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Conserved domains on  [gi|20070354|ref|NP_114408|]
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polyamine deacetylase HDAC10 isoform 1 [Homo sapiens]

Protein Classification

histone deacetylase 10( domain architecture ID 10184839)

histone deacetylase 10 (HD10) is a class IIb Zn-dependent histone deacetylase, which functions as polyamine deacetylase (PDAC) that acts preferentially on N(8)-acetylspermidine, and also on acetylcadaverine and acetylputrescine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 18-354 0e+00

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: 669.65  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  18 WDDPECEIERPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSLVRETQVLGKEELQALSGQFDAIYFHP 97
Cdd:cd11683   1 WDDPECEIEVPERLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRETQVMNKEELMAISGKYDAVYFHP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  98 STFHCARLAAGAGLQLVDAVLTGAVQNGLALVRPPGHHGQRAAANGFCVFNNVAIAAAHAKQKHGLHRILVVDWDVHHGQ 177
Cdd:cd11683  81 NTFHCARLAAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYAKKKYGLHRILIVDWDVHHGQ 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 178 GIQYLFEDDPSVLYFSWHRYEHGRFWPFLRESDADAVGRGQGLGFTVNLPWNQVGMGNADYVAAFLHLLLPLAFEFDPEL 257
Cdd:cd11683 161 GIQYIFEEDPSVLYFSWHRYEHQRFWPFLRESDYDAVGRGKGLGFNINLPWNKVGMGNADYLAAFFHVLLPLAFEFDPEL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 258 VLVSAGFDSAIGDPEGQMQATPECFAHLTQLLQVLAGGRVCAVLEGGYHLESLAESVCMTVQTLLGDPAPPLSGPMAPCQ 337
Cdd:cd11683 241 VLVSAGFDSAIGDPEGQMCATPECFAHLTHLLMVLAGGKLCAVLEGGYHLESLAESVCMTVQTLLGDPLPRLSGEMTPCQ 320

                       330
                ....*....|....*..
gi 20070354 338 SALESIQSARAAQAPHW 354
Cdd:cd11683 321 SALESIQNVRAAQAPYW 337
Arginase_HDAC super family cl17011
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 562-634 6.90e-07

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.


The actual alignment was detected with superfamily member cd11600:

Pssm-ID: 450134 [Multi-domain]  Cd Length: 313  Bit Score: 51.58  E-value: 6.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 562 LVLPLAYGFQPDLVLVALG--------PGHGLQGPHA-ALLAAMLRGLAGGRVLALLEE----NSTPQLAGILARVLNGE 628
Cdd:cd11600 228 IVMPIAYEFDPDLVIISAGfdaadgdeLGQCHVTPAGyAHMTHMLMSLAGGKLVVALEGgynlDAISDSALAVAKVLLGE 307


                ....*.
gi 20070354 629 APPSLG 634
Cdd:cd11600 308 APPKLP 313
 
Name Accession Description Interval E-value
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 18-354 0e+00

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: 669.65  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  18 WDDPECEIERPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSLVRETQVLGKEELQALSGQFDAIYFHP 97
Cdd:cd11683   1 WDDPECEIEVPERLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRETQVMNKEELMAISGKYDAVYFHP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  98 STFHCARLAAGAGLQLVDAVLTGAVQNGLALVRPPGHHGQRAAANGFCVFNNVAIAAAHAKQKHGLHRILVVDWDVHHGQ 177
Cdd:cd11683  81 NTFHCARLAAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYAKKKYGLHRILIVDWDVHHGQ 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 178 GIQYLFEDDPSVLYFSWHRYEHGRFWPFLRESDADAVGRGQGLGFTVNLPWNQVGMGNADYVAAFLHLLLPLAFEFDPEL 257
Cdd:cd11683 161 GIQYIFEEDPSVLYFSWHRYEHQRFWPFLRESDYDAVGRGKGLGFNINLPWNKVGMGNADYLAAFFHVLLPLAFEFDPEL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 258 VLVSAGFDSAIGDPEGQMQATPECFAHLTQLLQVLAGGRVCAVLEGGYHLESLAESVCMTVQTLLGDPAPPLSGPMAPCQ 337
Cdd:cd11683 241 VLVSAGFDSAIGDPEGQMCATPECFAHLTHLLMVLAGGKLCAVLEGGYHLESLAESVCMTVQTLLGDPLPRLSGEMTPCQ 320

                       330
                ....*....|....*..
gi 20070354 338 SALESIQSARAAQAPHW 354
Cdd:cd11683 321 SALESIQNVRAAQAPYW 337
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 26-321 4.07e-119

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


Pssm-ID: 425906 [Multi-domain]  Cd Length: 298  Bit Score: 357.32  E-value: 4.07e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354    26 ERPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSLVRETQVLGKEELQALSGQ-FDAIYFHPSTFHCAR 104
Cdd:pfam00850   3 ENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAAPEGGALLLLSYLSgDDDTPVSPGSYEAAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354   105 LAAGAGLQLVDAVLTGAVQNGLALVRPPGHHGQRAAANGFCVFNNVAIAAAHAKQKHGLHRILVVDWDVHHGQGIQYLFE 184
Cdd:pfam00850  83 LAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLKRVAIVDFDVHHGNGTQEIFY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354   185 DDPSVLYFSWHRYEHGrFWPFlrESDADAVGRGQGLGFTVNLPWNqVGMGNADYVAAFLHLLLPLAFEFDPELVLVSAGF 264
Cdd:pfam00850 163 DDPSVLTLSIHQYPGG-FYPG--TGFADETGEGKGKGYTLNVPLP-PGTGDAEYLAAFEEILLPALEEFQPDLILVSAGF 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354   265 DSAIGDPEGQMQATPECFAHLTQLLQVLA---GGRVCAVLEGGYHLESLAESVCMTVQTL 321
Cdd:pfam00850 239 DAHAGDPLGGLNLTTEGFAEITRILLELAdplCIRVVSVLEGGYNLDALARSATAVLAAL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 3-323 3.81e-101

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 311.27  E-value: 3.81e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354   3 TALVYHEDMTATRLLWDDPECeierPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSLVRETQVLGKee 82
Cdd:COG0123   1 TALIYHPDYLLHDLGPGHPEP----PERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAASLDGG-- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  83 lqalSGQFDAI-YFHPSTFHCARLAAGAGLQLVDAVLTGAVQNGLALVRPPGHHGQRAAANGFCVFNNVAIAAAHAkQKH 161
Cdd:COG0123  75 ----YGQLDPDtPVSPGTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGFCLFNNAAIAARYL-LAK 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 162 GLHRILVVDWDVHHGQGIQYLFEDDPSVLYFSWHRYehgRFWPFLreSDADAVGRGQGLGFTVNLPWnQVGMGNADYVAA 241
Cdd:COG0123 150 GLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD---PLYPGT--GAADETGEGAGEGSNLNVPL-PPGTGDAEYLAA 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 242 FLHLLLPLAFEFDPELVLVSAGFDSAIGDPEGQMQATPECFAHLTQLLQVLA---GGRVCAVLEGGYHLESLAESVCMTV 318
Cdd:COG0123 224 LEEALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELAdhcGGPVVSVLEGGYNLDALARSVAAHL 303


                ....*
gi 20070354 319 QTLLG 323
Cdd:COG0123 304 ETLLG 308
PTZ00063 PTZ00063
histone deacetylase; Provisional
 134-295 2.03e-15

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 79.08  E-value: 2.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  134 HHGQRAAANGFCVFNNVAIAAAHAKQKHGlhRILVVDWDVHHGQGIQYLFEDDPSVLYFSWHRYehGRFWPflRESDADA 213
Cdd:PTZ00063 137 HHAKRSEASGFCYINDIVLGILELLKYHA--RVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFP--GTGDVTD 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  214 VGRGQGLGFTVNLPWNQvGMGNADYVAAFLHLLLPLAFEFDPELVLVSAGFDSAIGDPEGQMQAT----PECFAHLTQL- 288
Cdd:PTZ00063 211 IGVAQGKYYSVNVPLND-GIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTikghAACVEFVRSLn 289


                 ....*....
gi 20070354  289 --LQVLAGG 295
Cdd:PTZ00063 290 ipLLVLGGG 298
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 562-634 6.90e-07

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: 51.58  E-value: 6.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 562 LVLPLAYGFQPDLVLVALG--------PGHGLQGPHA-ALLAAMLRGLAGGRVLALLEE----NSTPQLAGILARVLNGE 628
Cdd:cd11600 228 IVMPIAYEFDPDLVIISAGfdaadgdeLGQCHVTPAGyAHMTHMLMSLAGGKLVVALEGgynlDAISDSALAVAKVLLGE 307


                ....*.
gi 20070354 629 APPSLG 634
Cdd:cd11600 308 APPKLP 313
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 547-625 6.00e-03

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: 39.14  E-value: 6.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354   547 PLPVMTG--GFLSCILGLVLPLAYGFQPDLVLVALG-------PGHGLQGPHAAL--LAAMLRGLA---GGRVLALLE-- 610
Cdd:pfam00850 202 PLPPGTGdaEYLAAFEEILLPALEEFQPDLILVSAGfdahagdPLGGLNLTTEGFaeITRILLELAdplCIRVVSVLEgg 281

                          90
                  ....*....|....*..
gi 20070354   611 --ENSTPQLAGILARVL 625
Cdd:pfam00850 282 ynLDALARSATAVLAAL 298
 
Name Accession Description Interval E-value
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 18-354 0e+00

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: 669.65  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  18 WDDPECEIERPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSLVRETQVLGKEELQALSGQFDAIYFHP 97
Cdd:cd11683   1 WDDPECEIEVPERLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRETQVMNKEELMAISGKYDAVYFHP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  98 STFHCARLAAGAGLQLVDAVLTGAVQNGLALVRPPGHHGQRAAANGFCVFNNVAIAAAHAKQKHGLHRILVVDWDVHHGQ 177
Cdd:cd11683  81 NTFHCARLAAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYAKKKYGLHRILIVDWDVHHGQ 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 178 GIQYLFEDDPSVLYFSWHRYEHGRFWPFLRESDADAVGRGQGLGFTVNLPWNQVGMGNADYVAAFLHLLLPLAFEFDPEL 257
Cdd:cd11683 161 GIQYIFEEDPSVLYFSWHRYEHQRFWPFLRESDYDAVGRGKGLGFNINLPWNKVGMGNADYLAAFFHVLLPLAFEFDPEL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 258 VLVSAGFDSAIGDPEGQMQATPECFAHLTQLLQVLAGGRVCAVLEGGYHLESLAESVCMTVQTLLGDPAPPLSGPMAPCQ 337
Cdd:cd11683 241 VLVSAGFDSAIGDPEGQMCATPECFAHLTHLLMVLAGGKLCAVLEGGYHLESLAESVCMTVQTLLGDPLPRLSGEMTPCQ 320

                       330
                ....*....|....*..
gi 20070354 338 SALESIQSARAAQAPHW 354
Cdd:cd11683 321 SALESIQNVRAAQAPYW 337
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 18-354 0e+00

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: 571.56  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  18 WDDPECEIERPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSLVRETQVLGKEELQALSGQFDAIYFHP 97
Cdd:cd10002   1 CNWDSNHIECPERLEAILERLTQDGLLERCVKIPAREAEEDEILLVHSQEYIDLVKSTETMEKEELESLCSGYDSVYLCP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  98 STFHCARLAAGAGLQLVDAVLTGAVQNGLALVRPPGHHGQRAAANGFCVFNNVAIAAAHAKQKHGLHRILVVDWDVHHGQ 177
Cdd:cd10002  81 STYEAARLAAGSTIELVKAVMAGKIQNGFALIRPPGHHAMRNEANGYCIFNNVAIAAKYAIEKLGLKRILIVDWDVHHGQ 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 178 GIQYLFEDDPSVLYFSWHRYEHGRFWPFLRESDADAVGRGQGLGFTVNLPWNQVGMGNADYVAAFLHLLLPLAFEFDPEL 257
Cdd:cd10002 161 GTQQGFYEDPRVLYFSIHRYEHGRFWPHLFESDYDYIGVGHGYGFNVNVPLNQTGLGDADYLAIFHHILLPLALEFQPEL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 258 VLVSAGFDSAIGDPEGQMQATPECFAHLTQLLQVLAGGRVCAVLEGGYHLESLAESVCMTVQTLLGDPAPPLSgPMAPCQ 337
Cdd:cd10002 241 VLVSAGFDASIGDPEGEMAVTPAGYAHLTRLLMGLAGGKLLLVLEGGYLLESLAESVSMTLRGLLGDPLPPLA-PPIPIR 319

                       330
                ....*....|....*..
gi 20070354 338 SALESIQSARAAQAPHW 354
Cdd:cd10002 320 SVLETILNAIAHLSPRW 336
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
 7-357 4.18e-175

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: 502.64  E-value: 4.18e-175
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354   7 YHEDMTATRLLWDD--PECeierPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSLVRETQVLGKEELQ 84
Cdd:cd10003   1 YDQRMMNHHNLWDPghPEC----PQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHLDEMKSLEKMKPRELN 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  85 ALSGQFDAIYFHPSTFHCARLAAGAGLQLVDAVLTGAVQNGLALVRPPGHHGQRAAANGFCVFNNVAIAAAHAKQKHGLH 164
Cdd:cd10003  77 RLGKEYDSIYIHPDSYQCALLAAGCVLQVVEAVLTGESRNGVAIVRPPGHHAEQDTACGFCFFNNVAIAARYAQKKYGLK 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 165 RILVVDWDVHHGQGIQYLFEDDPSVLYFSWHRYEHGRFWPFLRESDADAVGRGQGLGFTVNLPWNQVGMGNADYVAAFLH 244
Cdd:cd10003 157 RILIVDWDVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSPEGNYDVVGKGKGEGFNVNIPWNKGGMGDAEYIAAFQQ 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 245 LLLPLAFEFDPELVLVSAGFDSAIGDPEGQMQATPECFAHLTQLLQVLAGGRVCAVLEGGYHLESLAESVCMTVQTLLGD 324
Cdd:cd10003 237 VVLPIAYEFNPELVLVSAGFDAARGDPLGGCKVTPEGYAHMTHMLMSLAGGRVIVILEGGYNLTSISESMSMCTKTLLGD 316

                       330       340       350
                ....*....|....*....|....*....|...
gi 20070354 325 PAPPLSGPMAPCQSALESIQSARAAQAPHWKSL 357
Cdd:cd10003 317 PPPVLDLPRPPCSSALKSINNVLQVHQKYWKSL 349
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
 17-354 7.95e-163

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: 470.87  E-value: 7.95e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  17 LWDD--PECeierPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSLVRETQVLGKEELQALSGQFDAIY 94
Cdd:cd11682   2 LWDEsfPEC----PERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYVALMKSTQYMTEEELRTLADTYDSVY 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  95 FHPSTFHCARLAAGAGLQLVDAVLTGAVQNGLALVRPPGHHGQRAAANGFCVFNNVAIAAAHAKQKHGLHRILVVDWDVH 174
Cdd:cd11682  78 LHPNSYSCACLAVGSVLQLVDKVLGGEIRNGLAIVRPPGHHAQHDKMDGYCMFNNVAIAARYAQQKHGVQRVLIVDWDVH 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 175 HGQGIQYLFEDDPSVLYFSWHRYEHGRFWPFLRESDADAVGRGQGLGFTVNLPWNQVGMGNADYVAAFLHLLLPLAFEFD 254
Cdd:cd11682 158 HGQGTQFIFEQDPSVLYFSIHRYEQGRFWPHLKESDSSAVGFGRGEGYNINVPWNQVGMRDADYIAAFLHVLLPVALEFQ 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 255 PELVLVSAGFDSAIGDPEGQMQATPECFAHLTQLLQVLAGGRVCAVLEGGYHLESLAESVCMTVQTLLGDPAPPLSGPMA 334
Cdd:cd11682 238 PQLVLVAAGFDAVIGDPKGEMAATPACFAHLTHLLMGLAGGKLILSLEGGYNLRSLAEGVCASLKALLGDPCPMLESPGA 317

                       330       340
                ....*....|....*....|
gi 20070354 335 PCQSALESIQSARAAQAPHW 354
Cdd:cd11682 318 PCRSALASVSCTISALEPFW 337
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
 26-322 5.40e-131

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: 387.62  E-value: 5.40e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  26 ERPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSLVRETQvlgkeelQALSGQFDA-IYFHPSTFHCAR 104
Cdd:cd09992   3 ERPERLLAILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYIERVEETC-------EAGGGYLDPdTYVSPGSYEAAL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 105 LAAGAGLQLVDAVLTGAVQNGLALVRPPGHHGQRAAANGFCVFNNVAIAAAHAKQKHGLHRILVVDWDVHHGQGIQYLFE 184
Cdd:cd09992  76 LAAGAALAAVDAVLSGEAENAFALVRPPGHHAEPDRAMGFCLFNNVAIAARYAQKRYGLKRVLIVDWDVHHGNGTQDIFY 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 185 DDPSVLYFSWHRYEhgrFWPFlrESDADAVGRGQGLGFTVNLPWNQvGMGNADYVAAFLHLLLPLAFEFDPELVLVSAGF 264
Cdd:cd09992 156 DDPSVLYFSIHQYP---FYPG--TGAAEETGGGAGEGFTINVPLPP-GSGDAEYLAAFEEVLLPIAREFQPDLVLVSAGF 229

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20070354 265 DSAIGDPEGQMQATPECFAHLTQLLQVLA----GGRVCAVLEGGYHLESLAESVCMTVQTLL 322
Cdd:cd09992 230 DAHRGDPLGGMNLTPEGYARLTRLLKELAdehcGGRLVFVLEGGYNLEALAESVLAVLEALL 291
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 26-330 8.81e-128

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


Pssm-ID: 212542 [Multi-domain]  Cd Length: 313  Bit Score: 380.15  E-value: 8.81e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  26 ERPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSLVRETQVLGKEELQALSGQF--DAIYFHPSTFHCA 103
Cdd:cd11600   5 EDPSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEHWDRVEATEKMSDEQLKDRTEIFerDSLYVNNDTAFCA 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 104 RLAAGAGLQLVDAVLTGAVQNGLALVRPPGHHGQRAAANGFCVFNNVAIAAAHAKQKHGLH--RILVVDWDVHHGQGIQY 181
Cdd:cd11600  85 RLSCGGAIEACRAVAEGRVKNAFAVVRPPGHHAEPDESMGFCFFNNVAVAAKWLQTEYPDKikKILILDWDIHHGNGTQR 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 182 LFEDDPSVLYFSWHRYEHGRFWPFLRESDADAVGRGQGLGFTVNLPWNQVGMGNADYVAAFLHLLLPLAFEFDPELVLVS 261
Cdd:cd11600 165 AFYDDPNVLYISLHRFENGGFYPGTPYGDYESVGEGAGLGFNVNIPWPQGGMGDADYIYAFQRIVMPIAYEFDPDLVIIS 244

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20070354 262 AGFDSAIGDPEGQMQATPECFAHLTQLLQVLAGGRVCAVLEGGYHLESLAESVCMTVQTLLGDPAPPLS 330
Cdd:cd11600 245 AGFDAADGDELGQCHVTPAGYAHMTHMLMSLAGGKLVVALEGGYNLDAISDSALAVAKVLLGEAPPKLP 313
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 26-321 4.07e-119

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


Pssm-ID: 425906 [Multi-domain]  Cd Length: 298  Bit Score: 357.32  E-value: 4.07e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354    26 ERPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSLVRETQVLGKEELQALSGQ-FDAIYFHPSTFHCAR 104
Cdd:pfam00850   3 ENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAAPEGGALLLLSYLSgDDDTPVSPGSYEAAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354   105 LAAGAGLQLVDAVLTGAVQNGLALVRPPGHHGQRAAANGFCVFNNVAIAAAHAKQKHGLHRILVVDWDVHHGQGIQYLFE 184
Cdd:pfam00850  83 LAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLKRVAIVDFDVHHGNGTQEIFY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354   185 DDPSVLYFSWHRYEHGrFWPFlrESDADAVGRGQGLGFTVNLPWNqVGMGNADYVAAFLHLLLPLAFEFDPELVLVSAGF 264
Cdd:pfam00850 163 DDPSVLTLSIHQYPGG-FYPG--TGFADETGEGKGKGYTLNVPLP-PGTGDAEYLAAFEEILLPALEEFQPDLILVSAGF 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354   265 DSAIGDPEGQMQATPECFAHLTQLLQVLA---GGRVCAVLEGGYHLESLAESVCMTVQTL 321
Cdd:pfam00850 239 DAHAGDPLGGLNLTTEGFAEITRILLELAdplCIRVVSVLEGGYNLDALARSATAVLAAL 298
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 2-354 3.07e-111

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: 340.09  E-value: 3.07e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354   2 GTALVYHEDMTATRLLWDDPECEIERPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSL------VRET 75
Cdd:cd11681   2 TTGLAYDPLMLKHQCICGNNSSHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTLLygtnplSRLK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  76 QVLGKEELQALS----------GQFDAIYFHP-STFHCARLAAGAGLQLVDAVLTGAVQNGLALVRPPGHHGQRAAANGF 144
Cdd:cd11681  82 LDPTKLAGLPQKsfvrlpcggiGVDSDTVWNElHTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQAMGF 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 145 CVFNNVAIAAAHAKQKHGLHRILVVDWDVHHGQGIQYLFEDDPSVLYFSWHRYEHGRFWPflRESDADAVGRGQGLGFTV 224
Cdd:cd11681 162 CFFNSVAIAAKQLQQKLKLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFP--GTGAPTEVGSGAGEGFNV 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 225 NLPWN---QVGMGNADYVAAFLHLLLPLAFEFDPELVLVSAGFDSAIGDPE--GQMQATPECFAHLTQLLQVLAGGRVCA 299
Cdd:cd11681 240 NIAWSgglDPPMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPPplGGYKVSPACFGYMTRQLMNLAGGKVVL 319

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 20070354 300 VLEGGYHLESLAESVCMTVQTLLGDPAPPLSGPM---APCQSALESIQSARAAQAPHW 354
Cdd:cd11681 320 ALEGGYDLTAICDASEACVRALLGDELDPLSEEElerRPNPNAVTSLEKVIAIQSPYW 377
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 3-323 3.81e-101

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 311.27  E-value: 3.81e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354   3 TALVYHEDMTATRLLWDDPECeierPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSLVRETQVLGKee 82
Cdd:COG0123   1 TALIYHPDYLLHDLGPGHPEP----PERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAASLDGG-- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  83 lqalSGQFDAI-YFHPSTFHCARLAAGAGLQLVDAVLTGAVQNGLALVRPPGHHGQRAAANGFCVFNNVAIAAAHAkQKH 161
Cdd:COG0123  75 ----YGQLDPDtPVSPGTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGFCLFNNAAIAARYL-LAK 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 162 GLHRILVVDWDVHHGQGIQYLFEDDPSVLYFSWHRYehgRFWPFLreSDADAVGRGQGLGFTVNLPWnQVGMGNADYVAA 241
Cdd:COG0123 150 GLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD---PLYPGT--GAADETGEGAGEGSNLNVPL-PPGTGDAEYLAA 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 242 FLHLLLPLAFEFDPELVLVSAGFDSAIGDPEGQMQATPECFAHLTQLLQVLA---GGRVCAVLEGGYHLESLAESVCMTV 318
Cdd:COG0123 224 LEEALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELAdhcGGPVVSVLEGGYNLDALARSVAAHL 303


                ....*
gi 20070354 319 QTLLG 323
Cdd:COG0123 304 ETLLG 308
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
 26-322 1.14e-86

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: 272.85  E-value: 1.14e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  26 ERPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSLVRetQVLGKEELQALSGqfDAIYfHPSTFHCARL 105
Cdd:cd11599   3 ESPERLEAILDALIASGLDRLLRQLEAPPATREQLLRVHDAAYVDRLE--AAAPEEGLVQLDP--DTAM-SPGSLEAALR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 106 AAGAGLQLVDAVLTGAVQNGLALVRPPGHHGQRAAANGFCVFNNVAIAAAHAKQKHGLHRILVVDWDVHHGQGIQYLFED 185
Cdd:cd11599  78 AAGAVVAAVDAVMAGEARNAFCAVRPPGHHAERDKAMGFCLFNNVAIAAAHALAHHGLERVAIVDFDVHHGNGTEDIFRD 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 186 DPSVLYFSWHRYehgRFWPFlrESDADAVGRGQglgfTVNLPWNQvGMGNADYVAAFLHLLLPLAFEFDPELVLVSAGFD 265
Cdd:cd11599 158 DPRVLFCSSHQH---PLYPG--TGAPDETGHGN----IVNVPLPA-GTGGAEFREAVEDRWLPALDAFKPDLILISAGFD 227

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20070354 266 SAIGDPEGQMQATPECFAHLTQLLQVLA----GGRVCAVLEGGYHLESLAESVCMTVQTLL 322
Cdd:cd11599 228 AHRDDPLAQLNLTEEDYAWITEQLMDVAdrycDGRIVSVLEGGYDLSALARSVAAHVRALM 288
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
 3-341 1.90e-84

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


Pssm-ID: 212521 [Multi-domain]  Cd Length: 359  Bit Score: 269.82  E-value: 1.90e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354   3 TALVYHEDM-----------TATRLLWDDPECEIERPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSL 71
Cdd:cd09996   1 TGFVWDERYlwhdtgtgalfLPVGGLLVQPGRHPENPETKRRIKNLLEVSGLSDHLVLITPRPATDEELLRVHTPEYIDR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  72 VRETQVLGKEELQALSgqfdaiYFHPSTFHCARLAAGAGLQLVDAVLTGAVQNGLALVRPPGHHGQRAAANGFCVFNNVA 151
Cdd:cd09996  81 VKAASAAGGGEAGGGT------PFGPGSYEIALLAAGGAIAAVDAVLDGEVDNAYALVRPPGHHAEPDQGMGFCLFNNVA 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 152 IAAAHAKQKHGLHRILVVDWDVHHGQGIQYLFEDDPSVLYFSWHryEHGRFWPflRESDADAVGRGQGLGFTVNLPWNQv 231
Cdd:cd09996 155 IAARHALAVGGVKRVAVVDWDVHHGNGTQAIFYDDPDVLTISLH--QDRCFPP--DSGAVEERGEGAGEGYNLNIPLPP- 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 232 GMGNADYVAAFLHLLLPLAFEFDPELVLVSAGFDSAIGDPEGQMQATPECFAHLTQLLQVLA----GGRVCAVLEGGYHL 307
Cdd:cd09996 230 GSGDGAYLHAFERIVLPALRAFRPELIIVASGFDASAFDPLGRMMLTSDGFRALTRKLRDLAdelcGGRLVMVHEGGYSE 309

                       330       340       350
                ....*....|....*....|....*....|....
gi 20070354 308 ESLAESVCMTVQTLLGDPApPLSGPMAPCQSALE 341
Cdd:cd09996 310 AYVPFCGLAVLEELSGVRT-GIADPLLYYPEAQG 342
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
 3-354 2.10e-84

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: 270.34  E-value: 2.10e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354   3 TALVYHEDMTATRLLWDDPECEIERPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVsLVRETQVLGKEE 82
Cdd:cd10008   3 TGLVYDSVMLKHQCSCGDNSNHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHV-LLYGTNPLSRLK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  83 LQ--ALSGQF-----------------DAIYFHPSTFHCARLAAGAGLQLVDAVLTGAVQNGLALVRPPGHHGQRAAANG 143
Cdd:cd10008  82 LDngKLAGLLaqrmfvmlpcggvgvdtDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMG 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 144 FCVFNNVAIAAAHAKQKHGLHRILVVDWDVHHGQGIQYLFEDDPSVLYFSWHRYEHGRFWPflRESDADAVGRGQGLGFT 223
Cdd:cd10008 162 FCFFNSVAIACRQLQQQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFP--GSGAVDEVGAGSGEGFN 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 224 VNLPWN---QVGMGNADYVAAFLHLLLPLAFEFDPELVLVSAGFDSAIGDPE--GQMQATPECFAHLTQLLQVLAGGRVC 298
Cdd:cd10008 240 VNVAWAgglDPPMGDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHPAplGGYHVSAKCFGYMTQQLMNLAGGAVV 319

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20070354 299 AVLEGGYHLESLAESVCMTVQTLLG---DPAPPLSGPMAPCQSALESIQSARAAQAPHW 354
Cdd:cd10008 320 LALEGGHDLTAICDASEACVAALLGnevDPLSEESWKQKPNLNAIRSLEAVIRVHSKYW 378
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
 3-364 1.53e-83

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: 269.21  E-value: 1.53e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354   3 TALVYHEDMTATRLLWDDPECEIERPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSL-----VRETQV 77
Cdd:cd10006   6 TGLVYDTLMLKHQCTCGNSNSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLygtnpLNRQKL 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  78 LGKEELQALSGQF------------DAIYFHPSTFHCARLAAGAGLQLVDAVLTGAVQNGLALVRPPGHHGQRAAANGFC 145
Cdd:cd10006  86 DSKKLLGSLASVFvrlpcggvgvdsDTIWNEVHSSGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFC 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 146 VFNNVAIAAAHAKQKHGLHRILVVDWDVHHGQGIQYLFEDDPSVLYFSWHRYEHGRFWPflRESDADAVGRGQGLGFTVN 225
Cdd:cd10006 166 YFNSVAIAAKLLQQRLNVSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYDDGNFFP--GSGAPDEVGTGPGVGFNVN 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 226 LPWN---QVGMGNADYVAAFLHLLLPLAFEFDPELVLVSAGFDSAIGDPE--GQMQATPECFAHLTQLLQVLAGGRVCAV 300
Cdd:cd10006 244 MAFTgglDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTplGGYNLSAKCFGYLTKQLMGLAGGRIVLA 323

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20070354 301 LEGGYHLESLAESVCMTVQTLLG---DPAPPLSGPMAPCQSALESIQSARAAQAPHWKSLQQQDVTA 364
Cdd:cd10006 324 LEGGHDLTAICDASEACVSALLGnelDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTA 390
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
 3-359 6.33e-83

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: 268.01  E-value: 6.33e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354   3 TALVYHEDMTATRLLWDDPECEIERPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSpEYVSLVRETQVLGKEE 82
Cdd:cd10007   5 TGLVYDTFMLKHQCTCGNTNVHPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHS-EHHTLLYGTSPLNRQK 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  83 LQA------LSGQF-------------DAIYFHPSTFHCARLAAGAGLQLVDAVLTGAVQNGLALVRPPGHHGQRAAANG 143
Cdd:cd10007  84 LDSkkllgpLSQKMyavlpcggigvdsDTVWNEMHSSSAVRMAVGCLIELAFKVAAGELKNGFAVIRPPGHHAEESTAMG 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 144 FCVFNNVAIAAAHAKQKHGLHRILVVDWDVHHGQGIQYLFEDDPSVLYFSWHRYEHGRFWPflRESDADAVGRGQGLGFT 223
Cdd:cd10007 164 FCFFNSVAIAAKLLQQKLNVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGNFFP--GSGAPDEVGAGPGVGFN 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 224 VNLPWN---QVGMGNADYVAAFLHLLLPLAFEFDPELVLVSAGFDSAIG--DPEGQMQATPECFAHLTQLLQVLAGGRVC 298
Cdd:cd10007 242 VNIAWTggvDPPIGDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGhqSPLGGYSVTAKCFGHLTKQLMTLAGGRVV 321

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20070354 299 AVLEGGYHLESLAESVCMTVQTLLGDPAPPLSGPM---APCQSALESIQSARAAQAPHWKSLQQ 359
Cdd:cd10007 322 LALEGGHDLTAICDASEACVSALLGMELTPLDNTVlqqKPNDNAVATLERVIEIQSKHWSCLKR 385
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
 3-355 6.52e-71

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: 234.91  E-value: 6.52e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354   3 TALVYHEDMTATRLLWDDPECEIERPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSpEYVSLVRETQVLGKEE 82
Cdd:cd10009   3 TGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHS-EHHSLLYGTNPLDGQK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  83 LQ-------------------ALSGQFDAIYFHPSTFHCARLAAGAGLQLVDAVLTGAVQNGLALVRPPGHHGQRAAANG 143
Cdd:cd10009  82 LDprillgddsqkffsslpcgGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMG 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 144 FCVFNNVAIAAAHAKQKHGLHRILVVDWDVHHGQGIQYLFEDDPSVLYFSWHRYEHGRFWPflRESDADAVGRGQGLGFT 223
Cdd:cd10009 162 FCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFP--GSGAPNEVGTGLGEGYN 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 224 VNLPWN---QVGMGNADYVAAFLHLLLPLAFEFDPELVLVSAGFDSAIGD--PEGQMQATPECFAHLTQLLQVLAGGRVC 298
Cdd:cd10009 240 INIAWTgglDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLADGRVV 319

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 299 AVLEGGYHLESLAESVCMTVQTLLGDPAPPLSGPM---APCQSALESIQSARAAQAPHWK 355
Cdd:cd10009 320 LALEGGHDLTAICDASEACVNALLGNELEPLAEDIlhqSPNMNAVISLQKIIEIQSKYWK 379
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
 26-314 1.41e-69

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: 228.58  E-value: 1.41e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  26 ERPERLTAALDRLRQRGLEqrcLRLSAREASEEELGLVHSPEYVSLVREtqvlgkeelqalsgqFDAI-YFHPSTFHCAR 104
Cdd:cd10001  27 ENPERAEAILDALKRAGLG---EVLPPRDFGLEPILAVHDPDYVDFLET---------------ADTDtPISEGTWEAAL 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 105 LAAGAGLQLVDAVLTGAvQNGLALVRPPGHHGQRAAANGFCVFNNVAIAAAHAKQKHGlhRILVVDWDVHHGQGIQYLFE 184
Cdd:cd10001  89 AAADTALTAADLVLEGE-RAAYALCRPPGHHAGRDRAGGFCYFNNAAIAAQYLRDRAG--RVAILDVDVHHGNGTQEIFY 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 185 DDPSVLYFSWHRYEHGrFWPFlRESDADAVGRGQGLGFTVNLPWnQVGMGNADYVAAFLHLLLPLAfEFDPELVLVSAGF 264
Cdd:cd10001 166 ERPDVLYVSIHGDPRT-FYPF-FLGFADETGEGEGEGYNLNLPL-PPGTGDDDYLAALDEALAAIA-AFGPDALVVSLGF 241

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 20070354 265 DSAIGDPEGQMQATPECFAHLTQLLQVLaGGRVCAVLEGGYHLESLAESV 314
Cdd:cd10001 242 DTHEGDPLSDFKLTTEDYARIGRRIAAL-GLPTVFVQEGGYNVDALGRNA 290
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
 30-321 3.11e-60

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: 203.05  E-value: 3.11e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  30 RLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSLVRETQVLGKEELQALSGQFDAIYFHPSTFHCARLAAGA 109
Cdd:cd09301   1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKANFAVATITESKPVIFGPNFPVQRHYFRGARLSTGG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 110 GLQLVDAVLTGAVQNGLALVRPPGHHGQRAAANGFCVFNNVAIAAAHAKQKhGLHRILVVDWDVHHGQGIQYLFEDDPSV 189
Cdd:cd09301  81 VVEAAELVAKGELERAFAVVGAGGHHAGKSRAWGFCYFNDVVLAIKFLRER-GISRILIIDTDAHHGDGTREAFYDDDRV 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 190 LYFSWHRYehgrfwpflresDADAVGRGQGLGFTVNLPWNQvGMGNADYVAAFLHLLLPLAFEFDPELVLVSAGFDSAIG 269
Cdd:cd09301 160 LHMSFHNY------------DIYPFGRGKGKGYKINVPLED-GLGDEEYLDAVERVISKVLEEFEPEVVVLQFGHDTHEG 226

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 20070354 270 DPEGQMQATPECFAHLTQLLQVLA-GGRVCAVLEGGYHLESLAESVCMTVQTL 321
Cdd:cd09301 227 DRLGGFNLSEKGFVKLAEIVKEFArGGPILMVLGGGYNPEAAARIWTAIIKEL 279
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
 27-311 4.18e-53

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: 185.07  E-value: 4.18e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  27 RPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSLVRETQVLGKEELQALS--GQFDAIYFhPSTFHCAR 104
Cdd:cd09994  20 NPPRLSLTKDLLRALGLLPPVDLVPPRPATEEELLLFHTPDYIEAVKEASRGQEPEGRGRLglGTEDNPVF-PGMHEAAA 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 105 LAAGAGLQLVDAVLTGAVQNGlalVRPPG--HHGQRAAANGFCVFNNVAIAAAHAkQKHGLHRILVVDWDVHHGQGIQYL 182
Cdd:cd09994  99 LVVGGTLLAARLVLEGEARRA---FNPAGglHHAMRGRASGFCVYNDAAVAIERL-RDKGGLRVAYVDIDAHHGDGVQAA 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 183 FEDDPSVLYFSWHryEHGR-FWPFlrESDADAVGRGQGLGFTVNLPWNQvGMGNADYVAAFLHLLLPLAFEFDPELVLVS 261
Cdd:cd09994 175 FYDDPRVLTISLH--ESGRyLFPG--TGFVDEIGEGEGYGYAVNIPLPP-GTGDDEFLRAFEAVVPPLLRAFRPDVIVSQ 249

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 20070354 262 AGFDSAIGDPEGQMQATPECFAHLTQLLQVLA----GGRVCAVLEGGYHLESLA 311
Cdd:cd09994 250 HGADAHAGDPLTHLNLSNRAYRAAVRRIRELAdeycGGRWLALGGGGYNPDVVA 303
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 28-328 5.15e-35

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: 136.31  E-value: 5.15e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  28 PERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSLVRE-TQVLGKEELQALSGQFDAIYFHPST---FHCA 103
Cdd:cd10000  20 PNRASMVHSLIEAYGLLKQLRVVKPRVATEEELASFHSDEYIQFLKKaSNEGDNDEEPSEQQEFGLGYDCPIFegiYDYA 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 104 RLAAGAGLQLVDAVLTGAVQngLALVRPPG-HHGQRAAANGFCVFNNVAIAAAHAKQKhgLHRILVVDWDVHHGQGIQYL 182
Cdd:cd10000 100 AAVAGATLTAAQLLIDGKCK--VAINWFGGwHHAQRDEASGFCYVNDIVLGILKLREK--FDRVLYVDLDLHHGDGVEDA 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 183 FEDDPSVLYFSWHRYEHGrFWPflRESDADAVGRGQGLGFTVNLPWNQvGMGNADYVAAFlHLLLPLAFE-FDPELVLVS 261
Cdd:cd10000 176 FSFTSKVMTVSLHKYSPG-FFP--GTGDVSDVGLGKGKYYTVNVPLRD-GIQDEQYLQIF-TAVVPEIVAaFRPEAVVLQ 250

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 262 AGFDSAIGDPEGQMQATPECFAHLTQLlqVLAGGRVCAVL-EGGYHLESLAEsvCMTVQT--LLGDPAPP 328
Cdd:cd10000 251 CGADTLAGDPMGAFNLTPVGIGKCLKY--VLGWKLPTLILgGGGYNLANTAR--CWTYLTglILGEPLSS 316
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 36-306 3.64e-32

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: 125.69  E-value: 3.64e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  36 DRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSLVRETQVLGKEELQALSGQFDAIyFHPStfhcaRLAAGAglqlvd 115
Cdd:cd09993  13 EALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLESLKSGELSREEIRRIGFPWSPEL-VERT-----RLAVGG------ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 116 AVLTG--AVQNGLAlVRPPG--HHGQRAAANGFCVFNNVAIAAAHAKQKHGLHRILVVDWDVHHGQGIQYLFEDDPSVLY 191
Cdd:cd09993  81 TILAArlALEHGLA-INLAGgtHHAFPDRGEGFCVFNDIAIAARVLLAEGLVRRVLIVDLDVHQGNGTAAIFADDPSVFT 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 192 FSWHryeHGRFWPFLRE-SDADavgrgqglgftVNLPWnqvGMGNADYVAAfLHLLLPLAF-EFDPELVLVSAGFDSAIG 269
Cdd:cd09993 160 FSMH---GEKNYPFRKEpSDLD-----------VPLPD---GTGDDEYLAA-LEEALPRLLaEFRPDLVFYNAGVDVLAG 221

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 20070354 270 DPEGQMQATPEcfahltQLLQ----VLAGGR-----VCAVLEGGYH 306
Cdd:cd09993 222 DRLGRLSLSLE------GLRErdrlVLRFARargipVAMVLGGGYS 261
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
 27-320 8.88e-29

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


Pssm-ID: 212517 [Multi-domain]  Cd Length: 306  Bit Score: 116.91  E-value: 8.88e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  27 RPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSLVR----ETQVLGKEELQALSGQFDAIYFhPSTFHC 102
Cdd:cd09991  18 KPHRIRMTHSLILSYGLYKKMEIYRPRPATAEELTKFHSDDYIDFLRsvspDNMKEFKKQLERFNVGEDCPVF-DGLYEY 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 103 ARLAAGAGLQLVDAVLTGAVQ------NGLalvrppgHHGQRAAANGFCVFNNVAIAAAHAKQKHGlhRILVVDWDVHHG 176
Cdd:cd09991  97 CQLYAGGSIAAAVKLNRGQADiainwaGGL-------HHAKKSEASGFCYVNDIVLAILELLKYHQ--RVLYIDIDIHHG 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 177 QGIQYLFEDDPSVLYFSWHRYEHGRFwPFlreSDADAVGRGQGLGFTVNLPWNQvGMGNADYVAAFLHLLLPLAFEFDPE 256
Cdd:cd09991 168 DGVEEAFYTTDRVMTVSFHKFGEYFF-PG---TGLRDIGAGKGKYYAVNVPLKD-GIDDESYLQIFEPVLSKVMEVFQPS 242

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20070354 257 LVLVSAGFDSAIGDPEGQMQATP----ECFAHLTQL---LQVLAGgrvcavleGGYHLESLAEsvCMTVQT 320
Cdd:cd09991 243 AVVLQCGADSLAGDRLGCFNLSIkghaKCVKFVKSFnipLLVLGG--------GGYTLRNVAR--CWTYET 303
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
 43-306 5.28e-25

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: 105.42  E-value: 5.28e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  43 LEQRCLRLSAREASEEELGLVHSPEYVSlvretQVLGKEELQalsgqFDAIYFhPSTFHCARLAAGAGLQLVDAVLTGAV 122
Cdd:cd11680  35 LQHFDEIIEPERATRKDLTKYHDKDYVD-----FLLKKYGLE-----DDCPVF-PFLSMYVQLVAGSSLALAKHLITQVE 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 123 QNgLALVRPPG-HHGQRAAANGFCVFNNVAIAAAHAKQKhGLHRILVVDWDVHHGQGIQYLFEDDPSVLYFSWHRYEHGr 201
Cdd:cd11680 104 RD-IAINWYGGrHHAQKSRASGFCYVNDIVLAILRLRRA-RFRRVFYLDLDLHHGDGVESAFFFSKNVLTCSIHRYDPG- 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 202 FWPFLRESDADAVgrgqglGFTVNLPWNQvGMGNADYVAAFLHLLLPLAFEFDPELVLVSAGFDSAIGDPEGQMQATPEC 281
Cdd:cd11680 181 FFPGTGSLKNSSD------KGMLNIPLKR-GLSDKTLLRIIDSIVRPLIEKFEPEVIVIQCGCDGLSGDPHKEWNLTIRG 253

                       250       260
                ....*....|....*....|....*.
gi 20070354 282 FAHLTQLLQVLAGGRVCAVL-EGGYH 306
Cdd:cd11680 254 YGSVIELLLKEFKDKPTLLLgGGGYN 279
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
 27-315 1.32e-21

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: 95.99  E-value: 1.32e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  27 RPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSLVR-----ETQVLGKEELQALSGQFDAIYFHPSTFH 101
Cdd:cd11598  21 KPFRLTLTKHLVMGYGLHKAMDTYEARAATREELRQFHDADYLDFLSkvspeNANQLRFDKAEPFNIGDDCPVFDGMYDY 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 102 CaRLAAGAGLQLVDAVLTGavQNGLALVRPPG-HHGQRAAANGFCVFNNVAIAAAHAKQKHGlhRILVVDWDVHHGQGIQ 180
Cdd:cd11598 101 C-QLYAGASLDAARKLCSG--QSDIAINWSGGlHHAKKSEASGFCYVNDIVLAILNLLRYFP--RVLYIDIDVHHGDGVE 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 181 YLFEDDPSVLYFSWHRYeHGRFWPflRESDADAVGRGQGLGFTVNLPWNQvGMGNADYVAAFLHLLLPLAFEFDPELVLV 260
Cdd:cd11598 176 EAFYRTDRVMTLSFHKY-NGEFFP--GTGDLDDNGGTPGKHFALNVPLED-GIDDEQYNLLFKSIIGPTIEKFQPSAIVL 251

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20070354 261 SAGFDSAIGDPEG----QMQATPECFAHLTQ--LLQVLAGGrvcavleGGYHLESLAESVC 315
Cdd:cd11598 252 QCGADSLGGDRLGqfnlNIKAHGACVKFVKSfgIPMLVVGG-------GGYTPRNVARAWC 305
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
 27-320 2.59e-20

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: 93.21  E-value: 2.59e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  27 RPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSLVRETQVLGKEELQALSGQFDAIYFHP---STFHCA 103
Cdd:cd10010  28 KPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPvfdGLFEFC 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 104 RLAAGAglQLVDAVLTGAVQNGLALVRPPG-HHGQRAAANGFCVFNNVAIAAAHAKQKHglHRILVVDWDVHHGQGIQYL 182
Cdd:cd10010 108 QLSAGG--SVASAVKLNKQQTDIAVNWAGGlHHAKKSEASGFCYVNDIVLAILELLKYH--QRVLYIDIDIHHGDGVEEA 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 183 FEDDPSVLYFSWHRYehGRFWPflRESDADAVGRGQGLGFTVNLPWNQvGMGNADYVAAFLHLLLPLAFEFDPELVLVSA 262
Cdd:cd10010 184 FYTTDRVMTVSFHKY--GEYFP--GTGDLRDIGAGKGKYYAVNYPLRD-GIDDESYEAIFKPVMSKVMEMFQPSAVVLQC 258

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20070354 263 GFDSAIGDPEGQMQATPECFAHLTQLLQ------VLAGGrvcavleGGYHLESLAEsvCMTVQT 320
Cdd:cd10010 259 GADSLSGDRLGCFNLTIKGHAKCVEFVKsfnlpmLMLGG-------GGYTIRNVAR--CWTYET 313
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
 25-305 6.12e-20

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: 91.74  E-value: 6.12e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  25 IERPERLTAALDRLR-----QRGLEQRcLRLSAREASEEELGLVHSPEYvslvretqvLGKEELQALSGQFDAIyfhpst 99
Cdd:cd09998  23 VERPERLRASVLGLSaavhgSKWSAEL-IEMCDMAEAKLAKGESEIPAH---------LPQGDLYLCPESLDAI------ 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 100 fhcaRLAAGAGLQLVDAVLTGAV---QNGLALVRPPGHHGQRAAANGFCVFNNVAIAAAHAKQKHGLHRILVVDWDVHHG 176
Cdd:cd09998  87 ----QGALGAVCEAVDSVFKPESpgtKRAFVAIRPPGHHCSESTPSGFCWVNNVHVGAAHAYLTHGITRVVILDIDLHHG 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 177 QGIQYL------------------------FEDDPSVLYFSWHRY-----EHGRfwpFLRESDADAVGRGQGLGFTVNL- 226
Cdd:cd09998 163 NGTQDIawrinaeankqalesssyddfkpaGAPGLRIFYSSLHDInsfpcEDGD---PAKVKDASVSIDGAHGQWIWNVh 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 227 --PWNQVGMGNADYVAAFLHLL------LPLAFEFDPE--LVLVSAGFDSAIGDPEGqMQ----ATPECFAH-----LTQ 287
Cdd:cd09998 240 lqPWTTEEDFWELYYPKYRILFekaaefLRLTTAATPFktLVFISAGFDASEHEYES-MQrhgvNVPTSFYYrfardAVR 318

                       330
                ....*....|....*...
gi 20070354 288 LLQVLAGGRVCAVLEGGY 305
Cdd:cd09998 319 FADAHAHGRLISVLEGGY 336
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
 27-324 2.11e-16

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: 81.39  E-value: 2.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  27 RPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVS-LVRET----QVLGKEELQALSGQ----FDAIYFHP 97
Cdd:cd10004  24 KPHRIRMAHSLVMNYGLYKKMEIYRAKPATKNEMTQFHTDEYIDfLSRVTpdnmEKFQKEQVKYNVGDdcpvFDGLFEFC 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  98 STFHCARLAAGAGLQLVDAVLTGAVQNGLalvrppgHHGQRAAANGFCVFNNVAIAAAHAKQKHglHRILVVDWDVHHGQ 177
Cdd:cd10004 104 SISAGGSMEGAARLNRGKCDIAVNWAGGL-------HHAKKSEASGFCYVNDIVLGILELLRYH--QRVLYIDIDVHHGD 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 178 GIQYLFEDDPSVLYFSWHRYehGRFWPFLREsdADAVGRGQGLGFTVNLPWNQvGMGNADYVAAFLHLLLPLAFEFDPEL 257
Cdd:cd10004 175 GVEEAFYTTDRVMTCSFHKY--GEYFPGTGE--LRDIGIGTGKNYAVNVPLRD-GIDDESYKSIFEPVIKHVMEWYQPEA 249

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20070354 258 VLVSAGFDSAIGDPEG----QMQATPECFAHLTQ--LLQVLAGGrvcavleGGYHLESLAESVCMTVQTLLGD 324
Cdd:cd10004 250 VVLQCGGDSLSGDRLGcfnlSMKGHANCVNFVKSfnLPMLVLGG-------GGYTMRNVARTWAFETGLLAGE 315
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
 27-320 4.46e-16

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: 80.49  E-value: 4.46e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  27 RPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSLVRETQVLGKEELQALSGQFDAIYFHP---STFHCA 103
Cdd:cd10011  24 KPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPvfdGLFEFC 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 104 RLAAGAglQLVDAVLTGAVQNGLALVRPPG-HHGQRAAANGFCVFNNVAIAAAHAKQKHglHRILVVDWDVHHGQGIQYL 182
Cdd:cd10011 104 QLSTGG--SVAGAVKLNRQQTDMAVNWAGGlHHAKKSEASGFCYVNDIVLAILELLKYH--QRVLYIDIDIHHGDGVEEA 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 183 FEDDPSVLYFSwhryEHGRFWPFLRESDADAVGRGQGLGFTVNLPWNQvGMGNADYVAAFLHLLLPLAFEFDPELVLVSA 262
Cdd:cd10011 180 FYTTDRVMTVS----FHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRD-GIDDESYGQIFKPIISKVMEMYQPSAVVLQC 254

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20070354 263 GFDSAIGDPEGQMQATPECFAHLTQLLQ------VLAGGrvcavleGGYHLESLAEsvCMTVQT 320
Cdd:cd10011 255 GADSLSGDRLGCFNLTVKGHAKCVEVVKtfnlplLMLGG-------GGYTIRNVAR--CWTYET 309
PTZ00063 PTZ00063
histone deacetylase; Provisional
 134-295 2.03e-15

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 79.08  E-value: 2.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  134 HHGQRAAANGFCVFNNVAIAAAHAKQKHGlhRILVVDWDVHHGQGIQYLFEDDPSVLYFSWHRYehGRFWPflRESDADA 213
Cdd:PTZ00063 137 HHAKRSEASGFCYINDIVLGILELLKYHA--RVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFP--GTGDVTD 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  214 VGRGQGLGFTVNLPWNQvGMGNADYVAAFLHLLLPLAFEFDPELVLVSAGFDSAIGDPEGQMQAT----PECFAHLTQL- 288
Cdd:PTZ00063 211 IGVAQGKYYSVNVPLND-GIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTikghAACVEFVRSLn 289


                 ....*....
gi 20070354  289 --LQVLAGG 295
Cdd:PTZ00063 290 ipLLVLGGG 298
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
 27-322 1.80e-14

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: 75.51  E-value: 1.80e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  27 RPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSLVRETQVLGKEELQALSGQF----DAIYFhPSTFHC 102
Cdd:cd10005  23 KPHRLALTHSLVLHYGLYKKMQVYKPYRASAHDMCRFHSEDYIDFLQRVTPQNIQGFTKSLNQFnvgdDCPVF-PGLFDF 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 103 ARLAAGAGLQlvdavltGAVQ--NGL---ALVRPPG-HHGQRAAANGFCVFNNVAIAAAHAKQKHGlhRILVVDWDVHHG 176
Cdd:cd10005 102 CSMYTGASLE-------GATKlnHKIcdiAINWSGGlHHAKKFEASGFCYVNDIVIAILELLKYHP--RVLYIDIDIHHG 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 177 QGIQYLFEDDPSVLYFSWHRYeHGRFWPflRESDADAVGRGQGLGFTVNLPWNQvGMGNADYVAAFLHLLLPLAFEFDPE 256
Cdd:cd10005 173 DGVQEAFYLTDRVMTVSFHKY-GNYFFP--GTGDMYEVGAESGRYYSVNVPLKD-GIDDQSYLQLFKPVIQQVIDFYQPT 248

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20070354 257 LVLVSAGFDSAIGDPEG----QMQATPECFAHLTQL---LQVLAGgrvcavleGGYHLESLAEsvCMTVQTLL 322
Cdd:cd10005 249 CIVLQCGADSLGCDRLGcfnlSIKGHGECVEFVKSFnipLLVLGG--------GGYTVRNVAR--CWTYETSL 311
PTZ00346 PTZ00346
histone deacetylase; Provisional
 27-328 2.28e-12

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 69.29  E-value: 2.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354   27 RPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSlvretqVLGKEELQAL--SGQFDAIYFH----PSTF 100
Cdd:PTZ00346  46 KPYRVLAAMEIVRSLKIDAHCRTVVPPLVKVEELMAYHTDTYLA------NLGLHSCRSWlwNAETSKVFFSgdcpPVEG 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  101 HCARLAAGAGLQLVDAVLTGAVQNGLALVRPPG-HHGQRAAANGFCVFNNVAIAAAHAKQKHglHRILVVDWDVHHGQGI 179
Cdd:PTZ00346 120 LMEHSIATASGTLMGAVLLNSGQVDVAVHWGGGmHHSKCGECSGFCYVNDIVLGILELLKCH--DRVLYVDIDMHHGDGV 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  180 QYLFEDDPSVLYFSWHRYEHGRFWPFLRESDadaVGRGQGLGFTVNLP-WNqvGMGNADYVAAFLHLLLPLAFEFDPELV 258
Cdd:PTZ00346 198 DEAFCTSDRVFTLSLHKFGESFFPGTGHPRD---VGYGRGRYYSMNLAvWD--GITDFYYLGLFEHALHSIVRRYSPDAI 272

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354  259 LVSAGFDSAIGDPEGQMQATPECFAHLTQLLQVLaGGRVCAVLEGGYHLESLAESVCMTVQTLLGDPAPP 328
Cdd:PTZ00346 273 VLQCGADSLAGDRLGLLNLSSFGHGQCVQAVRDL-GIPMLALGGGGYTIRNVAKLWAYETSILTGHPLPP 341
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 562-634 6.90e-07

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: 51.58  E-value: 6.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 562 LVLPLAYGFQPDLVLVALG--------PGHGLQGPHA-ALLAAMLRGLAGGRVLALLEE----NSTPQLAGILARVLNGE 628
Cdd:cd11600 228 IVMPIAYEFDPDLVIISAGfdaadgdeLGQCHVTPAGyAHMTHMLMSLAGGKLVVALEGgynlDAISDSALAVAKVLLGE 307


                ....*.
gi 20070354 629 APPSLG 634
Cdd:cd11600 308 APPKLP 313
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 562-635 9.73e-07

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: 51.16  E-value: 9.73e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 562 LVLPLAYGFQPDLVLVALG-------PGHGLQ-GPHA-ALLAAMLRGLAGGRVLALLE----ENSTPQLAGILARVLNGE 628
Cdd:cd10002 228 ILLPLALEFQPELVLVSAGfdasigdPEGEMAvTPAGyAHLTRLLMGLAGGKLLLVLEggylLESLAESVSMTLRGLLGD 307


                ....*..
gi 20070354 629 APPSLGP 635
Cdd:cd10002 308 PLPPLAP 314
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
 553-610 4.01e-04

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: 42.92  E-value: 4.01e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20070354 553 GGFLSCILGLVLPLAYGFQPDLVLVALG-------PGHGLQGPHA--ALLAAMLRGLAGGRVLALLE 610
Cdd:cd11682 219 ADYIAAFLHVLLPVALEFQPQLVLVAAGfdavigdPKGEMAATPAcfAHLTHLLMGLAGGKLILSLE 285
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 547-625 6.00e-03

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: 39.14  E-value: 6.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354   547 PLPVMTG--GFLSCILGLVLPLAYGFQPDLVLVALG-------PGHGLQGPHAAL--LAAMLRGLA---GGRVLALLE-- 610
Cdd:pfam00850 202 PLPPGTGdaEYLAAFEEILLPALEEFQPDLILVSAGfdahagdPLGGLNLTTEGFaeITRILLELAdplCIRVVSVLEgg 281

                          90
                  ....*....|....*..
gi 20070354   611 --ENSTPQLAGILARVL 625
Cdd:pfam00850 282 ynLDALARSATAVLAAL 298
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 118-282 7.29e-03

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: 38.51  E-value: 7.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 118 LTGAVQNGLALVRPP----GHHGQraaangfcvfnNVAIAAAHAkQKHGlhRILVVDWDVHHGQGIQYLF---------- 183
Cdd:cd09987  14 LAGVVVAVLKDGKVPvvlgGDHSI-----------ANGAIRAVA-ELHP--DLGVIDVDAHHDVRTPEAFgkgnhhtprh 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070354 184 ----EDDPSVLYFSWHRYEHGRFwpflresdaDAVGRGQGLGFTVNLPWNQVgmGNADYVAAFLHLLLPLafEFDPELVL 259
Cdd:cd09987  80 llcePLISDVHIVSIGIRGVSNG---------EAGGAYARKLGVVYFSMTEV--DKLGLGDVFEEIVSYL--GDKGDNVY 146

                       170       180
                ....*....|....*....|...
gi 20070354 260 VSAGFDSAIGDPEGQMqATPECF 282
Cdd:cd09987 147 LSVDVDGLDPSFAPGT-GTPGPG 168
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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