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Conserved domains on  [gi|41054267|ref|NP_956069|]
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polyamine deacetylase HDAC10 [Danio rerio]

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 ...
 20-356 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: 693.14  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  20 WTDPACEIEVPERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQTPGMNVEELMAFSKKYNDVYFHQ 99
Cdd:cd11683   1 WDDPECEIEVPERLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRETQVMNKEELMAISGKYDAVYFHP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 100 NIYHCAKLAAGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAFAALYAKKNYNLNRILIVDWDVHHGQ 179
Cdd:cd11683  81 NTFHCARLAAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYAKKKYGLHRILIVDWDVHHGQ 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 180 GIQYCFEEDPSVLYFSWHRYEHQSFWPNLPESDYSSVGKGKGSGFNINLPWNKVGMTNSDYLAAFFHVLLPVAYEFDPEL 259
Cdd:cd11683 161 GIQYIFEEDPSVLYFSWHRYEHQRFWPFLRESDYDAVGRGKGLGFNINLPWNKVGMGNADYLAAFFHVLLPLAFEFDPEL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 260 VIVSAGFDSAIGDPEGEMCALPEIFAHLTHLLMPLAAGKMCVVLEGGYNLTSLGQSVCQTVHSLLGDPTPRISGLGTACD 339
Cdd:cd11683 241 VLVSAGFDSAIGDPEGQMCATPECFAHLTHLLMVLAGGKLCAVLEGGYHLESLAESVCMTVQTLLGDPLPRLSGEMTPCQ 320

                       330
                ....*....|....*..
gi 41054267 340 SALESIQNVRNVQSSYW 356
Cdd:cd11683 321 SALESIQNVRAAQAPYW 337
Arginase_HDAC super family cl17011
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 559-665 2.57e-06

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 cd10002:

Pssm-ID: 450134 [Multi-domain]  Cd Length: 336  Bit Score: 50.00  E-value: 2.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 559 AGFMQALLGLILPVAYEFNPALVL---------GIVE-ETAAKTRLmrvWGHMTCLIQGLARGRMLTLLQG-YDKDLL-- 625
Cdd:cd10002 219 ADYLAIFHHILLPLALEFQPELVLvsagfdasiGDPEgEMAVTPAG---YAHLTRLLMGLAGGKLLLVLEGgYLLESLae 295

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 41054267 626 --ELTVSALSGASISPLGPLrAPKPEDVEMMEKQRQRLQERW 665
Cdd:cd10002 296 svSMTLRGLLGDPLPPLAPP-IPIRSVLETILNAIAHLSPRW 336
 
Name Accession Description Interval E-value
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 20-356 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: 693.14  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  20 WTDPACEIEVPERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQTPGMNVEELMAFSKKYNDVYFHQ 99
Cdd:cd11683   1 WDDPECEIEVPERLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRETQVMNKEELMAISGKYDAVYFHP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 100 NIYHCAKLAAGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAFAALYAKKNYNLNRILIVDWDVHHGQ 179
Cdd:cd11683  81 NTFHCARLAAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYAKKKYGLHRILIVDWDVHHGQ 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 180 GIQYCFEEDPSVLYFSWHRYEHQSFWPNLPESDYSSVGKGKGSGFNINLPWNKVGMTNSDYLAAFFHVLLPVAYEFDPEL 259
Cdd:cd11683 161 GIQYIFEEDPSVLYFSWHRYEHQRFWPFLRESDYDAVGRGKGLGFNINLPWNKVGMGNADYLAAFFHVLLPLAFEFDPEL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 260 VIVSAGFDSAIGDPEGEMCALPEIFAHLTHLLMPLAAGKMCVVLEGGYNLTSLGQSVCQTVHSLLGDPTPRISGLGTACD 339
Cdd:cd11683 241 VLVSAGFDSAIGDPEGQMCATPECFAHLTHLLMVLAGGKLCAVLEGGYHLESLAESVCMTVQTLLGDPLPRLSGEMTPCQ 320

                       330
                ....*....|....*..
gi 41054267 340 SALESIQNVRNVQSSYW 356
Cdd:cd11683 321 SALESIQNVRAAQAPYW 337
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 28-323 4.95e-123

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: 367.72  E-value: 4.95e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267    28 EVPERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQT-PGMNVEELMAFSKKYNDVYFHQNIYHCAK 106
Cdd:pfam00850   3 ENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAaPEGGALLLLSYLSGDDDTPVSPGSYEAAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267   107 LAAGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAFAALYAKKNYNLNRILIVDWDVHHGQGIQYCFE 186
Cdd:pfam00850  83 LAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLKRVAIVDFDVHHGNGTQEIFY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267   187 EDPSVLYFSWHRYEHQSFwpnlPES-DYSSVGKGKGSGFNINLPWNKvGMTNSDYLAAFFHVLLPVAYEFDPELVIVSAG 265
Cdd:pfam00850 163 DDPSVLTLSIHQYPGGFY----PGTgFADETGEGKGKGYTLNVPLPP-GTGDAEYLAAFEEILLPALEEFQPDLILVSAG 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41054267   266 FDSAIGDPEGEMCALPEIFAHLTHLLMPLA---AGKMCVVLEGGYNLTSLGQSVCQTVHSL 323
Cdd:pfam00850 238 FDAHAGDPLGGLNLTTEGFAEITRILLELAdplCIRVVSVLEGGYNLDALARSATAVLAAL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 6-325 7.98e-93

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 290.08  E-value: 7.98e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267   6 ALIFDEEMSRYKLLWTDPaceiEVPERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQ-TPGMNVEE 84
Cdd:COG0123   2 ALIYHPDYLLHDLGPGHP----EPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAaSLDGGYGQ 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  85 LMAfskkynDVYFHQNIYHCAKLAAGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAFAALYAKKNYn 164
Cdd:COG0123  78 LDP------DTPVSPGTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGFCLFNNAAIAARYLLAKG- 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 165 LNRILIVDWDVHHGQGIQYCFEEDPSVLYFSWHRYehqsfwPNLPESDYSS-VGKGKGSGFNINLPWnKVGMTNSDYLAA 243
Cdd:COG0123 151 LERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD------PLYPGTGAADeTGEGAGEGSNLNVPL-PPGTGDAEYLAA 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 244 FFHVLLPVAYEFDPELVIVSAGFDSAIGDPEGEMCALPEIFAHLTHLLMPLAA---GKMCVVLEGGYNLTSLGQSVCQTV 320
Cdd:COG0123 224 LEEALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELADhcgGPVVSVLEGGYNLDALARSVAAHL 303


                ....*
gi 41054267 321 HSLLG 325
Cdd:COG0123 304 ETLLG 308
PTZ00063 PTZ00063
histone deacetylase; Provisional
 30-275 3.09e-17

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 84.86  E-value: 3.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267   30 PERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQTPGMNVEELMAFSKKYN-----DVYFHQNIYHC 104
Cdd:PTZ00063  27 PQRIRMAHALILSYDLYKHMEIYRPHKSVEPELVLFHDEEYVDFLSSISPENYRDFTYQLKRFNvgeatDCPVFDGLFEF 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  105 AKLAAGATLqlvDSVMKREVRNGMALVRPPG--HHSQRSAANGFCVFNNVAFAALYAKKNYNlnRILIVDWDVHHGQGIQ 182
Cdd:PTZ00063 107 QQSCAGASI---DGAYKLNNHQADICVNWSGglHHAKRSEASGFCYINDIVLGILELLKYHA--RVMYIDIDVHHGDGVE 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  183 YCFEEDPSVLYFSWHRYehQSFWPNlpESDYSSVGKGKGSGFNINLPWNKvGMTNSDYLAAFFHVLLPVAYEFDPELVIV 262
Cdd:PTZ00063 182 EAFYVTHRVMTVSFHKF--GDFFPG--TGDVTDIGVAQGKYYSVNVPLND-GIDDDSFVDLFKPVISKCVEVYRPGAIVL 256

                        250
                 ....*....|...
gi 41054267  263 SAGFDSAIGDPEG 275
Cdd:PTZ00063 257 QCGADSLTGDRLG 269
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 559-665 2.57e-06

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: 50.00  E-value: 2.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 559 AGFMQALLGLILPVAYEFNPALVL---------GIVE-ETAAKTRLmrvWGHMTCLIQGLARGRMLTLLQG-YDKDLL-- 625
Cdd:cd10002 219 ADYLAIFHHILLPLALEFQPELVLvsagfdasiGDPEgEMAVTPAG---YAHLTRLLMGLAGGKLLLVLEGgYLLESLae 295

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 41054267 626 --ELTVSALSGASISPLGPLrAPKPEDVEMMEKQRQRLQERW 665
Cdd:cd10002 296 svSMTLRGLLGDPLPPLAPP-IPIRSVLETILNAIAHLSPRW 336
 
Name Accession Description Interval E-value
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 20-356 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: 693.14  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  20 WTDPACEIEVPERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQTPGMNVEELMAFSKKYNDVYFHQ 99
Cdd:cd11683   1 WDDPECEIEVPERLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRETQVMNKEELMAISGKYDAVYFHP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 100 NIYHCAKLAAGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAFAALYAKKNYNLNRILIVDWDVHHGQ 179
Cdd:cd11683  81 NTFHCARLAAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYAKKKYGLHRILIVDWDVHHGQ 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 180 GIQYCFEEDPSVLYFSWHRYEHQSFWPNLPESDYSSVGKGKGSGFNINLPWNKVGMTNSDYLAAFFHVLLPVAYEFDPEL 259
Cdd:cd11683 161 GIQYIFEEDPSVLYFSWHRYEHQRFWPFLRESDYDAVGRGKGLGFNINLPWNKVGMGNADYLAAFFHVLLPLAFEFDPEL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 260 VIVSAGFDSAIGDPEGEMCALPEIFAHLTHLLMPLAAGKMCVVLEGGYNLTSLGQSVCQTVHSLLGDPTPRISGLGTACD 339
Cdd:cd11683 241 VLVSAGFDSAIGDPEGQMCATPECFAHLTHLLMVLAGGKLCAVLEGGYHLESLAESVCMTVQTLLGDPLPRLSGEMTPCQ 320

                       330
                ....*....|....*..
gi 41054267 340 SALESIQNVRNVQSSYW 356
Cdd:cd11683 321 SALESIQNVRAAQAPYW 337
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 20-356 7.55e-180

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: 514.17  E-value: 7.55e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  20 WTDPACEIEVPERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQTPGMNVEELMAFSKKYNDVYFHQ 99
Cdd:cd10002   1 CNWDSNHIECPERLEAILERLTQDGLLERCVKIPAREAEEDEILLVHSQEYIDLVKSTETMEKEELESLCSGYDSVYLCP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 100 NIYHCAKLAAGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAFAALYAKKNYNLNRILIVDWDVHHGQ 179
Cdd:cd10002  81 STYEAARLAAGSTIELVKAVMAGKIQNGFALIRPPGHHAMRNEANGYCIFNNVAIAAKYAIEKLGLKRILIVDWDVHHGQ 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 180 GIQYCFEEDPSVLYFSWHRYEHQSFWPNLPESDYSSVGKGKGSGFNINLPWNKVGMTNSDYLAAFFHVLLPVAYEFDPEL 259
Cdd:cd10002 161 GTQQGFYEDPRVLYFSIHRYEHGRFWPHLFESDYDYIGVGHGYGFNVNVPLNQTGLGDADYLAIFHHILLPLALEFQPEL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 260 VIVSAGFDSAIGDPEGEMCALPEIFAHLTHLLMPLAAGKMCVVLEGGYNLTSLGQSVCQTVHSLLGDPTPRISgLGTACD 339
Cdd:cd10002 241 VLVSAGFDASIGDPEGEMAVTPAGYAHLTRLLMGLAGGKLLLVLEGGYLLESLAESVSMTLRGLLGDPLPPLA-PPIPIR 319

                       330
                ....*....|....*..
gi 41054267 340 SALESIQNVRNVQSSYW 356
Cdd:cd10002 320 SVLETILNAIAHLSPRW 336
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
 9-360 3.17e-174

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: 500.33  E-value: 3.17e-174
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267   9 FDEEMSRYKLLWtDPAcEIEVPERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQTPGMNVEELMAF 88
Cdd:cd10003   1 YDQRMMNHHNLW-DPG-HPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHLDEMKSLEKMKPRELNRL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  89 SKKYNDVYFHQNIYHCAKLAAGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAFAALYAKKNYNLNRI 168
Cdd:cd10003  79 GKEYDSIYIHPDSYQCALLAAGCVLQVVEAVLTGESRNGVAIVRPPGHHAEQDTACGFCFFNNVAIAARYAQKKYGLKRI 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 169 LIVDWDVHHGQGIQYCFEEDPSVLYFSWHRYEHQSFWPNLPESDYSSVGKGKGSGFNINLPWNKVGMTNSDYLAAFFHVL 248
Cdd:cd10003 159 LIVDWDVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSPEGNYDVVGKGKGEGFNVNIPWNKGGMGDAEYIAAFQQVV 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 249 LPVAYEFDPELVIVSAGFDSAIGDPEGEMCALPEIFAHLTHLLMPLAAGKMCVVLEGGYNLTSLGQSVCQTVHSLLGDPT 328
Cdd:cd10003 239 LPIAYEFNPELVLVSAGFDAARGDPLGGCKVTPEGYAHMTHMLMSLAGGRVIVILEGGYNLTSISESMSMCTKTLLGDPP 318

                       330       340       350
                ....*....|....*....|....*....|..
gi 41054267 329 PRISGLGTACDSALESIQNVRNVQSSYWSSFK 360
Cdd:cd10003 319 PVLDLPRPPCSSALKSINNVLQVHQKYWKSLR 350
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
 19-356 9.97e-158

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: 458.16  E-value: 9.97e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  19 LWTD--PACeievPERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQTPGMNVEELMAFSKKYNDVY 96
Cdd:cd11682   2 LWDEsfPEC----PERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYVALMKSTQYMTEEELRTLADTYDSVY 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  97 FHQNIYHCAKLAAGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAFAALYAKKNYNLNRILIVDWDVH 176
Cdd:cd11682  78 LHPNSYSCACLAVGSVLQLVDKVLGGEIRNGLAIVRPPGHHAQHDKMDGYCMFNNVAIAARYAQQKHGVQRVLIVDWDVH 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 177 HGQGIQYCFEEDPSVLYFSWHRYEHQSFWPNLPESDYSSVGKGKGSGFNINLPWNKVGMTNSDYLAAFFHVLLPVAYEFD 256
Cdd:cd11682 158 HGQGTQFIFEQDPSVLYFSIHRYEQGRFWPHLKESDSSAVGFGRGEGYNINVPWNQVGMRDADYIAAFLHVLLPVALEFQ 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 257 PELVIVSAGFDSAIGDPEGEMCALPEIFAHLTHLLMPLAAGKMCVVLEGGYNLTSLGQSVCQTVHSLLGDPTPRISGLGT 336
Cdd:cd11682 238 PQLVLVAAGFDAVIGDPKGEMAATPACFAHLTHLLMGLAGGKLILSLEGGYNLRSLAEGVCASLKALLGDPCPMLESPGA 317

                       330       340
                ....*....|....*....|
gi 41054267 337 ACDSALESIQNVRNVQSSYW 356
Cdd:cd11682 318 PCRSALASVSCTISALEPFW 337
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 28-332 7.34e-129

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


Pssm-ID: 212542 [Multi-domain]  Cd Length: 313  Bit Score: 383.23  E-value: 7.34e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  28 EVPERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQTPGMNVEEL--MAFSKKYNDVYFHQNIYHCA 105
Cdd:cd11600   5 EDPSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEHWDRVEATEKMSDEQLkdRTEIFERDSLYVNNDTAFCA 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 106 KLAAGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAFAALYAKKNY--NLNRILIVDWDVHHGQGIQY 183
Cdd:cd11600  85 RLSCGGAIEACRAVAEGRVKNAFAVVRPPGHHAEPDESMGFCFFNNVAVAAKWLQTEYpdKIKKILILDWDIHHGNGTQR 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 184 CFEEDPSVLYFSWHRYEHQSFWPNLPESDYSSVGKGKGSGFNINLPWNKVGMTNSDYLAAFFHVLLPVAYEFDPELVIVS 263
Cdd:cd11600 165 AFYDDPNVLYISLHRFENGGFYPGTPYGDYESVGEGAGLGFNVNIPWPQGGMGDADYIYAFQRIVMPIAYEFDPDLVIIS 244

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41054267 264 AGFDSAIGDPEGEMCALPEIFAHLTHLLMPLAAGKMCVVLEGGYNLTSLGQSVCQTVHSLLGDPTPRIS 332
Cdd:cd11600 245 AGFDAADGDELGQCHVTPAGYAHMTHMLMSLAGGKLVVALEGGYNLDAISDSALAVAKVLLGEAPPKLP 313
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
 28-324 4.50e-127

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: 377.61  E-value: 4.50e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  28 EVPERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQTPGMnveelmAFSKKYNDVYFHQNIYHCAKL 107
Cdd:cd09992   3 ERPERLLAILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYIERVEETCEA------GGGYLDPDTYVSPGSYEAALL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 108 AAGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAFAALYAKKNYNLNRILIVDWDVHHGQGIQYCFEE 187
Cdd:cd09992  77 AAGAALAAVDAVLSGEAENAFALVRPPGHHAEPDRAMGFCLFNNVAIAARYAQKRYGLKRVLIVDWDVHHGNGTQDIFYD 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 188 DPSVLYFSWHRYEhqsFWPNlpESDYSSVGKGKGSGFNINLPWNKvGMTNSDYLAAFFHVLLPVAYEFDPELVIVSAGFD 267
Cdd:cd09992 157 DPSVLYFSIHQYP---FYPG--TGAAEETGGGAGEGFTINVPLPP-GSGDAEYLAAFEEVLLPIAREFQPDLVLVSAGFD 230

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41054267 268 SAIGDPEGEMCALPEIFAHLTHLLMPLAA----GKMCVVLEGGYNLTSLGQSVCQTVHSLL 324
Cdd:cd09992 231 AHRGDPLGGMNLTPEGYARLTRLLKELADehcgGRLVFVLEGGYNLEALAESVLAVLEALL 291
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 28-323 4.95e-123

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: 367.72  E-value: 4.95e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267    28 EVPERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQT-PGMNVEELMAFSKKYNDVYFHQNIYHCAK 106
Cdd:pfam00850   3 ENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAaPEGGALLLLSYLSGDDDTPVSPGSYEAAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267   107 LAAGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAFAALYAKKNYNLNRILIVDWDVHHGQGIQYCFE 186
Cdd:pfam00850  83 LAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLKRVAIVDFDVHHGNGTQEIFY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267   187 EDPSVLYFSWHRYEHQSFwpnlPES-DYSSVGKGKGSGFNINLPWNKvGMTNSDYLAAFFHVLLPVAYEFDPELVIVSAG 265
Cdd:pfam00850 163 DDPSVLTLSIHQYPGGFY----PGTgFADETGEGKGKGYTLNVPLPP-GTGDAEYLAAFEEILLPALEEFQPDLILVSAG 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41054267   266 FDSAIGDPEGEMCALPEIFAHLTHLLMPLA---AGKMCVVLEGGYNLTSLGQSVCQTVHSL 323
Cdd:pfam00850 238 FDAHAGDPLGGLNLTTEGFAEITRILLELAdplCIRVVSVLEGGYNLDALARSATAVLAAL 298
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 3-356 1.17e-101

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: 315.44  E-value: 1.17e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267   3 SGSALIFDEEMSRYKLLWTDPACEIEVPERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEY--LEAVKQTPGM 80
Cdd:cd11681   1 FTTGLAYDPLMLKHQCICGNNSSHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHtlLYGTNPLSRL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  81 NVEE---LMAFSKKY-----------NDVYFH-QNIYHCAKLAAGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANG 145
Cdd:cd11681  81 KLDPtklAGLPQKSFvrlpcggigvdSDTVWNeLHTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQAMG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 146 FCVFNNVAFAALYAKKNYNLNRILIVDWDVHHGQGIQYCFEEDPSVLYFSWHRYEHQSFWPNLPESDysSVGKGKGSGFN 225
Cdd:cd11681 161 FCFFNSVAIAAKQLQQKLKLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFPGTGAPT--EVGSGAGEGFN 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 226 INLPWN---KVGMTNSDYLAAFFHVLLPVAYEFDPELVIVSAGFDSAIGDPE--GEMCALPEIFAHLTHLLMPLAAGKMC 300
Cdd:cd11681 239 VNIAWSgglDPPMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPPplGGYKVSPACFGYMTRQLMNLAGGKVV 318

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41054267 301 VVLEGGYNLTSLGQSVCQTVHSLLGDPTPRISGLGTA---CDSALESIQNVRNVQSSYW 356
Cdd:cd11681 319 LALEGGYDLTAICDASEACVRALLGDELDPLSEEELErrpNPNAVTSLEKVIAIQSPYW 377
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 6-325 7.98e-93

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 290.08  E-value: 7.98e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267   6 ALIFDEEMSRYKLLWTDPaceiEVPERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQ-TPGMNVEE 84
Cdd:COG0123   2 ALIYHPDYLLHDLGPGHP----EPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAaSLDGGYGQ 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  85 LMAfskkynDVYFHQNIYHCAKLAAGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAFAALYAKKNYn 164
Cdd:COG0123  78 LDP------DTPVSPGTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGFCLFNNAAIAARYLLAKG- 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 165 LNRILIVDWDVHHGQGIQYCFEEDPSVLYFSWHRYehqsfwPNLPESDYSS-VGKGKGSGFNINLPWnKVGMTNSDYLAA 243
Cdd:COG0123 151 LERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD------PLYPGTGAADeTGEGAGEGSNLNVPL-PPGTGDAEYLAA 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 244 FFHVLLPVAYEFDPELVIVSAGFDSAIGDPEGEMCALPEIFAHLTHLLMPLAA---GKMCVVLEGGYNLTSLGQSVCQTV 320
Cdd:COG0123 224 LEEALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELADhcgGPVVSVLEGGYNLDALARSVAAHL 303


                ....*
gi 41054267 321 HSLLG 325
Cdd:COG0123 304 ETLLG 308
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
 6-310 2.71e-81

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: 261.73  E-value: 2.71e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267   6 ALIFDEEM-----------SRYKLLWTDPACEIEVPERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAV 74
Cdd:cd09996   2 GFVWDERYlwhdtgtgalfLPVGGLLVQPGRHPENPETKRRIKNLLEVSGLSDHLVLITPRPATDEELLRVHTPEYIDRV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  75 KQTPGMNVEELMAFSkkyndvYFHQNIYHCAKLAAGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAF 154
Cdd:cd09996  82 KAASAAGGGEAGGGT------PFGPGSYEIALLAAGGAIAAVDAVLDGEVDNAYALVRPPGHHAEPDQGMGFCLFNNVAI 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 155 AALYAKKNYNLNRILIVDWDVHHGQGIQYCFEEDPSVLYFSWHryEHQSFWPNLpeSDYSSVGKGKGSGFNINLPW-NKV 233
Cdd:cd09996 156 AARHALAVGGVKRVAVVDWDVHHGNGTQAIFYDDPDVLTISLH--QDRCFPPDS--GAVEERGEGAGEGYNLNIPLpPGS 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 234 GmtNSDYLAAFFHVLLPVAYEFDPELVIVSAGFDSAIGDPEGEMCALPEIFAHLTHLLMPLAA----GKMCVVLEGGYNL 309
Cdd:cd09996 232 G--DGAYLHAFERIVLPALRAFRPELIIVASGFDASAFDPLGRMMLTSDGFRALTRKLRDLADelcgGRLVMVHEGGYSE 309


                .
gi 41054267 310 T 310
Cdd:cd09996 310 A 310
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
 5-356 4.56e-76

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: 248.77  E-value: 4.56e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267   5 SALIFDEEMSRYKLLWTDPACEIEVPERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQTP------ 78
Cdd:cd10008   3 TGLVYDSVMLKHQCSCGDNSNHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPlsrlkl 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  79 ------GMNVEELMAF------SKKYNDVYFHQNIYHCAKLAAGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGF 146
Cdd:cd10008  83 dngklaGLLAQRMFVMlpcggvGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGF 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 147 CVFNNVAFAALYAKKNYNLNRILIVDWDVHHGQGIQYCFEEDPSVLYFSWHRYEHQSFWPNLPESDysSVGKGKGSGFNI 226
Cdd:cd10008 163 CFFNSVAIACRQLQQQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVD--EVGAGSGEGFNV 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 227 NLPWN---KVGMTNSDYLAAFFHVLLPVAYEFDPELVIVSAGFDSAIGDPE--GEMCALPEIFAHLTHLLMPLAAGKMCV 301
Cdd:cd10008 241 NVAWAgglDPPMGDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHPAplGGYHVSAKCFGYMTQQLMNLAGGAVVL 320

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41054267 302 VLEGGYNLTSLGQSVCQTVHSLLG---DPTPRISGLGTACDSALESIQNVRNVQSSYW 356
Cdd:cd10008 321 ALEGGHDLTAICDASEACVAALLGnevDPLSEESWKQKPNLNAIRSLEAVIRVHSKYW 378
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
 5-363 7.62e-76

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: 249.52  E-value: 7.62e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267   5 SALIFDEEMSRYKLLWTDPACEIEVPERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQTPgMNVEE 84
Cdd:cd10007   5 TGLVYDTFMLKHQCTCGNTNVHPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHSEHHTLLYGTSP-LNRQK 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  85 LMA------FSKKY-------------NDVYFHQNIYHCAKLAAGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANG 145
Cdd:cd10007  84 LDSkkllgpLSQKMyavlpcggigvdsDTVWNEMHSSSAVRMAVGCLIELAFKVAAGELKNGFAVIRPPGHHAEESTAMG 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 146 FCVFNNVAFAALYAKKNYNLNRILIVDWDVHHGQGIQYCFEEDPSVLYFSWHRYEHQSFWPNLPESDysSVGKGKGSGFN 225
Cdd:cd10007 164 FCFFNSVAIAAKLLQQKLNVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGNFFPGSGAPD--EVGAGPGVGFN 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 226 INLPWN---KVGMTNSDYLAAFFHVLLPVAYEFDPELVIVSAGFDSAIG--DPEGEMCALPEIFAHLTHLLMPLAAGKMC 300
Cdd:cd10007 242 VNIAWTggvDPPIGDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGhqSPLGGYSVTAKCFGHLTKQLMTLAGGRVV 321

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41054267 301 VVLEGGYNLTSLGQSVCQTVHSLLGD---PTPRISGLGTACDSALESIQNVRNVQSSYWSSFKHLA 363
Cdd:cd10007 322 LALEGGHDLTAICDASEACVSALLGMeltPLDNTVLQQKPNDNAVATLERVIEIQSKHWSCLKRFA 387
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
 28-324 1.42e-75

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: 244.34  E-value: 1.42e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  28 EVPERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQT-PGMNVEELMAfskkynDVYFHQNIYHCAK 106
Cdd:cd11599   3 ESPERLEAILDALIASGLDRLLRQLEAPPATREQLLRVHDAAYVDRLEAAaPEEGLVQLDP------DTAMSPGSLEAAL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 107 LAAGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAFAALYAKKNYNLNRILIVDWDVHHGQGIQYCFE 186
Cdd:cd11599  77 RAAGAVVAAVDAVMAGEARNAFCAVRPPGHHAERDKAMGFCLFNNVAIAAAHALAHHGLERVAIVDFDVHHGNGTEDIFR 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 187 EDPSVLYFSWHRYEhqsFWPnlpesdYSSVGKGKGSGFNINLPWNKvGMTNSDYLAAFFHVLLPVAYEFDPELVIVSAGF 266
Cdd:cd11599 157 DDPRVLFCSSHQHP---LYP------GTGAPDETGHGNIVNVPLPA-GTGGAEFREAVEDRWLPALDAFKPDLILISAGF 226

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41054267 267 DSAIGDPEGEMCALPEIFAHLTHLLMPLAA----GKMCVVLEGGYNLTSLGQSVCQTVHSLL 324
Cdd:cd11599 227 DAHRDDPLAQLNLTEEDYAWITEQLMDVADrycdGRIVSVLEGGYDLSALARSVAAHVRALM 288
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
 5-365 3.78e-74

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: 244.56  E-value: 3.78e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267   5 SALIFDEEMSRYKLLWTDPACEIEVPERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQTPgMNVEE 84
Cdd:cd10006   6 TGLVYDTLMLKHQCTCGNSNSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNP-LNRQK 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  85 LMAFSKK----------------------YNDVYFHQniyhCAKLAAGATLQLVDSVMKREVRNGMALVRPPGHHSQRSA 142
Cdd:cd10006  85 LDSKKLLgslasvfvrlpcggvgvdsdtiWNEVHSSG----AARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEEST 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 143 ANGFCVFNNVAFAALYAKKNYNLNRILIVDWDVHHGQGIQYCFEEDPSVLYFSWHRYEHQSFWPNLPESDysSVGKGKGS 222
Cdd:cd10006 161 PMGFCYFNSVAIAAKLLQQRLNVSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYDDGNFFPGSGAPD--EVGTGPGV 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 223 GFNINLPWN---KVGMTNSDYLAAFFHVLLPVAYEFDPELVIVSAGFDSAIGDPE--GEMCALPEIFAHLTHLLMPLAAG 297
Cdd:cd10006 239 GFNVNMAFTgglDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTplGGYNLSAKCFGYLTKQLMGLAGG 318

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41054267 298 KMCVVLEGGYNLTSLGQSVCQTVHSLLG---DPTPRISGLGTACDSALESIQNVRNVQSSYWSSFKHLAQS 365
Cdd:cd10006 319 RIVLALEGGHDLTAICDASEACVSALLGnelDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTST 389
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
 3-356 8.97e-68

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: 226.82  E-value: 8.97e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267   3 SGSALIFDEEMSRYKLLWTDPACEIEVPERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEY--------LEAV 74
Cdd:cd10009   1 SATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHsllygtnpLDGQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  75 KQTP----GMNVEELMA------FSKKYNDVYFHQNIYHCAKLAAGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAAN 144
Cdd:cd10009  81 KLDPrillGDDSQKFFSslpcggLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAM 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 145 GFCVFNNVAFAALYAKKNYNLNRILIVDWDVHHGQGIQYCFEEDPSVLYFSWHRYEHQSFWPNlpESDYSSVGKGKGSGF 224
Cdd:cd10009 161 GFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPG--SGAPNEVGTGLGEGY 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 225 NINLPWN---KVGMTNSDYLAAFFHVLLPVAYEFDPELVIVSAGFDSAIGD--PEGEMCALPEIFAHLTHLLMPLAAGKM 299
Cdd:cd10009 239 NINIAWTgglDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLADGRV 318

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 300 CVVLEGGYNLTSLGQSVCQTVHSLLG---DPTPRISGLGTACDSALESIQNVRNVQSSYW 356
Cdd:cd10009 319 VLALEGGHDLTAICDASEACVNALLGnelEPLAEDILHQSPNMNAVISLQKIIEIQSKYW 378
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
 28-316 1.83e-61

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: 207.01  E-value: 1.83e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  28 EVPERLTVSYEALRTHGLAqrcKAVPVRQATEQEILLAHSEEYLEAVKQTPGmnveelmafskkynDVYFHQNIYHCAKL 107
Cdd:cd10001  27 ENPERAEAILDALKRAGLG---EVLPPRDFGLEPILAVHDPDYVDFLETADT--------------DTPISEGTWEAALA 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 108 AAGATLQLVDSVMKREvRNGMALVRPPGHHSQRSAANGFCVFNNVAFAALYAKKNYnlNRILIVDWDVHHGQGIQYCFEE 187
Cdd:cd10001  90 AADTALTAADLVLEGE-RAAYALCRPPGHHAGRDRAGGFCYFNNAAIAAQYLRDRA--GRVAILDVDVHHGNGTQEIFYE 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 188 DPSVLYFSWHRYehqsfwpnlPESDY-------SSVGKGKGSGFNIN--LPWnkvGMTNSDYLAAFFHVLLPVAyEFDPE 258
Cdd:cd10001 167 RPDVLYVSIHGD---------PRTFYpfflgfaDETGEGEGEGYNLNlpLPP---GTGDDDYLAALDEALAAIA-AFGPD 233

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41054267 259 LVIVSAGFDSAIGDPEGEMCALPEIFAHLTHLLMPLAAGKMcVVLEGGYNLTSLGQSV 316
Cdd:cd10001 234 ALVVSLGFDTHEGDPLSDFKLTTEDYARIGRRIAALGLPTV-FVQEGGYNVDALGRNA 290
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
 32-312 1.52e-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: 204.21  E-value: 1.52e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  32 RLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQTPGMNVEElmaFSKKYNDVYFHQNIYHC---AKLA 108
Cdd:cd09301   1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKANFAVATIT---ESKPVIFGPNFPVQRHYfrgARLS 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 109 AGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAFAALYAKKnYNLNRILIVDWDVHHGQGIQYCFEED 188
Cdd:cd09301  78 TGGVVEAAELVAKGELERAFAVVGAGGHHAGKSRAWGFCYFNDVVLAIKFLRE-RGISRILIIDTDAHHGDGTREAFYDD 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 189 PSVLYFSWHRYehqsfwpnlpesDYSSVGKGKGSGFNINLPWNKvGMTNSDYLAAFFHVLLPVAYEFDPELVIVSAGFDS 268
Cdd:cd09301 157 DRVLHMSFHNY------------DIYPFGRGKGKGYKINVPLED-GLGDEEYLDAVERVISKVLEEFEPEVVVLQFGHDT 223

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 41054267 269 AIGDPEGEMCALPEIFAHLTHLLMPLAAGKMCV-VLEGGYNLTSL 312
Cdd:cd09301 224 HEGDRLGGFNLSEKGFVKLAEIVKEFARGGPILmVLGGGYNPEAA 268
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
 30-309 1.15e-52

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: 183.92  E-value: 1.15e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  30 PERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQ-TPGMNVEELMAFSKKYNDVYFHQNIYHCAKLA 108
Cdd:cd09994  21 PPRLSLTKDLLRALGLLPPVDLVPPRPATEEELLLFHTPDYIEAVKEaSRGQEPEGRGRLGLGTEDNPVFPGMHEAAALV 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 109 AGATLQLVDSVMKREVRNGmalVRPPG--HHSQRSAANGFCVFNNVAFAALYAKKNYNLnRILIVDWDVHHGQGIQYCFE 186
Cdd:cd09994 101 VGGTLLAARLVLEGEARRA---FNPAGglHHAMRGRASGFCVYNDAAVAIERLRDKGGL-RVAYVDIDAHHGDGVQAAFY 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 187 EDPSVLYFSWHRYeHQSFWPNlpESDYSSVGKGKGSGFNINLPWNKvGMTNSDYLAAFFHVLLPVAYEFDPELVIVSAGF 266
Cdd:cd09994 177 DDPRVLTISLHES-GRYLFPG--TGFVDEIGEGEGYGYAVNIPLPP-GTGDDEFLRAFEAVVPPLLRAFRPDVIVSQHGA 252

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 41054267 267 DSAIGDPEGEMCALPEIFAHLTHLLMPLA----AGKMCVVLEGGYNL 309
Cdd:cd09994 253 DAHAGDPLTHLNLSNRAYRAAVRRIRELAdeycGGRWLALGGGGYNP 299
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 29-330 4.78e-41

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: 153.65  E-value: 4.78e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  29 VPERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQ-TPGMNVEELMAFSKKYN---DVYFHQNIYHC 104
Cdd:cd10000  19 VPNRASMVHSLIEAYGLLKQLRVVKPRVATEEELASFHSDEYIQFLKKaSNEGDNDEEPSEQQEFGlgyDCPIFEGIYDY 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 105 AKLAAGATLQLVDSVMKREVRngMALVRPPG-HHSQRSAANGFCVFNNVAFAALYAKKNYnlNRILIVDWDVHHGQGIQY 183
Cdd:cd10000  99 AAAVAGATLTAAQLLIDGKCK--VAINWFGGwHHAQRDEASGFCYVNDIVLGILKLREKF--DRVLYVDLDLHHGDGVED 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 184 CFEEDPSVLYFSWHRYEhQSFWPNlpESDYSSVGKGKGSGFNINLPWnKVGMTNSDYLAAFFHVLLPVAYEFDPELVIVS 263
Cdd:cd10000 175 AFSFTSKVMTVSLHKYS-PGFFPG--TGDVSDVGLGKGKYYTVNVPL-RDGIQDEQYLQIFTAVVPEIVAAFRPEAVVLQ 250

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 264 AGFDSAIGDPegeMCALpeifaHLThllmPLAAGK-MCVVLE----------GGYNLTSLgqSVCQT--VHSLLGDPTPR 330
Cdd:cd10000 251 CGADTLAGDP---MGAF-----NLT----PVGIGKcLKYVLGwklptlilggGGYNLANT--ARCWTylTGLILGEPLSS 316
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
 30-312 1.59e-34

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: 133.48  E-value: 1.59e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  30 PERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQTPGMNVEELMAFSKKYN---DVYFHQNIYHCAK 106
Cdd:cd09991  19 PHRIRMTHSLILSYGLYKKMEIYRPRPATAEELTKFHSDDYIDFLRSVSPDNMKEFKKQLERFNvgeDCPVFDGLYEYCQ 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 107 LAAGATLQLVdsvmkREVRNGMA--LVRPPG--HHSQRSAANGFCVFNNVAFAALYAKKNYnlNRILIVDWDVHHGQGIQ 182
Cdd:cd09991  99 LYAGGSIAAA-----VKLNRGQAdiAINWAGglHHAKKSEASGFCYVNDIVLAILELLKYH--QRVLYIDIDIHHGDGVE 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 183 YCFEEDPSVLYFSWHRYEHQSFwpnlPESDYSSVGKGKGSGFNINLPWNKvGMTNSDYLAAFFHVLLPVAYEFDPELVIV 262
Cdd:cd09991 172 EAFYTTDRVMTVSFHKFGEYFF----PGTGLRDIGAGKGKYYAVNVPLKD-GIDDESYLQIFEPVLSKVMEVFQPSAVVL 246

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 41054267 263 SAGFDSAIGDPEGE----MCALPEIFAHLTHLLMPlaagkMCVVLEGGYNLTSL 312
Cdd:cd09991 247 QCGADSLAGDRLGCfnlsIKGHAKCVKFVKSFNIP-----LLVLGGGGYTLRNV 295
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 37-308 7.28e-33

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: 127.61  E-value: 7.28e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  37 YEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQtpGMNVEELMafsKKYNDVYFHQNIYHcAKLAAGATLQLV 116
Cdd:cd09993  12 REALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLESLKS--GELSREEI---RRIGFPWSPELVER-TRLAVGGTILAA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 117 DSVMKRevrnGMAlVRPPG--HHSQRSAANGFCVFNNVAFAALYAKKNYNLNRILIVDWDVHHGQGIQYCFEEDPSVLYF 194
Cdd:cd09993  86 RLALEH----GLA-INLAGgtHHAFPDRGEGFCVFNDIAIAARVLLAEGLVRRVLIVDLDVHQGNGTAAIFADDPSVFTF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 195 SWHryeHQSFWPNLPEsdyssvgkgkGSGFNINLPWnkvGMTNSDYLAAFFHVLLPVAYEFDPELVIVSAGFDSAIGDPE 274
Cdd:cd09993 161 SMH---GEKNYPFRKE----------PSDLDVPLPD---GTGDDEYLAALEEALPRLLAEFRPDLVFYNAGVDVLAGDRL 224

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 41054267 275 GEMCALPE--------IFAHLTHLLMPLAagkmcVVLEGGYN 308
Cdd:cd09993 225 GRLSLSLEglrerdrlVLRFARARGIPVA-----MVLGGGYS 261
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
 9-272 3.98e-28

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: 115.25  E-value: 3.98e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267   9 FDEEMSRYKLLWTDPAceieVPERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQ-TPG----MNVE 83
Cdd:cd11598   5 FNSRVEDYHFGRTHPM----KPFRLTLTKHLVMGYGLHKAMDTYEARAATREELRQFHDADYLDFLSKvSPEnanqLRFD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  84 ELMAFsKKYNDVYFHQNIYHCAKLAAGATLQlvdsvMKREVRNG---MALVRPPG-HHSQRSAANGFCVFNNVAFAALYA 159
Cdd:cd11598  81 KAEPF-NIGDDCPVFDGMYDYCQLYAGASLD-----AARKLCSGqsdIAINWSGGlHHAKKSEASGFCYVNDIVLAILNL 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 160 KKNYNlnRILIVDWDVHHGQGIQYCFEEDPSVLYFSWHRYEHQsFWPNlpESDYSSVGKGKGSGFNINLPWNKvGMTNSD 239
Cdd:cd11598 155 LRYFP--RVLYIDIDVHHGDGVEEAFYRTDRVMTLSFHKYNGE-FFPG--TGDLDDNGGTPGKHFALNVPLED-GIDDEQ 228

                       250       260       270
                ....*....|....*....|....*....|...
gi 41054267 240 YLAAFFHVLLPVAYEFDPELVIVSAGFDSAIGD 272
Cdd:cd11598 229 YNLLFKSIIGPTIEKFQPSAIVLQCGADSLGGD 261
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
 32-310 2.72e-26

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: 109.28  E-value: 2.72e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  32 RLTVSYEALRTHGLAQ-RCKAVPVRQATEQEILLAHSEEYLEAVKqtpgmnveelmafsKKYN---DVYFHQNIYHCAKL 107
Cdd:cd11680  21 RSSLVHSLIRAYGLLQhFDEIIEPERATRKDLTKYHDKDYVDFLL--------------KKYGledDCPVFPFLSMYVQL 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 108 AAGATLQLVDSVmKREVRNGMALVRPPG-HHSQRSAANGFCVFNNVAFAALYAKKnYNLNRILIVDWDVHHGQGIQYCFE 186
Cdd:cd11680  87 VAGSSLALAKHL-ITQVERDIAINWYGGrHHAQKSRASGFCYVNDIVLAILRLRR-ARFRRVFYLDLDLHHGDGVESAFF 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 187 EDPSVLYFSWHRYEhQSFWPNLPESDYSSVgkgkgsGFNINLPwNKVGMTNSDYLAAFFHVLLPVAYEFDPELVIVSAGF 266
Cdd:cd11680 165 FSKNVLTCSIHRYD-PGFFPGTGSLKNSSD------KGMLNIP-LKRGLSDKTLLRIIDSIVRPLIEKFEPEVIVIQCGC 236

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 41054267 267 DSAIGDPEGEMCALPEIFAHLTHLLMPLAAGKMCVVL-EGGYNLT 310
Cdd:cd11680 237 DGLSGDPHKEWNLTIRGYGSVIELLLKEFKDKPTLLLgGGGYNHT 281
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
 30-275 1.77e-22

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


Pssm-ID: 212534 [Multi-domain]  Cd Length: 371  Bit Score: 99.75  E-value: 1.77e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  30 PERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQTPGMNVEELMAFSKKYN---DVYFHQNIYHCAK 106
Cdd:cd10010  29 PHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNvgeDCPVFDGLFEFCQ 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 107 LAAGATlqlVDSVMKREVRNGMALVRPPG--HHSQRSAANGFCVFNNVAFAALYAKKNYNlnRILIVDWDVHHGQGIQYC 184
Cdd:cd10010 109 LSAGGS---VASAVKLNKQQTDIAVNWAGglHHAKKSEASGFCYVNDIVLAILELLKYHQ--RVLYIDIDIHHGDGVEEA 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 185 FEEDPSVLYFSWHRYehQSFWPNlpESDYSSVGKGKGSGFNINLPWnKVGMTNSDYLAAFFHVLLPVAYEFDPELVIVSA 264
Cdd:cd10010 184 FYTTDRVMTVSFHKY--GEYFPG--TGDLRDIGAGKGKYYAVNYPL-RDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQC 258

                       250
                ....*....|.
gi 41054267 265 GFDSAIGDPEG 275
Cdd:cd10010 259 GADSLSGDRLG 269
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
 9-312 2.93e-22

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


Pssm-ID: 212522 [Multi-domain]  Cd Length: 353  Bit Score: 98.68  E-value: 2.93e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267   9 FDEEMSRYKLLWTDPACEIEVPERLTVS--YEALRTHGLAQRCKAVPVRQATEQEILLAHSEeyleaVKQTpgmnveelm 86
Cdd:cd09998   5 YKHRYSRSKTSKSYLSTIVERPERLRASvlGLSAAVHGSKWSAELIEMCDMAEAKLAKGESE-----IPAH--------- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  87 afskkyndvyFHQN-IYHCAK------LAAGATLQLVDSVMKREV---RNGMALVRPPGHHSQRSAANGFCVFNNVAFAA 156
Cdd:cd09998  71 ----------LPQGdLYLCPEsldaiqGALGAVCEAVDSVFKPESpgtKRAFVAIRPPGHHCSESTPSGFCWVNNVHVGA 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 157 LYAKKNYNLNRILIVDWDVHHGQGIQ-YCFE-----------------------EDPSVLYFSWH---RYEHQSFWPNLP 209
Cdd:cd09998 141 AHAYLTHGITRVVILDIDLHHGNGTQdIAWRinaeankqalesssyddfkpagaPGLRIFYSSLHdinSFPCEDGDPAKV 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 210 ESDYSSVGKGKGSGF-NINL-PWNkvgmTNSDY---LAAFFHVLLPVAYEF-------DPE--LVIVSAGFDSAIGDPEG 275
Cdd:cd09998 221 KDASVSIDGAHGQWIwNVHLqPWT----TEEDFwelYYPKYRILFEKAAEFlrlttaaTPFktLVFISAGFDASEHEYES 296

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 41054267 276 eM----CALP-EIFAHLT----HLLMPLAAGKMCVVLEGGYNLTSL 312
Cdd:cd09998 297 -MqrhgVNVPtSFYYRFArdavRFADAHAHGRLISVLEGGYSDRAL 341
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
 30-275 2.75e-20

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


Pssm-ID: 212535 [Multi-domain]  Cd Length: 366  Bit Score: 93.20  E-value: 2.75e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  30 PERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQTPGMNVEELMAFSKKYN---DVYFHQNIYHCAK 106
Cdd:cd10011  25 PHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNvgeDCPVFDGLFEFCQ 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 107 LAAGATLqlVDSVMKREVRNGMALVRPPG-HHSQRSAANGFCVFNNVAFAALYAKKNYnlNRILIVDWDVHHGQGIQYCF 185
Cdd:cd10011 105 LSTGGSV--AGAVKLNRQQTDMAVNWAGGlHHAKKSEASGFCYVNDIVLAILELLKYH--QRVLYIDIDIHHGDGVEEAF 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 186 EEDPSVLYFSwhryeHQSFWPNLPES-DYSSVGKGKGSGFNINLPWnKVGMTNSDYLAAFFHVLLPVAYEFDPELVIVSA 264
Cdd:cd10011 181 YTTDRVMTVS-----FHKYGEYFPGTgDLRDIGAGKGKYYAVNFPM-RDGIDDESYGQIFKPIISKVMEMYQPSAVVLQC 254

                       250
                ....*....|.
gi 41054267 265 GFDSAIGDPEG 275
Cdd:cd10011 255 GADSLSGDRLG 265
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
 30-275 7.42e-19

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


Pssm-ID: 212528 [Multi-domain]  Cd Length: 375  Bit Score: 89.10  E-value: 7.42e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  30 PERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQTPGMNVEELMAFSKKYN---DVYFHQNIYHCAK 106
Cdd:cd10004  25 PHRIRMAHSLVMNYGLYKKMEIYRAKPATKNEMTQFHTDEYIDFLSRVTPDNMEKFQKEQVKYNvgdDCPVFDGLFEFCS 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 107 LAAGATLQLVDSVMKREVRngMALVRPPG-HHSQRSAANGFCVFNNVAFAALYAKKNYNlnRILIVDWDVHHGQGIQYCF 185
Cdd:cd10004 105 ISAGGSMEGAARLNRGKCD--IAVNWAGGlHHAKKSEASGFCYVNDIVLGILELLRYHQ--RVLYIDIDVHHGDGVEEAF 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 186 EEDPSVLYFSWHRYehQSFWPNLPESDYSSVGKGKGSGFNINLpwnKVGMTNSDYLAAFFHVLLPVAYEFDPELVIVSAG 265
Cdd:cd10004 181 YTTDRVMTCSFHKY--GEYFPGTGELRDIGIGTGKNYAVNVPL---RDGIDDESYKSIFEPVIKHVMEWYQPEAVVLQCG 255

                       250
                ....*....|
gi 41054267 266 FDSAIGDPEG 275
Cdd:cd10004 256 GDSLSGDRLG 265
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
 30-272 3.59e-18

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: 87.07  E-value: 3.59e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  30 PERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQTPGMNVEELMAFSKKYN---DVYFHQNIYHCAK 106
Cdd:cd10005  24 PHRLALTHSLVLHYGLYKKMQVYKPYRASAHDMCRFHSEDYIDFLQRVTPQNIQGFTKSLNQFNvgdDCPVFPGLFDFCS 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 107 LAAGATLQLVDSVMKREVrnGMALVRPPG-HHSQRSAANGFCVFNNVAFAALYAKKNYNlnRILIVDWDVHHGQGIQYCF 185
Cdd:cd10005 104 MYTGASLEGATKLNHKIC--DIAINWSGGlHHAKKFEASGFCYVNDIVIAILELLKYHP--RVLYIDIDIHHGDGVQEAF 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 186 EEDPSVLYFSWHRYEHQsFWPNlpESDYSSVGKGKGSGFNINLPWnKVGMTNSDYLAAFFHVLLPVAYEFDPELVIVSAG 265
Cdd:cd10005 180 YLTDRVMTVSFHKYGNY-FFPG--TGDMYEVGAESGRYYSVNVPL-KDGIDDQSYLQLFKPVIQQVIDFYQPTCIVLQCG 255


                ....*..
gi 41054267 266 FDSAIGD 272
Cdd:cd10005 256 ADSLGCD 262
PTZ00063 PTZ00063
histone deacetylase; Provisional
 30-275 3.09e-17

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 84.86  E-value: 3.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267   30 PERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQTPGMNVEELMAFSKKYN-----DVYFHQNIYHC 104
Cdd:PTZ00063  27 PQRIRMAHALILSYDLYKHMEIYRPHKSVEPELVLFHDEEYVDFLSSISPENYRDFTYQLKRFNvgeatDCPVFDGLFEF 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  105 AKLAAGATLqlvDSVMKREVRNGMALVRPPG--HHSQRSAANGFCVFNNVAFAALYAKKNYNlnRILIVDWDVHHGQGIQ 182
Cdd:PTZ00063 107 QQSCAGASI---DGAYKLNNHQADICVNWSGglHHAKRSEASGFCYINDIVLGILELLKYHA--RVMYIDIDVHHGDGVE 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  183 YCFEEDPSVLYFSWHRYehQSFWPNlpESDYSSVGKGKGSGFNINLPWNKvGMTNSDYLAAFFHVLLPVAYEFDPELVIV 262
Cdd:PTZ00063 182 EAFYVTHRVMTVSFHKF--GDFFPG--TGDVTDIGVAQGKYYSVNVPLND-GIDDDSFVDLFKPVISKCVEVYRPGAIVL 256

                        250
                 ....*....|...
gi 41054267  263 SAGFDSAIGDPEG 275
Cdd:PTZ00063 257 QCGADSLTGDRLG 269
PTZ00346 PTZ00346
histone deacetylase; Provisional
 30-275 2.30e-14

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 75.84  E-value: 2.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267   30 PERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVkqtpGMNVEELMAFSKKYNDVYFHQN-------IY 102
Cdd:PTZ00346  47 PYRVLAAMEIVRSLKIDAHCRTVVPPLVKVEELMAYHTDTYLANL----GLHSCRSWLWNAETSKVFFSGDcppveglME 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  103 HCAKLAAGAtlqLVDSVMKREVRNGMALVRPPG-HHSQRSAANGFCVFNNVAFAALYAKKNYnlNRILIVDWDVHHGQGI 181
Cdd:PTZ00346 123 HSIATASGT---LMGAVLLNSGQVDVAVHWGGGmHHSKCGECSGFCYVNDIVLGILELLKCH--DRVLYVDIDMHHGDGV 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267  182 QYCFEEDPSVLYFSWHRYeHQSFWPNLPESdySSVGKGKGSGFNINLP-WNkvGMTNSDYLAAFFHVLLPVAYEFDPELV 260
Cdd:PTZ00346 198 DEAFCTSDRVFTLSLHKF-GESFFPGTGHP--RDVGYGRGRYYSMNLAvWD--GITDFYYLGLFEHALHSIVRRYSPDAI 272

                        250
                 ....*....|....*
gi 41054267  261 IVSAGFDSAIGDPEG 275
Cdd:PTZ00346 273 VLQCGADSLAGDRLG 287
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 559-665 2.57e-06

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: 50.00  E-value: 2.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 559 AGFMQALLGLILPVAYEFNPALVL---------GIVE-ETAAKTRLmrvWGHMTCLIQGLARGRMLTLLQG-YDKDLL-- 625
Cdd:cd10002 219 ADYLAIFHHILLPLALEFQPELVLvsagfdasiGDPEgEMAVTPAG---YAHLTRLLMGLAGGKLLLVLEGgYLLESLae 295

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 41054267 626 --ELTVSALSGASISPLGPLrAPKPEDVEMMEKQRQRLQERW 665
Cdd:cd10002 296 svSMTLRGLLGDPLPPLAPP-IPIRSVLETILNAIAHLSPRW 336
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 559-665 1.75e-05

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: 47.55  E-value: 1.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 559 AGFMQALLGLILPVAYEFNPALVL-------GIVEETAAKTRLMRVWGHMTCLIQGLARGRMLTLLQ-GYD-KDLLE--- 626
Cdd:cd11683 219 ADYLAAFFHVLLPLAFEFDPELVLvsagfdsAIGDPEGQMCATPECFAHLTHLLMVLAGGKLCAVLEgGYHlESLAEsvc 298

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 41054267 627 LTVSALSGASISPLGPLRAPKPEDVEMMEKQRQRLQERW 665
Cdd:cd11683 299 MTVQTLLGDPLPRLSGEMTPCQSALESIQNVRAAQAPYW 337
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 559-633 2.72e-04

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: 43.49  E-value: 2.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 559 AGFMQALLGLILPVAYEFNPALVLGIVEETAAKTR---LMRV----WGHMTCLIQGLARGRMLTLLQ-GYDKDllELTVS 630
Cdd:cd11600 219 ADYIYAFQRIVMPIAYEFDPDLVIISAGFDAADGDelgQCHVtpagYAHMTHMLMSLAGGKLVVALEgGYNLD--AISDS 296


                ...
gi 41054267 631 ALS 633
Cdd:cd11600 297 ALA 299
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 105-268 1.66e-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: 40.44  E-value: 1.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 105 AKLAAGATLQLVdsvmkREVRNGMALVrppGHHSQrsaANGfcvfNNVAFAALYakknynlNRILIVDWDVHHG------ 178
Cdd:cd09987  11 HELLAGVVVAVL-----KDGKVPVVLG---GDHSI---ANG----AIRAVAELH-------PDLGVIDVDAHHDvrtpea 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054267 179 --------QGIQYCFEEDPSVLYFSWHRYEHQSFWPNlpesdyssvGKGKGSGFNINLPWNKVgmTNSDYLAAFFHVLLP 250
Cdd:cd09987  69 fgkgnhhtPRHLLCEPLISDVHIVSIGIRGVSNGEAG---------GAYARKLGVVYFSMTEV--DKLGLGDVFEEIVSY 137

                       170
                ....*....|....*...
gi 41054267 251 VayEFDPELVIVSAGFDS 268
Cdd:cd09987 138 L--GDKGDNVYLSVDVDG 153
 
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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