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Conserved domains on  [gi|193206283|ref|NP_001122780|]
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UBP-type domain-containing protein [Caenorhabditis elegans]

Protein Classification

histone deacetylase 6( domain architecture ID 10345624)

histone deacetylase 6 (HD6) is a class IIb Zn-dependent enzyme that catalyzes hydrolysis of N(6)-acetyl-lysine of a histone to yield a deacetylated histone (EC 3.5.1.98)

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 ...
440-795 1.98e-148

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 cd10003:

Pssm-ID: 450134 [Multi-domain]  Cd Length: 350  Bit Score: 443.70  E-value: 1.98e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 440 HFDLEEDNHPEKPARTRRILKTLRESGVLEKCVdRNCERIATNEEIRLVHTKKMLEHLRTTETMKDEELMEEAEKeFNSI 519
Cdd:cd10003    8 HHNLWDPGHPECPQRISRIYERHNDLGLLERCL-RLPSRLATEDELLLCHSEEHLDEMKSLEKMKPRELNRLGKE-YDSI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 520 YLTRDTLKVARKAVGAVLQSVDEIFEKDAgqRNALVIVRPPGHHASASKSSGFCIFNNVAVAAKYAQRRHKAKRVLILDW 599
Cdd:cd10003   86 YIHPDSYQCALLAAGCVLQVVEAVLTGES--RNGVAIVRPPGHHAEQDTACGFCFFNNVAIAARYAQKKYGLKRILIVDW 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 600 DVHHGNGTQEIFYEDSNVMYMSIHRHDKGNFYPIGEPKDYSDVGEGAGEGMSVNVPFSGVQMGDNEYQMAFQRVIMPIAY 679
Cdd:cd10003  164 DVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSPEGNYDVVGKGKGEGFNVNIPWNKGGMGDAEYIAAFQQVVLPIAY 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 680 QFNPDLVLISAGFDAAVDDPLGEYKVTPETFALMTYQLSSLAGGRIITVLEGGYNLTSISNSAQAVCEVLQNRSmLRRLr 759
Cdd:cd10003  244 EFNPELVLVSAGFDAARGDPLGGCKVTPEGYAHMTHMLMSLAGGRVIVILEGGYNLTSISESMSMCTKTLLGDP-PPVL- 321
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 193206283 760 eekeqfaTKPQKIESSCIKTIREVCAVQQKYWSILK 795
Cdd:cd10003  322 -------DLPRPPCSSALKSINNVLQVHQKYWKSLR 350
Arginase_HDAC super family cl17011
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
32-366 1.56e-125

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: 383.58  E-value: 1.56e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  32 PTHPESSDRILKIKEALTKTKILEKCTVLTNFlEIDDADLEVTHDKSMVKDLMESEKKTQEDINSQCEKYDSVFMTefQN 111
Cdd:cd10002    5 SNHIECPERLEAILERLTQDGLLERCVKIPAR-EAEEDEILLVHSQEYIDLVKSTETMEKEELESLCSGYDSVYLC--PS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 112 SMKVAKDGVACVRDLTNRIMANEASNGFAVVRPPGHHADSVSPCGFCLFNNVAQAAEEAF-FSGAERILIVDLDVHHGHG 190
Cdd:cd10002   82 TYEAARLAAGSTIELVKAVMAGKIQNGFALIRPPGHHAMRNEANGYCIFNNVAIAAKYAIeKLGLKRILIVDWDVHHGQG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 191 TQRIFYDDKRVLYFSIHRHEHGLFWPHLPESDFDHIGSGKGLGYNANLALNETGCTDSDYLSIIFHVLLPLATQFDPHFV 270
Cdd:cd10002  162 TQQGFYEDPRVLYFSIHRYEHGRFWPHLFESDYDYIGVGHGYGFNVNVPLNQTGLGDADYLAIFHHILLPLALEFQPELV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 271 IISAGFDALLGDPLGGMCLTPDGYSHILYHLKSLAQGRMLVVLEGGYNHQISAVAVQRCVRVLLGYAPFSIELNeAPKES 350
Cdd:cd10002  242 LVSAGFDASIGDPEGEMAVTPAGYAHLTRLLMGLAGGKLLLVLEGGYLLESLAESVSMTLRGLLGDPLPPLAPP-IPIRS 320
                        330
                 ....*....|....*.
gi 193206283 351 TVDSCVSLVSVLRHHW 366
Cdd:cd10002  321 VLETILNAIAHLSPRW 336
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
877-939 1.79e-22

Zn-finger in ubiquitin-hydrolases and other protein;


:

Pssm-ID: 460464  Cd Length: 63  Bit Score: 91.55  E-value: 1.79e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193206283  877 CSECQIGAEVWTCLTCYKYNCGRFVNEHAMMHHLSSSHPMALSMADLSVWCYPCDSYVHNPAL 939
Cdd:pfam02148   1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPSL 63
 
Name Accession Description Interval E-value
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
440-795 1.98e-148

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: 443.70  E-value: 1.98e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 440 HFDLEEDNHPEKPARTRRILKTLRESGVLEKCVdRNCERIATNEEIRLVHTKKMLEHLRTTETMKDEELMEEAEKeFNSI 519
Cdd:cd10003    8 HHNLWDPGHPECPQRISRIYERHNDLGLLERCL-RLPSRLATEDELLLCHSEEHLDEMKSLEKMKPRELNRLGKE-YDSI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 520 YLTRDTLKVARKAVGAVLQSVDEIFEKDAgqRNALVIVRPPGHHASASKSSGFCIFNNVAVAAKYAQRRHKAKRVLILDW 599
Cdd:cd10003   86 YIHPDSYQCALLAAGCVLQVVEAVLTGES--RNGVAIVRPPGHHAEQDTACGFCFFNNVAIAARYAQKKYGLKRILIVDW 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 600 DVHHGNGTQEIFYEDSNVMYMSIHRHDKGNFYPIGEPKDYSDVGEGAGEGMSVNVPFSGVQMGDNEYQMAFQRVIMPIAY 679
Cdd:cd10003  164 DVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSPEGNYDVVGKGKGEGFNVNIPWNKGGMGDAEYIAAFQQVVLPIAY 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 680 QFNPDLVLISAGFDAAVDDPLGEYKVTPETFALMTYQLSSLAGGRIITVLEGGYNLTSISNSAQAVCEVLQNRSmLRRLr 759
Cdd:cd10003  244 EFNPELVLVSAGFDAARGDPLGGCKVTPEGYAHMTHMLMSLAGGRVIVILEGGYNLTSISESMSMCTKTLLGDP-PPVL- 321
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 193206283 760 eekeqfaTKPQKIESSCIKTIREVCAVQQKYWSILK 795
Cdd:cd10003  322 -------DLPRPPCSSALKSINNVLQVHQKYWKSLR 350
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
448-749 3.62e-126

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: 383.90  E-value: 3.62e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  448 HPEKPARTRRILKTLRESGVLEKCVDrNCERIATNEEIRLVHTKKMLEHLRTTETMKDEELMEEAEKEFNSIYLTRDTLK 527
Cdd:pfam00850   1 HPENPERLKAILEALREAGLLPDLEI-IAPRPATEEELLLVHSPEYLEFLEEAAPEGGALLLLSYLSGDDDTPVSPGSYE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  528 VARKAVGAVLQSVDEIFEKDAgqRNALVIVRPPGHHASASKSSGFCIFNNVAVAAKYAQRRHKAKRVLILDWDVHHGNGT 607
Cdd:pfam00850  80 AALLAAGGTLAAADAVLSGEA--RNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLKRVAIVDFDVHHGNGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  608 QEIFYEDSNVMYMSIHRHDkGNFYPigEPKDYSDVGEGAGEGMSVNVPFSgVQMGDNEYQMAFQRVIMPIAYQFNPDLVL 687
Cdd:pfam00850 158 QEIFYDDPSVLTLSIHQYP-GGFYP--GTGFADETGEGKGKGYTLNVPLP-PGTGDAEYLAAFEEILLPALEEFQPDLIL 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193206283  688 ISAGFDAAVDDPLGEYKVTPETFALMTYQLSSLA---GGRIITVLEGGYNLTSISNSAQAVCEVL 749
Cdd:pfam00850 234 VSAGFDAHAGDPLGGLNLTTEGFAEITRILLELAdplCIRVVSVLEGGYNLDALARSATAVLAAL 298
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
32-366 1.56e-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: 383.58  E-value: 1.56e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  32 PTHPESSDRILKIKEALTKTKILEKCTVLTNFlEIDDADLEVTHDKSMVKDLMESEKKTQEDINSQCEKYDSVFMTefQN 111
Cdd:cd10002    5 SNHIECPERLEAILERLTQDGLLERCVKIPAR-EAEEDEILLVHSQEYIDLVKSTETMEKEELESLCSGYDSVYLC--PS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 112 SMKVAKDGVACVRDLTNRIMANEASNGFAVVRPPGHHADSVSPCGFCLFNNVAQAAEEAF-FSGAERILIVDLDVHHGHG 190
Cdd:cd10002   82 TYEAARLAAGSTIELVKAVMAGKIQNGFALIRPPGHHAMRNEANGYCIFNNVAIAAKYAIeKLGLKRILIVDWDVHHGQG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 191 TQRIFYDDKRVLYFSIHRHEHGLFWPHLPESDFDHIGSGKGLGYNANLALNETGCTDSDYLSIIFHVLLPLATQFDPHFV 270
Cdd:cd10002  162 TQQGFYEDPRVLYFSIHRYEHGRFWPHLFESDYDYIGVGHGYGFNVNVPLNQTGLGDADYLAIFHHILLPLALEFQPELV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 271 IISAGFDALLGDPLGGMCLTPDGYSHILYHLKSLAQGRMLVVLEGGYNHQISAVAVQRCVRVLLGYAPFSIELNeAPKES 350
Cdd:cd10002  242 LVSAGFDASIGDPEGEMAVTPAGYAHLTRLLMGLAGGKLLLVLEGGYLLESLAESVSMTLRGLLGDPLPPLAPP-IPIRS 320
                        330
                 ....*....|....*.
gi 193206283 351 TVDSCVSLVSVLRHHW 366
Cdd:cd10002  321 VLETILNAIAHLSPRW 336
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
429-749 5.69e-101

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 318.20  E-value: 5.69e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 429 TLIYFnegDDAHFDLE-EDNHPEKPARTRRILKTLRESGVLEKCVDRNCERiATNEEIRLVHTKKMLEHLRTTEtmkdee 507
Cdd:COG0123    1 TALIY---HPDYLLHDlGPGHPEPPERLRAILDALEASGLLDDLELVEPPP-ATEEDLLRVHTPDYVDALRAAS------ 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 508 lmeeAEKEFNSI----YLTRDTLKVARKAVGAVLQSVDEIFEKDAgqRNALVIVRPPGHHASASKSSGFCIFNNVAVAAK 583
Cdd:COG0123   71 ----LDGGYGQLdpdtPVSPGTWEAALLAAGGALAAADAVLEGEA--RNAFALVRPPGHHAERDRAMGFCLFNNAAIAAR 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 584 YAQRrHKAKRVLILDWDVHHGNGTQEIFYEDSNVMYMSIHRHdkgNFYPiGEpKDYSDVGEGAGEGMSVNVPFSgVQMGD 663
Cdd:COG0123  145 YLLA-KGLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD---PLYP-GT-GAADETGEGAGEGSNLNVPLP-PGTGD 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 664 NEYQMAFQRVIMPIAYQFNPDLVLISAGFDAAVDDPLGEYKVTPETFALMTYQLSSLA---GGRIITVLEGGYNLTSISN 740
Cdd:COG0123  218 AEYLAALEEALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELAdhcGGPVVSVLEGGYNLDALAR 297

                 ....*....
gi 193206283 741 SAQAVCEVL 749
Cdd:COG0123  298 SVAAHLETL 306
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
34-333 6.44e-93

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: 296.46  E-value: 6.44e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283   34 HPESSDRILKIKEALTKTKILEKCTVLTnFLEIDDADLEVTHDKSMVKDLMESEKKTQEDINSQCEK-YDSVFMteFQNS 112
Cdd:pfam00850   1 HPENPERLKAILEALREAGLLPDLEIIA-PRPATEEELLLVHSPEYLEFLEEAAPEGGALLLLSYLSgDDDTPV--SPGS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  113 MKVAKDGVACVRDLTNRIMANEASNGFAVVRPPGHHADSVSPCGFCLFNNVAQAAEEAF-FSGAERILIVDLDVHHGHGT 191
Cdd:pfam00850  78 YEAALLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLReKYGLKRVAIVDFDVHHGNGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  192 QRIFYDDKRVLYFSIHRHEHGLFwphlPES-DFDHIGSGKGLGYNANLALNeTGCTDSDYLSIIFHVLLPLATQFDPHFV 270
Cdd:pfam00850 158 QEIFYDDPSVLTLSIHQYPGGFY----PGTgFADETGEGKGKGYTLNVPLP-PGTGDAEYLAAFEEILLPALEEFQPDLI 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193206283  271 IISAGFDALLGDPLGGMCLTPDGYSHILYHLKSLAQ---GRMLVVLEGGYNHQISAVAVQRCVRVL 333
Cdd:pfam00850 233 LVSAGFDAHAGDPLGGLNLTTEGFAEITRILLELADplcIRVVSVLEGGYNLDALARSATAVLAAL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
32-335 2.02e-79

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 260.42  E-value: 2.02e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  32 PTHPESSDRILKIKEALTKTKILEKCTVLTnFLEIDDADLEVTHDKSMVKDLME-SEKKTQEDINSqcekyDSVFmteFQ 110
Cdd:COG0123   16 PGHPEPPERLRAILDALEASGLLDDLELVE-PPPATEEDLLRVHTPDYVDALRAaSLDGGYGQLDP-----DTPV---SP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 111 NSMKVAKDGVACVRDLTNRIMANEASNGFAVVRPPGHHADSVSPCGFCLFNNVAQAAEEAFFSGAERILIVDLDVHHGHG 190
Cdd:COG0123   87 GTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGFCLFNNAAIAARYLLAKGLERVAIVDFDVHHGNG 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 191 TQRIFYDDKRVLYFSIhrHEHGLFwphlPESDFDH-IGSGKGLGYNANLALnETGCTDSDYLSIIFHVLLPLATQFDPHF 269
Cdd:COG0123  167 TQDIFYDDPDVLTISI--HQDPLY----PGTGAADeTGEGAGEGSNLNVPL-PPGTGDAEYLAALEEALLPALEAFKPDL 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193206283 270 VIISAGFDALLGDPLGGMCLTPDGYSHILYHLKSLA---QGRMLVVLEGGYNHQISAVAVQRCVRVLLG 335
Cdd:COG0123  240 IVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELAdhcGGPVVSVLEGGYNLDALARSVAAHLETLLG 308
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
877-939 1.79e-22

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 91.55  E-value: 1.79e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193206283  877 CSECQIGAEVWTCLTCYKYNCGRFVNEHAMMHHLSSSHPMALSMADLSVWCYPCDSYVHNPAL 939
Cdd:pfam02148   1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPSL 63
PTZ00063 PTZ00063
histone deacetylase; Provisional
562-706 2.59e-18

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 88.71  E-value: 2.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 562 HHASASKSSGFCIFNNVAVAAKYAQRRHKakRVLILDWDVHHGNGTQEIFYEDSNVMYMSIHRHdkGNFYPigEPKDYSD 641
Cdd:PTZ00063 137 HHAKRSEASGFCYINDIVLGILELLKYHA--RVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFP--GTGDVTD 210
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193206283 642 VGEGAGEGMSVNVPFSGvQMGDNEYQMAFQRVIMPIAYQFNPDLVLISAGFDAAVDDPLGEYKVT 706
Cdd:PTZ00063 211 IGVAQGKYYSVNVPLND-GIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLT 274
PTZ00063 PTZ00063
histone deacetylase; Provisional
147-329 7.64e-17

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 84.09  E-value: 7.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 147 HHADSVSPCGFCLFNNVAQAAEEAFFSGAeRILIVDLDVHHGHGTQRIFYDDKRVLYFSIHRheHGLFWPHlpESDFDHI 226
Cdd:PTZ00063 137 HHAKRSEASGFCYINDIVLGILELLKYHA-RVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHK--FGDFFPG--TGDVTDI 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 227 GSGKGLGYNANLALNEtGCTDSDYLSIIFHVLLPLATQFDPHFVIISAGFDALLGDPLGGMCLTPDGYSHILYHLKSLaQ 306
Cdd:PTZ00063 212 GVAQGKYYSVNVPLND-GIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAACVEFVRSL-N 289
                        170       180
                 ....*....|....*....|...
gi 193206283 307 GRMLVVLEGGYNhqISAVAvqRC 329
Cdd:PTZ00063 290 IPLLVLGGGGYT--IRNVA--RC 308
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
877-925 4.06e-09

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 53.14  E-value: 4.06e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 193206283   877 CSECQIGAEVWTCLTCYKYNCGRFVNEHAMMHHLSSSHPMALSMADLSV 925
Cdd:smart00290   2 CSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
886-939 3.48e-04

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 44.23  E-value: 3.48e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 193206283 886 VWTCLTCYKYNCGRFVNEHAMMHHLSSSHPMALSMADLSVWCYPCDSYVHNPAL 939
Cdd:cd02669   28 VYACLVCGKYFQGRGKGSHAYTHSLEDNHHVFLNLETLKFYCLPDNYEIIDSSL 81
 
Name Accession Description Interval E-value
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
440-795 1.98e-148

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: 443.70  E-value: 1.98e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 440 HFDLEEDNHPEKPARTRRILKTLRESGVLEKCVdRNCERIATNEEIRLVHTKKMLEHLRTTETMKDEELMEEAEKeFNSI 519
Cdd:cd10003    8 HHNLWDPGHPECPQRISRIYERHNDLGLLERCL-RLPSRLATEDELLLCHSEEHLDEMKSLEKMKPRELNRLGKE-YDSI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 520 YLTRDTLKVARKAVGAVLQSVDEIFEKDAgqRNALVIVRPPGHHASASKSSGFCIFNNVAVAAKYAQRRHKAKRVLILDW 599
Cdd:cd10003   86 YIHPDSYQCALLAAGCVLQVVEAVLTGES--RNGVAIVRPPGHHAEQDTACGFCFFNNVAIAARYAQKKYGLKRILIVDW 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 600 DVHHGNGTQEIFYEDSNVMYMSIHRHDKGNFYPIGEPKDYSDVGEGAGEGMSVNVPFSGVQMGDNEYQMAFQRVIMPIAY 679
Cdd:cd10003  164 DVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSPEGNYDVVGKGKGEGFNVNIPWNKGGMGDAEYIAAFQQVVLPIAY 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 680 QFNPDLVLISAGFDAAVDDPLGEYKVTPETFALMTYQLSSLAGGRIITVLEGGYNLTSISNSAQAVCEVLQNRSmLRRLr 759
Cdd:cd10003  244 EFNPELVLVSAGFDAARGDPLGGCKVTPEGYAHMTHMLMSLAGGRVIVILEGGYNLTSISESMSMCTKTLLGDP-PPVL- 321
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 193206283 760 eekeqfaTKPQKIESSCIKTIREVCAVQQKYWSILK 795
Cdd:cd10003  322 -------DLPRPPCSSALKSINNVLQVHQKYWKSLR 350
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
448-750 2.20e-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: 386.47  E-value: 2.20e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 448 HPEKPARTRRILKTLRESGVLEKCVdRNCERIATNEEIRLVHTKKMLEHLRTTETMKDEELmeeaekeFNSIYLTRDTLK 527
Cdd:cd09992    1 HPERPERLLAILEALEEEGLLDRLV-FVEPRPATEEELLRVHTPEYIERVEETCEAGGGYL-------DPDTYVSPGSYE 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 528 VARKAVGAVLQSVDEIFEKDAgqRNALVIVRPPGHHASASKSSGFCIFNNVAVAAKYAQRRHKAKRVLILDWDVHHGNGT 607
Cdd:cd09992   73 AALLAAGAALAAVDAVLSGEA--ENAFALVRPPGHHAEPDRAMGFCLFNNVAIAARYAQKRYGLKRVLIVDWDVHHGNGT 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 608 QEIFYEDSNVMYMSIHRHDkgnFYP-IGEPkdySDVGEGAGEGMSVNVPFSGVqMGDNEYQMAFQRVIMPIAYQFNPDLV 686
Cdd:cd09992  151 QDIFYDDPSVLYFSIHQYP---FYPgTGAA---EETGGGAGEGFTINVPLPPG-SGDAEYLAAFEEVLLPIAREFQPDLV 223
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193206283 687 LISAGFDAAVDDPLGEYKVTPETFALMTYQLSSLA----GGRIITVLEGGYNLTSISNSAQAVCEVLQ 750
Cdd:cd09992  224 LVSAGFDAHRGDPLGGMNLTPEGYARLTRLLKELAdehcGGRLVFVLEGGYNLEALAESVLAVLEALL 291
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
446-749 4.26e-127

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: 386.70  E-value: 4.26e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 446 DNHPEKPARTRRILKTLRESGvLEKCVDRNCERIATNEEIRLVHTKKMLEHLRTTETMKDEE-LMEEAEKEFNSIYLTRD 524
Cdd:cd11600    1 DPHPEDPSRISRIFEKLKEAG-LINRMLRIPIREATKEEILLVHSEEHWDRVEATEKMSDEQlKDRTEIFERDSLYVNND 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 525 TLKVARKAVGAVLQSVDEIFEKDAgqRNALVIVRPPGHHASASKSSGFCIFNNVAVAAKYAQRRH--KAKRVLILDWDVH 602
Cdd:cd11600   80 TAFCARLSCGGAIEACRAVAEGRV--KNAFAVVRPPGHHAEPDESMGFCFFNNVAVAAKWLQTEYpdKIKKILILDWDIH 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 603 HGNGTQEIFYEDSNVMYMSIHRHDKGNFYPIGEPKDYSDVGEGAGEGMSVNVPFSGVQMGDNEYQMAFQRVIMPIAYQFN 682
Cdd:cd11600  158 HGNGTQRAFYDDPNVLYISLHRFENGGFYPGTPYGDYESVGEGAGLGFNVNIPWPQGGMGDADYIYAFQRIVMPIAYEFD 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193206283 683 PDLVLISAGFDAAVDDPLGEYKVTPETFALMTYQLSSLAGGRIITVLEGGYNLTSISNSAQAVCEVL 749
Cdd:cd11600  238 PDLVIISAGFDAADGDELGQCHVTPAGYAHMTHMLMSLAGGKLVVALEGGYNLDAISDSALAVAKVL 304
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
448-749 3.62e-126

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: 383.90  E-value: 3.62e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  448 HPEKPARTRRILKTLRESGVLEKCVDrNCERIATNEEIRLVHTKKMLEHLRTTETMKDEELMEEAEKEFNSIYLTRDTLK 527
Cdd:pfam00850   1 HPENPERLKAILEALREAGLLPDLEI-IAPRPATEEELLLVHSPEYLEFLEEAAPEGGALLLLSYLSGDDDTPVSPGSYE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  528 VARKAVGAVLQSVDEIFEKDAgqRNALVIVRPPGHHASASKSSGFCIFNNVAVAAKYAQRRHKAKRVLILDWDVHHGNGT 607
Cdd:pfam00850  80 AALLAAGGTLAAADAVLSGEA--RNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLKRVAIVDFDVHHGNGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  608 QEIFYEDSNVMYMSIHRHDkGNFYPigEPKDYSDVGEGAGEGMSVNVPFSgVQMGDNEYQMAFQRVIMPIAYQFNPDLVL 687
Cdd:pfam00850 158 QEIFYDDPSVLTLSIHQYP-GGFYP--GTGFADETGEGKGKGYTLNVPLP-PGTGDAEYLAAFEEILLPALEEFQPDLIL 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193206283  688 ISAGFDAAVDDPLGEYKVTPETFALMTYQLSSLA---GGRIITVLEGGYNLTSISNSAQAVCEVL 749
Cdd:pfam00850 234 VSAGFDAHAGDPLGGLNLTTEGFAEITRILLELAdplCIRVVSVLEGGYNLDALARSATAVLAAL 298
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
32-366 1.56e-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: 383.58  E-value: 1.56e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  32 PTHPESSDRILKIKEALTKTKILEKCTVLTNFlEIDDADLEVTHDKSMVKDLMESEKKTQEDINSQCEKYDSVFMTefQN 111
Cdd:cd10002    5 SNHIECPERLEAILERLTQDGLLERCVKIPAR-EAEEDEILLVHSQEYIDLVKSTETMEKEELESLCSGYDSVYLC--PS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 112 SMKVAKDGVACVRDLTNRIMANEASNGFAVVRPPGHHADSVSPCGFCLFNNVAQAAEEAF-FSGAERILIVDLDVHHGHG 190
Cdd:cd10002   82 TYEAARLAAGSTIELVKAVMAGKIQNGFALIRPPGHHAMRNEANGYCIFNNVAIAAKYAIeKLGLKRILIVDWDVHHGQG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 191 TQRIFYDDKRVLYFSIHRHEHGLFWPHLPESDFDHIGSGKGLGYNANLALNETGCTDSDYLSIIFHVLLPLATQFDPHFV 270
Cdd:cd10002  162 TQQGFYEDPRVLYFSIHRYEHGRFWPHLFESDYDYIGVGHGYGFNVNVPLNQTGLGDADYLAIFHHILLPLALEFQPELV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 271 IISAGFDALLGDPLGGMCLTPDGYSHILYHLKSLAQGRMLVVLEGGYNHQISAVAVQRCVRVLLGYAPFSIELNeAPKES 350
Cdd:cd10002  242 LVSAGFDASIGDPEGEMAVTPAGYAHLTRLLMGLAGGKLLLVLEGGYLLESLAESVSMTLRGLLGDPLPPLAPP-IPIRS 320
                        330
                 ....*....|....*.
gi 193206283 351 TVDSCVSLVSVLRHHW 366
Cdd:cd10002  321 VLETILNAIAHLSPRW 336
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
19-369 1.75e-115

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: 357.80  E-value: 1.75e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  19 FNQTQNEHENTVCPTHPESSDRILKIKEALTKTKILEKCTVLTNFLEIDDaDLEVTHDKSMVKDLMESEKKTQEDINSQC 98
Cdd:cd10003    1 YDQRMMNHHNLWDPGHPECPQRISRIYERHNDLGLLERCLRLPSRLATED-ELLLCHSEEHLDEMKSLEKMKPRELNRLG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  99 EKYDSVFMTefQNSMKVAKDGVACVRDLTNRIMANEASNGFAVVRPPGHHADSVSPCGFCLFNNVAQAAEEAF-FSGAER 177
Cdd:cd10003   80 KEYDSIYIH--PDSYQCALLAAGCVLQVVEAVLTGESRNGVAIVRPPGHHAEQDTACGFCFFNNVAIAARYAQkKYGLKR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 178 ILIVDLDVHHGHGTQRIFYDDKRVLYFSIHRHEHGLFWPHLPESDFDHIGSGKGLGYNANLALNETGCTDSDYLSIIFHV 257
Cdd:cd10003  158 ILIVDWDVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSPEGNYDVVGKGKGEGFNVNIPWNKGGMGDAEYIAAFQQV 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 258 LLPLATQFDPHFVIISAGFDALLGDPLGGMCLTPDGYSHILYHLKSLAQGRMLVVLEGGYNHQISAVAVQRCVRVLLGYA 337
Cdd:cd10003  238 VLPIAYEFNPELVLVSAGFDAARGDPLGGCKVTPEGYAHMTHMLMSLAGGRVIVILEGGYNLTSISESMSMCTKTLLGDP 317
                        330       340       350
                 ....*....|....*....|....*....|..
gi 193206283 338 PFSIELNEAPKESTVDSCVSLVSVLRHHWNCF 369
Cdd:cd10003  318 PPVLDLPRPPCSSALKSINNVLQVHQKYWKSL 349
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
447-791 3.19e-110

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: 345.10  E-value: 3.19e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 447 NHPEKPARTRRILKTLRESGVLEKCvDRNCERIATNEEIRLVHTKK--MLEHLRTTETMKDEELMEEAEKEFNSIYLT-- 522
Cdd:cd11681   23 SHPEHGGRLQSIWSRLQETGLVNRC-ERLRGRKATLEELQLVHSEVhtLLYGTNPLSRLKLDPTKLAGLPQKSFVRLPcg 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 523 ------------RDTLKVARKAVGAVlqsVDEIFEKDAGQ-RNALVIVRPPGHHASASKSSGFCIFNNVAVAAKYAQRRH 589
Cdd:cd11681  102 gigvdsdtvwneLHTSNAARMAVGCV---IDLAFKVATGElKNGFAVVRPPGHHAEPSQAMGFCFFNSVAIAAKQLQQKL 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 590 KAKRVLILDWDVHHGNGTQEIFYEDSNVMYMSIHRHDKGNFYP-IGEPkdySDVGEGAGEGMSVNVPFSG---VQMGDNE 665
Cdd:cd11681  179 KLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFPgTGAP---TEVGSGAGEGFNVNIAWSGgldPPMGDAE 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 666 YQMAFQRVIMPIAYQFNPDLVLISAGFDAAVDDP--LGEYKVTPETFALMTYQLSSLAGGRIITVLEGGYNLTSISNSAQ 743
Cdd:cd11681  256 YLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPppLGGYKVSPACFGYMTRQLMNLAGGKVVLALEGGYDLTAICDASE 335
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 193206283 744 AVCEVLQnRSMLRRLREekEQFATKPQKiesSCIKTIREVCAVQQKYW 791
Cdd:cd11681  336 ACVRALL-GDELDPLSE--EELERRPNP---NAVTSLEKVIAIQSPYW 377
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
446-791 4.83e-104

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: 327.34  E-value: 4.83e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 446 DNHPEKPARTRRILKTLRESGVLEKCVDRNcERIATNEEIRLVHTKKMLEHLRTTETMKDEELMEEAEKeFNSIYLTRDT 525
Cdd:cd10002    5 SNHIECPERLEAILERLTQDGLLERCVKIP-AREAEEDEILLVHSQEYIDLVKSTETMEKEELESLCSG-YDSVYLCPST 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 526 LKVARKAVGAVLQSVDEIFEKDAgqRNALVIVRPPGHHASASKSSGFCIFNNVAVAAKYAQRRHKAKRVLILDWDVHHGN 605
Cdd:cd10002   83 YEAARLAAGSTIELVKAVMAGKI--QNGFALIRPPGHHAMRNEANGYCIFNNVAIAAKYAIEKLGLKRILIVDWDVHHGQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 606 GTQEIFYEDSNVMYMSIHRHDKGNFYPIGEPKDYSDVGEGAGEGMSVNVPFSGVQMGDNEYQMAFQRVIMPIAYQFNPDL 685
Cdd:cd10002  161 GTQQGFYEDPRVLYFSIHRYEHGRFWPHLFESDYDYIGVGHGYGFNVNVPLNQTGLGDADYLAIFHHILLPLALEFQPEL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 686 VLISAGFDAAVDDPLGEYKVTPETFALMTYQLSSLAGGRIITVLEGGYNLTSISNSAQAVCEVLQNRSMLRrlreekeqf 765
Cdd:cd10002  241 VLVSAGFDASIGDPEGEMAVTPAGYAHLTRLLMGLAGGKLLLVLEGGYLLESLAESVSMTLRGLLGDPLPP--------- 311
                        330       340
                 ....*....|....*....|....*.
gi 193206283 766 aTKPQKIESSCIKTIREVCAVQQKYW 791
Cdd:cd10002  312 -LAPPIPIRSVLETILNAIAHLSPRW 336
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
429-749 5.69e-101

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 318.20  E-value: 5.69e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 429 TLIYFnegDDAHFDLE-EDNHPEKPARTRRILKTLRESGVLEKCVDRNCERiATNEEIRLVHTKKMLEHLRTTEtmkdee 507
Cdd:COG0123    1 TALIY---HPDYLLHDlGPGHPEPPERLRAILDALEASGLLDDLELVEPPP-ATEEDLLRVHTPDYVDALRAAS------ 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 508 lmeeAEKEFNSI----YLTRDTLKVARKAVGAVLQSVDEIFEKDAgqRNALVIVRPPGHHASASKSSGFCIFNNVAVAAK 583
Cdd:COG0123   71 ----LDGGYGQLdpdtPVSPGTWEAALLAAGGALAAADAVLEGEA--RNAFALVRPPGHHAERDRAMGFCLFNNAAIAAR 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 584 YAQRrHKAKRVLILDWDVHHGNGTQEIFYEDSNVMYMSIHRHdkgNFYPiGEpKDYSDVGEGAGEGMSVNVPFSgVQMGD 663
Cdd:COG0123  145 YLLA-KGLERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD---PLYP-GT-GAADETGEGAGEGSNLNVPLP-PGTGD 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 664 NEYQMAFQRVIMPIAYQFNPDLVLISAGFDAAVDDPLGEYKVTPETFALMTYQLSSLA---GGRIITVLEGGYNLTSISN 740
Cdd:COG0123  218 AEYLAALEEALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELAdhcGGPVVSVLEGGYNLDALAR 297

                 ....*....
gi 193206283 741 SAQAVCEVL 749
Cdd:COG0123  298 SVAAHLETL 306
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
443-750 4.68e-99

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: 314.10  E-value: 4.68e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 443 LEEDNHPEKPARTRRILKTLRESGVLEKCVDRNCeRIATNEEIRLVHTKKMLEHLRTTETMKDEELMEEAEKeFNSIYLT 522
Cdd:cd11682    2 LWDESFPECPERLHAIREKLIQEGLLERCVSVQA-REASEEELLLVHSPEYVALMKSTQYMTEEELRTLADT-YDSVYLH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 523 RDTLKVARKAVGAVLQSVDEIFEKDAgqRNALVIVRPPGHHASASKSSGFCIFNNVAVAAKYAQRRHKAKRVLILDWDVH 602
Cdd:cd11682   80 PNSYSCACLAVGSVLQLVDKVLGGEI--RNGLAIVRPPGHHAQHDKMDGYCMFNNVAIAARYAQQKHGVQRVLIVDWDVH 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 603 HGNGTQEIFYEDSNVMYMSIHRHDKGNFYPIGEPKDYSDVGEGAGEGMSVNVPFSGVQMGDNEYQMAFQRVIMPIAYQFN 682
Cdd:cd11682  158 HGQGTQFIFEQDPSVLYFSIHRYEQGRFWPHLKESDSSAVGFGRGEGYNINVPWNQVGMRDADYIAAFLHVLLPVALEFQ 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193206283 683 PDLVLISAGFDAAVDDPLGEYKVTPETFALMTYQLSSLAGGRIITVLEGGYNLTSIsnsAQAVCEVLQ 750
Cdd:cd11682  238 PQLVLVAAGFDAVIGDPKGEMAATPACFAHLTHLLMGLAGGKLILSLEGGYNLRSL---AEGVCASLK 302
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
34-334 6.29e-94

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: 298.64  E-value: 6.29e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  34 HPESSDRILKIKEALTKTKILEKCtVLTNFLEIDDADLEVTHDKSMVKDLMESEKKTQEdinsqcEKYDSVFMTEfqNSM 113
Cdd:cd09992    1 HPERPERLLAILEALEEEGLLDRL-VFVEPRPATEEELLRVHTPEYIERVEETCEAGGG------YLDPDTYVSP--GSY 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 114 KVAKDGVACVRDLTNRIMANEASNGFAVVRPPGHHADSVSPCGFCLFNNVAQAAEEAF-FSGAERILIVDLDVHHGHGTQ 192
Cdd:cd09992   72 EAALLAAGAALAAVDAVLSGEAENAFALVRPPGHHAEPDRAMGFCLFNNVAIAARYAQkRYGLKRVLIVDWDVHHGNGTQ 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 193 RIFYDDKRVLYFSIHRHEhglFWPHlpESDFDHIGSGKGLGYNANLALNEtGCTDSDYLSIIFHVLLPLATQFDPHFVII 272
Cdd:cd09992  152 DIFYDDPSVLYFSIHQYP---FYPG--TGAAEETGGGAGEGFTINVPLPP-GSGDAEYLAAFEEVLLPIAREFQPDLVLV 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193206283 273 SAGFDALLGDPLGGMCLTPDGYSHILYHLKSLA----QGRMLVVLEGGYNHQISAVAVQRCVRVLL 334
Cdd:cd09992  226 SAGFDAHRGDPLGGMNLTPEGYARLTRLLKELAdehcGGRLVFVLEGGYNLEALAESVLAVLEALL 291
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
450-791 6.39e-93

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: 297.93  E-value: 6.39e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 450 EKPARTRRILKTLRESGVLEKCVdRNCERIATNEEIRLVHTKKMLEHLRTTETMKdEELMEEAEKEFNSIYLTRDTLKVA 529
Cdd:cd11683    9 EVPERLTASYERLRQYGLVQRCL-RLPAREASEEEILLVHSPEYLSLVRETQVMN-KEELMAISGKYDAVYFHPNTFHCA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 530 RKAVGAVLQSVDEIFEKDAgqRNALVIVRPPGHHASASKSSGFCIFNNVAVAAKYAQRRHKAKRVLILDWDVHHGNGTQE 609
Cdd:cd11683   87 RLAAGATLQLVDAVLTGEV--QNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYAKKKYGLHRILIVDWDVHHGQGIQY 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 610 IFYEDSNVMYMSIHRHDKGNFYPIGEPKDYSDVGEGAGEGMSVNVPFSGVQMGDNEYQMAFQRVIMPIAYQFNPDLVLIS 689
Cdd:cd11683  165 IFEEDPSVLYFSWHRYEHQRFWPFLRESDYDAVGRGKGLGFNINLPWNKVGMGNADYLAAFFHVLLPLAFEFDPELVLVS 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 690 AGFDAAVDDPLGEYKVTPETFALMTYQLSSLAGGRIITVLEGGYNLTSIsnsAQAVCEVLQNrsmlrRLREEKEQFaTKP 769
Cdd:cd11683  245 AGFDSAIGDPEGQMCATPECFAHLTHLLMVLAGGKLCAVLEGGYHLESL---AESVCMTVQT-----LLGDPLPRL-SGE 315
                        330       340
                 ....*....|....*....|..
gi 193206283 770 QKIESSCIKTIREVCAVQQKYW 791
Cdd:cd11683  316 MTPCQSALESIQNVRAAQAPYW 337
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
34-333 6.44e-93

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: 296.46  E-value: 6.44e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283   34 HPESSDRILKIKEALTKTKILEKCTVLTnFLEIDDADLEVTHDKSMVKDLMESEKKTQEDINSQCEK-YDSVFMteFQNS 112
Cdd:pfam00850   1 HPENPERLKAILEALREAGLLPDLEIIA-PRPATEEELLLVHSPEYLEFLEEAAPEGGALLLLSYLSgDDDTPV--SPGS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  113 MKVAKDGVACVRDLTNRIMANEASNGFAVVRPPGHHADSVSPCGFCLFNNVAQAAEEAF-FSGAERILIVDLDVHHGHGT 191
Cdd:pfam00850  78 YEAALLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLReKYGLKRVAIVDFDVHHGNGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  192 QRIFYDDKRVLYFSIHRHEHGLFwphlPES-DFDHIGSGKGLGYNANLALNeTGCTDSDYLSIIFHVLLPLATQFDPHFV 270
Cdd:pfam00850 158 QEIFYDDPSVLTLSIHQYPGGFY----PGTgFADETGEGKGKGYTLNVPLP-PGTGDAEYLAAFEEILLPALEEFQPDLI 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193206283  271 IISAGFDALLGDPLGGMCLTPDGYSHILYHLKSLAQ---GRMLVVLEGGYNHQISAVAVQRCVRVL 333
Cdd:pfam00850 233 LVSAGFDAHAGDPLGGLNLTTEGFAEITRILLELADplcIRVVSVLEGGYNLDALARSATAVLAAL 298
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
34-338 8.03e-93

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: 296.56  E-value: 8.03e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  34 HPESSDRILKIKEALTKTKiLEKCTVLTNFLEIDDADLEVTHDKSMVKDLMESEKKTQEDINSQCEKYDsvfmtefQNSM 113
Cdd:cd11600    3 HPEDPSRISRIFEKLKEAG-LINRMLRIPIREATKEEILLVHSEEHWDRVEATEKMSDEQLKDRTEIFE-------RDSL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 114 KVAKDGVACVR-------DLTNRIMANEASNGFAVVRPPGHHADSVSPCGFCLFNNVAQAAEEAFFSGAE---RILIVDL 183
Cdd:cd11600   75 YVNNDTAFCARlscggaiEACRAVAEGRVKNAFAVVRPPGHHAEPDESMGFCFFNNVAVAAKWLQTEYPDkikKILILDW 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 184 DVHHGHGTQRIFYDDKRVLYFSIHRHEHGLFWPHLPESDFDHIGSGKGLGYNANLALNETGCTDSDYLSIIFHVLLPLAT 263
Cdd:cd11600  155 DIHHGNGTQRAFYDDPNVLYISLHRFENGGFYPGTPYGDYESVGEGAGLGFNVNIPWPQGGMGDADYIYAFQRIVMPIAY 234
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193206283 264 QFDPHFVIISAGFDALLGDPLGGMCLTPDGYSHILYHLKSLAQGRMLVVLEGGYN-HQISAVAVQrCVRVLLGYAP 338
Cdd:cd11600  235 EFDPDLVIISAGFDAADGDELGQCHVTPAGYAHMTHMLMSLAGGKLVVALEGGYNlDAISDSALA-VAKVLLGEAP 309
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
33-366 5.67e-92

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: 295.22  E-value: 5.67e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  33 THPESSDRILKIKEALTKTKILEKCtVLTNFLEIDDADLEVTHDKSMVkDLMES-EKKTQEDINSQCEKYDSVFMteFQN 111
Cdd:cd11682    6 SFPECPERLHAIREKLIQEGLLERC-VSVQAREASEEELLLVHSPEYV-ALMKStQYMTEEELRTLADTYDSVYL--HPN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 112 SMKVAKDGVACVRDLTNRIMANEASNGFAVVRPPGHHADSVSPCGFCLFNNVAQAAEEAFFS-GAERILIVDLDVHHGHG 190
Cdd:cd11682   82 SYSCACLAVGSVLQLVDKVLGGEIRNGLAIVRPPGHHAQHDKMDGYCMFNNVAIAARYAQQKhGVQRVLIVDWDVHHGQG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 191 TQRIFYDDKRVLYFSIHRHEHGLFWPHLPESDFDHIGSGKGLGYNANLALNETGCTDSDYLSIIFHVLLPLATQFDPHFV 270
Cdd:cd11682  162 TQFIFEQDPSVLYFSIHRYEQGRFWPHLKESDSSAVGFGRGEGYNINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 271 IISAGFDALLGDPLGGMCLTPDGYSHILYHLKSLAQGRMLVVLEGGYNHQISAVAVQRCVRVLLGYAPFSIELNEAPKES 350
Cdd:cd11682  242 LVAAGFDAVIGDPKGEMAATPACFAHLTHLLMGLAGGKLILSLEGGYNLRSLAEGVCASLKALLGDPCPMLESPGAPCRS 321
                        330
                 ....*....|....*.
gi 193206283 351 TVDSCVSLVSVLRHHW 366
Cdd:cd11682  322 ALASVSCTISALEPFW 337
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
448-744 5.67e-90

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: 288.26  E-value: 5.67e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 448 HPEKPARTRRILKTLRESGVLEKCVDRNCERiATNEEIRLVHTKKMLEHLRTtetmkdeelmEEAEKEFNSI----YLTR 523
Cdd:cd11599    1 HPESPERLEAILDALIASGLDRLLRQLEAPP-ATREQLLRVHDAAYVDRLEA----------AAPEEGLVQLdpdtAMSP 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 524 DTLKVARKAVGAVLQSVDEIFEKDAgqRNALVIVRPPGHHASASKSSGFCIFNNVAVAAKYAQRRHKAKRVLILDWDVHH 603
Cdd:cd11599   70 GSLEAALRAAGAVVAAVDAVMAGEA--RNAFCAVRPPGHHAERDKAMGFCLFNNVAIAAAHALAHHGLERVAIVDFDVHH 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 604 GNGTQEIFYEDSNVMYMSIHRHdkgNFYPigepkdYSDVGEGAGEGMSVNVPFS-GVqmGDNEYQMAFQRVIMPIAYQFN 682
Cdd:cd11599  148 GNGTEDIFRDDPRVLFCSSHQH---PLYP------GTGAPDETGHGNIVNVPLPaGT--GGAEFREAVEDRWLPALDAFK 216
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193206283 683 PDLVLISAGFDAAVDDPLGEYKVTPETFALMTYQLSSLA----GGRIITVLEGGYNLTSISNSAQA 744
Cdd:cd11599  217 PDLILISAGFDAHRDDPLAQLNLTEEDYAWITEQLMDVAdrycDGRIVSVLEGGYDLSALARSVAA 282
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
444-791 6.48e-89

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: 288.83  E-value: 6.48e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 444 EEDNHPEKPARTRRILKTLRESGVLEKCvdrNC--ERIATNEEIRLVHTKKM--------LEHLRT---------TETMK 504
Cdd:cd10008   20 DNSNHPEHAGRIQSIWSRLQERGLRSQC---EClrGRKASLEELQSVHSERHvllygtnpLSRLKLdngklagllAQRMF 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 505 DEELMEEAEKEFNSIYLTRDTLKVARKAVGAVLQSVDEIFEKDAgqRNALVIVRPPGHHASASKSSGFCIFNNVAVAAKY 584
Cdd:cd10008   97 VMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASREL--KNGFAVVRPPGHHADHSTAMGFCFFNSVAIACRQ 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 585 AQRRHKAKRVLILDWDVHHGNGTQEIFYEDSNVMYMSIHRHDKGNFYPIGEPKDysDVGEGAGEGMSVNVPFSG---VQM 661
Cdd:cd10008  175 LQQQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVD--EVGAGSGEGFNVNVAWAGgldPPM 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 662 GDNEYQMAFQRVIMPIAYQFNPDLVLISAGFDAAVDD--PLGEYKVTPETFALMTYQLSSLAGGRIITVLEGGYNLTSIS 739
Cdd:cd10008  253 GDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHpaPLGGYHVSAKCFGYMTQQLMNLAGGAVVLALEGGHDLTAIC 332
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 193206283 740 NSAQA-VCEVLQNRsmLRRLREEkeqfaTKPQKIESSCIKTIREVCAVQQKYW 791
Cdd:cd10008  333 DASEAcVAALLGNE--VDPLSEE-----SWKQKPNLNAIRSLEAVIRVHSKYW 378
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
430-745 3.38e-88

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: 283.66  E-value: 3.38e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 430 LIYFNEGDDAH------FDLEEDNHPEKPARTRRILKTLRESGVLEKCVDRNCERiatnEEIRLVHTKKMLEHLRTTETm 503
Cdd:cd10001    1 KIVYSEDHLLHhpktelSRGKLVPHPENPERAEAILDALKRAGLGEVLPPRDFGL----EPILAVHDPDYVDFLETADT- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 504 kdeelmeeaekefnSIYLTRDTLKVARKAVGAVLQSVDEIFEkdaGQRNALVIVRPPGHHASASKSSGFCIFNNVAVAAK 583
Cdd:cd10001   76 --------------DTPISEGTWEAALAAADTALTAADLVLE---GERAAYALCRPPGHHAGRDRAGGFCYFNNAAIAAQ 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 584 YAQRRHKakRVLILDWDVHHGNGTQEIFYEDSNVMYMSIHRHDKgNFYP--IGEPkdySDVGEGAGEGMSVNVPFSGvQM 661
Cdd:cd10001  139 YLRDRAG--RVAILDVDVHHGNGTQEIFYERPDVLYVSIHGDPR-TFYPffLGFA---DETGEGEGEGYNLNLPLPP-GT 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 662 GDNEYQMAFQRVIMPIAyQFNPDLVLISAGFDAAVDDPLGEYKVTPETFALMTYQLSSLaGGRIITVLEGGYNLTSISNS 741
Cdd:cd10001  212 GDDDYLAALDEALAAIA-AFGPDALVVSLGFDTHEGDPLSDFKLTTEDYARIGRRIAAL-GLPTVFVQEGGYNVDALGRN 289

                 ....
gi 193206283 742 AQAV 745
Cdd:cd10001  290 AVAF 293
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
36-366 4.19e-86

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: 279.82  E-value: 4.19e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  36 ESSDRILKIKEALTKTKILEKCTVLTnFLEIDDADLEVTHDKSMVKDLMESEKKTQEDINSQCEKYDSVFMteFQNSMKV 115
Cdd:cd11683    9 EVPERLTASYERLRQYGLVQRCLRLP-AREASEEEILLVHSPEYLSLVRETQVMNKEELMAISGKYDAVYF--HPNTFHC 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 116 AKDGVACVRDLTNRIMANEASNGFAVVRPPGHHADSVSPCGFCLFNNVAQAAEEAFFS-GAERILIVDLDVHHGHGTQRI 194
Cdd:cd11683   86 ARLAAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYAKKKyGLHRILIVDWDVHHGQGIQYI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 195 FYDDKRVLYFSIHRHEHGLFWPHLPESDFDHIGSGKGLGYNANLALNETGCTDSDYLSIIFHVLLPLATQFDPHFVIISA 274
Cdd:cd11683  166 FEEDPSVLYFSWHRYEHQRFWPFLRESDYDAVGRGKGLGFNINLPWNKVGMGNADYLAAFFHVLLPLAFEFDPELVLVSA 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 275 GFDALLGDPLGGMCLTPDGYSHILYHLKSLAQGRMLVVLEGGYNHQISAVAVQRCVRVLLGYAPFSIELNEAPKESTVDS 354
Cdd:cd11683  246 GFDSAIGDPEGQMCATPECFAHLTHLLMVLAGGKLCAVLEGGYHLESLAESVCMTVQTLLGDPLPRLSGEMTPCQSALES 325
                        330
                 ....*....|..
gi 193206283 355 CVSLVSVLRHHW 366
Cdd:cd11683  326 IQNVRAAQAPYW 337
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
446-805 8.45e-85

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: 278.84  E-value: 8.45e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 446 DNHPEKPARTRRILKTLRESGVLEKCvdrNC--ERIATNEEIRLVHTKKMLEHLRTTETMKDEELMEEAEKEFNSIYL-- 521
Cdd:cd10006   25 NSHPEHAGRIQSIWSRLQETGLRGKC---ECirGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVrl 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 522 -------TRDTL-------KVARKAVGAVlqsVDEIFEKDAGQ-RNALVIVRPPGHHASASKSSGFCIFNNVAVAAKYAQ 586
Cdd:cd10006  102 pcggvgvDSDTIwnevhssGAARLAVGCV---VELVFKVATGElKNGFAVVRPPGHHAEESTPMGFCYFNSVAIAAKLLQ 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 587 RRHKAKRVLILDWDVHHGNGTQEIFYEDSNVMYMSIHRHDKGNFYP-IGEPkdySDVGEGAGEGMSVNVPFSG---VQMG 662
Cdd:cd10006  179 QRLNVSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYDDGNFFPgSGAP---DEVGTGPGVGFNVNMAFTGgldPPMG 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 663 DNEYQMAFQRVIMPIAYQFNPDLVLISAGFDAAVDD--PLGEYKVTPETFALMTYQLSSLAGGRIITVLEGGYNLTSISN 740
Cdd:cd10006  256 DAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHptPLGGYNLSAKCFGYLTKQLMGLAGGRIVLALEGGHDLTAICD 335
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193206283 741 SAQA-VCEVLQNRsmLRRLREEKEQfatkpQKIESSCIKTIREVCAVQQKYWSILkgfQVTPSNYG 805
Cdd:cd10006  336 ASEAcVSALLGNE--LDPLPEKVLQ-----QRPNANAVRSMEKVMEIHSKYWRCL---QRTTSTAG 391
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
441-749 9.82e-85

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: 276.75  E-value: 9.82e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 441 FDLEEDNHPEKPARTRRILKTLRESGVLEKCVDRNcERIATNEEIRLVHTKKMLEHLRttETMKDEELMEEAEKEFNsiy 520
Cdd:cd09996   26 LLVQPGRHPENPETKRRIKNLLEVSGLSDHLVLIT-PRPATDEELLRVHTPEYIDRVK--AASAAGGGEAGGGTPFG--- 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 521 ltRDTLKVARKAVGAVLQSVDEIFEKDAgqRNALVIVRPPGHHASASKSSGFCIFNNVAVAAKYAQRRHKAKRVLILDWD 600
Cdd:cd09996  100 --PGSYEIALLAAGGAIAAVDAVLDGEV--DNAYALVRPPGHHAEPDQGMGFCLFNNVAIAARHALAVGGVKRVAVVDWD 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 601 VHHGNGTQEIFYEDSNVMYMSIHRHdkGNFypigePKDYS---DVGEGAGEGMSVNVPF-SGVqmGDNEYQMAFQRVIMP 676
Cdd:cd09996  176 VHHGNGTQAIFYDDPDVLTISLHQD--RCF-----PPDSGaveERGEGAGEGYNLNIPLpPGS--GDGAYLHAFERIVLP 246
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193206283 677 IAYQFNPDLVLISAGFDAAVDDPLGEYKVTPETFALMTYQLSSLA----GGRIITVLEGGYNLTSISNSAQAVCEVL 749
Cdd:cd09996  247 ALRAFRPELIIVASGFDASAFDPLGRMMLTSDGFRALTRKLRDLAdelcGGRLVMVHEGGYSEAYVPFCGLAVLEEL 323
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
446-800 3.88e-84

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: 277.25  E-value: 3.88e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 446 DNHPEKPARTRRILKTLRESGVLEKCvDRNCERIATNEEIRLVHT-------------------KKMLEHLrtTETMKDE 506
Cdd:cd10007   24 NVHPEHAGRIQSVWSRLQETGLLGKC-ERVRGRKATLDEIQTVHSehhtllygtsplnrqkldsKKLLGPL--SQKMYAV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 507 ELMEEAEKEFNSIYLTRDTLKVARKAVGAVLQSVdeiFEKDAGQ-RNALVIVRPPGHHASASKSSGFCIFNNVAVAAKYA 585
Cdd:cd10007  101 LPCGGIGVDSDTVWNEMHSSSAVRMAVGCLIELA---FKVAAGElKNGFAVIRPPGHHAEESTAMGFCFFNSVAIAAKLL 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 586 QRRHKAKRVLILDWDVHHGNGTQEIFYEDSNVMYMSIHRHDKGNFYP-IGEPKdysDVGEGAGEGMSVNVPFSG---VQM 661
Cdd:cd10007  178 QQKLNVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGNFFPgSGAPD---EVGAGPGVGFNVNIAWTGgvdPPI 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 662 GDNEYQMAFQRVIMPIAYQFNPDLVLISAGFDAAVD--DPLGEYKVTPETFALMTYQLSSLAGGRIITVLEGGYNLTSIS 739
Cdd:cd10007  255 GDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGhqSPLGGYSVTAKCFGHLTKQLMTLAGGRVVLALEGGHDLTAIC 334
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193206283 740 NSAQAVCEVLqnrsmlrrLREEKEQF--ATKPQKIESSCIKTIREVCAVQQKYWSILKGFQVT 800
Cdd:cd10007  335 DASEACVSAL--------LGMELTPLdnTVLQQKPNDNAVATLERVIEIQSKHWSCLKRFAAT 389
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
32-335 2.02e-79

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 260.42  E-value: 2.02e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  32 PTHPESSDRILKIKEALTKTKILEKCTVLTnFLEIDDADLEVTHDKSMVKDLME-SEKKTQEDINSqcekyDSVFmteFQ 110
Cdd:COG0123   16 PGHPEPPERLRAILDALEASGLLDDLELVE-PPPATEEDLLRVHTPDYVDALRAaSLDGGYGQLDP-----DTPV---SP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 111 NSMKVAKDGVACVRDLTNRIMANEASNGFAVVRPPGHHADSVSPCGFCLFNNVAQAAEEAFFSGAERILIVDLDVHHGHG 190
Cdd:COG0123   87 GTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGFCLFNNAAIAARYLLAKGLERVAIVDFDVHHGNG 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 191 TQRIFYDDKRVLYFSIhrHEHGLFwphlPESDFDH-IGSGKGLGYNANLALnETGCTDSDYLSIIFHVLLPLATQFDPHF 269
Cdd:COG0123  167 TQDIFYDDPDVLTISI--HQDPLY----PGTGAADeTGEGAGEGSNLNVPL-PPGTGDAEYLAALEEALLPALEAFKPDL 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193206283 270 VIISAGFDALLGDPLGGMCLTPDGYSHILYHLKSLA---QGRMLVVLEGGYNHQISAVAVQRCVRVLLG 335
Cdd:COG0123  240 IVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELAdhcGGPVVSVLEGGYNLDALARSVAAHLETLLG 308
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
33-366 4.14e-76

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: 254.19  E-value: 4.14e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  33 THPESSDRILKIKEALTKTKILEKCTVLTN---FLEiddaDLEVTHDK---SMVKDLMESEKKTqeDINSQCEKYDSVFM 106
Cdd:cd11681   23 SHPEHGGRLQSIWSRLQETGLVNRCERLRGrkaTLE----ELQLVHSEvhtLLYGTNPLSRLKL--DPTKLAGLPQKSFV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 107 ------------TEF--QNSMKVAKDGVACVRDLTNRIMANEASNGFAVVRPPGHHADSVSPCGFCLFNNVAQAAEEAFF 172
Cdd:cd11681   97 rlpcggigvdsdTVWneLHTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQAMGFCFFNSVAIAAKQLQQ 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 173 -SGAERILIVDLDVHHGHGTQRIFYDDKRVLYFSIHRHEHGLFWPHlpESDFDHIGSGKGLGYNANLALN---ETGCTDS 248
Cdd:cd11681  177 kLKLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFPG--TGAPTEVGSGAGEGFNVNIAWSgglDPPMGDA 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 249 DYLSIIFHVLLPLATQFDPHFVIISAGFDALLGDP--LGGMCLTPDGYSHILYHLKSLAQGRMLVVLEGGYNHQISAVAV 326
Cdd:cd11681  255 EYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPppLGGYKVSPACFGYMTRQLMNLAGGKVVLALEGGYDLTAICDAS 334
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 193206283 327 QRCVRVLLGYAPFSI---ELNEAPKESTVDSCVSLVSVLRHHW 366
Cdd:cd11681  335 EACVRALLGDELDPLseeELERRPNPNAVTSLEKVIAIQSPYW 377
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
447-791 2.08e-72

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: 244.16  E-value: 2.08e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 447 NHPEKPARTRRILKTLRESGVLEKCvDRNCERIATNEEIRLVHTK--KML--------EHLRTTETMKDEELMEEAEKEF 516
Cdd:cd10009   23 THPEHAGRIQSIWSRLQETGLLNKC-ERIQGRKASLEEIQLVHSEhhSLLygtnpldgQKLDPRILLGDDSQKFFSSLPC 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 517 NSIYLTRDTL-------KVARKAVGAVLQSVDEIFEKDAgqRNALVIVRPPGHHASASKSSGFCIFNNVAVAAKYAQRRH 589
Cdd:cd10009  102 GGLGVDSDTIwnelhssGAARMAVGCVIELASKVASGEL--KNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQL 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 590 KAKRVLILDWDVHHGNGTQEIFYEDSNVMYMSIHRHDKGNFYP-IGEPkdySDVGEGAGEGMSVNVPFSG---VQMGDNE 665
Cdd:cd10009  180 NISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPgSGAP---NEVGTGLGEGYNINIAWTGgldPPMGDVE 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 666 YQMAFQRVIMPIAYQFNPDLVLISAGFDA--AVDDPLGEYKVTPETFALMTYQLSSLAGGRIITVLEGGYNLTSISNSAQ 743
Cdd:cd10009  257 YLEAFRTIVKPVAKEFDPDMVLVSAGFDAleGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVLALEGGHDLTAICDASE 336
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 193206283 744 AVCEVLqnrsmlrrLREEKEQFATK--PQKIESSCIKTIREVCAVQQKYW 791
Cdd:cd10009  337 ACVNAL--------LGNELEPLAEDilHQSPNMNAVISLQKIIEIQSKYW 378
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
34-331 2.54e-62

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: 213.14  E-value: 2.54e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  34 HPESSDRILKIKEALTKTKILEKCTVLTnFLEIDDADLEVTHDKSMVKDLME-SEKKTQEDINSqcekyDSVFMtefQNS 112
Cdd:cd11599    1 HPESPERLEAILDALIASGLDRLLRQLE-APPATREQLLRVHDAAYVDRLEAaAPEEGLVQLDP-----DTAMS---PGS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 113 MKVAKDGVACVRDLTNRIMANEASNGFAVVRPPGHHADSVSPCGFCLFNNVAQAAEEAF-FSGAERILIVDLDVHHGHGT 191
Cdd:cd11599   72 LEAALRAAGAVVAAVDAVMAGEARNAFCAVRPPGHHAERDKAMGFCLFNNVAIAAAHALaHHGLERVAIVDFDVHHGNGT 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 192 QRIFYDDKRVLYFSIHRHEhglFWPH---LPESDFDHIgsgkglgynANLALNEtGCTDSDYLSIIFHVLLPLATQFDPH 268
Cdd:cd11599  152 EDIFRDDPRVLFCSSHQHP---LYPGtgaPDETGHGNI---------VNVPLPA-GTGGAEFREAVEDRWLPALDAFKPD 218
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193206283 269 FVIISAGFDALLGDPLGGMCLTPDGYSHILYHLKSLA----QGRMLVVLEGGYNHQisavAVQRCVR 331
Cdd:cd11599  219 LILISAGFDAHRDDPLAQLNLTEEDYAWITEQLMDVAdrycDGRIVSVLEGGYDLS----ALARSVA 281
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
33-318 3.69e-62

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: 215.12  E-value: 3.69e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  33 THPESSDRILKIKEALTKTKILEKCTVLTnFLEIDDADLEVTHDKSMVKDLME-SEKKTQEDINSQCEKYDSvfmteFQN 111
Cdd:cd09996   32 RHPENPETKRRIKNLLEVSGLSDHLVLIT-PRPATDEELLRVHTPEYIDRVKAaSAAGGGEAGGGTPFGPGS-----YEI 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 112 SMKVAkdGVACvrDLTNRIMANEASNGFAVVRPPGHHADSVSPCGFCLFNNVAQAAEEAF-FSGAERILIVDLDVHHGHG 190
Cdd:cd09996  106 ALLAA--GGAI--AAVDAVLDGEVDNAYALVRPPGHHAEPDQGMGFCLFNNVAIAARHALaVGGVKRVAVVDWDVHHGNG 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 191 TQRIFYDDKRVLYFSIhrHEHGLFwpHLPESDFDHIGSGKGLGYNANLALnETGCTDSDYLSIIFHVLLPLATQFDPHFV 270
Cdd:cd09996  182 TQAIFYDDPDVLTISL--HQDRCF--PPDSGAVEERGEGAGEGYNLNIPL-PPGSGDGAYLHAFERIVLPALRAFRPELI 256
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 193206283 271 IISAGFDALLGDPLGGMCLTPDGYSHILYHLKSLA----QGRMLVVLEGGYN 318
Cdd:cd09996  257 IVASGFDASAFDPLGRMMLTSDGFRALTRKLRDLAdelcGGRLVMVHEGGYS 308
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
33-382 1.25e-61

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: 215.29  E-value: 1.25e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  33 THPESSDRILKIKEALTKTKILEKCTVLTN---FLEiddaDLEVTHDKSMV-----KDLMESEKKTQEDINSQCEKY--- 101
Cdd:cd10006   26 SHPEHAGRIQSIWSRLQETGLRGKCECIRGrkaTLE----ELQTVHSEAHTllygtNPLNRQKLDSKKLLGSLASVFvrl 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 102 -------DSVFMTEFQNSMKVAKDGVACVRDLTNRIMANEASNGFAVVRPPGHHADSVSPCGFCLFNNVAQAAE--EAFF 172
Cdd:cd10006  102 pcggvgvDSDTIWNEVHSSGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAIAAKllQQRL 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 173 SgAERILIVDLDVHHGHGTQRIFYDDKRVLYFSIHRHEHGLFWPHlpESDFDHIGSGKGLGYNANLALN---ETGCTDSD 249
Cdd:cd10006  182 N-VSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYDDGNFFPG--SGAPDEVGTGPGVGFNVNMAFTgglDPPMGDAE 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 250 YLSIIFHVLLPLATQFDPHFVIISAGFDALLGD--PLGGMCLTPDGYSHILYHLKSLAQGRMLVVLEGGynHQISAV--A 325
Cdd:cd10006  259 YLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHptPLGGYNLSAKCFGYLTKQLMGLAGGRIVLALEGG--HDLTAIcdA 336
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193206283 326 VQRCVRVLLGYA----PFSIeLNEAPKESTVDSCVSLVSVLRHHWNCFDYFPSRT--SLRLAQ 382
Cdd:cd10006  337 SEACVSALLGNEldplPEKV-LQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAgySLIEAQ 398
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
34-337 6.49e-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: 209.32  E-value: 6.49e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  34 HPESSDRILKIKEALTKTKilekCTVLTNFLEIDDADLEVTHDKSMVKDLmesekktqedinsqcEKYD-SVFMTEfqNS 112
Cdd:cd10001   25 HPENPERAEAILDALKRAG----LGEVLPPRDFGLEPILAVHDPDYVDFL---------------ETADtDTPISE--GT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 113 MKVAKDGVACVRDLTNRIMANEASNgFAVVRPPGHHAdSVSPC-GFCLFNNVAQAAEeAFFSGAERILIVDLDVHHGHGT 191
Cdd:cd10001   84 WEAALAAADTALTAADLVLEGERAA-YALCRPPGHHA-GRDRAgGFCYFNNAAIAAQ-YLRDRAGRVAILDVDVHHGNGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 192 QRIFYDDKRVLYFSIHRHEHGLFwPHlpesdF----DHIGSGKGLGYNANLALnETGCTDSDYLSIIFHVLLPLAtQFDP 267
Cdd:cd10001  161 QEIFYERPDVLYVSIHGDPRTFY-PF-----FlgfaDETGEGEGEGYNLNLPL-PPGTGDDDYLAALDEALAAIA-AFGP 232
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193206283 268 HFVIISAGFDALLGDPLGGMCLTPDGYSHILYHLKSLaQGRMLVVLEGGYNhqisAVAVQRCVR-VLLGYA 337
Cdd:cd10001  233 DALVVSLGFDTHEGDPLSDFKLTTEDYARIGRRIAAL-GLPTVFVQEGGYN----VDALGRNAVaFLAGFE 298
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
102-382 7.58e-61

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: 213.31  E-value: 7.58e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 102 DSVFmTEFQNSMKVaKDGVACVRDLTNRIMANEASNGFAVVRPPGHHADSVSPCGFCLFNNVAQAAEEAFFS-GAERILI 180
Cdd:cd10007  111 DTVW-NEMHSSSAV-RMAVGCLIELAFKVAAGELKNGFAVIRPPGHHAEESTAMGFCFFNSVAIAAKLLQQKlNVGKILI 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 181 VDLDVHHGHGTQRIFYDDKRVLYFSIHRHEHGLFWPHLPESdfDHIGSGKGLGYNANLALN---ETGCTDSDYLSIIFHV 257
Cdd:cd10007  189 VDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGNFFPGSGAP--DEVGAGPGVGFNVNIAWTggvDPPIGDVEYLTAFRTV 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 258 LLPLATQFDPHFVIISAGFDALLG--DPLGGMCLTPDGYSHILYHLKSLAQGRMLVVLEGGynHQISAV--AVQRCVRVL 333
Cdd:cd10007  267 VMPIANEFSPDVVLVSAGFDAVEGhqSPLGGYSVTAKCFGHLTKQLMTLAGGRVVLALEGG--HDLTAIcdASEACVSAL 344
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 193206283 334 LGYAPFSIE---LNEAPKESTVDSCVSLVSVLRHHWNCFDYFPSRT--SLRLAQ 382
Cdd:cd10007  345 LGMELTPLDntvLQQKPNDNAVATLERVIEIQSKHWSCLKRFAATLgfSLLEAQ 398
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
111-366 1.25e-59

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: 208.71  E-value: 1.25e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 111 NSMKVAKDGVACVRDLTNRIMANEASNGFAVVRPPGHHADSVSPCGFCLFNNVAQAAEEAFFSG-AERILIVDLDVHHGH 189
Cdd:cd10008  116 HSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGFCFFNSVAIACRQLQQQGkASKILIVDWDVHHGN 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 190 GTQRIFYDDKRVLYFSIHRHEHGLFWPHlpESDFDHIGSGKGLGYNANLALN---ETGCTDSDYLSIIFHVLLPLATQFD 266
Cdd:cd10008  196 GTQQTFYQDPSVLYISLHRHDDGNFFPG--SGAVDEVGAGSGEGFNVNVAWAgglDPPMGDPEYLAAFRIVVMPIAREFS 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 267 PHFVIISAGFDALLGD--PLGGMCLTPDGYSHILYHLKSLAQGRMLVVLEGGynHQISAV--AVQRCVRVLLG--YAPFS 340
Cdd:cd10008  274 PDLVLVSAGFDAAEGHpaPLGGYHVSAKCFGYMTQQLMNLAGGAVVLALEGG--HDLTAIcdASEACVAALLGneVDPLS 351
                        250       260
                 ....*....|....*....|....*..
gi 193206283 341 IE-LNEAPKESTVDSCVSLVSVLRHHW 366
Cdd:cd10008  352 EEsWKQKPNLNAIRSLEAVIRVHSKYW 378
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
454-749 3.48e-59

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: 3.48e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 454 RTRRILKTLRESGVLEKCVDRNCERiATNEEIRLVHTKKMLEHLRTTETMKDEELMEEAEKEFNsIYLTRDTLKVARKAV 533
Cdd:cd09301    1 RIRDLIEALKELGLRPKIELIECRE-ATEELLLKVHTEEYLNELKANFAVATITESKPVIFGPN-FPVQRHYFRGARLST 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 534 GAVLQSVDEIFEKDAgqRNALVIVRPPGHHASASKSSGFCIFNNVAVAAKYAQRRhKAKRVLILDWDVHHGNGTQEIFYE 613
Cdd:cd09301   79 GGVVEAAELVAKGEL--ERAFAVVGAGGHHAGKSRAWGFCYFNDVVLAIKFLRER-GISRILIIDTDAHHGDGTREAFYD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 614 DSNVMYMSIHRHDKGNFypigepkdysdvGEGAGEGMSVNVPFSGVqMGDNEYQMAFQRVIMPIAYQFNPDLVLISAGFD 693
Cdd:cd09301  156 DDRVLHMSFHNYDIYPF------------GRGKGKGYKINVPLEDG-LGDEEYLDAVERVISKVLEEFEPEVVVLQFGHD 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 193206283 694 AAVDDPLGEYKVTPETFALMTYQLSSLA-GGRIITVLEGGYNLTSISNSAQAVCEVL 749
Cdd:cd09301  223 THEGDRLGGFNLSEKGFVKLAEIVKEFArGGPILMVLGGGYNPEAAARIWTAIIKEL 279
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
33-366 5.83e-53

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: 189.84  E-value: 5.83e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  33 THPESSDRILKIKEALTKTKILEKCT-VLTNFLEIDDADLEVTHDKSMV---KDLMESEKKTQEDINSQCEKY------- 101
Cdd:cd10009   23 THPEHAGRIQSIWSRLQETGLLNKCErIQGRKASLEEIQLVHSEHHSLLygtNPLDGQKLDPRILLGDDSQKFfsslpcg 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 102 ----DSVFMTEFQNSMKVAKDGVACVRDLTNRIMANEASNGFAVVRPPGHHADSVSPCGFCLFNNVAQAAEEAFFS-GAE 176
Cdd:cd10009  103 glgvDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQlNIS 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 177 RILIVDLDVHHGHGTQRIFYDDKRVLYFSIHRHEHGLFWPHlpESDFDHIGSGKGLGYNANLALN---ETGCTDSDYLSI 253
Cdd:cd10009  183 KILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPG--SGAPNEVGTGLGEGYNINIAWTgglDPPMGDVEYLEA 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 254 IFHVLLPLATQFDPHFVIISAGFDALLGD--PLGGMCLTPDGYSHILYHLKSLAQGRMLVVLEGGynHQISAV--AVQRC 329
Cdd:cd10009  261 FRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLADGRVVLALEGG--HDLTAIcdASEAC 338
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 193206283 330 VRVLLG--YAPFSIE-LNEAPKESTVDSCVSLVSVLRHHW 366
Cdd:cd10009  339 VNALLGneLEPLAEDiLHQSPNMNAVISLQKIIEIQSKYW 378
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
446-735 9.75e-53

Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin utilization protein) is a class I deacetylase found only in bacteria and is involved in post-translational control of the acetyl-coenzyme A synthetase (AcsA). Deacetylase AcuC works in coordination with deacetylase SrtN (class III), possibly to maintain AcsA in active (deacetylated) form and let the cell grow under low concentration of acetate. B. subtilis AcuC is a member of operon acuABC; this operon is repressed by the presence of glucose and does not show induction by acetoin; acetoin is a bacterial fermentation product that can be converted to acetate via the butanediol cycle in absence of other carbon sources. Inactivation of AcuC leads to slower growth and lower cell yield under low-acetate conditions in Bacillus subtilis. In general, Class I histone deacetylases (HDACs) are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues in histone amino termini to yield a deacetylated histone (EC 3.5.1.98). Enzymes belonging to this group participate in regulation of a number of processes through protein (mostly different histones) modification (deacetylation). Class I histone deacetylases in general act via the formation of large multiprotein complexes. Members of this class are involved in cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and in posttranslational control of the acetyl coenzyme A synthetase.


Pssm-ID: 212520 [Multi-domain]  Cd Length: 313  Bit Score: 187.00  E-value: 9.75e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 446 DNHPEKPARTRRILKTLRESGVLEKcVDRNCERIATNEEIRLVHTKKMLEHLRttetMKDEELMEEAEKEFNsiYLTRDT 525
Cdd:cd09994   15 PNHPFNPPRLSLTKDLLRALGLLPP-VDLVPPRPATEEELLLFHTPDYIEAVK----EASRGQEPEGRGRLG--LGTEDN 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 526 ------LKVARKAVGAVLQSVDEIFEKdagqrNALVIVRPPG--HHASASKSSGFCIFNNVAVAAKYAqRRHKAKRVLIL 597
Cdd:cd09994   88 pvfpgmHEAAALVVGGTLLAARLVLEG-----EARRAFNPAGglHHAMRGRASGFCVYNDAAVAIERL-RDKGGLRVAYV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 598 DWDVHHGNGTQEIFYEDSNVMYMSIHRHDKGnFYPiGEpKDYSDVGEGAGEGMSVNVP---FsgvqMGDNEYQMAFQRVI 674
Cdd:cd09994  162 DIDAHHGDGVQAAFYDDPRVLTISLHESGRY-LFP-GT-GFVDEIGEGEGYGYAVNIPlppG----TGDDEFLRAFEAVV 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193206283 675 MPIAYQFNPDLVLISAGFDAAVDDPLGEYKVTPETFALMTYQLSSLA----GGRIITVLEGGYNL 735
Cdd:cd09994  235 PPLLRAFRPDVIVSQHGADAHAGDPLTHLNLSNRAYRAAVRRIRELAdeycGGRWLALGGGGYNP 299
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
40-333 6.39e-50

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: 178.01  E-value: 6.39e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  40 RILKIKEALTKTKILEKCTvLTNFLEIDDADLEVTHDKSMVKDLMESEKktqedINSQCEKYDSVFMTEFQNSMKV---A 116
Cdd:cd09301    1 RIRDLIEALKELGLRPKIE-LIECREATEELLLKVHTEEYLNELKANFA-----VATITESKPVIFGPNFPVQRHYfrgA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 117 KDGVACVRDLTNRIMANEASNGFAVVRPPGHHADSVSPCGFCLFNNVAQAAEEAFFSGAERILIVDLDVHHGHGTQRIFY 196
Cdd:cd09301   75 RLSTGGVVEAAELVAKGELERAFAVVGAGGHHAGKSRAWGFCYFNDVVLAIKFLRERGISRILIIDTDAHHGDGTREAFY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 197 DDKRVLYFSIHRhehglfwphlpeSDFDHIGSGKGLGYNANLALnETGCTDSDYLSIIFHVLLPLATQFDPHFVIISAGF 276
Cdd:cd09301  155 DDDRVLHMSFHN------------YDIYPFGRGKGKGYKINVPL-EDGLGDEEYLDAVERVISKVLEEFEPEVVVLQFGH 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 193206283 277 DALLGDPLGGMCLTPDGYSHILYHLKSLAQ-GRMLVVLEGGYNHQISAVAVQRCVRVL 333
Cdd:cd09301  222 DTHEGDRLGGFNLSEKGFVKLAEIVKEFARgGPILMVLGGGYNPEAAARIWTAIIKEL 279
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
32-329 1.14e-41

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: 155.41  E-value: 1.14e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  32 PTHPESSDRIlkikeALTKtKILEKCTVLT--NFLE---IDDADLEVTHDKSMVKDLMESEkktQEDINSQCEKYD---- 102
Cdd:cd09994   15 PNHPFNPPRL-----SLTK-DLLRALGLLPpvDLVPprpATEEELLLFHTPDYIEAVKEAS---RGQEPEGRGRLGlgte 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 103 --SVFMTEFQNSMKVAKDGVACVRdltnRIMANEASNGFAvvrPPG--HHA--DSVSpcGFCLFNNVAQAAEEAFFSGAE 176
Cdd:cd09994   86 dnPVFPGMHEAAALVVGGTLLAAR----LVLEGEARRAFN---PAGglHHAmrGRAS--GFCVYNDAAVAIERLRDKGGL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 177 RILIVDLDVHHGHGTQRIFYDDKRVLYFSIhrHEHGL-FWPHlpESDFDHIGSGKGLGYNANLALnETGCTDSDYLSIIF 255
Cdd:cd09994  157 RVAYVDIDAHHGDGVQAAFYDDPRVLTISL--HESGRyLFPG--TGFVDEIGEGEGYGYAVNIPL-PPGTGDDEFLRAFE 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193206283 256 HVLLPLATQFDPHFVIISAGFDALLGDPLGGMCLTPDGYSHILYHLKSLA----QGRMLVVLEGGYNHQisavAVQRC 329
Cdd:cd09994  232 AVVPPLLRAFRPDVIVSQHGADAHAGDPLTHLNLSNRAYRAAVRRIRELAdeycGGRWLALGGGGYNPD----VVARA 305
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
446-739 4.53e-37

Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that catalyzes hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. HDAC8 is found in human cytoskeleton-bound protein fraction and insoluble cell pellets. It plays a crucial role in intramembraneous bone formation; germline deletion of HDAC8 is detrimental to skull bone formation. HDAC8 is possibly associated with the smooth muscle actin cytockeleton and may regulate the contractive capacity of smooth muscle cells. HDAC8 is also involved in the metabolic control of the estrogen receptor related receptor (ERR)-alpha/peroxisome proliferator activated receptor (PPAR) gamma coactivator 1 alpha (PGC1-alpha) transcriptional complex as well as in the development of neuroblastoma and T-cell lymphoma. HDAC8-selective small-molecule inhibitors could be a therapeutic drug option for these diseases.


Pssm-ID: 212524 [Multi-domain]  Cd Length: 364  Bit Score: 143.63  E-value: 4.53e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 446 DNHPEKPARTRrILKTLRES-GVLEKCVDRNCeRIATNEEIRLVHTKKMLEHLRTTETMKDEELMEEAEKEFNSIY---L 521
Cdd:cd10000   14 DRLPKVPNRAS-MVHSLIEAyGLLKQLRVVKP-RVATEEELASFHSDEYIQFLKKASNEGDNDEEPSEQQEFGLGYdcpI 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 522 TRDTLKVARKAVGAVLQSVDEIFEKDAgqrnALVIVRPPG-HHASASKSSGFCIFNNVAVAAKYAqrRHKAKRVLILDWD 600
Cdd:cd10000   92 FEGIYDYAAAVAGATLTAAQLLIDGKC----KVAINWFGGwHHAQRDEASGFCYVNDIVLGILKL--REKFDRVLYVDLD 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 601 VHHGNGTQEIFYEDSNVMYMSIHRHDKGnFYP-IGepkDYSDVGEGAGEGMSVNVPF-SGVQmgDNEYQMAFQRVIMPIA 678
Cdd:cd10000  166 LHHGDGVEDAFSFTSKVMTVSLHKYSPG-FFPgTG---DVSDVGLGKGKYYTVNVPLrDGIQ--DEQYLQIFTAVVPEIV 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193206283 679 YQFNPDLVLISAGFDAAVDDPLGEYKVTPETFA-----LMTYQLSSL-AGGriitvleGGYNLTSIS 739
Cdd:cd10000  240 AAFRPEAVVLQCGADTLAGDPMGAFNLTPVGIGkclkyVLGWKLPTLiLGG-------GGYNLANTA 299
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
34-325 3.40e-35

Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone deacetylases (HDAC11; EC 3.5.1.98) are predicted Zn-dependent enzymes. This class includes animal HDAC11, plant HDA2 and related bacterial deacetylases. Enzymes in this subfamily participate in regulation of a number of different processes through protein modification (deacetylation). They catalyze hydrolysis of N(6)-acetyl-lysine of histones (or other proteins) to yield a deacetylated proteins. Histone deacetylases often act as members of large multi-protein complexes such as mSin3A or SMRT/N-CoR. Human HDAC11 does not associate with them but can interact with HDAC6 in vivo. It has been suggested that HDAC11 and HDAC6 may use non-histone proteins as their substrates and play a role other than to directly modulate chromatin structure. In normal tissues, expression of HDAC11 is limited to kidney, heart, brain, skeletal muscle and testis, suggesting that its function might be tissue-specific. In mammals, HDAC11 proteins are known to be involved in progression of various tumors. HDAC11 plays an essential role in regulating OX40 ligand (OX40L) expression in Hodgkin lymphoma (HL); selective inhibition of HDAC11 expression significantly up-regulates OX40L and induces apoptosis in HL cell lines. Thus, inhibition of HDAC11 could be a therapeutic drug option for antitumor immune response in HL patients.


Pssm-ID: 212519 [Multi-domain]  Cd Length: 275  Bit Score: 135.32  E-value: 3.40e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  34 HPESSDRILKIKEALTKTKILEKCTVLTNfLEIDDADLEVTHDKSMVKDLMESEKKTQEdinsqcekydsVFMTEFQNSM 113
Cdd:cd09993    1 HRFPMRKYGLLREALLEEGLVLPEDIVEP-EPATREDLLRVHDPEYLESLKSGELSREE-----------IRRIGFPWSP 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 114 KVAKDG-------VACVRD-LTNRIMANEASnGFavvrppgHHADSVSPCGFCLFNNVAQAAEEAFFSG-AERILIVDLD 184
Cdd:cd09993   69 ELVERTrlavggtILAARLaLEHGLAINLAG-GT-------HHAFPDRGEGFCVFNDIAIAARVLLAEGlVRRVLIVDLD 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 185 VHHGHGTQRIFYDDKRVLYFSIHrHEHGlfWPHLPE-SDFDhigsgkglgynanLALnETGCTDSDYLSIIFHVLLPLAT 263
Cdd:cd09993  141 VHQGNGTAAIFADDPSVFTFSMH-GEKN--YPFRKEpSDLD-------------VPL-PDGTGDDEYLAALEEALPRLLA 203
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193206283 264 QFDPHFVIISAGFDALLGDPLGGMCLTPDGyshilyhLK-------SLAQGR---MLVVLEGGYNHQISAVA 325
Cdd:cd09993  204 EFRPDLVFYNAGVDVLAGDRLGRLSLSLEG-------LRerdrlvlRFARARgipVAMVLGGGYSRDIARLV 268
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
448-734 4.92e-32

Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone deacetylases (HDAC11; EC 3.5.1.98) are predicted Zn-dependent enzymes. This class includes animal HDAC11, plant HDA2 and related bacterial deacetylases. Enzymes in this subfamily participate in regulation of a number of different processes through protein modification (deacetylation). They catalyze hydrolysis of N(6)-acetyl-lysine of histones (or other proteins) to yield a deacetylated proteins. Histone deacetylases often act as members of large multi-protein complexes such as mSin3A or SMRT/N-CoR. Human HDAC11 does not associate with them but can interact with HDAC6 in vivo. It has been suggested that HDAC11 and HDAC6 may use non-histone proteins as their substrates and play a role other than to directly modulate chromatin structure. In normal tissues, expression of HDAC11 is limited to kidney, heart, brain, skeletal muscle and testis, suggesting that its function might be tissue-specific. In mammals, HDAC11 proteins are known to be involved in progression of various tumors. HDAC11 plays an essential role in regulating OX40 ligand (OX40L) expression in Hodgkin lymphoma (HL); selective inhibition of HDAC11 expression significantly up-regulates OX40L and induces apoptosis in HL cell lines. Thus, inhibition of HDAC11 could be a therapeutic drug option for antitumor immune response in HL patients.


Pssm-ID: 212519 [Multi-domain]  Cd Length: 275  Bit Score: 126.07  E-value: 4.92e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 448 HPEKPARTRRILKTLRESGVLEkCVDRNCERIATNEEIRLVHTKKMLEHLRTTETMKDEELMEEaekeF-NSI-YLTRdt 525
Cdd:cd09993    1 HRFPMRKYGLLREALLEEGLVL-PEDIVEPEPATREDLLRVHDPEYLESLKSGELSREEIRRIG----FpWSPeLVER-- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 526 lkvARKAVGAVLQSVDEIFEKD-----AGqrnalvivrppG-HHASASKSSGFCIFNNVAVAAKYAQRRHKAKRVLILDW 599
Cdd:cd09993   74 ---TRLAVGGTILAARLALEHGlainlAG-----------GtHHAFPDRGEGFCVFNDIAIAARVLLAEGLVRRVLIVDL 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 600 DVHHGNGTQEIFYEDSNVMYMSIHrhdKGNFYPIgePKDYSDVgegagegmSVNVPfSGvqMGDNEYQMAFQRVIMPIAY 679
Cdd:cd09993  140 DVHQGNGTAAIFADDPSVFTFSMH---GEKNYPF--RKEPSDL--------DVPLP-DG--TGDDEYLAALEEALPRLLA 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 193206283 680 QFNPDLVLISAGFDAAVDDPLGEYKVTPETFA---LMTYQLSSLAGGRIITVLEGGYN 734
Cdd:cd09993  204 EFRPDLVFYNAGVDVLAGDRLGRLSLSLEGLRerdRLVLRFARARGIPVAMVLGGGYS 261
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
446-739 6.77e-31

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: 123.85  E-value: 6.77e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 446 DNHPEKPARTRrILKTLRESGVLEKCVDRNCERIATNEEIRLVHTKKMLEHLR--TTETMKDEELMEEAekeFNsiyLTR 523
Cdd:cd09991   13 QGHPMKPHRIR-MTHSLILSYGLYKKMEIYRPRPATAEELTKFHSDDYIDFLRsvSPDNMKEFKKQLER---FN---VGE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 524 DT------LKVARKAVGAvlqSVDEIFEKDAGQRNalVIVRPPG--HHASASKSSGFCIFNNVAVAAKYAQRRHKakRVL 595
Cdd:cd09991   86 DCpvfdglYEYCQLYAGG---SIAAAVKLNRGQAD--IAINWAGglHHAKKSEASGFCYVNDIVLAILELLKYHQ--RVL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 596 ILDWDVHHGNGTQEIFYEDSNVMYMSIHRHdkGNFYPIGEpkDYSDVGEGAGEGMSVNVPF-SGvqMGDNEYQMAFQRVI 674
Cdd:cd09991  159 YIDIDIHHGDGVEEAFYTTDRVMTVSFHKF--GEYFFPGT--GLRDIGAGKGKYYAVNVPLkDG--IDDESYLQIFEPVL 232
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193206283 675 MPIAYQFNPDLVLISAGFDAAVDDPLGEYKVTPETFA-----LMTYQLSSLA-GGriitvleGGYNLTSIS 739
Cdd:cd09991  233 SKVMEVFQPSAVVLQCGADSLAGDRLGCFNLSIKGHAkcvkfVKSFNIPLLVlGG-------GGYTLRNVA 296
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
60-329 1.62e-30

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


Pssm-ID: 212517 [Multi-domain]  Cd Length: 306  Bit Score: 122.69  E-value: 1.62e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  60 LTNFLEI------DDADLEVTHDKSMVKDLMESEKKTQEDINSQCEKYDS-----VF--MTEFQNSmkVAKDGVACVRDL 126
Cdd:cd09991   34 LYKKMEIyrprpaTAEELTKFHSDDYIDFLRSVSPDNMKEFKKQLERFNVgedcpVFdgLYEYCQL--YAGGSIAAAVKL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 127 tNRIMANEASN---GFavvrppgHHADSVSPCGFCLFNNVAQAAEEaFFSGAERILIVDLDVHHGHGTQRIFYDDKRVLY 203
Cdd:cd09991  112 -NRGQADIAINwagGL-------HHAKKSEASGFCYVNDIVLAILE-LLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMT 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 204 FSIHRHEHGLFwphlPESDFDHIGSGKGLGYNANLALNEtGCTDSDYLSIIFHVLLPLATQFDPHFVIISAGFDALLGDP 283
Cdd:cd09991  183 VSFHKFGEYFF----PGTGLRDIGAGKGKYYAVNVPLKD-GIDDESYLQIFEPVLSKVMEVFQPSAVVLQCGADSLAGDR 257
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 193206283 284 LGGMCLTPDGYSHILYHLKSLaQGRMLVVLEGGYNhqISAVAvqRC 329
Cdd:cd09991  258 LGCFNLSIKGHAKCVKFVKSF-NIPLLVLGGGGYT--LRNVA--RC 298
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
517-746 8.21e-30

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: 121.79  E-value: 8.21e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 517 NSIYLTRDTLKVARKAVGAVLQSVDEIFEKDAGQ-RNALVIVRPPGHHASASKSSGFCIFNNVAVAAKYAQRRHKAKRVL 595
Cdd:cd09998   74 GDLYLCPESLDAIQGALGAVCEAVDSVFKPESPGtKRAFVAIRPPGHHCSESTPSGFCWVNNVHVGAAHAYLTHGITRVV 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 596 ILDWDVHHGNGTQEI----------------FYEDSN--------VMYMSIHrhdKGNFYPI--GEP---KDYSDVGEGA 646
Cdd:cd09998  154 ILDIDLHHGNGTQDIawrinaeankqalessSYDDFKpagapglrIFYSSLH---DINSFPCedGDPakvKDASVSIDGA 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 647 gEGMSV-NV---PFSGVQ----MGDNEYQMAFQRVIMPIAYQFNPD----LVLISAGFDA-----------AVDDPLGEY 703
Cdd:cd09998  231 -HGQWIwNVhlqPWTTEEdfweLYYPKYRILFEKAAEFLRLTTAATpfktLVFISAGFDAseheyesmqrhGVNVPTSFY 309
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 193206283 704 kvtpETFALMTYQLSSL-AGGRIITVLEGGYnltsisnSAQAVC 746
Cdd:cd09998  310 ----YRFARDAVRFADAhAHGRLISVLEGGY-------SDRALC 342
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
147-335 4.35e-27

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: 113.97  E-value: 4.35e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 147 HHADSVSPCGFCLFNNVA---QAAEEAFfsgaERILIVDLDVHHGHGTQRIFYDDKRVLYFSIHRHEHGLFwphlPES-D 222
Cdd:cd10000  129 HHAQRDEASGFCYVNDIVlgiLKLREKF----DRVLYVDLDLHHGDGVEDAFSFTSKVMTVSLHKYSPGFF----PGTgD 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 223 FDHIGSGKGLGYNANLALnETGCTDSDYLSiIFHVLLPLATQ-FDPHFVIISAGFDALLGDPLGGMCLTPDGYSHIlyhL 301
Cdd:cd10000  201 VSDVGLGKGKYYTVNVPL-RDGIQDEQYLQ-IFTAVVPEIVAaFRPEAVVLQCGADTLAGDPMGAFNLTPVGIGKC---L 275
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 193206283 302 KSLAQGR--MLVVLEGGYNHqisaVAVQRCVRVLLG 335
Cdd:cd10000  276 KYVLGWKlpTLILGGGGYNL----ANTARCWTYLTG 307
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
147-319 6.67e-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: 108.89  E-value: 6.67e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 147 HHADSVSPCGFCLFNNVAQAAEEAFFSGAERILIVDLDVHHGHGTQRIFYDDKRVLYFSIHRHEHGLFwPhlpesdfdhi 226
Cdd:cd11680  115 HHAQKSRASGFCYVNDIVLAILRLRRARFRRVFYLDLDLHHGDGVESAFFFSKNVLTCSIHRYDPGFF-P---------- 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 227 GSGKGLGYNANLALN---ETGCTDSDYLSIIFHVLLPLATQFDPHFVIISAGFDALLGDPLGGMCLTPDGYSH-ILYHLK 302
Cdd:cd11680  184 GTGSLKNSSDKGMLNiplKRGLSDKTLLRIIDSIVRPLIEKFEPEVIVIQCGCDGLSGDPHKEWNLTIRGYGSvIELLLK 263
                        170
                 ....*....|....*..
gi 193206283 303 SLAQGRMLVVLEGGYNH 319
Cdd:cd11680  264 EFKDKPTLLLGGGGYNH 280
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
432-703 1.17e-24

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: 105.62  E-value: 1.17e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 432 YFNEG-DDAHFDleeDNHPEKPARTRrILKTLRESGVLEKCVDRNCERIATNEEIRLVHTKKMLEHLR--TTETMKDEEL 508
Cdd:cd11598    4 HFNSRvEDYHFG---RTHPMKPFRLT-LTKHLVMGYGLHKAMDTYEARAATREELRQFHDADYLDFLSkvSPENANQLRF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 509 MEEAEKE-------FNSIY-----LTRDTLKVARKAVgavlqsvdeifekdAGQRNALVIVRPPGHHASASKSSGFCIFN 576
Cdd:cd11598   80 DKAEPFNigddcpvFDGMYdycqlYAGASLDAARKLC--------------SGQSDIAINWSGGLHHAKKSEASGFCYVN 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 577 NVAVAAKYAQRRHKakRVLILDWDVHHGNGTQEIFYEDSNVMYMSIHRHDkGNFYPigEPKDYSDVGEGAGEGMSVNVPF 656
Cdd:cd11598  146 DIVLAILNLLRYFP--RVLYIDIDVHHGDGVEEAFYRTDRVMTLSFHKYN-GEFFP--GTGDLDDNGGTPGKHFALNVPL 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 193206283 657 -SGVqmGDNEYQMAFQRVIMPIAYQFNPDLVLISAGFDAAVDDPLGEY 703
Cdd:cd11598  221 eDGI--DDEQYNLLFKSIIGPTIEKFQPSAIVLQCGADSLGGDRLGQF 266
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
562-736 4.67e-23

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: 100.42  E-value: 4.67e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 562 HHASASKSSGFCIFNNVaVAAKYAQRRHKAKRVLILDWDVHHGNGTQEIFYEDSNVMYMSIHRHDKGnFYPI-GEPKDYS 640
Cdd:cd11680  115 HHAQKSRASGFCYVNDI-VLAILRLRRARFRRVFYLDLDLHHGDGVESAFFFSKNVLTCSIHRYDPG-FFPGtGSLKNSS 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 641 DVGegagegmSVNVPFS-GvqMGDNEYQMAFQRVIMPIAYQFNPDLVLISAGFDAAVDDPLGEYKVTPETFALMTYQLS- 718
Cdd:cd11680  193 DKG-------MLNIPLKrG--LSDKTLLRIIDSIVRPLIEKFEPEVIVIQCGCDGLSGDPHKEWNLTIRGYGSVIELLLk 263
                        170
                 ....*....|....*...
gi 193206283 719 SLAGGRIITVLEGGYNLT 736
Cdd:cd11680  264 EFKDKPTLLLGGGGYNHT 281
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
877-939 1.79e-22

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 91.55  E-value: 1.79e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193206283  877 CSECQIGAEVWTCLTCYKYNCGRFVNEHAMMHHLSSSHPMALSMADLSVWCYPCDSYVHNPAL 939
Cdd:pfam02148   1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPSL 63
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
562-739 1.95e-21

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: 97.57  E-value: 1.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 562 HHASASKSSGFCIFNNVAVAAKYAQRRHKakRVLILDWDVHHGNGTQEIFYEDSNVMYMSIHRHdkGNFYP-IGEPKdys 640
Cdd:cd10004  133 HHAKKSEASGFCYVNDIVLGILELLRYHQ--RVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKY--GEYFPgTGELR--- 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 641 DVGEGAGEGMSVNVPF-SGVQmgDNEYQMAFQRVIMPIAYQFNPDLVLISAGFDAAVDDPLGEYKVTPETFALMTYQLSS 719
Cdd:cd10004  206 DIGIGTGKNYAVNVPLrDGID--DESYKSIFEPVIKHVMEWYQPEAVVLQCGGDSLSGDRLGCFNLSMKGHANCVNFVKS 283
                        170       180
                 ....*....|....*....|
gi 193206283 720 LaGGRIITVLEGGYNLTSIS 739
Cdd:cd10004  284 F-NLPMLVLGGGGYTMRNVA 302
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
432-739 6.68e-21

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: 95.90  E-value: 6.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 432 YFNEGDDAHFDLEEdNHPEKPARTRRILKTLRESGVLEKCVDRNCERiATNEEIRLVHTKKMLEHLRTT--ETMKDEELM 509
Cdd:cd10010   10 YYYDGDVGNYYYGQ-GHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHK-ANAEEMTKYHSDDYIKFLRSIrpDNMSEYSKQ 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 510 EEAEKEFNSIYLTRDTLKVARKAVGAvlqSVDEIFEKDAGQRNALVIVRPPGHHASASKSSGFCIFNNVAVAAKYAQRRH 589
Cdd:cd10010   88 MQRFNVGEDCPVFDGLFEFCQLSAGG---SVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYH 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 590 KakRVLILDWDVHHGNGTQEIFYEDSNVMYMSIHRHdkGNFYPigEPKDYSDVGEGAGEGMSVNVPFSGvQMGDNEYQMA 669
Cdd:cd10010  165 Q--RVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKY--GEYFP--GTGDLRDIGAGKGKYYAVNYPLRD-GIDDESYEAI 237
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193206283 670 FQRVIMPIAYQFNPDLVLISAGFDAAVDDPLGEYKVTPETFA-----LMTYQLSSLAGGriitvlEGGYNLTSIS 739
Cdd:cd10010  238 FKPVMSKVMEMFQPSAVVLQCGADSLSGDRLGCFNLTIKGHAkcvefVKSFNLPMLMLG------GGGYTIRNVA 306
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
147-317 2.61e-20

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: 92.90  E-value: 2.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 147 HHADSVSPCGFCLFNNVAQAAEEA--FFSgaeRILIVDLDVHHGHGTQRIFYDDKRVLYFSIHRHEHGLFwphlPES-DF 223
Cdd:cd11598  131 HHAKKSEASGFCYVNDIVLAILNLlrYFP---RVLYIDIDVHHGDGVEEAFYRTDRVMTLSFHKYNGEFF----PGTgDL 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 224 DHIGSGKGLGYNANLALNEtGCTDSDYLSIIFHVLLPLATQFDPHFVIISAGFDALLGDPLGGMCLTPDGYSHILYHLKS 303
Cdd:cd11598  204 DDNGGTPGKHFALNVPLED-GIDDEQYNLLFKSIIGPTIEKFQPSAIVLQCGADSLGGDRLGQFNLNIKAHGACVKFVKS 282
                        170
                 ....*....|....
gi 193206283 304 LAQgRMLVVLEGGY 317
Cdd:cd11598  283 FGI-PMLVVGGGGY 295
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
147-329 1.67e-19

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: 91.67  E-value: 1.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 147 HHADSVSPCGFCLFNNVAQAAEEaFFSGAERILIVDLDVHHGHGTQRIFYDDKRVLyfSIHRHEHGLFWPHlpESDFDHI 226
Cdd:cd10010  137 HHAKKSEASGFCYVNDIVLAILE-LLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVM--TVSFHKYGEYFPG--TGDLRDI 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 227 GSGKGLGYNANLALNEtGCTDSDYLSIIFHVLLPLATQFDPHFVIISAGFDALLGDPLGGMCLTPDGYSHILYHLKSLaq 306
Cdd:cd10010  212 GAGKGKYYAVNYPLRD-GIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEFVKSF-- 288
                        170       180
                 ....*....|....*....|...
gi 193206283 307 gRMLVVLEGGYNHQISAVAvqRC 329
Cdd:cd10010  289 -NLPMLMLGGGGYTIRNVA--RC 308
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
147-317 1.21e-18

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: 1.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 147 HHADSVSPCGFCLFNNVAQAAEEaFFSGAERILIVDLDVHHGHGTQRIFYDDKRVLYFSIHRheHGLFWPHLPEsdFDHI 226
Cdd:cd10004  133 HHAKKSEASGFCYVNDIVLGILE-LLRYHQRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHK--YGEYFPGTGE--LRDI 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 227 GSGKGLGYNANLALNEtGCTDSDYLSIIFHVLLPLATQFDPHFVIISAGFDALLGDPLGGMCLTPDGYSHILYHLKSLAQ 306
Cdd:cd10004  208 GIGTGKNYAVNVPLRD-GIDDESYKSIFEPVIKHVMEWYQPEAVVLQCGGDSLSGDRLGCFNLSMKGHANCVNFVKSFNL 286
                        170
                 ....*....|.
gi 193206283 307 gRMLVVLEGGY 317
Cdd:cd10004  287 -PMLVLGGGGY 296
PTZ00063 PTZ00063
histone deacetylase; Provisional
562-706 2.59e-18

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 88.71  E-value: 2.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 562 HHASASKSSGFCIFNNVAVAAKYAQRRHKakRVLILDWDVHHGNGTQEIFYEDSNVMYMSIHRHdkGNFYPigEPKDYSD 641
Cdd:PTZ00063 137 HHAKRSEASGFCYINDIVLGILELLKYHA--RVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFP--GTGDVTD 210
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193206283 642 VGEGAGEGMSVNVPFSGvQMGDNEYQMAFQRVIMPIAYQFNPDLVLISAGFDAAVDDPLGEYKVT 706
Cdd:PTZ00063 211 IGVAQGKYYSVNVPLND-GIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLT 274
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
432-739 1.18e-17

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: 85.89  E-value: 1.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 432 YFNEGDDAHFDLEEdNHPEKPARTRRILKTLRESGVLEKCVDRNCERiATNEEIRLVHTKKMLEHLRTTETMKdeelmee 511
Cdd:cd10011    6 YYYDGDIGNYYYGQ-GHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHK-ATAEEMTKYHSDEYIKFLRSIRPDN------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 512 aekefnsiyLTRDTLKVARKAVGAVLQSVDEIFE--------------KDAGQRNALVIVRPPG-HHASASKSSGFCIFN 576
Cdd:cd10011   77 ---------MSEYSKQMQRFNVGEDCPVFDGLFEfcqlstggsvagavKLNRQQTDMAVNWAGGlHHAKKSEASGFCYVN 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 577 NVAVAAKYAQRRHKakRVLILDWDVHHGNGTQEIFYEDSNVMYMSiHRHDKGNFYPIGepkDYSDVGEGAGEGMSVNVPF 656
Cdd:cd10011  148 DIVLAILELLKYHQ--RVLYIDIDIHHGDGVEEAFYTTDRVMTVS-FHKYGEYFPGTG---DLRDIGAGKGKYYAVNFPM 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 657 SGvQMGDNEYQMAFQRVIMPIAYQFNPDLVLISAGFDAAVDDPLGEYKVTPETFA-----LMTYQLSSLAGGriitvlEG 731
Cdd:cd10011  222 RD-GIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAkcvevVKTFNLPLLMLG------GG 294

                 ....*...
gi 193206283 732 GYNLTSIS 739
Cdd:cd10011  295 GYTIRNVA 302
PTZ00063 PTZ00063
histone deacetylase; Provisional
147-329 7.64e-17

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 84.09  E-value: 7.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 147 HHADSVSPCGFCLFNNVAQAAEEAFFSGAeRILIVDLDVHHGHGTQRIFYDDKRVLYFSIHRheHGLFWPHlpESDFDHI 226
Cdd:PTZ00063 137 HHAKRSEASGFCYINDIVLGILELLKYHA-RVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHK--FGDFFPG--TGDVTDI 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 227 GSGKGLGYNANLALNEtGCTDSDYLSIIFHVLLPLATQFDPHFVIISAGFDALLGDPLGGMCLTPDGYSHILYHLKSLaQ 306
Cdd:PTZ00063 212 GVAQGKYYSVNVPLND-GIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAACVEFVRSL-N 289
                        170       180
                 ....*....|....*....|...
gi 193206283 307 GRMLVVLEGGYNhqISAVAvqRC 329
Cdd:PTZ00063 290 IPLLVLGGGGYT--IRNVA--RC 308
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
562-701 1.70e-16

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: 82.44  E-value: 1.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 562 HHASASKSSGFCIFNNVAVAAKYAQRRHKakRVLILDWDVHHGNGTQEIFYEDSNVMYMSIHRHdkGN-FYPigEPKDYS 640
Cdd:cd10005  132 HHAKKFEASGFCYVNDIVIAILELLKYHP--RVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKY--GNyFFP--GTGDMY 205
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193206283 641 DVGEGAGEGMSVNVPFSGvQMGDNEYQMAFQRVIMPIAYQFNPDLVLISAGFDAAVDDPLG 701
Cdd:cd10005  206 EVGAESGRYYSVNVPLKD-GIDDQSYLQLFKPVIQQVIDFYQPTCIVLQCGADSLGCDRLG 265
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
85-317 1.10e-15

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: 79.80  E-value: 1.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283  85 ESEKKTQEDINSQCEKYDSVFMTEfqnsmkvakdgvacvRDLTNRimaneasnGFAVVRPPGHHADSVSPCGFCLFNNVA 164
Cdd:cd09998   81 ESLDAIQGALGAVCEAVDSVFKPE---------------SPGTKR--------AFVAIRPPGHHCSESTPSGFCWVNNVH 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 165 QAAEEAFFS-GAERILIVDLDVHHGHGTQRI----------------FYDDK--------RVLYFSIH------------ 207
Cdd:cd09998  138 VGAAHAYLThGITRVVILDIDLHHGNGTQDIawrinaeankqalessSYDDFkpagapglRIFYSSLHdinsfpcedgdp 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 208 ----------RHEHGLF-WP-HL----PESDFDHIgsgkglgynanlalnetgcTDSDYLSIIFHVL--LPLATQFDPH- 268
Cdd:cd09998  218 akvkdasvsiDGAHGQWiWNvHLqpwtTEEDFWEL-------------------YYPKYRILFEKAAefLRLTTAATPFk 278
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 193206283 269 -FVIISAGFDALLGDpLGGMCL----TPDGYSH-----ILYHLKSLAQGRMLVVLEGGY 317
Cdd:cd09998  279 tLVFISAGFDASEHE-YESMQRhgvnVPTSFYYrfardAVRFADAHAHGRLISVLEGGY 336
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
147-329 1.24e-15

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: 79.75  E-value: 1.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 147 HHADSVSPCGFCLFNNVAQAAEEaFFSGAERILIVDLDVHHGHGTQRIFYDDKRVLYFSIHRHeHGLFWPHlpESDFDHI 226
Cdd:cd10005  132 HHAKKFEASGFCYVNDIVIAILE-LLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKY-GNYFFPG--TGDMYEV 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 227 GSGKGLGYNANLALNEtGCTDSDYLSIIFHVLLPLATQFDPHFVIISAGFDALLGDPLGGMCLTPDGYSHILYHLKSLAQ 306
Cdd:cd10005  208 GAESGRYYSVNVPLKD-GIDDQSYLQLFKPVIQQVIDFYQPTCIVLQCGADSLGCDRLGCFNLSIKGHGECVEFVKSFNI 286
                        170       180
                 ....*....|....*....|...
gi 193206283 307 gRMLVVLEGGYNhqISAVAvqRC 329
Cdd:cd10005  287 -PLLVLGGGGYT--VRNVA--RC 304
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
147-329 2.36e-15

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: 78.95  E-value: 2.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 147 HHADSVSPCGFCLFNNVAQAAEEaFFSGAERILIVDLDVHHGHGTQRIFYDDKRVLYFSihrhEHGLFWPHLPESDFDHI 226
Cdd:cd10011  133 HHAKKSEASGFCYVNDIVLAILE-LLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVS----FHKYGEYFPGTGDLRDI 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 227 GSGKGLGYNANLALNEtGCTDSDYLSIIFHVLLPLATQFDPHFVIISAGFDALLGDPLGGMCLTPDGYSHILYHLKSLaq 306
Cdd:cd10011  208 GAGKGKYYAVNFPMRD-GIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTF-- 284
                        170       180
                 ....*....|....*....|...
gi 193206283 307 gRMLVVLEGGYNHQISAVAvqRC 329
Cdd:cd10011  285 -NLPLLMLGGGGYTIRNVA--RC 304
PTZ00346 PTZ00346
histone deacetylase; Provisional
562-701 1.61e-12

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 70.83  E-value: 1.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 562 HHASASKSSGFCIFNNVAVAAKYAQRRHKakRVLILDWDVHHGNGTQEIFYEDSNVMYMSIHRHDKGNFYPIGEPKdysD 641
Cdd:PTZ00346 154 HHSKCGECSGFCYVNDIVLGILELLKCHD--RVLYVDIDMHHGDGVDEAFCTSDRVFTLSLHKFGESFFPGTGHPR---D 228
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193206283 642 VGEGAGEGMSVNVP-FSGVQmgDNEYQMAFQRVIMPIAYQFNPDLVLISAGFDAAVDDPLG 701
Cdd:PTZ00346 229 VGYGRGRYYSMNLAvWDGIT--DFYYLGLFEHALHSIVRRYSPDAIVLQCGADSLAGDRLG 287
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
526-750 1.29e-10

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: 62.01  E-value: 1.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 526 LKVARKAVGAVLQSVdeifeKDAgqRNALVIVrppGHHAsaskssgfcIFNNVAVAAKYAQrrhkaKRVLILDWDVHHGN 605
Cdd:cd09987    8 AEAHELLAGVVVAVL-----KDG--KVPVVLG---GDHS---------IANGAIRAVAELH-----PDLGVIDVDAHHDV 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 606 GTQEIFYE--------------DSNVMYMSIHRHDKGNFYPigepkdysdVGEGAGEGMSVNVPFSGVqmGDNEYQMAFQ 671
Cdd:cd09987   64 RTPEAFGKgnhhtprhllceplISDVHIVSIGIRGVSNGEA---------GGAYARKLGVVYFSMTEV--DKLGLGDVFE 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 672 RVIMPIayQFNPDLVLISAGFDA--AVDDP----LGEYKVTPETFALMTYQLSSLAGGRIITVLEGGYNLTSISNSAQAV 745
Cdd:cd09987  133 EIVSYL--GDKGDNVYLSVDVDGldPSFAPgtgtPGPGGLSYREGLYITERIAKTNLVVGLDIVEVNPLLDETGRTARLA 210

                 ....*
gi 193206283 746 CEVLQ 750
Cdd:cd09987  211 AALTL 215
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
877-925 4.06e-09

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 53.14  E-value: 4.06e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 193206283   877 CSECQIGAEVWTCLTCYKYNCGRFVNEHAMMHHLSSSHPMALSMADLSV 925
Cdd:smart00290   2 CSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
146-333 4.46e-05

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: 45.83  E-value: 4.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 146 GHHAdsvspcgfcLFNNVAQAAEEAFfsgaERILIVDLDVHHGHGTQRIFYD--------------DKRVLYFSIHRHEH 211
Cdd:cd09987   33 GDHS---------IANGAIRAVAELH----PDLGVIDVDAHHDVRTPEAFGKgnhhtprhllceplISDVHIVSIGIRGV 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206283 212 glfwphlpeSDFDHIGSGKGLGYNANLALneTGCTDSDYLSIIFHVLLPLatQFDPHFVIISAGFDALLGDPLGGM-CLT 290
Cdd:cd09987  100 ---------SNGEAGGAYARKLGVVYFSM--TEVDKLGLGDVFEEIVSYL--GDKGDNVYLSVDVDGLDPSFAPGTgTPG 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 193206283 291 PDG--YSHILYHLKSLAQGRMLVVLE-GGYN-----HQISAVAVQRCVRVL 333
Cdd:cd09987  167 PGGlsYREGLYITERIAKTNLVVGLDiVEVNplldeTGRTARLAAALTLEL 217
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
886-939 3.48e-04

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 44.23  E-value: 3.48e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 193206283 886 VWTCLTCYKYNCGRFVNEHAMMHHLSSSHPMALSMADLSVWCYPCDSYVHNPAL 939
Cdd:cd02669   28 VYACLVCGKYFQGRGKGSHAYTHSLEDNHHVFLNLETLKFYCLPDNYEIIDSSL 81
 
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.
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