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Conserved domains on  [gi|1958790669|ref|XP_038935552|]
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polyamine deacetylase HDAC10 isoform X2 [Rattus norvegicus]

Protein Classification

arginase family protein( domain architecture ID 98571)

arginase family protein is a metal-dependent enzyme that catalyzes the hydrolysis of an amide bond, such as arginase-like amidino hydrolases and histone/histone-like deacetylases

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Arginase_HDAC super family cl17011
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
18-322 4.88e-146

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 cd11683:

Pssm-ID: 450134 [Multi-domain]  Cd Length: 337  Bit Score: 426.59  E-value: 4.88e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  18 WDDPECEIECPERLTAALDGLRQRGLEERCQCLSVCEASEEELGLVHSPEYIALVQKTQTLDKEELHTLSKQYDAVYFHP 97
Cdd:cd11683     1 WDDPECEIEVPERLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRETQVMNKEELMAISGKYDAVYFHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  98 DTFHCARLAAGAALRLVDAVLTGAVHNGVALVRPPGHHSQRAAANGFCVFNNVAIAARHAKQKYGLQRILIVDWDVHHGQ 177
Cdd:cd11683    81 NTFHCARLAAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYAKKKYGLHRILIVDWDVHHGQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 178 GIQYIFEDDPSVLYFSWHRYEHGNFWPFLPESDADTVGRGRGQGFTVNLPWNQVGMGNADYLAAFLHVLLPLAFEVTVCL 257
Cdd:cd11683   161 GIQYIFEEDPSVLYFSWHRYEHQRFWPFLRESDYDAVGRGKGLGFNINLPWNKVGMGNADYLAAFFHVLLPLAFEFDPEL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 258 TL-------------------SWCWCQLDSTLL---------------------------LGTLRGRCRPPLSALpilhs 291
Cdd:cd11683   241 VLvsagfdsaigdpegqmcatPECFAHLTHLLMvlaggklcavleggyhleslaesvcmtVQTLLGDPLPRLSGE----- 315
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1958790669 292 cyrcwlvagFVLCWSALESIQSVRTAQTPHW 322
Cdd:cd11683   316 ---------MTPCQSALESIQNVRAAQAPYW 337
 
Name Accession Description Interval E-value
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
18-322 4.88e-146

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: 426.59  E-value: 4.88e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  18 WDDPECEIECPERLTAALDGLRQRGLEERCQCLSVCEASEEELGLVHSPEYIALVQKTQTLDKEELHTLSKQYDAVYFHP 97
Cdd:cd11683     1 WDDPECEIEVPERLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRETQVMNKEELMAISGKYDAVYFHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  98 DTFHCARLAAGAALRLVDAVLTGAVHNGVALVRPPGHHSQRAAANGFCVFNNVAIAARHAKQKYGLQRILIVDWDVHHGQ 177
Cdd:cd11683    81 NTFHCARLAAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYAKKKYGLHRILIVDWDVHHGQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 178 GIQYIFEDDPSVLYFSWHRYEHGNFWPFLPESDADTVGRGRGQGFTVNLPWNQVGMGNADYLAAFLHVLLPLAFEVTVCL 257
Cdd:cd11683   161 GIQYIFEEDPSVLYFSWHRYEHQRFWPFLRESDYDAVGRGKGLGFNINLPWNKVGMGNADYLAAFFHVLLPLAFEFDPEL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 258 TL-------------------SWCWCQLDSTLL---------------------------LGTLRGRCRPPLSALpilhs 291
Cdd:cd11683   241 VLvsagfdsaigdpegqmcatPECFAHLTHLLMvlaggklcavleggyhleslaesvcmtVQTLLGDPLPRLSGE----- 315
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1958790669 292 cyrcwlvagFVLCWSALESIQSVRTAQTPHW 322
Cdd:cd11683   316 ---------MTPCQSALESIQNVRAAQAPYW 337
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
26-250 3.35e-79

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: 252.93  E-value: 3.35e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  26 ECPERLTAALDGLRQRGLEERCQCLSVCEASEEELGLVHSPEYIALVQKT-QTLDKEELHTLSKQYDAVYFHPDTFHCAR 104
Cdd:pfam00850   3 ENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAaPEGGALLLLSYLSGDDDTPVSPGSYEAAL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 105 LAAGAALRLVDAVLTGAVHNGVALVRPPGHHSQRAAANGFCVFNNVAIAARHAKQKYGLQRILIVDWDVHHGQGIQYIFE 184
Cdd:pfam00850  83 LAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLKRVAIVDFDVHHGNGTQEIFY 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958790669 185 DDPSVLYFSWHRYeHGNFWPFlpESDADTVGRGRGQGFTVNLPWNqVGMGNADYLAAFLHVLLPLA 250
Cdd:pfam00850 163 DDPSVLTLSIHQY-PGGFYPG--TGFADETGEGKGKGYTLNVPLP-PGTGDAEYLAAFEEILLPAL 224
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
3-250 1.64e-64

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 214.59  E-value: 1.64e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669   3 TALVYHEDMTATRLLWDDPECeiecPERLTAALDGLRQRGLEERCQCLSVCEASEEELGLVHSPEYIALVQKTQTLDKEE 82
Cdd:COG0123     1 TALIYHPDYLLHDLGPGHPEP----PERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAASLDGGYG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  83 lhtlskQYDA-VYFHPDTFHCARLAAGAALRLVDAVLTGAVHNGVALVRPPGHHSQRAAANGFCVFNNVAIAARHAkQKY 161
Cdd:COG0123    77 ------QLDPdTPVSPGTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGFCLFNNAAIAARYL-LAK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 162 GLQRILIVDWDVHHGQGIQYIFEDDPSVLYFSWHryEHGNFwPFLpeSDADTVGRGRGQGFTVNLPwnqV--GMGNADYL 239
Cdd:COG0123   150 GLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIH--QDPLY-PGT--GAADETGEGAGEGSNLNVP---LppGTGDAEYL 221
                         250
                  ....*....|.
gi 1958790669 240 AAFLHVLLPLA 250
Cdd:COG0123   222 AALEEALLPAL 232
PTZ00063 PTZ00063
histone deacetylase; Provisional
134-242 9.32e-12

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 67.53  E-value: 9.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 134 HHSQRAAANGFCVFNNVAIA-----ARHAkqkyglqRILIVDWDVHHGQGIQYIFEDDPSVLYFSWHRYehGNFWPflPE 208
Cdd:PTZ00063  137 HHAKRSEASGFCYINDIVLGilellKYHA-------RVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFP--GT 205
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958790669 209 SDADTVGRGRGQGFTVNLPWNQvGMGNADYLAAF 242
Cdd:PTZ00063  206 GDVTDIGVAQGKYYSVNVPLND-GIDDDSFVDLF 238
 
Name Accession Description Interval E-value
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
18-322 4.88e-146

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: 426.59  E-value: 4.88e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  18 WDDPECEIECPERLTAALDGLRQRGLEERCQCLSVCEASEEELGLVHSPEYIALVQKTQTLDKEELHTLSKQYDAVYFHP 97
Cdd:cd11683     1 WDDPECEIEVPERLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRETQVMNKEELMAISGKYDAVYFHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  98 DTFHCARLAAGAALRLVDAVLTGAVHNGVALVRPPGHHSQRAAANGFCVFNNVAIAARHAKQKYGLQRILIVDWDVHHGQ 177
Cdd:cd11683    81 NTFHCARLAAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYAKKKYGLHRILIVDWDVHHGQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 178 GIQYIFEDDPSVLYFSWHRYEHGNFWPFLPESDADTVGRGRGQGFTVNLPWNQVGMGNADYLAAFLHVLLPLAFEVTVCL 257
Cdd:cd11683   161 GIQYIFEEDPSVLYFSWHRYEHQRFWPFLRESDYDAVGRGKGLGFNINLPWNKVGMGNADYLAAFFHVLLPLAFEFDPEL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 258 TL-------------------SWCWCQLDSTLL---------------------------LGTLRGRCRPPLSALpilhs 291
Cdd:cd11683   241 VLvsagfdsaigdpegqmcatPECFAHLTHLLMvlaggklcavleggyhleslaesvcmtVQTLLGDPLPRLSGE----- 315
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1958790669 292 cyrcwlvagFVLCWSALESIQSVRTAQTPHW 322
Cdd:cd11683   316 ---------MTPCQSALESIQNVRAAQAPYW 337
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
18-252 8.40e-125

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: 372.41  E-value: 8.40e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  18 WDDPECEIECPERLTAALDGLRQRGLEERCQCLSVCEASEEELGLVHSPEYIALVQKTQTLDKEELHTLSKQYDAVYFHP 97
Cdd:cd10002     1 CNWDSNHIECPERLEAILERLTQDGLLERCVKIPAREAEEDEILLVHSQEYIDLVKSTETMEKEELESLCSGYDSVYLCP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  98 DTFHCARLAAGAALRLVDAVLTGAVHNGVALVRPPGHHSQRAAANGFCVFNNVAIAARHAKQKYGLQRILIVDWDVHHGQ 177
Cdd:cd10002    81 STYEAARLAAGSTIELVKAVMAGKIQNGFALIRPPGHHAMRNEANGYCIFNNVAIAAKYAIEKLGLKRILIVDWDVHHGQ 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958790669 178 GIQYIFEDDPSVLYFSWHRYEHGNFWPFLPESDADTVGRGRGQGFTVNLPWNQVGMGNADYLAAFLHVLLPLAFE 252
Cdd:cd10002   161 GTQQGFYEDPRVLYFSIHRYEHGRFWPHLFESDYDYIGVGHGYGFNVNVPLNQTGLGDADYLAIFHHILLPLALE 235
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
7-325 9.58e-111

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: 336.62  E-value: 9.58e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669   7 YHEDMTATRLLWDdpECEIECPERLTAALDGLRQRGLEERCQCLSVCEASEEELGLVHSPEYIALVQKTQTLDKEELHTL 86
Cdd:cd10003     1 YDQRMMNHHNLWD--PGHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHLDEMKSLEKMKPRELNRL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  87 SKQYDAVYFHPDTFHCARLAAGAALRLVDAVLTGAVHNGVALVRPPGHHSQRAAANGFCVFNNVAIAARHAKQKYGLQRI 166
Cdd:cd10003    79 GKEYDSIYIHPDSYQCALLAAGCVLQVVEAVLTGESRNGVAIVRPPGHHAEQDTACGFCFFNNVAIAARYAQKKYGLKRI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 167 LIVDWDVHHGQGIQYIFEDDPSVLYFSWHRYEHGNFWPFLPESDADTVGRGRGQGFTVNLPWNQVGMGNADYLAAFLHVL 246
Cdd:cd10003   159 LIVDWDVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSPEGNYDVVGKGKGEGFNVNIPWNKGGMGDAEYIAAFQQVV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 247 LPLAFE--------------------------------------------VTVCL-------TLSWCWCQLDSTLLlgtl 275
Cdd:cd10003   239 LPIAYEfnpelvlvsagfdaargdplggckvtpegyahmthmlmslaggrVIVILeggynltSISESMSMCTKTLL---- 314
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958790669 276 rGRCRPPLSALpilhscyrcwlvagFVLCWSALESIQSVRTAQTPHWTSL 325
Cdd:cd10003   315 -GDPPPVLDLP--------------RPPCSSALKSINNVLQVHQKYWKSL 349
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
17-252 1.69e-108

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: 330.28  E-value: 1.69e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  17 LWDdpECEIECPERLTAALDGLRQRGLEERCQCLSVCEASEEELGLVHSPEYIALVQKTQTLDKEELHTLSKQYDAVYFH 96
Cdd:cd11682     2 LWD--ESFPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYVALMKSTQYMTEEELRTLADTYDSVYLH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  97 PDTFHCARLAAGAALRLVDAVLTGAVHNGVALVRPPGHHSQRAAANGFCVFNNVAIAARHAKQKYGLQRILIVDWDVHHG 176
Cdd:cd11682    80 PNSYSCACLAVGSVLQLVDKVLGGEIRNGLAIVRPPGHHAQHDKMDGYCMFNNVAIAARYAQQKHGVQRVLIVDWDVHHG 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958790669 177 QGIQYIFEDDPSVLYFSWHRYEHGNFWPFLPESDADTVGRGRGQGFTVNLPWNQVGMGNADYLAAFLHVLLPLAFE 252
Cdd:cd11682   160 QGTQFIFEQDPSVLYFSIHRYEQGRFWPHLKESDSSAVGFGRGEGYNINVPWNQVGMRDADYIAAFLHVLLPVALE 235
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
26-252 1.48e-86

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: 272.06  E-value: 1.48e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  26 ECPERLTAALDGLRQRGLEERCQCLSVCEASEEELGLVHSPEYIALVQKTQTLDKEELHtlskqyDAVYFHPDTFHCARL 105
Cdd:cd09992     3 ERPERLLAILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYIERVEETCEAGGGYLD------PDTYVSPGSYEAALL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 106 AAGAALRLVDAVLTGAVHNGVALVRPPGHHSQRAAANGFCVFNNVAIAARHAKQKYGLQRILIVDWDVHHGQGIQYIFED 185
Cdd:cd09992    77 AAGAALAAVDAVLSGEAENAFALVRPPGHHAEPDRAMGFCLFNNVAIAARYAQKRYGLKRVLIVDWDVHHGNGTQDIFYD 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958790669 186 DPSVLYFSWHRYehgNFWPFlpESDADTVGRGRGQGFTVNLPWNQvGMGNADYLAAFLHVLLPLAFE 252
Cdd:cd09992   157 DPSVLYFSIHQY---PFYPG--TGAAEETGGGAGEGFTINVPLPP-GSGDAEYLAAFEEVLLPIARE 217
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
26-252 5.60e-80

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: 255.73  E-value: 5.60e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  26 ECPERLTAALDGLRQRGLEERCQCLSVCEASEEELGLVHSPEYIALVQKTQTLDKEELHTLSKQY--DAVYFHPDTFHCA 103
Cdd:cd11600     5 EDPSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEHWDRVEATEKMSDEQLKDRTEIFerDSLYVNNDTAFCA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 104 RLAAGAALRLVDAVLTGAVHNGVALVRPPGHHSQRAAANGFCVFNNVAIAARHAKQKY--GLQRILIVDWDVHHGQGIQY 181
Cdd:cd11600    85 RLSCGGAIEACRAVAEGRVKNAFAVVRPPGHHAEPDESMGFCFFNNVAVAAKWLQTEYpdKIKKILILDWDIHHGNGTQR 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958790669 182 IFEDDPSVLYFSWHRYEHGNFWPFLPESDADTVGRGRGQGFTVNLPWNQVGMGNADYLAAFLHVLLPLAFE 252
Cdd:cd11600   165 AFYDDPNVLYISLHRFENGGFYPGTPYGDYESVGEGAGLGFNVNIPWPQGGMGDADYIYAFQRIVMPIAYE 235
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
26-250 3.35e-79

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: 252.93  E-value: 3.35e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  26 ECPERLTAALDGLRQRGLEERCQCLSVCEASEEELGLVHSPEYIALVQKT-QTLDKEELHTLSKQYDAVYFHPDTFHCAR 104
Cdd:pfam00850   3 ENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAaPEGGALLLLSYLSGDDDTPVSPGSYEAAL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 105 LAAGAALRLVDAVLTGAVHNGVALVRPPGHHSQRAAANGFCVFNNVAIAARHAKQKYGLQRILIVDWDVHHGQGIQYIFE 184
Cdd:pfam00850  83 LAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLKRVAIVDFDVHHGNGTQEIFY 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958790669 185 DDPSVLYFSWHRYeHGNFWPFlpESDADTVGRGRGQGFTVNLPWNqVGMGNADYLAAFLHVLLPLA 250
Cdd:pfam00850 163 DDPSVLTLSIHQY-PGGFYPG--TGFADETGEGKGKGYTLNVPLP-PGTGDAEYLAAFEEILLPAL 224
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
3-250 1.64e-64

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 214.59  E-value: 1.64e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669   3 TALVYHEDMTATRLLWDDPECeiecPERLTAALDGLRQRGLEERCQCLSVCEASEEELGLVHSPEYIALVQKTQTLDKEE 82
Cdd:COG0123     1 TALIYHPDYLLHDLGPGHPEP----PERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAASLDGGYG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  83 lhtlskQYDA-VYFHPDTFHCARLAAGAALRLVDAVLTGAVHNGVALVRPPGHHSQRAAANGFCVFNNVAIAARHAkQKY 161
Cdd:COG0123    77 ------QLDPdTPVSPGTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGFCLFNNAAIAARYL-LAK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 162 GLQRILIVDWDVHHGQGIQYIFEDDPSVLYFSWHryEHGNFwPFLpeSDADTVGRGRGQGFTVNLPwnqV--GMGNADYL 239
Cdd:COG0123   150 GLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIH--QDPLY-PGT--GAADETGEGAGEGSNLNVP---LppGTGDAEYL 221
                         250
                  ....*....|.
gi 1958790669 240 AAFLHVLLPLA 250
Cdd:COG0123   222 AALEEALLPAL 232
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
2-252 3.03e-62

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: 211.05  E-value: 3.03e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669   2 GTALVYHEDMTATRLLWDDPECEIECPERLTAALDGLRQRGLEERCQCLSVCEASEEELGLVHSPEYIALV----QKTQT 77
Cdd:cd11681     2 TTGLAYDPLMLKHQCICGNNSSHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTLLYgtnpLSRLK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  78 LDKEELHTLSKQY-------------DAVYFHPDTFHCARLAAGAALRLVDAVLTGAVHNGVALVRPPGHHSQRAAANGF 144
Cdd:cd11681    82 LDPTKLAGLPQKSfvrlpcggigvdsDTVWNELHTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQAMGF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 145 CVFNNVAIAARHAKQKYGLQRILIVDWDVHHGQGIQYIFEDDPSVLYFSWHRYEHGNFWPflPESDADTVGRGRGQGFTV 224
Cdd:cd11681   162 CFFNSVAIAAKQLQQKLKLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFP--GTGAPTEVGSGAGEGFNV 239
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958790669 225 NLPWN---QVGMGNADYLAAFLHVLLPLAFE 252
Cdd:cd11681   240 NIAWSgglDPPMGDAEYLAAFRTVVMPIARE 270
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
3-250 5.20e-57

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: 196.63  E-value: 5.20e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669   3 TALVYHEDM-----------TATRLLWDDPECEIECPERLTAALDGLRQRGLEERCQCLSVCEASEEELGLVHSPEYIAL 71
Cdd:cd09996     1 TGFVWDERYlwhdtgtgalfLPVGGLLVQPGRHPENPETKRRIKNLLEVSGLSDHLVLITPRPATDEELLRVHTPEYIDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  72 VQKTQTLDKEELHTLSkqydavYFHPDTFHCARLAAGAALRLVDAVLTGAVHNGVALVRPPGHHSQRAAANGFCVFNNVA 151
Cdd:cd09996    81 VKAASAAGGGEAGGGT------PFGPGSYEIALLAAGGAIAAVDAVLDGEVDNAYALVRPPGHHAEPDQGMGFCLFNNVA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 152 IAARHAKQKYGLQRILIVDWDVHHGQGIQYIFEDDPSVLYFSWHryEHGNFwPflPES-DADTVGRGRGQGFTVNLPWNQ 230
Cdd:cd09996   155 IAARHALAVGGVKRVAVVDWDVHHGNGTQAIFYDDPDVLTISLH--QDRCF-P--PDSgAVEERGEGAGEGYNLNIPLPP 229
                         250       260
                  ....*....|....*....|
gi 1958790669 231 vGMGNADYLAAFLHVLLPLA 250
Cdd:cd09996   230 -GSGDGAYLHAFERIVLPAL 248
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
26-248 4.38e-53

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: 183.48  E-value: 4.38e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  26 ECPERLTAALDGLRQRGLEERCQCLSVCEASEEELGLVHSPEYIALVQKTQtlDKEELHTLskqyDA-VYFHPDTFHCAR 104
Cdd:cd11599     3 ESPERLEAILDALIASGLDRLLRQLEAPPATREQLLRVHDAAYVDRLEAAA--PEEGLVQL----DPdTAMSPGSLEAAL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 105 LAAGAALRLVDAVLTGAVHNGVALVRPPGHHSQRAAANGFCVFNNVAIAARHAKQKYGLQRILIVDWDVHHGQGIQYIFE 184
Cdd:cd11599    77 RAAGAVVAAVDAVMAGEARNAFCAVRPPGHHAERDKAMGFCLFNNVAIAAAHALAHHGLERVAIVDFDVHHGNGTEDIFR 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958790669 185 DDPSVLYFSWHRYehgnfwPFLPESDAdtvGRGRGQGFTVNLPWNQvGMGNADYLAAFLHVLLP 248
Cdd:cd11599   157 DDPRVLFCSSHQH------PLYPGTGA---PDETGHGNIVNVPLPA-GTGGAEFREAVEDRWLP 210
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
3-259 8.43e-52

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: 182.90  E-value: 8.43e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669   3 TALVYHEDMTATRLLWDDPECEIECPERLTAALDGLRQRGLEERCQCLSVCEASEEELGLVHSPEYIALVQKTQ----TL 78
Cdd:cd10008     3 TGLVYDSVMLKHQCSCGDNSNHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPlsrlKL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  79 DKEELHTLSKQYDAVYF-------HPDT----FHCARLAAGAALRLVD---AVLTGAVHNGVALVRPPGHHSQRAAANGF 144
Cdd:cd10008    83 DNGKLAGLLAQRMFVMLpcggvgvDTDTiwneLHSSNAARWAAGSVTDlafKVASRELKNGFAVVRPPGHHADHSTAMGF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 145 CVFNNVAIAARHAKQKYGLQRILIVDWDVHHGQGIQYIFEDDPSVLYFSWHRYEHGNFWPflPESDADTVGRGRGQGFTV 224
Cdd:cd10008   163 CFFNSVAIACRQLQQQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFP--GSGAVDEVGAGSGEGFNV 240
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958790669 225 NLPWN---QVGMGNADYLAAFLHVLLPLAFEVTVCLTL 259
Cdd:cd10008   241 NVAWAgglDPPMGDPEYLAAFRIVVMPIAREFSPDLVL 278
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
26-250 7.95e-50

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: 175.03  E-value: 7.95e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  26 ECPERLTAALDGLRQRGLEERcqcLSVCEASEEELGLVHSPEYIALVQKTQTldkeelhtlskqydAVYFHPDTFHcarl 105
Cdd:cd10001    27 ENPERAEAILDALKRAGLGEV---LPPRDFGLEPILAVHDPDYVDFLETADT--------------DTPISEGTWE---- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 106 aagAALRLVDAVLTGA--VHNGV----ALVRPPGHHSQRAAANGFCVFNNVAIAARHAKQKYGlqRILIVDWDVHHGQGI 179
Cdd:cd10001    86 ---AALAAADTALTAAdlVLEGEraayALCRPPGHHAGRDRAGGFCYFNNAAIAAQYLRDRAG--RVAILDVDVHHGNGT 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958790669 180 QYIFEDDPSVLYFSWHRYEHgNFWPFLPeSDADTVGRGRGQGFTVNLPWnQVGMGNADYLAAFLHVLLPLA 250
Cdd:cd10001   161 QEIFYERPDVLYVSIHGDPR-TFYPFFL-GFADETGEGEGEGYNLNLPL-PPGTGDDDYLAALDEALAAIA 228
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
3-252 9.13e-50

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: 178.31  E-value: 9.13e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669   3 TALVYHEDMTATRLLWDDPECEIECPERLTAALDGLRQRGLEERCQCLSVCEASEEELGLVHSPEYIALVQKT----QTL 78
Cdd:cd10006     6 TGLVYDTLMLKHQCTCGNSNSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNplnrQKL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  79 D-KEELHTLSKQY-----DAVYFHPDTF----HCARLAAGAALRLVD---AVLTGAVHNGVALVRPPGHHSQRAAANGFC 145
Cdd:cd10006    86 DsKKLLGSLASVFvrlpcGGVGVDSDTIwnevHSSGAARLAVGCVVElvfKVATGELKNGFAVVRPPGHHAEESTPMGFC 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 146 VFNNVAIAARHAKQKYGLQRILIVDWDVHHGQGIQYIFEDDPSVLYFSWHRYEHGNFWPflPESDADTVGRGRGQGFTVN 225
Cdd:cd10006   166 YFNSVAIAAKLLQQRLNVSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYDDGNFFP--GSGAPDEVGTGPGVGFNVN 243
                         250       260       270
                  ....*....|....*....|....*....|
gi 1958790669 226 LPWN---QVGMGNADYLAAFLHVLLPLAFE 252
Cdd:cd10006   244 MAFTgglDPPMGDAEYLAAFRTVVMPIASE 273
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
3-254 2.20e-48

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: 174.79  E-value: 2.20e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669   3 TALVYHEDMTATRLLWDDPECEIECPERLTAALDGLRQRGLEERCQCLSVCEASEEELGLVHSpEYIALVQKTQTLDKEE 82
Cdd:cd10007     5 TGLVYDTFMLKHQCTCGNTNVHPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHS-EHHTLLYGTSPLNRQK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  83 LH------TLSKQYDAVY------FHPDT----FHCARLAAGAALRLVD---AVLTGAVHNGVALVRPPGHHSQRAAANG 143
Cdd:cd10007    84 LDskkllgPLSQKMYAVLpcggigVDSDTvwneMHSSSAVRMAVGCLIElafKVAAGELKNGFAVIRPPGHHAEESTAMG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 144 FCVFNNVAIAARHAKQKYGLQRILIVDWDVHHGQGIQYIFEDDPSVLYFSWHRYEHGNFWPflPESDADTVGRGRGQGFT 223
Cdd:cd10007   164 FCFFNSVAIAAKLLQQKLNVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGNFFP--GSGAPDEVGAGPGVGFN 241
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958790669 224 VNLPWN---QVGMGNADYLAAFLHVLLPLAFEVT 254
Cdd:cd10007   242 VNIAWTggvDPPIGDVEYLTAFRTVVMPIANEFS 275
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
3-252 1.27e-39

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: 149.40  E-value: 1.27e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669   3 TALVYHEDMTATRLLWDDPECEIECPERLTAALDGLRQRGLEERCQCLSVCEASEEELGLVHSpEYIALVQKTQTLDKEE 82
Cdd:cd10009     3 TGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHS-EHHSLLYGTNPLDGQK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  83 LHT-------------------LSKQYDAVYFHPDTFHCARLAAGAALRLVDAVLTGAVHNGVALVRPPGHHSQRAAANG 143
Cdd:cd10009    82 LDPrillgddsqkffsslpcggLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 144 FCVFNNVAIAARHAKQKYGLQRILIVDWDVHHGQGIQYIFEDDPSVLYFSWHRYEHGNFWPflPESDADTVGRGRGQGFT 223
Cdd:cd10009   162 FCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFP--GSGAPNEVGTGLGEGYN 239
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958790669 224 VNLPWN---QVGMGNADYLAAFLHVLLPLAFE 252
Cdd:cd10009   240 INIAWTgglDPPMGDVEYLEAFRTIVKPVAKE 271
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
28-250 5.15e-39

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: 145.78  E-value: 5.15e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  28 PERLTAALDGLRQRGLEERCQCLSVCEASEEELGLVHSPEYIALVQ---KTQTLDKEELHTLSKqYDAVYFhPDTFHCAR 104
Cdd:cd09994    21 PPRLSLTKDLLRALGLLPPVDLVPPRPATEEELLLFHTPDYIEAVKeasRGQEPEGRGRLGLGT-EDNPVF-PGMHEAAA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 105 LAAGAALRLVDAVLTGAVHNGVAlvrPPG--HHSQRAAANGFCVFNNVAIAARHAKQKYGlQRILIVDWDVHHGQGIQYI 182
Cdd:cd09994    99 LVVGGTLLAARLVLEGEARRAFN---PAGglHHAMRGRASGFCVYNDAAVAIERLRDKGG-LRVAYVDIDAHHGDGVQAA 174
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958790669 183 FEDDPSVLYFSWHryEHGN-FWPFlpESDADTVGRGRGQGFTVNLPWNQvGMGNADYLAAFLHVLLPLA 250
Cdd:cd09994   175 FYDDPRVLTISLH--ESGRyLFPG--TGFVDEIGEGEGYGYAVNIPLPP-GTGDDEFLRAFEAVVPPLL 238
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
30-252 1.24e-38

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: 143.73  E-value: 1.24e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  30 RLTAALDGLRQRGLEERCQCLSVCEASEEELGLVHSPEYIALVqKTQTLDKEELHtlSKQYDAVYFHPDTFHCARLAAGA 109
Cdd:cd09301     1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNEL-KANFAVATITE--SKPVIFGPNFPVQRHYFRGARLS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 110 ALRLVDA---VLTGAVHNGVALVRPPGHHSQRAAANGFCVFNNVAIAARHAkQKYGLQRILIVDWDVHHGQGIQYIFEDD 186
Cdd:cd09301    78 TGGVVEAaelVAKGELERAFAVVGAGGHHAGKSRAWGFCYFNDVVLAIKFL-RERGISRILIIDTDAHHGDGTREAFYDD 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958790669 187 PSVLYFSWHRYEHGNFwpflpesdadtvGRGRGQGFTVNLPWNQvGMGNADYLAAFLHVLLPLAFE 252
Cdd:cd09301   157 DRVLHMSFHNYDIYPF------------GRGKGKGYKINVPLED-GLGDEEYLDAVERVISKVLEE 209
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
42-252 1.58e-25

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: 108.58  E-value: 1.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  42 GLEERCQCLSVCEASEEELGLVHSPEYIALVQK-TQTLDKEELHTLSKQ----YDAVYFhPDTFHCARLAAGAALRLVDA 116
Cdd:cd10000    34 GLLKQLRVVKPRVATEEELASFHSDEYIQFLKKaSNEGDNDEEPSEQQEfglgYDCPIF-EGIYDYAAAVAGATLTAAQL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 117 VLTGAVHngVALVRPPG-HHSQRAAANGFCVFNNVAIAARHAKQKYglQRILIVDWDVHHGQGIQYIFEDDPSVLYFSWH 195
Cdd:cd10000   113 LIDGKCK--VAINWFGGwHHAQRDEASGFCYVNDIVLGILKLREKF--DRVLYVDLDLHHGDGVEDAFSFTSKVMTVSLH 188
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958790669 196 RYEHGnfwpFLPES-DADTVGRGRGQGFTVNLPWNQvGMGNADYLAAFlHVLLPLAFE 252
Cdd:cd10000   189 KYSPG----FFPGTgDVSDVGLGKGKYYTVNVPLRD-GIQDEQYLQIF-TAVVPEIVA 240
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
54-252 4.32e-22

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: 96.41  E-value: 4.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  54 EASEEELGLVHSPEYIALVqKTQTLDKEELHTLskqydavyFHPDTFHcarlaagaalrLVDAVLTG----------AVH 123
Cdd:cd09993    31 PATREDLLRVHDPEYLESL-KSGELSREEIRRI--------GFPWSPE-----------LVERTRLAvggtilaarlALE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 124 NGVAlVRPPG--HHSQRAAANGFCVFNNVAIAARHAKQKYGLQRILIVDWDVHHGQGIQYIFEDDPSVLYFSWHryeHGN 201
Cdd:cd09993    91 HGLA-INLAGgtHHAFPDRGEGFCVFNDIAIAARVLLAEGLVRRVLIVDLDVHQGNGTAAIFADDPSVFTFSMH---GEK 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958790669 202 FWPFLPE-SDADtvgrgrgqgftVNLPWnqvGMGNADYLAAfLHVLLPLAFE 252
Cdd:cd09993   167 NYPFRKEpSDLD-----------VPLPD---GTGDDEYLAA-LEEALPRLLA 203
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
28-249 2.96e-20

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: 91.88  E-value: 2.96e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  28 PERLTAALDGLRQRGLEERCQCLSVCEASEEELGLVHSPEYIALVQKTQTLDKEELHTLSKQY---------DAVYfhpd 98
Cdd:cd09991    19 PHRIRMTHSLILSYGLYKKMEIYRPRPATAEELTKFHSDDYIDFLRSVSPDNMKEFKKQLERFnvgedcpvfDGLY---- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  99 TFHCARlaagaalrlVDAVLTGAVH--NG---VAlVRPPG--HHSQRAAANGFCVFNNVAIAARHAKQKYglQRILIVDW 171
Cdd:cd09991    95 EYCQLY---------AGGSIAAAVKlnRGqadIA-INWAGglHHAKKSEASGFCYVNDIVLAILELLKYH--QRVLYIDI 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958790669 172 DVHHGQGIQYIFEDDPSVLYFSWHRYehGNFwpFLPESDADTVGRGRGQGFTVNLPWNQvGMGNADYLAAFLHVLLPL 249
Cdd:cd09991   163 DIHHGDGVEEAFYTTDRVMTVSFHKF--GEY--FFPGTGLRDIGAGKGKYYAVNVPLKD-GIDDESYLQIFEPVLSKV 235
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
25-182 1.12e-16

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: 81.73  E-value: 1.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  25 IECPERLTAALDGLR-----QRGLEERcqcLSVCEASEEELGLVHSpeyialvQKTQTLDKEELHTLSKQYDAVyfhpdt 99
Cdd:cd09998    23 VERPERLRASVLGLSaavhgSKWSAEL---IEMCDMAEAKLAKGES-------EIPAHLPQGDLYLCPESLDAI------ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 100 fhcaRLAAGAALRLVDAVLTGAVH---NGVALVRPPGHHSQRAAANGFCVFNNVAIAARHAKQKYGLQRILIVDWDVHHG 176
Cdd:cd09998    87 ----QGALGAVCEAVDSVFKPESPgtkRAFVAIRPPGHHCSESTPSGFCWVNNVHVGAAHAYLTHGITRVVILDIDLHHG 162

                  ....*.
gi 1958790669 177 QGIQYI 182
Cdd:cd09998   163 NGTQDI 168
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
134-249 5.35e-14

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: 73.26  E-value: 5.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 134 HHSQRAAANGFCVFNNVAIAARHAKQKYglQRILIVDWDVHHGQGIQYIFEDDPSVLYFSWHRYeHGNFWPflPESDADT 213
Cdd:cd11598   131 HHAKKSEASGFCYVNDIVLAILNLLRYF--PRVLYIDIDVHHGDGVEEAFYRTDRVMTLSFHKY-NGEFFP--GTGDLDD 205
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958790669 214 VGRGRGQGFTVNLPWNQvGMGNADYLAAFLHVLLPL 249
Cdd:cd11598   206 NGGTPGKHFALNVPLED-GIDDEQYNLLFKSIIGPT 240
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
28-246 1.30e-12

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: 69.71  E-value: 1.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  28 PERLTAALDGLRQRGLEERCQCLSVCEASEEELGLVHSPEYIALVQktqTLDKEELHTLSKQYDAVYFHPDtfhCARLAA 107
Cdd:cd10010    29 PHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLR---SIRPDNMSEYSKQMQRFNVGED---CPVFDG 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 108 GAALRLVDAvlTGAVHNGVALVRPPG----------HHSQRAAANGFCVFNNVAIAARHAKQKYglQRILIVDWDVHHGQ 177
Cdd:cd10010   103 LFEFCQLSA--GGSVASAVKLNKQQTdiavnwagglHHAKKSEASGFCYVNDIVLAILELLKYH--QRVLYIDIDIHHGD 178
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958790669 178 GIQYIFEDDPSVLYFSWHRYehGNFWPflPESDADTVGRGRGQGFTVNLPWNQvGMGNADYLAAFLHVL 246
Cdd:cd10010   179 GVEEAFYTTDRVMTVSFHKY--GEYFP--GTGDLRDIGAGKGKYYAVNYPLRD-GIDDESYEAIFKPVM 242
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
134-249 2.46e-12

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: 68.06  E-value: 2.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 134 HHSQRAAANGFCVFNNVAIAARHAKqKYGLQRILIVDWDVHHGQGIQYIFEDDPSVLYFSWHRYEHGnFWPFLPESDAdt 213
Cdd:cd11680   115 HHAQKSRASGFCYVNDIVLAILRLR-RARFRRVFYLDLDLHHGDGVESAFFFSKNVLTCSIHRYDPG-FFPGTGSLKN-- 190
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958790669 214 vgrgRGQGFTVNLPWNQvGMGNADYLAAFLHVLLPL 249
Cdd:cd11680   191 ----SSDKGMLNIPLKR-GLSDKTLLRIIDSIVRPL 221
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
28-242 5.90e-12

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: 67.81  E-value: 5.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  28 PERLTAALDGLRQRGLEERCQCLSVCEASEEELGLVHSPEYIALVQKTQTLDKEELHTLSKQY----DAVYFhPDTFH-C 102
Cdd:cd10005    24 PHRLALTHSLVLHYGLYKKMQVYKPYRASAHDMCRFHSEDYIDFLQRVTPQNIQGFTKSLNQFnvgdDCPVF-PGLFDfC 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 103 ARLaagaalrlVDAVLTGAV---HN--GVALVRPPG-HHSQRAAANGFCVFNNVAIAARHAkQKYGlQRILIVDWDVHHG 176
Cdd:cd10005   103 SMY--------TGASLEGATklnHKicDIAINWSGGlHHAKKFEASGFCYVNDIVIAILEL-LKYH-PRVLYIDIDIHHG 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958790669 177 QGIQYIFEDDPSVLYFSWHRYehGNFwpFLPES-DADTVGRGRGQGFTVNLPWNQvGMGNADYLAAF 242
Cdd:cd10005   173 DGVQEAFYLTDRVMTVSFHKY--GNY--FFPGTgDMYEVGAESGRYYSVNVPLKD-GIDDQSYLQLF 234
PTZ00063 PTZ00063
histone deacetylase; Provisional
134-242 9.32e-12

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 67.53  E-value: 9.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 134 HHSQRAAANGFCVFNNVAIA-----ARHAkqkyglqRILIVDWDVHHGQGIQYIFEDDPSVLYFSWHRYehGNFWPflPE 208
Cdd:PTZ00063  137 HHAKRSEASGFCYINDIVLGilellKYHA-------RVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFP--GT 205
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958790669 209 SDADTVGRGRGQGFTVNLPWNQvGMGNADYLAAF 242
Cdd:PTZ00063  206 GDVTDIGVAQGKYYSVNVPLND-GIDDDSFVDLF 238
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
134-246 1.96e-11

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: 65.98  E-value: 1.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 134 HHSQRAAANGFCVFNNVAIAARHAKQKYglQRILIVDWDVHHGQGIQYIFEDDPSVLYFSWHRYehGNFWPFLPEsdADT 213
Cdd:cd10004   133 HHAKKSEASGFCYVNDIVLGILELLRYH--QRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKY--GEYFPGTGE--LRD 206
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958790669 214 VGRGRGQGFTVNLPWNQvGMGNADYLAAFLHVL 246
Cdd:cd10004   207 IGIGTGKNYAVNVPLRD-GIDDESYKSIFEPVI 238
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
28-227 5.06e-09

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: 58.54  E-value: 5.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669  28 PERLTAALDGLRQRGLEERCQCLSVCEASEEELGLVHSPEYIALVQktqTLDKEELHTLSKQYDAVYFHPDtfhCARLAA 107
Cdd:cd10011    25 PHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLR---SIRPDNMSEYSKQMQRFNVGED---CPVFDG 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 108 GAALRLVDAvlTGAVHNGVALVRPPG----------HHSQRAAANGFCVFNNVAIAARHAKQKYglQRILIVDWDVHHGQ 177
Cdd:cd10011    99 LFEFCQLST--GGSVAGAVKLNRQQTdmavnwagglHHAKKSEASGFCYVNDIVLAILELLKYH--QRVLYIDIDIHHGD 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958790669 178 GIQYIFEDDPSVLYFSwhryEHGNFWPFLPESDADTVGRGRGQGFTVNLP 227
Cdd:cd10011   175 GVEEAFYTTDRVMTVS----FHKYGEYFPGTGDLRDIGAGKGKYYAVNFP 220
PTZ00346 PTZ00346
histone deacetylase; Provisional
121-246 2.82e-06

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 50.03  E-value: 2.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 121 AVHNGVALvrppgHHSQRAAANGFCVFNNVAIAARHAKQKYglQRILIVDWDVHHGQGIQYIFEDDPSVLYFSWHRYEHg 200
Cdd:PTZ00346  146 AVHWGGGM-----HHSKCGECSGFCYVNDIVLGILELLKCH--DRVLYVDIDMHHGDGVDEAFCTSDRVFTLSLHKFGE- 217
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1958790669 201 NFWPflPESDADTVGRGRGQGFTVNLP-WNqvGMGNADYLAAFLHVL 246
Cdd:PTZ00346  218 SFFP--GTGHPRDVGYGRGRYYSMNLAvWD--GITDFYYLGLFEHAL 260
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
118-202 7.29e-03

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


Pssm-ID: 212513  Cd Length: 217  Bit Score: 38.51  E-value: 7.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790669 118 LTGAVHNGVALVRPP----GHHSQraaANGfcvfnnvaiAARHAKQKYGlqRILIVDWDVHHGQGIQYIF---------- 183
Cdd:cd09987    14 LAGVVVAVLKDGKVPvvlgGDHSI---ANG---------AIRAVAELHP--DLGVIDVDAHHDVRTPEAFgkgnhhtprh 79
                          90       100
                  ....*....|....*....|...
gi 1958790669 184 ----EDDPSVLYFSWHRYEHGNF 202
Cdd:cd09987    80 llcePLISDVHIVSIGIRGVSNG 102
 
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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