NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1698285192|ref|XP_029703170|]
View 

histone deacetylase 3 [Takifugu rubripes]

Protein Classification

histone deacetylase 3( domain architecture ID 10178049)

histone deacetylase 3 (HD3) 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)

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
3-383 0e+00

Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that catalyzes hydrolysis of N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. In order to target specific chromatin regions, HDAC3 can interact with DNA-binding proteins (transcriptional factors) either directly or after forming complexes with a number of other proteins, as observed for the SMPT/N-CoR complex which recruits human HDAC3 to specific chromatin loci and activates deacetylation. Human HDAC3 is also involved in deacetylation of non-histone substrates such as RelA, SPY and p53 factors. This protein can also down-regulate p53 function and subsequently modulate cell growth and apoptosis. This gene is therefore regarded as a potential tumor suppressor gene. HDAC3 plays a role in various physiological processes, including subcellular protein localization, cell cycle progression, cell differentiation, apoptosis and survival. HDAC3 has been found to be overexpressed in some tumors including leukemia, lung carcinoma, colon cancer and maxillary carcinoma. Thus, inhibitors precisely targeting HDAC3 (in some cases together with retinoic acid or hyperthermia) could be a therapeutic drug option.


:

Pssm-ID: 212529  Cd Length: 381  Bit Score: 831.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192   3 NRTSYFYDPDVGNFHYGAGHPMKPHRLSLTHSLVLHYGLYKKMMVFKPYKASQHDMCRFHSEDYIDFLQKVSPNNMQGFT 82
Cdd:cd10005     1 KRVAYFYDPDVGNFHYGPGHPMKPHRLALTHSLVLHYGLYKKMQVYKPYRASAHDMCRFHSEDYIDFLQRVTPQNIQGFT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  83 KSLNTFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNHKICDIAINWAGGLHHAKKFEASGFCYVNDIVISILELLKYHP 162
Cdd:cd10005    81 KSLNQFNVGDDCPVFPGLFDFCSMYTGASLEGATKLNHKICDIAINWSGGLHHAKKFEASGFCYVNDIVIAILELLKYHP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 163 RVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYRQLFQPVIKQ 242
Cdd:cd10005   161 RVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYSVNVPLKDGIDDQSYLQLFKPVIQQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 243 VVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEFVKSFKIPLLVLGGGGYTVRNVARCWTFETSLLLEESISDE 322
Cdd:cd10005   241 VIDFYQPTCIVLQCGADSLGCDRLGCFNLSIKGHGECVEFVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVDEEISNE 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1698285192 323 LPYSEYFEYFAPDFTLHPDVSTRIENQNSRQYLEQIRQTVFENLKMLNHAPSVQIHDVPSD 383
Cdd:cd10005   321 LPYNEYFEYFAPDFTLHPDVSTRIENQNSKQYLDQIRQTVFENLKMLNHAPSVQMQDVPPD 381
 
Name Accession Description Interval E-value
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
3-383 0e+00

Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that catalyzes hydrolysis of N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. In order to target specific chromatin regions, HDAC3 can interact with DNA-binding proteins (transcriptional factors) either directly or after forming complexes with a number of other proteins, as observed for the SMPT/N-CoR complex which recruits human HDAC3 to specific chromatin loci and activates deacetylation. Human HDAC3 is also involved in deacetylation of non-histone substrates such as RelA, SPY and p53 factors. This protein can also down-regulate p53 function and subsequently modulate cell growth and apoptosis. This gene is therefore regarded as a potential tumor suppressor gene. HDAC3 plays a role in various physiological processes, including subcellular protein localization, cell cycle progression, cell differentiation, apoptosis and survival. HDAC3 has been found to be overexpressed in some tumors including leukemia, lung carcinoma, colon cancer and maxillary carcinoma. Thus, inhibitors precisely targeting HDAC3 (in some cases together with retinoic acid or hyperthermia) could be a therapeutic drug option.


Pssm-ID: 212529  Cd Length: 381  Bit Score: 831.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192   3 NRTSYFYDPDVGNFHYGAGHPMKPHRLSLTHSLVLHYGLYKKMMVFKPYKASQHDMCRFHSEDYIDFLQKVSPNNMQGFT 82
Cdd:cd10005     1 KRVAYFYDPDVGNFHYGPGHPMKPHRLALTHSLVLHYGLYKKMQVYKPYRASAHDMCRFHSEDYIDFLQRVTPQNIQGFT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  83 KSLNTFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNHKICDIAINWAGGLHHAKKFEASGFCYVNDIVISILELLKYHP 162
Cdd:cd10005    81 KSLNQFNVGDDCPVFPGLFDFCSMYTGASLEGATKLNHKICDIAINWSGGLHHAKKFEASGFCYVNDIVIAILELLKYHP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 163 RVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYRQLFQPVIKQ 242
Cdd:cd10005   161 RVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYSVNVPLKDGIDDQSYLQLFKPVIQQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 243 VVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEFVKSFKIPLLVLGGGGYTVRNVARCWTFETSLLLEESISDE 322
Cdd:cd10005   241 VIDFYQPTCIVLQCGADSLGCDRLGCFNLSIKGHGECVEFVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVDEEISNE 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1698285192 323 LPYSEYFEYFAPDFTLHPDVSTRIENQNSRQYLEQIRQTVFENLKMLNHAPSVQIHDVPSD 383
Cdd:cd10005   321 LPYNEYFEYFAPDFTLHPDVSTRIENQNSKQYLDQIRQTVFENLKMLNHAPSVQMQDVPPD 381
PTZ00063 PTZ00063
histone deacetylase; Provisional
1-394 0e+00

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 556.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192   1 MTNRTSYFYDPDVGNFHYGAGHPMKPHRLSLTHSLVLHYGLYKKMMVFKPYKASQHDMCRFHSEDYIDFLQKVSPNNMQG 80
Cdd:PTZ00063    2 MRKRVSYFYDPDIGSYYYGPGHPMKPQRIRMAHALILSYDLYKHMEIYRPHKSVEPELVLFHDEEYVDFLSSISPENYRD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  81 FTKSLNTFNVGD--DCPVFPGLFEFCSRYTGASLQGATQLNHKICDIAINWAGGLHHAKKFEASGFCYVNDIVISILELL 158
Cdd:PTZ00063   82 FTYQLKRFNVGEatDCPVFDGLFEFQQSCAGASIDGAYKLNNHQADICVNWSGGLHHAKRSEASGFCYINDIVLGILELL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 159 KYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNyFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYRQLFQP 238
Cdd:PTZ00063  162 KYHARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKFGD-FFPGTGDVTDIGVAQGKYYSVNVPLNDGIDDDSFVDLFKP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 239 VIKQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEFVKSFKIPLLVLGGGGYTVRNVARCWTFETSLLLEES 318
Cdd:PTZ00063  241 VISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAACVEFVRSLNIPLLVLGGGGYTIRNVARCWAYETGVILNKH 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698285192 319 --ISDELPYSEYFEYFAPDFTLHPDVSTrIENQNSRQYLEQIRQTVFENLKMLNHAPSVQIHDVPSDMLNYERNDEPD 394
Cdd:PTZ00063  321 deMSDQISLNDYYDYYAPDFQLHLQPSN-IPNYNSPEHLEKIKVKILENLRYLEHAPGVQFAYVPPDFFDRDIDDEDE 397
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Chromatin structure and ...
4-335 1.00e-116

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


Pssm-ID: 223201 [Multi-domain]  Cd Length: 340  Bit Score: 344.36  E-value: 1.00e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192   4 RTSYFYDPDVGNFHYGAGHPMKPHRLSLTHSLVLHYGLYKKMMVFKPYKASQHDMCRFHSEDYIDFLQKVSPNNMQGftk 83
Cdd:COG0123     3 KTALIYHPEFLEHEPPPGHPENPDRLRLILELLESSGLPDSLELVEPRPATLEELLLVHSPDYVEFLESLSEEEGYG--- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  84 slntfNVGDDCPVFPGLFEFCSRYTGASLQGATQLNHKICDIAINWAGGLHHAKKFEASGFCYVNDIVISILELLK-YHP 162
Cdd:COG0123    80 -----NLDGDTPVSPGTYEAARLAAGGALTAVDAVLEGEDNAFALVRPPGHHAGRDRASGFCLFNNVAIAAKYLLKkGVK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 163 RVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGaESGRYYCLNVPLRDGIDDQSYRQLFQPVIKQ 242
Cdd:COG0123   155 RVAIIDFDVHHGNGTQEIFYDDDDVLTVSLHQDGRPFYPGTGGADEIG-EGKEGNNVNIPLPPGTGDDSYLEALEEIVLP 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 243 VVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEFVKSF----KIPLLVLGGGGYTVRNVARCWTFETSLLLEES 318
Cdd:COG0123   234 LLEEFKPDLVIVSAGFDAHRGDPLGRLNLTEEGYAKIGRAVRKLaegyGGPVVAVLEGGYNLDALARSLVAFLAGLAGLV 313
                         330       340
                  ....*....|....*....|.
gi 1698285192 319 IS---DELPY-SEYFEYFAPD 335
Cdd:COG0123   314 EEeleEPLPEdLELRRAFRAD 334
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
22-314 6.56e-111

Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. Regulation of transcription is caused in part by this mechanism. Histone deacetylases catalyze the removal of the acetyl group. Histone deacetylases are related to other proteins.


Pssm-ID: 425906 [Multi-domain]  Cd Length: 298  Bit Score: 328.04  E-value: 6.56e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  22 HPMKPHRLSLTHSLVLHYGLYKKMMVFKPYKASQHDMCRFHSEDYIDFLQKVSPnnMQGFTKSLNTFNVGDDCPVFPGLF 101
Cdd:pfam00850   1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAAP--EGGALLLLSYLSGDDDTPVSPGSY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 102 EFCSRYTGASLQGATQLNHKICD--IAINWaGGLHHAKKFEASGFCYVNDIVISILELLKYH--PRVLYIDIDIHHGDGV 177
Cdd:pfam00850  79 EAALLAAGGTLAAADAVLSGEARnaFALVR-PPGHHAERDRASGFCIFNNVAIAAKYLREKYglKRVAIVDFDVHHGNGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 178 QEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYRQLFQPVIKQVVDFYQPTCIVLQCG 257
Cdd:pfam00850 158 QEIFYDDPSVLTLSIHQYPGGFYPGTGFADETGEGKGKGYTLNVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAG 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1698285192 258 ADSLGCDRLGCFNLSIRGHGECVEFVKSFK----IPLLVLGGGGYTVRNVARCWTFETSLL 314
Cdd:pfam00850 238 FDAHAGDPLGGLNLTTEGFAEITRILLELAdplcIRVVSVLEGGYNLDALARSATAVLAAL 298
 
Name Accession Description Interval E-value
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
3-383 0e+00

Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that catalyzes hydrolysis of N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. In order to target specific chromatin regions, HDAC3 can interact with DNA-binding proteins (transcriptional factors) either directly or after forming complexes with a number of other proteins, as observed for the SMPT/N-CoR complex which recruits human HDAC3 to specific chromatin loci and activates deacetylation. Human HDAC3 is also involved in deacetylation of non-histone substrates such as RelA, SPY and p53 factors. This protein can also down-regulate p53 function and subsequently modulate cell growth and apoptosis. This gene is therefore regarded as a potential tumor suppressor gene. HDAC3 plays a role in various physiological processes, including subcellular protein localization, cell cycle progression, cell differentiation, apoptosis and survival. HDAC3 has been found to be overexpressed in some tumors including leukemia, lung carcinoma, colon cancer and maxillary carcinoma. Thus, inhibitors precisely targeting HDAC3 (in some cases together with retinoic acid or hyperthermia) could be a therapeutic drug option.


Pssm-ID: 212529  Cd Length: 381  Bit Score: 831.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192   3 NRTSYFYDPDVGNFHYGAGHPMKPHRLSLTHSLVLHYGLYKKMMVFKPYKASQHDMCRFHSEDYIDFLQKVSPNNMQGFT 82
Cdd:cd10005     1 KRVAYFYDPDVGNFHYGPGHPMKPHRLALTHSLVLHYGLYKKMQVYKPYRASAHDMCRFHSEDYIDFLQRVTPQNIQGFT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  83 KSLNTFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNHKICDIAINWAGGLHHAKKFEASGFCYVNDIVISILELLKYHP 162
Cdd:cd10005    81 KSLNQFNVGDDCPVFPGLFDFCSMYTGASLEGATKLNHKICDIAINWSGGLHHAKKFEASGFCYVNDIVIAILELLKYHP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 163 RVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYRQLFQPVIKQ 242
Cdd:cd10005   161 RVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYSVNVPLKDGIDDQSYLQLFKPVIQQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 243 VVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEFVKSFKIPLLVLGGGGYTVRNVARCWTFETSLLLEESISDE 322
Cdd:cd10005   241 VIDFYQPTCIVLQCGADSLGCDRLGCFNLSIKGHGECVEFVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVDEEISNE 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1698285192 323 LPYSEYFEYFAPDFTLHPDVSTRIENQNSRQYLEQIRQTVFENLKMLNHAPSVQIHDVPSD 383
Cdd:cd10005   321 LPYNEYFEYFAPDFTLHPDVSTRIENQNSKQYLDQIRQTVFENLKMLNHAPSVQMQDVPPD 381
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
8-314 0e+00

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


Pssm-ID: 212517 [Multi-domain]  Cd Length: 306  Bit Score: 606.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192   8 FYDPDVGNFHYGAGHPMKPHRLSLTHSLVLHYGLYKKMMVFKPYKASQHDMCRFHSEDYIDFLQKVSPNNMQGFTKSLNT 87
Cdd:cd09991     1 FYDPDVGNYYYGQGHPMKPHRIRMTHSLILSYGLYKKMEIYRPRPATAEELTKFHSDDYIDFLRSVSPDNMKEFKKQLER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  88 FNVGDDCPVFPGLFEFCSRYTGASLQGATQLNHKICDIAINWAGGLHHAKKFEASGFCYVNDIVISILELLKYHPRVLYI 167
Cdd:cd09991    81 FNVGEDCPVFDGLYEYCQLYAGGSIAAAVKLNRGQADIAINWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 168 DIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDmYEVGAESGRYYCLNVPLRDGIDDQSYRQLFQPVIKQVVDFY 247
Cdd:cd09991   161 DIDIHHGDGVEEAFYTTDRVMTVSFHKFGEYFFPGTGL-RDIGAGKGKYYAVNVPLKDGIDDESYLQIFEPVLSKVMEVF 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698285192 248 QPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEFVKSFKIPLLVLGGGGYTVRNVARCWTFETSLL 314
Cdd:cd09991   240 QPSAVVLQCGADSLAGDRLGCFNLSIKGHAKCVKFVKSFNIPLLVLGGGGYTLRNVARCWTYETAVL 306
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
4-378 0e+00

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


Pssm-ID: 212528 [Multi-domain]  Cd Length: 375  Bit Score: 564.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192   4 RTSYFYDPDVGNFHYGAGHPMKPHRLSLTHSLVLHYGLYKKMMVFKPYKASQHDMCRFHSEDYIDFLQKVSPNNMQGFTK 83
Cdd:cd10004     3 KVAYFYDSDVGNYAYGPGHPMKPHRIRMAHSLVMNYGLYKKMEIYRAKPATKNEMTQFHTDEYIDFLSRVTPDNMEKFQK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  84 SLNTFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNHKICDIAINWAGGLHHAKKFEASGFCYVNDIVISILELLKYHPR 163
Cdd:cd10004    83 EQVKYNVGDDCPVFDGLFEFCSISAGGSMEGAARLNRGKCDIAVNWAGGLHHAKKSEASGFCYVNDIVLGILELLRYHQR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 164 VLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYfFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYRQLFQPVIKQV 243
Cdd:cd10004   163 VLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYGEY-FPGTGELRDIGIGTGKNYAVNVPLRDGIDDESYKSIFEPVIKHV 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 244 VDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEFVKSFKIPLLVLGGGGYTVRNVARCWTFETSLLLEESISDEL 323
Cdd:cd10004   242 MEWYQPEAVVLQCGGDSLSGDRLGCFNLSMKGHANCVNFVKSFNLPMLVLGGGGYTMRNVARTWAFETGLLAGEELDKDL 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1698285192 324 PYSEYFEYFAPDFTLhpDV-STRIENQNSRQYLEQIRQTVFENLKMLNHAPSVQIH 378
Cdd:cd10004   322 PYNEYYEYYGPDYEL--NVrPSNMENHNTPEYLDKITTAVIENLRNTSFAPSVQMQ 375
PTZ00063 PTZ00063
histone deacetylase; Provisional
1-394 0e+00

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 556.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192   1 MTNRTSYFYDPDVGNFHYGAGHPMKPHRLSLTHSLVLHYGLYKKMMVFKPYKASQHDMCRFHSEDYIDFLQKVSPNNMQG 80
Cdd:PTZ00063    2 MRKRVSYFYDPDIGSYYYGPGHPMKPQRIRMAHALILSYDLYKHMEIYRPHKSVEPELVLFHDEEYVDFLSSISPENYRD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  81 FTKSLNTFNVGD--DCPVFPGLFEFCSRYTGASLQGATQLNHKICDIAINWAGGLHHAKKFEASGFCYVNDIVISILELL 158
Cdd:PTZ00063   82 FTYQLKRFNVGEatDCPVFDGLFEFQQSCAGASIDGAYKLNNHQADICVNWSGGLHHAKRSEASGFCYINDIVLGILELL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 159 KYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNyFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYRQLFQP 238
Cdd:PTZ00063  162 KYHARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKFGD-FFPGTGDVTDIGVAQGKYYSVNVPLNDGIDDDSFVDLFKP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 239 VIKQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEFVKSFKIPLLVLGGGGYTVRNVARCWTFETSLLLEES 318
Cdd:PTZ00063  241 VISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAACVEFVRSLNIPLLVLGGGGYTIRNVARCWAYETGVILNKH 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698285192 319 --ISDELPYSEYFEYFAPDFTLHPDVSTrIENQNSRQYLEQIRQTVFENLKMLNHAPSVQIHDVPSDMLNYERNDEPD 394
Cdd:PTZ00063  321 deMSDQISLNDYYDYYAPDFQLHLQPSN-IPNYNSPEHLEKIKVKILENLRYLEHAPGVQFAYVPPDFFDRDIDDEDE 397
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
4-369 0e+00

Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme that catalyzes hydrolysis of N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. HDAC1 is involved in regulation through association with DNA binding proteins to target specific chromatin regions. In particular, HDAC1 appears to play a major role in pre-implantation embryogenesis in establishing a repressive chromatin state. Its interaction with retinoblastoma tumor-suppressor protein is essential in the control of cell proliferation and differentiation. Together with metastasis-associated protein-2 (MTA2), it deacetylates p53, thereby modulating its effect on cell growth and apoptosis. It participates in DNA-damage response, along with HDAC2; together, they promote DNA non-homologous end-joining. HDAC1 is also involved in tumorogenesis; its overexpression modulates cancer progression. Specific inhibitors of HDAC1 are currently used in cancer therapy.


Pssm-ID: 212534 [Multi-domain]  Cd Length: 371  Bit Score: 528.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192   4 RTSYFYDPDVGNFHYGAGHPMKPHRLSLTHSLVLHYGLYKKMMVFKPYKASQHDMCRFHSEDYIDFLQKVSPNNMQGFTK 83
Cdd:cd10010     7 KVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  84 SLNTFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNHKICDIAINWAGGLHHAKKFEASGFCYVNDIVISILELLKYHPR 163
Cdd:cd10010    87 QMQRFNVGEDCPVFDGLFEFCQLSAGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 164 VLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYfFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYRQLFQPVIKQV 243
Cdd:cd10010   167 VLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEY-FPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKV 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 244 VDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEFVKSFKIPLLVLGGGGYTVRNVARCWTFETSLLLEESISDEL 323
Cdd:cd10010   246 MEMFQPSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDSEIPNEL 325
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1698285192 324 PYSEYFEYFAPDFTLHPDVSTrIENQNSRQYLEQIRQTVFENLKML 369
Cdd:cd10010   326 PYNDYFEYFGPDFKLHISPSN-MTNQNTNEYLEKIKQRLFENLRML 370
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
4-369 0e+00

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


Pssm-ID: 212535 [Multi-domain]  Cd Length: 366  Bit Score: 513.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192   4 RTSYFYDPDVGNFHYGAGHPMKPHRLSLTHSLVLHYGLYKKMMVFKPYKASQHDMCRFHSEDYIDFLQKVSPNNMQGFTK 83
Cdd:cd10011     3 KVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  84 SLNTFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNHKICDIAINWAGGLHHAKKFEASGFCYVNDIVISILELLKYHPR 163
Cdd:cd10011    83 QMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 164 VLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYfFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYRQLFQPVIKQV 243
Cdd:cd10011   163 VLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEY-FPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQIFKPIISKV 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 244 VDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEFVKSFKIPLLVLGGGGYTVRNVARCWTFETSLLLEESISDEL 323
Cdd:cd10011   242 MEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLGGGGYTIRNVARCWTYETAVALDCEIPNEL 321
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1698285192 324 PYSEYFEYFAPDFTLHPDVSTrIENQNSRQYLEQIRQTVFENLKML 369
Cdd:cd10011   322 PYNDYFEYFGPDFKLHISPSN-MTNQNTPEYMEKIKQRLFENLRML 366
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
6-314 1.23e-174

Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I histone deacetylase (HDAC) Hos2 from Saccharomyces cerevisiae as well as a histone deacetylase Phd1 from Schizosaccharomyces pombe. Hos2 binds to the coding regions of genes during gene activation, specifically it deacetylates the lysines in H3 and H4 histone tails. It is preferentially associated with genes of high activity genome-wide and is shown to be necessary for efficient transcription. Thus, Hos2 is directly required for gene activation in contrast to other class I histone deacetylases. Protein encoded by phd1 is inhibited by trichostatin A (TSA), a specific inhibitor of histone deacetylase, and is involved in the meiotic cell cycle in S. pombe. Class 1 HDACs are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues in histone amino termini to yield a deacetylated histone (EC 3.5.1.98).


Pssm-ID: 212540 [Multi-domain]  Cd Length: 311  Bit Score: 490.43  E-value: 1.23e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192   6 SYFYDPDVGNFHYGAGHPMKPHRLSLTHSLVLHYGLYKKMMVFKPYKASQHDMCRFHSEDYIDFLQKVSPNNMQGFTKS- 84
Cdd:cd11598     2 SYHFNSRVEDYHFGRTHPMKPFRLTLTKHLVMGYGLHKAMDTYEARAATREELRQFHDADYLDFLSKVSPENANQLRFDk 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  85 LNTFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNHKICDIAINWAGGLHHAKKFEASGFCYVNDIVISILELLKYHPRV 164
Cdd:cd11598    82 AEPFNIGDDCPVFDGMYDYCQLYAGASLDAARKLCSGQSDIAINWSGGLHHAKKSEASGFCYVNDIVLAILNLLRYFPRV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 165 LYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYRQLFQPVIKQVV 244
Cdd:cd11598   162 LYIDIDVHHGDGVEEAFYRTDRVMTLSFHKYNGEFFPGTGDLDDNGGTPGKHFALNVPLEDGIDDEQYNLLFKSIIGPTI 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 245 DFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEFVKSFKIPLLVLGGGGYTVRNVARCWTFETSLL 314
Cdd:cd11598   242 EKFQPSAIVLQCGADSLGGDRLGQFNLNIKAHGACVKFVKSFGIPMLVVGGGGYTPRNVARAWCYETAVA 311
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
23-367 3.77e-145

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: 417.51  E-value: 3.77e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  23 PMKPHRLSLTHSLVLHYGLYKKMMVFKPYKASQHDMCRFHSEDYIDFLQKVSP--NNMQGFTKSLNtFNVGDDCPVFPGL 100
Cdd:cd10000    17 PKVPNRASMVHSLIEAYGLLKQLRVVKPRVATEEELASFHSDEYIQFLKKASNegDNDEEPSEQQE-FGLGYDCPIFEGI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 101 FEFCSRYTGASLQGATQLNHKICDIAINWAGGLHHAKKFEASGFCYVNDIVISILELLKYHPRVLYIDIDIHHGDGVQEA 180
Cdd:cd10000    96 YDYAAAVAGATLTAAQLLIDGKCKVAINWFGGWHHAQRDEASGFCYVNDIVLGILKLREKFDRVLYVDLDLHHGDGVEDA 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 181 FYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYRQLFQPVIKQVVDFYQPTCIVLQCGADS 260
Cdd:cd10000   176 FSFTSKVMTVSLHKYSPGFFPGTGDVSDVGLGKGKYYTVNVPLRDGIQDEQYLQIFTAVVPEIVAAFRPEAVVLQCGADT 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 261 LGCDRLGCFNLSIRGHGECVEFVKSFKIPLLVLGGGGYTVRNVARCWTFETSLLLEESISDELPYSEYFEYFAPDFTLHP 340
Cdd:cd10000   256 LAGDPMGAFNLTPVGIGKCLKYVLGWKLPTLILGGGGYNLANTARCWTYLTGLILGEPLSSDIPDHEFFTSYGPDYELEI 335
                         330       340
                  ....*....|....*....|....*..
gi 1698285192 341 DVSTRiENQNSRQYLEQIRQTVFENLK 367
Cdd:cd10000   336 SPSLR-PDLNEDQYIEKILETIKGNLK 361
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Chromatin structure and ...
4-335 1.00e-116

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


Pssm-ID: 223201 [Multi-domain]  Cd Length: 340  Bit Score: 344.36  E-value: 1.00e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192   4 RTSYFYDPDVGNFHYGAGHPMKPHRLSLTHSLVLHYGLYKKMMVFKPYKASQHDMCRFHSEDYIDFLQKVSPNNMQGftk 83
Cdd:COG0123     3 KTALIYHPEFLEHEPPPGHPENPDRLRLILELLESSGLPDSLELVEPRPATLEELLLVHSPDYVEFLESLSEEEGYG--- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  84 slntfNVGDDCPVFPGLFEFCSRYTGASLQGATQLNHKICDIAINWAGGLHHAKKFEASGFCYVNDIVISILELLK-YHP 162
Cdd:COG0123    80 -----NLDGDTPVSPGTYEAARLAAGGALTAVDAVLEGEDNAFALVRPPGHHAGRDRASGFCLFNNVAIAAKYLLKkGVK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 163 RVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGaESGRYYCLNVPLRDGIDDQSYRQLFQPVIKQ 242
Cdd:COG0123   155 RVAIIDFDVHHGNGTQEIFYDDDDVLTVSLHQDGRPFYPGTGGADEIG-EGKEGNNVNIPLPPGTGDDSYLEALEEIVLP 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 243 VVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEFVKSF----KIPLLVLGGGGYTVRNVARCWTFETSLLLEES 318
Cdd:COG0123   234 LLEEFKPDLVIVSAGFDAHRGDPLGRLNLTEEGYAKIGRAVRKLaegyGGPVVAVLEGGYNLDALARSLVAFLAGLAGLV 313
                         330       340
                  ....*....|....*....|.
gi 1698285192 319 IS---DELPY-SEYFEYFAPD 335
Cdd:COG0123   314 EEeleEPLPEdLELRRAFRAD 334
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
22-314 6.56e-111

Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. Regulation of transcription is caused in part by this mechanism. Histone deacetylases catalyze the removal of the acetyl group. Histone deacetylases are related to other proteins.


Pssm-ID: 425906 [Multi-domain]  Cd Length: 298  Bit Score: 328.04  E-value: 6.56e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  22 HPMKPHRLSLTHSLVLHYGLYKKMMVFKPYKASQHDMCRFHSEDYIDFLQKVSPnnMQGFTKSLNTFNVGDDCPVFPGLF 101
Cdd:pfam00850   1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAAP--EGGALLLLSYLSGDDDTPVSPGSY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 102 EFCSRYTGASLQGATQLNHKICD--IAINWaGGLHHAKKFEASGFCYVNDIVISILELLKYH--PRVLYIDIDIHHGDGV 177
Cdd:pfam00850  79 EAALLAAGGTLAAADAVLSGEARnaFALVR-PPGHHAERDRASGFCIFNNVAIAAKYLREKYglKRVAIVDFDVHHGNGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 178 QEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYRQLFQPVIKQVVDFYQPTCIVLQCG 257
Cdd:pfam00850 158 QEIFYDDPSVLTLSIHQYPGGFYPGTGFADETGEGKGKGYTLNVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAG 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1698285192 258 ADSLGCDRLGCFNLSIRGHGECVEFVKSFK----IPLLVLGGGGYTVRNVARCWTFETSLL 314
Cdd:pfam00850 238 FDAHAGDPLGGLNLTTEGFAEITRILLELAdplcIRVVSVLEGGYNLDALARSATAVLAAL 298
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
7-308 1.40e-110

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: 327.59  E-value: 1.40e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192   7 YFYDPDVGNFHYGAGHPMKPHRLSLTHSLVLHYGLYKKMMVFKPYKASQHDMCRFHSEDYIDFLQKVSPNnmqGFTKSLN 86
Cdd:cd09994     2 FIYSEEYLRYSFGPNHPFNPPRLSLTKDLLRALGLLPPVDLVPPRPATEEELLLFHTPDYIEAVKEASRG---QEPEGRG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  87 TFNVG-DDCPVFPGLFEFCSRYTGASLQGATQLNHKICDIAINWAGGLHHAKKFEASGFCYVNDIVISILELL-KYHPRV 164
Cdd:cd09994    79 RLGLGtEDNPVFPGMHEAAALVVGGTLLAARLVLEGEARRAFNPAGGLHHAMRGRASGFCVYNDAAVAIERLRdKGGLRV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 165 LYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYRQLFQPVIKQVV 244
Cdd:cd09994   159 AYVDIDAHHGDGVQAAFYDDPRVLTISLHESGRYLFPGTGFVDEIGEGEGYGYAVNIPLPPGTGDDEFLRAFEAVVPPLL 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1698285192 245 DFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEFVK-----SFKIPLLVLGGGGYTVRNVARCWT 308
Cdd:cd09994   239 RAFRPDVIVSQHGADAHAGDPLTHLNLSNRAYRAAVRRIReladeYCGGRWLALGGGGYNPDVVARAWA 307
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
28-314 9.61e-98

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: 294.17  E-value: 9.61e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  28 RLSLTHSLVLHYGL-YKKMMVFKPYKASQHDMCRFHSEDYIDFLqkvspnnmqgftksLNTFNVGDDCPVFPGLFEFCSR 106
Cdd:cd11680    21 RSSLVHSLIRAYGLlQHFDEIIEPERATRKDLTKYHDKDYVDFL--------------LKKYGLEDDCPVFPFLSMYVQL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 107 YTGASLQGATQLNH-KICDIAINWAGGLHHAKKFEASGFCYVNDIVISILELLKYH-PRVLYIDIDIHHGDGVQEAFYLT 184
Cdd:cd11680    87 VAGSSLALAKHLITqVERDIAINWYGGRHHAQKSRASGFCYVNDIVLAILRLRRARfRRVFYLDLDLHHGDGVESAFFFS 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 185 DRVMTVSFHKYGNYFFPGTGDMyevgAESGRYYCLNVPLRDGIDDQSYRQLFQPVIKQVVDFYQPTCIVLQCGADSLGCD 264
Cdd:cd11680   167 KNVLTCSIHRYDPGFFPGTGSL----KNSSDKGMLNIPLKRGLSDKTLLRIIDSIVRPLIEKFEPEVIVIQCGCDGLSGD 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1698285192 265 RLGCFNLSIRGHGECVEFV-KSFK-IPLLVLGGGGYTVRNVARCWTFETSLL 314
Cdd:cd11680   243 PHKEWNLTIRGYGSVIELLlKEFKdKPTLLLGGGGYNHTEAARAWTYLTSMV 294
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
28-314 4.96e-87

Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family includes Zn-dependent histone deacetylase classes I, II and IV (class III HDACs, also called sirtuins, are NAD-dependent and structurally unrelated, and therefore not part of this family). Histone deacetylases catalyze hydrolysis of N(6)-acetyl-lysine residues in histone amino termini to yield a deacetylated histone (EC 3.5.1.98), as opposed to the acetylation reaction by some histone acetyltransferases (EC 2.3.1.48). Deacetylases of this family are involved in signal transduction through histone and other protein modification, and can repress/activate transcription of a number of different genes. They usually act via the formation of large multiprotein complexes. They are involved in various cellular processes, including cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and post-translational control of the acetyl coenzyme A synthetase. In mammals, they are known to be involved in progression of different tumors. Specific inhibitors of mammalian histone deacetylases are an emerging class of promising novel anticancer drugs.


Pssm-ID: 212512 [Multi-domain]  Cd Length: 279  Bit Score: 266.22  E-value: 4.96e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  28 RLSLTHSLVLHYGLYKKMMVFKPYKASQHDMCRFHSEDYIDFLQKVSPNNMQGFTKSlntFNVGDDCPVFPGLFEFCSRY 107
Cdd:cd09301     1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKANFAVATITESKP---VIFGPNFPVQRHYFRGARLS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 108 TGASLQGATQLNHKICDIAINWA-GGLHHAKKFEASGFCYVNDIVISILELLKY-HPRVLYIDIDIHHGDGVQEAFYLTD 185
Cdd:cd09301    78 TGGVVEAAELVAKGELERAFAVVgAGGHHAGKSRAWGFCYFNDVVLAIKFLRERgISRILIIDTDAHHGDGTREAFYDDD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 186 RVMTVSFHKYGNYFFpgtgdmyevGAESGRYYCLNVPLRDGIDDQSYRQLFQPVIKQVVDFYQPTCIVLQCGADSLGCDR 265
Cdd:cd09301   158 RVLHMSFHNYDIYPF---------GRGKGKGYKINVPLEDGLGDEEYLDAVERVISKVLEEFEPEVVVLQFGHDTHEGDR 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1698285192 266 LGCFNLSIRGHGECVEFVKSF--KIPLLVLGGGGYTVRNVARCWTFETSLL 314
Cdd:cd09301   229 LGGFNLSEKGFVKLAEIVKEFarGGPILMVLGGGYNPEAAARIWTAIIKEL 279
PTZ00346 PTZ00346
histone deacetylase; Provisional
22-314 9.30e-86

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 268.44  E-value: 9.30e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  22 HPMKPHRLSLTHSLVLHYGLYKKMMVFKPYKASQHDMCRFHSEDYIDFLQKVSPNNMQGFTKSLNTFNVGDdCPVFPGLF 101
Cdd:PTZ00346   43 HAMKPYRVLAAMEIVRSLKIDAHCRTVVPPLVKVEELMAYHTDTYLANLGLHSCRSWLWNAETSKVFFSGD-CPPVEGLM 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 102 EFCSRYTGASLQGATQLNHKICDIAINWAGGLHHAKKFEASGFCYVNDIVISILELLKYHPRVLYIDIDIHHGDGVQEAF 181
Cdd:PTZ00346  122 EHSIATASGTLMGAVLLNSGQVDVAVHWGGGMHHSKCGECSGFCYVNDIVLGILELLKCHDRVLYVDIDMHHGDGVDEAF 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 182 YLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYRQLFQPVIKQVVDFYQPTCIVLQCGADSL 261
Cdd:PTZ00346  202 CTSDRVFTLSLHKFGESFFPGTGHPRDVGYGRGRYYSMNLAVWDGITDFYYLGLFEHALHSIVRRYSPDAIVLQCGADSL 281
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1698285192 262 GCDRLGCFNLSIRGHGECVEFVKSFKIPLLVLGGGGYTVRNVARCWTFETSLL 314
Cdd:PTZ00346  282 AGDRLGLLNLSSFGHGQCVQAVRDLGIPMLALGGGGYTIRNVAKLWAYETSIL 334
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
22-306 2.41e-44

Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues of histones (EC 3.5.1.98) and possibly other proteins to yield deacetylated histones/other proteins. This group includes animal HDAC4,5,6,7,8,9,10, fungal HOS3 and HDA1, plant HDA5 and HDA15 as well as other eukaryotes, archaeal and bacterial histone-like deacetylases. Eukaryotic deacetylases mostly use histones (H2, H3, H4) as substrates for deacetylation; however, non-histone substrates are known (for example, tubulin). Substrates for prokaryotic histone-like deacetylases are not known. Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. Interaction partners of class II deacetylases include 14-3-3 proteins, MEF2 family of transcriptional factors, CtBP, calmodulin (CaM), SMRT, N-CoR, BCL6, HP1alpha and SUMO. Histone deacetylases play a role in the regulation of cell cycle, cell differentiation and survival. Class II mammalian HDACs are differentially inhibited by structurally diverse compounds with known antitumor activities, thus presenting them as potential drug targets for human diseases resulting from aberrant acetylation.


Pssm-ID: 212518 [Multi-domain]  Cd Length: 291  Bit Score: 156.12  E-value: 2.41e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  22 HPMKPHRLSLTHSLVLHYGLYKKMMVFKPYKASQHDMCRFHSEDYIDFLQKVSPNNMQGFTkslntfnvgDDCPVFPGLF 101
Cdd:cd09992     1 HPERPERLLAILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYIERVEETCEAGGGYLD---------PDTYVSPGSY 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 102 EFCSRYTGASLQGATqlnhKICDIAINWAGGL-----HHAKKFEASGFCYVNDIVISILELLKYH--PRVLYIDIDIHHG 174
Cdd:cd09992    72 EAALLAAGAALAAVD----AVLSGEAENAFALvrppgHHAEPDRAMGFCLFNNVAIAARYAQKRYglKRVLIVDWDVHHG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 175 DGVQEAFYLTDRVMTVSFHKYGnyFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYRQLFQPVIKQVVDFYQPTCIVL 254
Cdd:cd09992   148 NGTQDIFYDDPSVLYFSIHQYP--FYPGTGAAEETGGGAGEGFTINVPLPPGSGDAEYLAAFEEVLLPIAREFQPDLVLV 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1698285192 255 QCGADSLGCDRLGCFNLSIRGHGECVEFVKSF-----KIPLLVLGGGGYTVRNVARC 306
Cdd:cd09992   226 SAGFDAHRGDPLGGMNLTPEGYARLTRLLKELadehcGGRLVFVLEGGYNLEALAES 282
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
8-348 4.41e-39

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  Cd Length: 359  Bit Score: 143.86  E-value: 4.41e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192   8 FYDPDVGNFHYGAGHPMKPHRLSLTHSLVLHYGLYKKMMVFKPYKASQHDMCRFHSEDYIDFLQKVSpnnmqgftkSLNT 87
Cdd:cd09996    19 LFLPVGGLLVQPGRHPENPETKRRIKNLLEVSGLSDHLVLITPRPATDEELLRVHTPEYIDRVKAAS---------AAGG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  88 FNVGDDCPVFPGLFEFCSRYTGASLQGATQLNHKICDIA---INWAGglHHAKKFEASGFCYVNDIVISILELLKYHP-- 162
Cdd:cd09996    90 GEAGGGTPFGPGSYEIALLAAGGAIAAVDAVLDGEVDNAyalVRPPG--HHAEPDQGMGFCLFNNVAIAARHALAVGGvk 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 163 RVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNyFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYRQLFQPVIKQ 242
Cdd:cd09996   168 RVAVVDWDVHHGNGTQAIFYDDPDVLTISLHQDRC-FPPDSGAVEERGEGAGEGYNLNIPLPPGSGDGAYLHAFERIVLP 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 243 VVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEFVKSFKIP-----LLVLGGGGYTVRNVARCW--TFETSLLL 315
Cdd:cd09996   247 ALRAFRPELIIVASGFDASAFDPLGRMMLTSDGFRALTRKLRDLADElcggrLVMVHEGGYSEAYVPFCGlaVLEELSGV 326
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1698285192 316 EESISDelPYSEYFEYFAPDfTLHPDVSTRIEN 348
Cdd:cd09996   327 RTGIAD--PLLYYPEAQGGQ-ELQPHQRAAIDA 356
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
62-306 1.56e-36

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: 135.36  E-value: 1.56e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  62 HSEDYIDFLQKVSPnnmqgftkslntfnvgdDCPVFPGLFEFCSRYTGASLQGAtqlnhkicDIAIN---WAGGL----- 133
Cdd:cd10001    62 HDPDYVDFLETADT-----------------DTPISEGTWEAALAAADTALTAA--------DLVLEgerAAYALcrppg 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 134 HHAKKFEASGFCYVNDIVISILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGT-GDMYEVGAE 212
Cdd:cd10001   117 HHAGRDRAGGFCYFNNAAIAAQYLRDRAGRVAILDVDVHHGNGTQEIFYERPDVLYVSIHGDPRTFYPFFlGFADETGEG 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 213 SGRYYCLNVPLRDGIDDQSYRQLFQPVIKQVVDFyQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEFVKSFKIPLLV 292
Cdd:cd10001   197 EGEGYNLNLPLPPGTGDDDYLAALDEALAAIAAF-GPDALVVSLGFDTHEGDPLSDFKLTTEDYARIGRRIAALGLPTVF 275
                         250
                  ....*....|....
gi 1698285192 293 LGGGGYTVRNVARC 306
Cdd:cd10001   276 VQEGGYNVDALGRN 289
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
22-305 1.52e-35

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: 132.24  E-value: 1.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  22 HPMKPHRLSLTHSLVLHYGLYKKMMVFKPYKASQHDMCRFHSEDYID-FLQK-VSPNNM--QGFtkslntfnvgddcPVF 97
Cdd:cd09993     1 HRFPMRKYGLLREALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLEsLKSGeLSREEIrrIGF-------------PWS 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  98 PGLFEFCSRYTGASLQGATQ-LNHKIcdiAINWAGGLHHAKKFEASGFCYVNDIVISILELLKYHP--RVLYIDIDIHHG 174
Cdd:cd09993    68 PELVERTRLAVGGTILAARLaLEHGL---AINLAGGTHHAFPDRGEGFCVFNDIAIAARVLLAEGLvrRVLIVDLDVHQG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 175 DGVQEAFYLTDRVMTVSFHkyGNYFFPGtgdmyeVGAESGryycLNVPLRDGIDDQSYRQLFQPVIKQVVDFYQPTCIVL 254
Cdd:cd09993   145 NGTAAIFADDPSVFTFSMH--GEKNYPF------RKEPSD----LDVPLPDGTGDDEYLAALEEALPRLLAEFRPDLVFY 212
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1698285192 255 QCGADSLGCDRLGCFNLSIRGHGE----CVEFVKSFKIPLLVLGGGGYTvRNVAR 305
Cdd:cd09993   213 NAGVDVLAGDRLGRLSLSLEGLRErdrlVLRFARARGIPVAMVLGGGYS-RDIAR 266
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
21-328 5.24e-31

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: 121.26  E-value: 5.24e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  21 GHPMKPHRLSLTHSLVLHYGLYKKMMVFKPYKASQHDMCRFHSEDYIDFLQKVSPNNMQGFTKSLNTFnvgDDCPVFPGL 100
Cdd:cd10002     6 NHIECPERLEAILERLTQDGLLERCVKIPAREAEEDEILLVHSQEYIDLVKSTETMEKEELESLCSGY---DSVYLCPST 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 101 FEFCSRYTGASLQGATQLNH-KICD-IAINWAGGlHHAKKFEASGFCYVNDIVI---SILELLKYHpRVLYIDIDIHHGD 175
Cdd:cd10002    83 YEAARLAAGSTIELVKAVMAgKIQNgFALIRPPG-HHAMRNEANGYCIFNNVAIaakYAIEKLGLK-RILIVDWDVHHGQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 176 GVQEAFYLTDRVMTVSFHKYGN-YFFPG--TGDMYEVGAESGRYYCLNVPLRD-GIDDQSYRQLFQPVIKQVVDFYQPTC 251
Cdd:cd10002   161 GTQQGFYEDPRVLYFSIHRYEHgRFWPHlfESDYDYIGVGHGYGFNVNVPLNQtGLGDADYLAIFHHILLPLALEFQPEL 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1698285192 252 IVLQCGADS-LGCDRlGCFNLSIRGHGECVEFVKSFKIP-LLVLGGGGYTVRNVARCWTFETSLLLeesiSDELPYSEY 328
Cdd:cd10002   241 VLVSAGFDAsIGDPE-GEMAVTPAGYAHLTRLLMGLAGGkLLLVLEGGYLLESLAESVSMTLRGLL----GDPLPPLAP 314
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
21-305 4.85e-30

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: 118.22  E-value: 4.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  21 GHPMKPHRLSLTHSLVLHYGLYKKMMVFKPYKASQHDMCRFHSEDYIDFLQKVSPNNMQGFtKSLNTFNVGDDCPVFPGL 100
Cdd:cd11600     2 PHPEDPSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEHWDRVEATEKMSDEQL-KDRTEIFERDSLYVNNDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 101 FeFCSRYtgaSLQGATQLNHKICD------IAINWAGGlHHAKKFEASGFCYVNDIVISILELLKYHP----RVLYIDID 170
Cdd:cd11600    81 A-FCARL---SCGGAIEACRAVAEgrvknaFAVVRPPG-HHAEPDESMGFCFFNNVAVAAKWLQTEYPdkikKILILDWD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 171 IHHGDGVQEAFYLTDRVMTVSFHKYGN-YFFPGT--GDMYEVGAESGRYYCLNVPLRD-GIDDQSYRQLFQPVIKQVVDF 246
Cdd:cd11600   156 IHHGNGTQRAFYDDPNVLYISLHRFENgGFYPGTpyGDYESVGEGAGLGFNVNIPWPQgGMGDADYIYAFQRIVMPIAYE 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 247 YQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEFVKSF-KIPLLVLGGGGYTVRNVAR 305
Cdd:cd11600   236 FDPDLVIISAGFDAADGDELGQCHVTPAGYAHMTHMLMSLaGGKLVVALEGGYNLDAISD 295
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
9-315 1.31e-29

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: 117.82  E-value: 1.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192   9 YDPDVGNFH--YGAGHPMKPHRLSLTHSLVLHYGLYKKMMVFKPYKASQHDMCRFHSEDYIDF---LQKVSPNNMQGFTK 83
Cdd:cd10003     1 YDQRMMNHHnlWDPGHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHLDEmksLEKMKPRELNRLGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  84 SLNTfnvgddcpVF--PGLFEFCSRYTGASLQGATQ-LNHKICD-IAINWAGGlHHAKKFEASGFCYVNDIVISI-LELL 158
Cdd:cd10003    81 EYDS--------IYihPDSYQCALLAAGCVLQVVEAvLTGESRNgVAIVRPPG-HHAEQDTACGFCFFNNVAIAArYAQK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 159 KYHP-RVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGN-YFFPGT--GDMYEVGAESGRYYCLNVPL-RDGIDDQSYR 233
Cdd:cd10003   152 KYGLkRILIVDWDVHHGNGTQHMFESDPSVLYISLHRYDNgSFFPNSpeGNYDVVGKGKGEGFNVNIPWnKGGMGDAEYI 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 234 QLFQPVIKQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEFVKSF---KIpLLVLgGGGYTVRNVARCWTFE 310
Cdd:cd10003   232 AAFQQVVLPIAYEFNPELVLVSAGFDAARGDPLGGCKVTPEGYAHMTHMLMSLaggRV-IVIL-EGGYNLTSISESMSMC 309

                  ....*
gi 1698285192 311 TSLLL 315
Cdd:cd10003   310 TKTLL 314
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
22-272 2.09e-27

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: 110.29  E-value: 2.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  22 HPMKPHRLSLTHSLVLHYGLYKKMMVFKPYKASQHDMCRFHSEDYIDFLQKVSPNNMQGFtkslntfnVGDDCPVFPGLF 101
Cdd:cd11599     1 HPESPERLEAILDALIASGLDRLLRQLEAPPATREQLLRVHDAAYVDRLEAAAPEEGLVQ--------LDPDTAMSPGSL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 102 EFCSRYTGASLQGATQ-LNHKI----CdiAINWAGglHHAKKFEASGFCYVNDIVISILELLKYHP--RVLYIDIDIHHG 174
Cdd:cd11599    73 EAALRAAGAVVAAVDAvMAGEArnafC--AVRPPG--HHAERDKAMGFCLFNNVAIAAAHALAHHGleRVAIVDFDVHHG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 175 DGVQEAFYLTDRVMTVSFHKYgnYFFPGTGDMYEVGAEsgryYCLNVPLRDGIDDQSYRQLFQPVIKQVVDFYQPTCIVL 254
Cdd:cd11599   149 NGTEDIFRDDPRVLFCSSHQH--PLYPGTGAPDETGHG----NIVNVPLPAGTGGAEFREAVEDRWLPALDAFKPDLILI 222
                         250
                  ....*....|....*...
gi 1698285192 255 QCGADSLGCDRLGCFNLS 272
Cdd:cd11599   223 SAGFDAHRDDPLAQLNLT 240
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
134-259 4.50e-25

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: 105.50  E-value: 4.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 134 HHAKKFEASGFCYVNDIVI--SILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKY--GNyFFPGTGDMYEV 209
Cdd:cd11681   151 HHAEPSQAMGFCFFNSVAIaaKQLQQKLKLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYddGN-FFPGTGAPTEV 229
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1698285192 210 GAESGRYYCLNVPLRDGID----DQSYRQLFQPVIKQVVDFYQPTCIVLQCGAD 259
Cdd:cd11681   230 GSGAGEGFNVNIAWSGGLDppmgDAEYLAAFRTVVMPIAREFSPDIVLVSAGFD 283
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
101-312 6.60e-25

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


Pssm-ID: 212513  Cd Length: 217  Bit Score: 101.68  E-value: 6.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 101 FEFCSRYTGASLQGAtqlnhKICDIAINWAGglHHAKkfeasgfcyVNDIVISILELlkyHPRVLYIDIDIHHGDGVQEA 180
Cdd:cd09987     8 AEAHELLAGVVVAVL-----KDGKVPVVLGG--DHSI---------ANGAIRAVAEL---HPDLGVIDVDAHHDVRTPEA 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 181 FY--------------LTDRVMTVSFHKYGNYFFPgtgdmyEVGAESGRYYCLNVPLRDGiDDQSYRQLFQPVIKQVVdf 246
Cdd:cd09987    69 FGkgnhhtprhllcepLISDVHIVSIGIRGVSNGE------AGGAYARKLGVVYFSMTEV-DKLGLGDVFEEIVSYLG-- 139
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1698285192 247 YQPTCIVLQCGADSL------GCDRLGCFNLSIRGHGECVEFVKSFKIPLLVLGGGGYT----VRNVARCWTFETS 312
Cdd:cd09987   140 DKGDNVYLSVDVDGLdpsfapGTGTPGPGGLSYREGLYITERIAKTNLVVGLDIVEVNPlldeTGRTARLAAALTL 215
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
134-316 7.43e-22

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: 96.98  E-value: 7.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 134 HHAKKFEASGFCYVNDIVISIlELLKYH---PRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGN-YFFPGTGDMYEV 209
Cdd:cd10007   154 HHAEESTAMGFCFFNSVAIAA-KLLQQKlnvGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDgNFFPGSGAPDEV 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 210 GAESGRYYCLNVPLRDGID----DQSYRQLFQPVIKQVVDFYQPTCIVLQCGADslgcdrlgcfnlSIRGHgecvefvks 285
Cdd:cd10007   233 GAGPGVGFNVNIAWTGGVDppigDVEYLTAFRTVVMPIANEFSPDVVLVSAGFD------------AVEGH--------- 291
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1698285192 286 fKIPLlvlggGGYTVrnVARCWTFETSLLLE 316
Cdd:cd10007   292 -QSPL-----GGYSV--TAKCFGHLTKQLMT 314
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
134-277 1.25e-20

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: 93.18  E-value: 1.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 134 HHAKKFEASGFCYVNDIVIS--ILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKY--GNyFFPGTGDMYEV 209
Cdd:cd10006   154 HHAEESTPMGFCYFNSVAIAakLLQQRLNVSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYddGN-FFPGSGAPDEV 232
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1698285192 210 GAESGRYYCLNVPLRDGID----DQSYRQLFQPVIKQVVDFYQPTCIVLQCGADSLGCD--RLGCFNLSIRGHG 277
Cdd:cd10006   233 GTGPGVGFNVNMAFTGGLDppmgDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHptPLGGYNLSAKCFG 306
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
134-260 1.37e-20

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: 92.77  E-value: 1.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 134 HHAKKFEASGFCYVNDIVISI--LELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKY--GNyFFPGTGDMYEV 209
Cdd:cd10008   152 HHADHSTAMGFCFFNSVAIACrqLQQQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHddGN-FFPGSGAVDEV 230
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1698285192 210 GAESGRYYCLNVPLRDGID----DQSYRQLFQPVIKQVVDFYQPTCIVLQCGADS 260
Cdd:cd10008   231 GAGSGEGFNVNVAWAGGLDppmgDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDA 285
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
134-261 1.68e-20

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


Pssm-ID: 212533 [Multi-domain]  Cd Length: 379  Bit Score: 92.39  E-value: 1.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 134 HHAKKFEASGFCYVNDIVISILELLKYH--PRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKY--GNyFFPGTGDMYEV 209
Cdd:cd10009   152 HHAEESTAMGFCFFNSVAITAKYLRDQLniSKILIVDLDVHHGNGTQQAFYADPSILYISLHRYdeGN-FFPGSGAPNEV 230
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1698285192 210 GAESGRYYCLNVPLRDGID----DQSYRQLFQPVIKQVVDFYQPTCIVLQCGADSL 261
Cdd:cd10009   231 GTGLGEGYNINIAWTGGLDppmgDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDAL 286
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
20-304 4.76e-20

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: 90.68  E-value: 4.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  20 AGHPMKPHRLSLTHSLVLHYGLYKKMMVFKPYKASQHDMCRFHSEDYIDFLQKVSPNNMQGFTKSLNTFnvgDDCPVFPG 99
Cdd:cd11682     5 ESFPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYVALMKSTQYMTEEELRTLADTY---DSVYLHPN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 100 LFEFCSRYTGASLQGATQLNH-KICD-IAINWAGGlHHAKKFEASGFCYVNDIVISILELLKYH--PRVLYIDIDIHHGD 175
Cdd:cd11682    82 SYSCACLAVGSVLQLVDKVLGgEIRNgLAIVRPPG-HHAQHDKMDGYCMFNNVAIAARYAQQKHgvQRVLIVDWDVHHGQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 176 GVQEAFYLTDRVMTVSFHKY-GNYFFP--GTGDMYEVGAESGRYYCLNVPL-RDGIDDQSYRQLFQPVIKQVVDFYQPTC 251
Cdd:cd11682   161 GTQFIFEQDPSVLYFSIHRYeQGRFWPhlKESDSSAVGFGRGEGYNINVPWnQVGMRDADYIAAFLHVLLPVALEFQPQL 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1698285192 252 IVLQCGADSLGCDRLGCFNLSIRGHGECVEFVKSFKIPLLVLG-GGGYTVRNVA 304
Cdd:cd11682   241 VLVAAGFDAVIGDPKGEMAATPACFAHLTHLLMGLAGGKLILSlEGGYNLRSLA 294
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
26-313 8.76e-14

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


Pssm-ID: 212546 [Multi-domain]  Cd Length: 337  Bit Score: 71.82  E-value: 8.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192  26 PHRLSLTHSLVLHYGLYKKMMVFKPYKASQHDMCRFHSEDYIDF---LQKVSPNNMQGFTKSLNTFNVgddcpvFPGLFE 102
Cdd:cd11683    11 PERLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLvreTQVMNKEELMAISGKYDAVYF------HPNTFH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 103 fCSRYT-GASLQGATQ-LNHKICD-IAINWAGGlHHAKKFEASGFCYVNDIVISILELLKYH--PRVLYIDIDIHHGDGV 177
Cdd:cd11683    85 -CARLAaGATLQLVDAvLTGEVQNgMALVRPPG-HHSQRNAANGFCVFNNVAIAAEYAKKKYglHRILIVDWDVHHGQGI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698285192 178 QEAFYLTDRVMTVSFHKYGN-YFFPG--TGDMYEVGAESGRYYCLNVPLRD-GIDDQSYRQLFQPVIKQVVDFYQPTCIV 253
Cdd:cd11683   163 QYIFEEDPSVLYFSWHRYEHqRFWPFlrESDYDAVGRGKGLGFNINLPWNKvGMGNADYLAAFFHVLLPLAFEFDPELVL 242
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698285192 254 LQCGADSLGCDRLGCFNLSirghGECVEFVKSFKIPL-----LVLGGGGYTVRNVAR--CWTFETSL 313
Cdd:cd11683   243 VSAGFDSAIGDPEGQMCAT----PECFAHLTHLLMVLaggklCAVLEGGYHLESLAEsvCMTVQTLL 305
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
134-179 8.27e-07

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


Pssm-ID: 212522 [Multi-domain]  Cd Length: 353  Bit Score: 50.53  E-value: 8.27e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1698285192 134 HHAKKFEASGFCYVNDIVISILELLKYH--PRVLYIDIDIHHGDGVQE 179
Cdd:cd09998   120 HHCSESTPSGFCWVNNVHVGAAHAYLTHgiTRVVILDIDLHHGNGTQD 167
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH