPL 663
Cdd:cd11600   301 AKVLLGEAPPKL 312
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 337-655 1.49e-125

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: 376.19  E-value: 1.49e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 337 HPEHAGRIQSIWSRLQETGLLSKCERIQGRKASLEEIQLVHSEHHSLLYGTSPLDGQKLDPRTLLGDDsrkffsslpcgg 416
Cdd:pfam00850   1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAAPEGGALLLLSYLSGD------------ 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 417 lgvdsDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESAAMGFCFFNSVAITAKYLRDQLNISK 496
Cdd:pfam00850  69 -----DDTPVSPGSYEAALLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLKR 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 497 ILIVDLDVHHGNGTQQAFYADPSILYISLHRYDeGNFFPGSGAPNEVGVGLGEGYNVNIAWTGGldppMGDVEYLEAFRT 576
Cdd:pfam00850 144 VAIVDFDVHHGNGTQEIFYDDPSVLTLSIHQYP-GGFYPGTGFADETGEGKGKGYTLNVPLPPG----TGDAEYLAAFEE 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 577 VVMPVAREFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLA---NGRVALALEGGHDLTAICDASEACIN 653
Cdd:pfam00850 219 ILLPALEEFQPDLILVSAGFDAHAGD--PLGGLNLTTEGFAEITRILLELAdplCIRVVSVLEGGYNLDALARSATAVLA 296


                  ..
gi 1720373353 654 AL 655
Cdd:pfam00850 297 AL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 316-657 1.92e-109

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 335.15  E-value: 1.92e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 316 TGIAYDPLMLKHQCicgsSTTHPEHAGRIQSIWSRLQETGLLSKCERIQGRKASLEEIQLVHSEHHsllygtspldgqkL 395
Cdd:COG0123     1 TALIYHPDYLLHDL----GPGHPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDY-------------V 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 396 DprtllgddsrKFFSSLPCGGLG-VDSDTIWNElHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESAAMG 474
Cdd:COG0123    64 D----------ALRAASLDGGYGqLDPDTPVSP-GTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMG 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 475 FCFFNSVAITAKYLRDQlNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdegNFFPGSGAPNEVGVGLGEGYNVN 554
Cdd:COG0123   133 FCLFNNAAIAARYLLAK-GLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD---PLYPGTGAADETGEGAGEGSNLN 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 555 IAwtggLDPPMGDVEYLEAFRTVVMPVAREFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLA---NGRV 631
Cdd:COG0123   209 VP----LPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHADD--PLGRLNLTTEGYAWRTRRVLELAdhcGGPV 282

                         330       340
                  ....*....|....*....|....*.
gi 1720373353 632 ALALEGGHDLTAICDASEACINALLG 657
Cdd:COG0123   283 VSVLEGGYNLDALARSVAAHLETLLG 308
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 336-691 1.12e-106

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: 328.89  E-value: 1.12e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 336 THPEHAGRIQSIWSRLQETGLLSKCERIQGRKASLEEIQLVHS-EHHSLLYGTspldgqkldprTLLGDDSRKFFSSlpc 414
Cdd:cd10002     6 NHIECPERLEAILERLTQDGLLERCVKIPAREAEEDEILLVHSqEYIDLVKST-----------ETMEKEELESLCS--- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 415 gglgvDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESAAMGFCFFNSVAITAKYLRDQLNI 494
Cdd:cd10002    72 -----GYDSVYLCPSTYEAARLAAGSTIELVKAVMAGKIQNGFALIRPPGHHAMRNEANGYCIFNNVAIAAKYAIEKLGL 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 495 SKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPN--EVGVGLGEGYNVNIAW--TGgldppMGDVEY 570
Cdd:cd10002   147 KRILIVDWDVHHGQGTQQGFYEDPRVLYFSIHRYEHGRFWPHLFESDydYIGVGHGYGFNVNVPLnqTG-----LGDADY 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 571 LEAFRTVVMPVAREFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLANGRVALALEGGHDLTAICDASEA 650
Cdd:cd10002   222 LAIFHHILLPLALEFQPELVLVSAGFDASIGD--PEGEMAVTPAGYAHLTRLLMGLAGGKLLLVLEGGYLLESLAESVSM 299

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1720373353 651 CINALLGNEPGPLEEDALHQSVntnaAASLQKTIDIQSKYW 691
Cdd:cd10002   300 TLRGLLGDPLPPLAPPIPIRSV----LETILNAIAHLSPRW 336
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
 343-655 6.26e-101

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: 312.06  E-value: 6.26e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 343 RIQSIWSRLQETGLLSKCERIQGRKASLEEIQLVHSEHHSLLYGTSPLDGQKLDprtllgddsrkffsslpcGGLGVDSD 422
Cdd:cd09301     1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKANFAVATITE------------------SKPVIFGP 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 423 TIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESAAMGFCFFNSVAITAKYLRdQLNISKILIVDL 502
Cdd:cd09301    63 NFPVQRHYFRGARLSTGGVVEAAELVAKGELERAFAVVGAGGHHAGKSRAWGFCYFNDVVLAIKFLR-ERGISRILIIDT 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 503 DVHHGNGTQQAFYADPSILYISLHRYDEGNFfpgsgapnevGVGLGEGYNVNIAWTGGldppMGDVEYLEAFRTVVMPVA 582
Cdd:cd09301   142 DAHHGDGTREAFYDDDRVLHMSFHNYDIYPF----------GRGKGKGYKINVPLEDG----LGDEEYLDAVERVISKVL 207

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720373353 583 REFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLAN-GRVALALEGGHDLTAICDASEACINAL 655
Cdd:cd09301   208 EEFEPEVVVLQFGHDTHEGD--RLGGFNLSEKGFVKLAEIVKEFARgGPILMVLGGGYNPEAAARIWTAIIKEL 279
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
 337-656 4.26e-87

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: 276.32  E-value: 4.26e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 337 HPEHAGRIQSIWSRLQETGLLSKCERIQGRKASLEEIQLVHSEHH-SLLYGTSPLDG-QKLDPRTLLGDDSrkffsslpc 414
Cdd:cd11599     1 HPESPERLEAILDALIASGLDRLLRQLEAPPATREQLLRVHDAAYvDRLEAAAPEEGlVQLDPDTAMSPGS--------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 415 gglgvdsdtiWNelhssgAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESAAMGFCFFNSVAITAKYLRDQLNI 494
Cdd:cd11599    72 ----------LE------AALRAAGAVVAAVDAVMAGEARNAFCAVRPPGHHAERDKAMGFCLFNNVAIAAAHALAHHGL 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 495 SKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdegNFFPGSGAPNEVGVGlgegyN-VNIAwtggLDPPMGDVEYLEA 573
Cdd:cd11599   136 ERVAIVDFDVHHGNGTEDIFRDDPRVLFCSSHQH---PLYPGTGAPDETGHG-----NiVNVP----LPAGTGGAEFREA 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 574 FRTVVMPVAREFDPDMVLVSAGFDAlegHT-PPLGGYKVTAKCFGHLTKQLMTLAN----GRVALALEGGHDLTAICDAS 648
Cdd:cd11599   204 VEDRWLPALDAFKPDLILISAGFDA---HRdDPLAQLNLTEEDYAWITEQLMDVADrycdGRIVSVLEGGYDLSALARSV 280


                  ....*...
gi 1720373353 649 EACINALL 656
Cdd:cd11599   281 AAHVRALM 288
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
 331-691 2.44e-85

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: 273.27  E-value: 2.44e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 331 CGSSTTHPEHAGRIQSIWSRLQETGLLSKCERIQGRKASLEEIQLVHS-EHHSLLYGTSPLDGQKLdpRTLlgddSRKFf 409
Cdd:cd11682     1 CLWDESFPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSpEYVALMKSTQYMTEEEL--RTL----ADTY- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 410 sslpcgglgvdsDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESAAMGFCFFNSVAITAKYLR 489
Cdd:cd11682    74 ------------DSVYLHPNSYSCACLAVGSVLQLVDKVLGGEIRNGLAIVRPPGHHAQHDKMDGYCMFNNVAIAARYAQ 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 490 DQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFP--GSGAPNEVGVGLGEGYNVNIAWTgglDPPMGD 567
Cdd:cd11682   142 QKHGVQRVLIVDWDVHHGQGTQFIFEQDPSVLYFSIHRYEQGRFWPhlKESDSSAVGFGRGEGYNINVPWN---QVGMRD 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 568 VEYLEAFRTVVMPVAREFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLANGRVALALEGGHDLTAICDA 647
Cdd:cd11682   219 ADYIAAFLHVLLPVALEFQPQLVLVAAGFDAVIGD--PKGEMAATPACFAHLTHLLMGLAGGKLILSLEGGYNLRSLAEG 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1720373353 648 SEACINALLGnEPGPLEEDALHQSvnTNAAASLQKTIDIQSKYW 691
Cdd:cd11682   297 VCASLKALLG-DPCPMLESPGAPC--RSALASVSCTISALEPFW 337
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
 316-657 2.16e-82

Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial as well as eukaryotic Class II histone deacetylase (HDAC) and related proteins. Deacetylases of class II are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues of histones (EC 3.5.1.98) and possibly other proteins to yield deacetylated histones/other proteins. Included in this family is a bacterial HDAC-like amidohydrolase (Bordetella/Alcaligenes species FB18817, denoted as FB188 HDAH) shown to be most similar in sequence and function to class II HDAC6 domain 3 or b (HDAC6b). FB188 HDAH is able to remove the acetyl moiety from acetylated histones, and can be inhibited by common HDAC inhibitors such as SAHA (suberoylanilide hydroxamic acid) as well as class II-specific but not class I specific inhibitors.


Pssm-ID: 212521 [Multi-domain]  Cd Length: 359  Bit Score: 266.35  E-value: 2.16e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 316 TGIAYDPLMLKHQCICGSSTT-----------HPEHAGRIQSIWSRLQETGLLSKCERIQGRKASLEEIQLVHSEHHsll 384
Cdd:cd09996     1 TGFVWDERYLWHDTGTGALFLpvggllvqpgrHPENPETKRRIKNLLEVSGLSDHLVLITPRPATDEELLRVHTPEY--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 385 ygtspLDGQKLdprtllgddsrkfFSSLPCGGLGvdSDTIWNElHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPG 464
Cdd:cd09996    78 -----IDRVKA-------------ASAAGGGEAG--GGTPFGP-GSYEIALLAAGGAIAAVDAVLDGEVDNAYALVRPPG 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 465 HHAEESAAMGFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRydEGNFFPGSGAPNEVG 544
Cdd:cd09996   137 HHAEPDQGMGFCLFNNVAIAARHALAVGGVKRVAVVDWDVHHGNGTQAIFYDDPDVLTISLHQ--DRCFPPDSGAVEERG 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 545 VGLGEGYNVNIAwtggLDPPMGDVEYLEAFRTVVMPVAREFDPDMVLVSAGFDAleGHTPPLGGYKVTAKCFGHLTKQLM 624
Cdd:cd09996   215 EGAGEGYNLNIP----LPPGSGDGAYLHAFERIVLPALRAFRPELIIVASGFDA--SAFDPLGRMMLTSDGFRALTRKLR 288

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1720373353 625 TLAN----GRVALALEGGHDLT--AICDAseACINALLG 657
Cdd:cd09996   289 DLADelcgGRLVMVHEGGYSEAyvPFCGL--AVLEELSG 325
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 343-691 1.49e-74

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


Pssm-ID: 212546 [Multi-domain]  Cd Length: 337  Bit Score: 244.77  E-value: 1.49e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 343 RIQSIWSRLQETGLLSKCERIQGRKASLEEIQLVHSEHHSLLYGTSPLDGQKLdprtlLGDDSRKFfsslpcgglgvdsD 422
Cdd:cd11683    13 RLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRETQVMNKEE-----LMAISGKY-------------D 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 423 TIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESAAMGFCFFNSVAITAKYLRDQLNISKILIVDL 502
Cdd:cd11683    75 AVYFHPNTFHCARLAAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYAKKKYGLHRILIVDW 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 503 DVHHGNGTQQAFYADPSILYISLHRYDEGNFFPG--SGAPNEVGVGLGEGYNVNIAWTgglDPPMGDVEYLEAFRTVVMP 580
Cdd:cd11683   155 DVHHGQGIQYIFEEDPSVLYFSWHRYEHQRFWPFlrESDYDAVGRGKGLGFNINLPWN---KVGMGNADYLAAFFHVLLP 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 581 VAREFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLANGRVALALEGGHDLTAICDASEACINALLGNEP 660
Cdd:cd11683   232 LAFEFDPELVLVSAGFDSAIGD--PEGQMCATPECFAHLTHLLMVLAGGKLCAVLEGGYHLESLAESVCMTVQTLLGDPL 309

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1720373353 661 GPLE-EDALHQSvntnAAASLQKTIDIQSKYW 691
Cdd:cd11683   310 PRLSgEMTPCQS----ALESIQNVRAAQAPYW 337
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
 318-656 1.70e-72

Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine amidohydrolase (APAH) as well as other Class II histone deacetylase (HDAC) and related proteins. Deacetylases of class II are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues of histones (EC 3.5.1.98) and possibly other proteins to yield deacetylated histones/other proteins. Mycoplana ramosa APAH exhibits broad substrate specificity and catalyzes the deacetylation of polyamines such as putrescine, spermidine, and spermine by cleavage of a non-peptide amide bond.


Pssm-ID: 212525 [Multi-domain]  Cd Length: 298  Bit Score: 238.21  E-value: 1.70e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 318 IAYDPLMLKHQ----CICGSSTTHPEHAGRIQSIWSRLQETGLLskcERIQGRKASLEEIQLVHSEHH-SLLygtspldg 392
Cdd:cd10001     2 IVYSEDHLLHHpkteLSRGKLVPHPENPERAEAILDALKRAGLG---EVLPPRDFGLEPILAVHDPDYvDFL-------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 393 QKLDPRTLLGDDSrkffsslpcgglgvdsdtiWNelhssgAARMAVGCVIELASKVASGElKNGFAVVRPPGHHAEESAA 472
Cdd:cd10001    71 ETADTDTPISEGT-------------------WE------AALAAADTALTAADLVLEGE-RAAYALCRPPGHHAGRDRA 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 473 MGFCFFNSVAITAKYLRDQLniSKILIVDLDVHHGNGTQQAFYADPSILYISLHRyDEGNFFPG-SGAPNEVGVGLGEGY 551
Cdd:cd10001   125 GGFCYFNNAAIAAQYLRDRA--GRVAILDVDVHHGNGTQEIFYERPDVLYVSIHG-DPRTFYPFfLGFADETGEGEGEGY 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 552 NVNIAwtggLDPPMGDVEYLEAFRTVVMPVaREFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLaNGRV 631
Cdd:cd10001   202 NLNLP----LPPGTGDDDYLAALDEALAAI-AAFGPDALVVSLGFDTHEGD--PLSDFKLTTEDYARIGRRIAAL-GLPT 273

                         330       340
                  ....*....|....*....|....*
gi 1720373353 632 ALALEGGHDLTAICDASEACINALL 656
Cdd:cd10001   274 VFVQEGGYNVDALGRNAVAFLAGFE 298
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
 337-638 3.83e-55

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: 192.00  E-value: 3.83e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 337 HPEHAGRIQSIWSRLQETGLLSKCERIQGRKASLEEIQLVHSEHHsllygtspLDGQKLDPRTLLGDDSRKFfsslpcgG 416
Cdd:cd09994    17 HPFNPPRLSLTKDLLRALGLLPPVDLVPPRPATEEELLLFHTPDY--------IEAVKEASRGQEPEGRGRL-------G 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 417 LGVDSDTIWNELHSsgAARMAVGCVIELASKVASGElknGFAVVRPPG--HHAEESAAMGFCFFNSVAITAKYLRDQlNI 494
Cdd:cd09994    82 LGTEDNPVFPGMHE--AAALVVGGTLLAARLVLEGE---ARRAFNPAGglHHAMRGRASGFCVYNDAAVAIERLRDK-GG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 495 SKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGnFFPGSGAPNEVGVGLGEGYNVNIAwtggLDPPMGDVEYLEAF 574
Cdd:cd09994   156 LRVAYVDIDAHHGDGVQAAFYDDPRVLTISLHESGRY-LFPGTGFVDEIGEGEGYGYAVNIP----LPPGTGDDEFLRAF 230

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720373353 575 RTVVMPVAREFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLA----NGRVaLALEGG 638
Cdd:cd09994   231 EAVVPPLLRAFRPDVIVSQHGADAHAGD--PLTHLNLSNRAYRAAVRRIRELAdeycGGRW-LALGGG 295
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 330-645 8.32e-37

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: 142.09  E-value: 8.32e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 330 ICGSSTTHPEHAGRIQSIwsrLQETGLLSKCERIQGRKASLEEIQLVHSEH--HSLLYGTSPLDGQKLDprtllgDDSRK 407
Cdd:cd10000    12 LCDRLPKVPNRASMVHSL---IEAYGLLKQLRVVKPRVATEEELASFHSDEyiQFLKKASNEGDNDEEP------SEQQE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 408 FfsslpcgGLGVDSDTIWNELHssgAARMAVGCVIELASKVASGELKngFAVVRPPG-HHAEESAAMGFCFFNSVAITAK 486
Cdd:cd10000    83 F-------GLGYDCPIFEGIYD---YAAAVAGATLTAAQLLIDGKCK--VAINWFGGwHHAQRDEASGFCYVNDIVLGIL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 487 YLRDQLniSKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGnFFPGSGAPNEVGVGLGEGYNVNIAWTGGLDppmg 566
Cdd:cd10000   151 KLREKF--DRVLYVDLDLHHGDGVEDAFSFTSKVMTVSLHKYSPG-FFPGTGDVSDVGLGKGKYYTVNVPLRDGIQ---- 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 567 DVEYLEAFRTVVMPVAREFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLmtLANGRVALALEGG---HDLTA 643
Cdd:cd10000   224 DEQYLQIFTAVVPEIVAAFRPEAVVLQCGADTLAGD--PMGAFNLTPVGIGKCLKYV--LGWKLPTLILGGGgynLANTA 299


                  ..
gi 1720373353 644 IC 645
Cdd:cd10000   300 RC 301
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 347-613 1.26e-36

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: 138.78  E-value: 1.26e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 347 IWSRLQETGLLSKCERIQGRKASLEEIQLVHSEH--HSLLYGTspldgqkLDPRtllgdDSRKFFssLPcgglgvdsdtI 424
Cdd:cd09993    11 LREALLEEGLVLPEDIVEPEPATREDLLRVHDPEylESLKSGE-------LSRE-----EIRRIG--FP----------W 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 425 WNELHSSgaARMAVGCVIeLASKVAsgeLKNGFAVvRPPG--HHAEESAAMGFCFFNSVAITAKYLRDQLNISKILIVDL 502
Cdd:cd09993    67 SPELVER--TRLAVGGTI-LAARLA---LEHGLAI-NLAGgtHHAFPDRGEGFCVFNDIAIAARVLLAEGLVRRVLIVDL 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 503 DVHHGNGTQQAFYADPSILYISLHryDEGNfFPGSGAPNEVGVGLGEGynvniawtggldppMGDVEYLEAFRTVVMPVA 582
Cdd:cd09993   140 DVHQGNGTAAIFADDPSVFTFSMH--GEKN-YPFRKEPSDLDVPLPDG--------------TGDDEYLAALEEALPRLL 202

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1720373353 583 REFDPDMVLVSAGFDALEGHtpPLGGYKVTA 613
Cdd:cd09993   203 AEFRPDLVFYNAGVDVLAGD--RLGRLSLSL 231
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
 337-621 2.77e-30

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


Pssm-ID: 212517 [Multi-domain]  Cd Length: 306  Bit Score: 121.54  E-value: 2.77e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 337 HPEHAGRIQSIWSRLQETGLLSKCERIQGRKASLEEIQLVHSEHH-SLLYGTSPldgqklDPRTLLGDDSRKFfsslpcg 415
Cdd:cd09991    15 HPMKPHRIRMTHSLILSYGLYKKMEIYRPRPATAEELTKFHSDDYiDFLRSVSP------DNMKEFKKQLERF------- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 416 GLGVD---SDTIWNelhssgAARMAVGCVIELASKVASGELKngfAVVRPPG--HHAEESAAMGFCFFNSVAITAKYLRD 490
Cdd:cd09991    82 NVGEDcpvFDGLYE------YCQLYAGGSIAAAVKLNRGQAD---IAINWAGglHHAKKSEASGFCYVNDIVLAILELLK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 491 QLniSKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGnfFPGSGAPNEVGVGLGEGYNVNIAwtggLDPPMGDVEY 570
Cdd:cd09991   153 YH--QRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKFGEY--FFPGTGLRDIGAGKGKYYAVNVP----LKDGIDDESY 224

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720373353 571 LEAFRTVVMPVAREFDPDMVLVSAGFDALEGHtpPLGGYKVT----AKCFGHLTK 621
Cdd:cd09991   225 LQIFEPVLSKVMEVFQPSAVVLQCGADSLAGD--RLGCFNLSikghAKCVKFVKS 277
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
 465-645 2.98e-28

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: 115.44  E-value: 2.98e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 465 HHAEESAAMGFCFFNSVAITAKYLRdQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGnFFPGSGAPNEVG 544
Cdd:cd11680   115 HHAQKSRASGFCYVNDIVLAILRLR-RARFRRVFYLDLDLHHGDGVESAFFFSKNVLTCSIHRYDPG-FFPGTGSLKNSS 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 545 VglgeGYNVNIAWTGGLDppmgDVEYLEAFRTVVMPVAREFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLM 624
Cdd:cd11680   193 D----KGMLNIPLKRGLS----DKTLLRIIDSIVRPLIEKFEPEVIVIQCGCDGLSGD--PHKEWNLTIRGYGSVIELLL 262

                         170       180
                  ....*....|....*....|....
gi 1720373353 625 TLANGRVALALEGG---HDLTAIC 645
Cdd:cd11680   263 KEFKDKPTLLLGGGgynHTEAARA 286
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
 335-618 8.41e-27

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


Pssm-ID: 212528 [Multi-domain]  Cd Length: 375  Bit Score: 112.98  E-value: 8.41e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 335 TTHPEHAGRIQSIWSRLQETGLLSKCERIQGRKASLEEIQLVHS-EHHSLLYGTSPLDGQKLDPRTL---LGDDSRKF-- 408
Cdd:cd10004    19 PGHPMKPHRIRMAHSLVMNYGLYKKMEIYRAKPATKNEMTQFHTdEYIDFLSRVTPDNMEKFQKEQVkynVGDDCPVFdg 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 409 ---FSSLPCGGlgvdsdtiwnelHSSGAARMAVG-CviELASKVASGElkngfavvrppgHHAEESAAMGFCFFNSVAIT 484
Cdd:cd10004    99 lfeFCSISAGG------------SMEGAARLNRGkC--DIAVNWAGGL------------HHAKKSEASGFCYVNDIVLG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 485 A-KYLRDQlniSKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdeGNFFPGSGAPNEVGVGLGEGYNVNIAWTGGLDp 563
Cdd:cd10004   153 IlELLRYH---QRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKY--GEYFPGTGELRDIGIGTGKNYAVNVPLRDGID- 226

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720373353 564 pmgDVEYLEAFRTVVMPVAREFDPDMVLVSAGFDALEGHTppLGGYKVTAKcfGH 618
Cdd:cd10004   227 ---DESYKSIFEPVIKHVMEWYQPEAVVLQCGGDSLSGDR--LGCFNLSMK--GH 274
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
 336-621 4.25e-26

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: 109.47  E-value: 4.25e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 336 THPEHAGRIQSIWSRLQETGLLSKCERIQGRKASLEEIQLVHSEHH-SLLYGTSPLDGQKLDPRTL----LGDDSRKF-- 408
Cdd:cd11598    17 THPMKPFRLTLTKHLVMGYGLHKAMDTYEARAATREELRQFHDADYlDFLSKVSPENANQLRFDKAepfnIGDDCPVFdg 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 409 ---FSSLPCGGlgvdsdtiwnelhSSGAARMavgcVIELASKVA---SGELkngfavvrppgHHAEESAAMGFCFFNSVA 482
Cdd:cd11598    97 mydYCQLYAGA-------------SLDAARK----LCSGQSDIAinwSGGL-----------HHAKKSEASGFCYVNDIV 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 483 ITakyLRDQLNI-SKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDeGNFFPGSGAPNEVGVGLGEGYNVNIAWTGGL 561
Cdd:cd11598   149 LA---ILNLLRYfPRVLYIDIDVHHGDGVEEAFYRTDRVMTLSFHKYN-GEFFPGTGDLDDNGGTPGKHFALNVPLEDGI 224

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 562 DppmgDVEYLEAFRTVVMPVAREFDPDMVLVSAGFDALEGHTppLGGYKVTAKCFGHLTK 621
Cdd:cd11598   225 D----DEQYNLLFKSIIGPTIEKFQPSAIVLQCGADSLGGDR--LGQFNLNIKAHGACVK 278
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
 437-655 5.59e-26

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


Pssm-ID: 212522 [Multi-domain]  Cd Length: 353  Bit Score: 110.23  E-value: 5.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 437 AVGCVIELASKVASGEL---KNGFAVVRPPGHHAEESAAMGFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQ-- 511
Cdd:cd09998    89 ALGAVCEAVDSVFKPESpgtKRAFVAIRPPGHHCSESTPSGFCWVNNVHVGAAHAYLTHGITRVVILDIDLHHGNGTQdi 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 512 ----------------------QAFYADPSILYISLHrydEGNFFP-GSGAPNEV---GVGLGEGYNVNIaWTGGLDPPM 565
Cdd:cd09998   169 awrinaeankqalesssyddfkPAGAPGLRIFYSSLH---DINSFPcEDGDPAKVkdaSVSIDGAHGQWI-WNVHLQPWT 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 566 GDVEYLEAFR---TVVMPVAREF-------DPD--MVLVSAGFDALEGHTPPLG--GYKVTAKCFGHLTKQLMTLA---- 627
Cdd:cd09998   245 TEEDFWELYYpkyRILFEKAAEFlrlttaaTPFktLVFISAGFDASEHEYESMQrhGVNVPTSFYYRFARDAVRFAdaha 324

                         250       260
                  ....*....|....*....|....*...
gi 1720373353 628 NGRVALALEGGHDLTAICDASEACINAL 655
Cdd:cd09998   325 HGRLISVLEGGYSDRALCSGVLAHLTGL 352
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 428-655 1.98e-25

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


Pssm-ID: 212513  Cd Length: 217  Bit Score: 104.76  E-value: 1.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 428 LHSSGAARMAVGCVIELASKVasgelKNGFAVVrppGHHAEESAAMgfcffnsVAITAKYlrdqlniSKILIVDLDVHHG 507
Cdd:cd09987     5 IRKAEAHELLAGVVVAVLKDG-----KVPVVLG---GDHSIANGAI-------RAVAELH-------PDLGVIDVDAHHD 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 508 NGTQQAFYA--------------DPSILYISLHRYDEGNFFPGsgapnevGVGLGEGYNVNIAWTGGLDPPMGDVeylea 573
Cdd:cd09987    63 VRTPEAFGKgnhhtprhllceplISDVHIVSIGIRGVSNGEAG-------GAYARKLGVVYFSMTEVDKLGLGDV----- 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 574 FRTVVMPVarEFDPDMVLVSAGFDALEGH----TPPLGGYKVTAKCFGHLTKQLMTLaNGRVALALEGGHDL----TAIC 645
Cdd:cd09987   131 FEEIVSYL--GDKGDNVYLSVDVDGLDPSfapgTGTPGPGGLSYREGLYITERIAKT-NLVVGLDIVEVNPLldetGRTA 207

                         250
                  ....*....|
gi 1720373353 646 DASEACINAL 655
Cdd:cd09987   208 RLAAALTLEL 217
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
 337-618 2.21e-24

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: 105.92  E-value: 2.21e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 337 HPEHAGRIQSIWSRLQETGLLSKCERIQGRKASLEEIQLVHSEHH-SLLYGTSP---LDGQKLDPRTLLGDDSRKF---- 408
Cdd:cd10010    25 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYiKFLRSIRPdnmSEYSKQMQRFNVGEDCPVFdglf 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 409 -FSSLPCGGlgvdsdtiwnelhssgaarmavgcviELASKVASGELKNGFAVVRPPG-HHAEESAAMGFCFFNSVAITAK 486
Cdd:cd10010   105 eFCQLSAGG--------------------------SVASAVKLNKQQTDIAVNWAGGlHHAKKSEASGFCYVNDIVLAIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 487 YLRDQLNisKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdeGNFFPGSGAPNEVGVGLGEGYNVNIAWTGGLDppmg 566
Cdd:cd10010   159 ELLKYHQ--RVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKY--GEYFPGTGDLRDIGAGKGKYYAVNYPLRDGID---- 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720373353 567 DVEYLEAFRTVVMPVAREFDPDMVLVSAGFDALEGHTppLGGYKVTAKcfGH 618
Cdd:cd10010   231 DESYEAIFKPVMSKVMEMFQPSAVVLQCGADSLSGDR--LGCFNLTIK--GH 278
PTZ00063 PTZ00063
histone deacetylase; Provisional
 465-618 1.01e-22

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 101.81  E-value: 1.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 465 HHAEESAAMGFCFFNSVAITA----KYLrdqlniSKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdeGNFFPGSGAP 540
Cdd:PTZ00063  137 HHAKRSEASGFCYINDIVLGIlellKYH------ARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFPGTGDV 208

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720373353 541 NEVGVGLGEGYNVNIAWTGGLDppmgDVEYLEAFRTVVMPVAREFDPDMVLVSAGFDALEGHTppLGGYKVTAKcfGH 618
Cdd:PTZ00063  209 TDIGVAQGKYYSVNVPLNDGID----DDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDR--LGRFNLTIK--GH 278
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
 465-618 1.12e-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: 97.85  E-value: 1.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 465 HHAEESAAMGFCFFNSVAITAKYLRDQLNisKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdeGN-FFPGSGAPNEV 543
Cdd:cd10005   132 HHAKKFEASGFCYVNDIVIAILELLKYHP--RVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKY--GNyFFPGTGDMYEV 207

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720373353 544 GVGLGEGYNVNIAWTGGLDppmgDVEYLEAFRTVVMPVAREFDPDMVLVSAGFDALEGHTppLGGYKVTAKcfGH 618
Cdd:cd10005   208 GAESGRYYSVNVPLKDGID----DQSYLQLFKPVIQQVIDFYQPTCIVLQCGADSLGCDR--LGCFNLSIK--GH 274
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
 337-618 2.77e-20

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


Pssm-ID: 212535 [Multi-domain]  Cd Length: 366  Bit Score: 93.20  E-value: 2.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 337 HPEHAGRIQSIWSRLQETGLLSKCERIQGRKASLEEIQLVHS-EHHSLLYGTSP---LDGQKLDPRTLLGDDSRKF---- 408
Cdd:cd10011    21 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSdEYIKFLRSIRPdnmSEYSKQMQRFNVGEDCPVFdglf 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 409 -FSSLPCGGlGVDSDTIWNELHSSGAARMAVGCvielaskvasgelkngfavvrppgHHAEESAAMGFCFFNSVAITAKY 487
Cdd:cd10011   101 eFCQLSTGG-SVAGAVKLNRQQTDMAVNWAGGL------------------------HHAKKSEASGFCYVNDIVLAILE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 488 LRDQLNisKILIVDLDVHHGNGTQQAFYADPSILYISlhRYDEGNFFPGSGAPNEVGVGLGEGYNVNIAWTGGLDppmgD 567
Cdd:cd10011   156 LLKYHQ--RVLYIDIDIHHGDGVEEAFYTTDRVMTVS--FHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGID----D 227

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720373353 568 VEYLEAFRTVVMPVAREFDPDMVLVSAGFDALEGHTppLGGYKVTAKcfGH 618
Cdd:cd10011   228 ESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDR--LGCFNLTVK--GH 274
PTZ00346 PTZ00346
histone deacetylase; Provisional
 465-638 4.60e-18

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 87.39  E-value: 4.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 465 HHAEESAAMGFCFFNSVAITAKYLRDQLNisKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEgNFFPGSGAPNEVG 544
Cdd:PTZ00346  154 HHSKCGECSGFCYVNDIVLGILELLKCHD--RVLYVDIDMHHGDGVDEAFCTSDRVFTLSLHKFGE-SFFPGTGHPRDVG 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373353 545 VGLGEGYNVNIA-WTGgldppMGDVEYLEAFRTVVMPVAREFDPDMVLVSAGFDALEGHTppLGGYKVTAKCFGHLTKQL 623
Cdd:PTZ00346  231 YGRGRYYSMNLAvWDG-----ITDFYYLGLFEHALHSIVRRYSPDAIVLQCGADSLAGDR--LGLLNLSSFGHGQCVQAV 303

                         170
                  ....*....|....*
gi 1720373353 624 MTLanGRVALALEGG 638
Cdd:PTZ00346  304 RDL--GIPMLALGGG 316
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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