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Conserved domains on  [gi|1387293808|ref|XP_024843695|]
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histone deacetylase 6 isoform X2 [Bos taurus]

Protein Classification

Graphical summary

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List of domain hits

 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 ...
 486-836 0e+00

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: 643.24  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  486 YDQQMMDHHNLWDNYHPEMPQRIHFIMHHLDELGLAKRCHSLPARPATDAELLTCHSAEHLERLRATEKMKTRELRREGA 565
Cdd:cd10003      1 YDQRMMNHHNLWDPGHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHLDEMKSLEKMKPRELNRLGK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  566 NYDSIYICSSTFACAQLAAGAACRLVEAVLAGEVLNGVAVVRPPGHHAEPDAACGFCFFNSVAVAARHAQAISGhALRIL 645
Cdd:cd10003     81 EYDSIYIHPDSYQCALLAAGCVLQVVEAVLTGESRNGVAIVRPPGHHAEQDTACGFCFFNNVAIAARYAQKKYG-LKRIL 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  646 IVDWDIHHGNGTQHIFEEDPSVLYISLHRYDHGTFFPMGNEGACTRIGKATGTGFTVNVAWNGPRMGDADYLAAWHRLVL 725
Cdd:cd10003    160 IVDWDVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSPEGNYDVVGKGKGEGFNVNIPWNKGGMGDAEYIAAFQQVVL 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  726 PVAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHQLMGLANGHIILILEGGYNLTSISESMAACTRSLLGDPLP 805
Cdd:cd10003    240 PIAYEFNPELVLVSAGFDAARGDPLGGCKVTPEGYAHMTHMLMSLAGGRVIVILEGGYNLTSISESMSMCTKTLLGDPPP 319

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1387293808  806 LLTRLRPPLSGAQASITKTIQVHRRYWRSLR 836
Cdd:cd10003    320 VLDLPRPPCSSALKSINNVLQVHQKYWKSLR 350
Arginase_HDAC super family cl17011
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 99-435 0e+00

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 cd11682:

Pssm-ID: 450134 [Multi-domain]  Cd Length: 337  Bit Score: 641.90  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808   99 CLWDDSFPERPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEEELHVLADTYDSVYLHP 178
Cdd:cd11682      1 CLWDESFPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYVALMKSTQYMTEEELRTLADTYDSVYLHP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  179 NSYTCACLASGSVLRLVDAVLEAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHDIQRVLIVDWDVHHGQ 258
Cdd:cd11682     81 NSYSCACLAVGSVLQLVDKVLGGEIRNGLAIVRPPGHHAQHDKMDGYCMFNNVAIAARYAQQKHGVQRVLIVDWDVHHGQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  259 GIQFAFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGLGQGQGYTINVPWNQVGMQDADYIAAFLHVLLPVAFEFQPQL 338
Cdd:cd11682    161 GTQFIFEQDPSVLYFSIHRYEQGRFWPHLKESDSSAVGFGRGEGYNINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQL 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  339 VLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAEGKLILSLEGGYNLHSLAEGVSATLHTLLGDPCPVLESPGAPCP 418
Cdd:cd11682    241 VLVAAGFDAVIGDPKGEMAATPACFAHLTHLLMGLAGGKLILSLEGGYNLRSLAEGVCASLKALLGDPCPMLESPGAPCR 320

                          330
                   ....*....|....*..
gi 1387293808  419 SAQASLSCTLEALEPFW 435
Cdd:cd11682    321 SALASVSCTISALEPFW 337
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
1047-1109 1.26e-23

Zn-finger in ubiquitin-hydrolases and other protein;


:

Pssm-ID: 460464  Cd Length: 63  Bit Score: 95.02  E-value: 1.26e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387293808 1047 CQDCGTLQENWVCLSCYQVYCGRYINAHMLQHHEGSGHPLVLSYADLSAWCYHCQAYVHHKDL 1109
Cdd:pfam02148    1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPSL 63
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
 865-989 4.58e-03

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd06917:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 277  Bit Score: 40.15  E-value: 4.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  865 ANVTTTVEGNILETGMGQAAS--EASVKESTPDQTESATAPVELTQGQSSDTATQGAALDQTISEGATGGAELIQNPPAS 942
Cdd:cd06917    130 ANILVTNTGNVKLCDFGVAASlnQNSSKRSTFVGTPYWMAPEVITEGKYYDTKADIWSLGITTYEMATGNPPYSDVDALR 209

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1387293808  943 C---INNRIPPALPVQGAtaqtspSKLMANLRILDLDSTTQEPSEEEGLL 989
Cdd:cd06917    210 AvmlIPKSKPPRLEGNGY------SPLLKEFVAACLDEEPKDRLSADELL 253
 
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 ...
 486-836 0e+00

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: 643.24  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  486 YDQQMMDHHNLWDNYHPEMPQRIHFIMHHLDELGLAKRCHSLPARPATDAELLTCHSAEHLERLRATEKMKTRELRREGA 565
Cdd:cd10003      1 YDQRMMNHHNLWDPGHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHLDEMKSLEKMKPRELNRLGK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  566 NYDSIYICSSTFACAQLAAGAACRLVEAVLAGEVLNGVAVVRPPGHHAEPDAACGFCFFNSVAVAARHAQAISGhALRIL 645
Cdd:cd10003     81 EYDSIYIHPDSYQCALLAAGCVLQVVEAVLTGESRNGVAIVRPPGHHAEQDTACGFCFFNNVAIAARYAQKKYG-LKRIL 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  646 IVDWDIHHGNGTQHIFEEDPSVLYISLHRYDHGTFFPMGNEGACTRIGKATGTGFTVNVAWNGPRMGDADYLAAWHRLVL 725
Cdd:cd10003    160 IVDWDVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSPEGNYDVVGKGKGEGFNVNIPWNKGGMGDAEYIAAFQQVVL 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  726 PVAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHQLMGLANGHIILILEGGYNLTSISESMAACTRSLLGDPLP 805
Cdd:cd10003    240 PIAYEFNPELVLVSAGFDAARGDPLGGCKVTPEGYAHMTHMLMSLAGGRVIVILEGGYNLTSISESMSMCTKTLLGDPPP 319

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1387293808  806 LLTRLRPPLSGAQASITKTIQVHRRYWRSLR 836
Cdd:cd10003    320 VLDLPRPPCSSALKSINNVLQVHQKYWKSLR 350
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
 99-435 0e+00

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: 641.90  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808   99 CLWDDSFPERPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEEELHVLADTYDSVYLHP 178
Cdd:cd11682      1 CLWDESFPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYVALMKSTQYMTEEELRTLADTYDSVYLHP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  179 NSYTCACLASGSVLRLVDAVLEAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHDIQRVLIVDWDVHHGQ 258
Cdd:cd11682     81 NSYSCACLAVGSVLQLVDKVLGGEIRNGLAIVRPPGHHAQHDKMDGYCMFNNVAIAARYAQQKHGVQRVLIVDWDVHHGQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  259 GIQFAFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGLGQGQGYTINVPWNQVGMQDADYIAAFLHVLLPVAFEFQPQL 338
Cdd:cd11682    161 GTQFIFEQDPSVLYFSIHRYEQGRFWPHLKESDSSAVGFGRGEGYNINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQL 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  339 VLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAEGKLILSLEGGYNLHSLAEGVSATLHTLLGDPCPVLESPGAPCP 418
Cdd:cd11682    241 VLVAAGFDAVIGDPKGEMAATPACFAHLTHLLMGLAGGKLILSLEGGYNLRSLAEGVCASLKALLGDPCPMLESPGAPCR 320

                          330
                   ....*....|....*..
gi 1387293808  419 SAQASLSCTLEALEPFW 435
Cdd:cd11682    321 SALASVSCTISALEPFW 337
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 501-799 5.91e-121

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: 374.27  E-value: 5.91e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  501 HPEMPQRIHFIMHHLDELGLAKRCHSLPARPATDAELLTCHSAEHLERLR-ATEKMKTRELRREGANYDSIYICSSTFAC 579
Cdd:pfam00850    1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEeAAPEGGALLLLSYLSGDDDTPVSPGSYEA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  580 AQLAAGAACRLVEAVLAGEVLNGVAVVRPPGHHAEPDAACGFCFFNSVAVAARHAQAISGHAlRILIVDWDIHHGNGTQH 659
Cdd:pfam00850   81 ALLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLK-RVAIVDFDVHHGNGTQE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  660 IFEEDPSVLYISLHRYdHGTFFPMgnEGACTRIGKATGTGFTVNVAWNgPRMGDADYLAAWHRLVLPVAYEFNPELVLVS 739
Cdd:pfam00850  160 IFYDDPSVLTLSIHQY-PGGFYPG--TGFADETGEGKGKGYTLNVPLP-PGTGDAEYLAAFEEILLPALEEFQPDLILVS 235

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387293808  740 AGFDAARGDPLGGCQVSPEGYAHLTHQLMGLANGH---IILILEGGYNLTSISESMAACTRSL 799
Cdd:pfam00850  236 AGFDAHAGDPLGGLNLTTEGFAEITRILLELADPLcirVVSVLEGGYNLDALARSATAVLAAL 298
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 106-402 7.71e-112

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: 350.00  E-value: 7.71e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  106 PERPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYID-LMETTQYMNEEELHVLADTYDSVYLHPNSYTCA 184
Cdd:pfam00850    2 PENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEfLEEAAPEGGALLLLSYLSGDDDTPVSPGSYEAA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  185 CLASGSVLRLVDAVLEAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHDIQRVLIVDWDVHHGQGIQFAF 264
Cdd:pfam00850   82 LLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLKRVAIVDFDVHHGNGTQEIF 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  265 DQDPSVLYFSIHRYEqGRFWPHLkaSNWSTTGLGQGQGYTINVPWNqVGMQDADYIAAFLHVLLPVAFEFQPQLVLVAAG 344
Cdd:pfam00850  162 YDDPSVLTLSIHQYP-GGFYPGT--GFADETGEGKGKGYTLNVPLP-PGTGDAEYLAAFEEILLPALEEFQPDLILVSAG 237

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387293808  345 FDALQGDPKGEMAATPAGFAQLTHLLMGLAE---GKLILSLEGGYNLHSLAEGVSATLHTL 402
Cdd:pfam00850  238 FDAHAGDPLGGLNLTTEGFAEITRILLELADplcIRVVSVLEGGYNLDALARSATAVLAAL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 86-404 3.42e-98

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 313.97  E-value: 3.42e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808   86 TGLVFDEQLNEfHCLWDDSfPERPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYmnEEELH 165
Cdd:COG0123      1 TALIYHPDYLL-HDLGPGH-PEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAASL--DGGYG 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  166 VL-ADTYdsvyLHPNSYTCACLASGSVLRLVDAVLEAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAqQKHDI 244
Cdd:COG0123     77 QLdPDTP----VSPGTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGFCLFNNAAIAARYL-LAKGL 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  245 QRVLIVDWDVHHGQGIQFAFDQDPSVLYFSIHryeQGRFWPHLKASnwSTTGLGQGQGYTINVPwnqV--GMQDADYIAA 322
Cdd:COG0123    152 ERVAIVDFDVHHGNGTQDIFYDDPDVLTISIH---QDPLYPGTGAA--DETGEGAGEGSNLNVP---LppGTGDAEYLAA 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  323 FLHVLLPVAFEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAE---GKLILSLEGGYNLHSLAEGVSATL 399
Cdd:COG0123    224 LEEALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELADhcgGPVVSVLEGGYNLDALARSVAAHL 303


                   ....*
gi 1387293808  400 HTLLG 404
Cdd:COG0123    304 ETLLG 308
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 482-801 7.20e-97

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 310.12  E-value: 7.20e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  482 TGLVYDQQMMDHHnlWDNYHPEMPQRIHFIMHHLDELGLAKRCHSLPARPATDAELLTCHSAEHLERLRATEkmktreLR 561
Cdd:COG0123      1 TALIYHPDYLLHD--LGPGHPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAAS------LD 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  562 REGANYDSI-YICSSTFACAQLAAGAACRLVEAVLAGEVLNGVAVVRPPGHHAEPDAACGFCFFNSVAVAARHAQAisGH 640
Cdd:COG0123     73 GGYGQLDPDtPVSPGTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGFCLFNNAAIAARYLLA--KG 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  641 ALRILIVDWDIHHGNGTQHIFEEDPSVLYISLHRYDhgtFFPMgnEGACTRIGKATGTGFTVNVAWnGPRMGDADYLAAW 720
Cdd:COG0123    151 LERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQDP---LYPG--TGAADETGEGAGEGSNLNVPL-PPGTGDAEYLAAL 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  721 HRLVLPVAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHQLMGLA---NGHIILILEGGYNLTSISESMAACTR 797
Cdd:COG0123    225 EEALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELAdhcGGPVVSVLEGGYNLDALARSVAAHLE 304


                   ....
gi 1387293808  798 SLLG 801
Cdd:COG0123    305 TLLG 308
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
1047-1109 1.26e-23

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 95.02  E-value: 1.26e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387293808 1047 CQDCGTLQENWVCLSCYQVYCGRYINAHMLQHHEGSGHPLVLSYADLSAWCYHCQAYVHHKDL 1109
Cdd:pfam02148    1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPSL 63
PTZ00063 PTZ00063
histone deacetylase; Provisional
 611-801 3.15e-16

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 82.55  E-value: 3.15e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  611 HHAEPDAACGFCFFNSVAVAArhAQAISGHAlRILIVDWDIHHGNGTQHIFEEDPSVLYISLHRYdhGTFFPmgNEGACT 690
Cdd:PTZ00063   137 HHAKRSEASGFCYINDIVLGI--LELLKYHA-RVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFP--GTGDVT 209

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  691 RIGKATGTGFTVNVAWNGPrMGDADYLAAWHRLVLPVAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHQLMGL 770
Cdd:PTZ00063   210 DIGVAQGKYYSVNVPLNDG-IDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAACVEFVRSL 288

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1387293808  771 aNGHIILILEGGYNLTSISESMAACTRSLLG 801
Cdd:PTZ00063   289 -NIPLLVLGGGGYTIRNVARCWAYETGVILN 318
PTZ00063 PTZ00063
histone deacetylase; Provisional
 215-409 3.86e-16

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 82.17  E-value: 3.86e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  215 HHAQHSLMDGYCMFNHVAVAARYAQQKHdiQRVLIVDWDVHHGQGIQFAFDQDPSVLYFSIHRYeqGRFWPhlKASNWST 294
Cdd:PTZ00063   137 HHAKRSEASGFCYINDIVLGILELLKYH--ARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFP--GTGDVTD 210

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  295 TGLGQGQGYTINVPWNQvGMQDADYIAAFLHVLLPVAFEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLA 374
Cdd:PTZ00063   211 IGVAQGKYYSVNVPLND-GIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAACVEFVRSLN 289

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1387293808  375 EGKLILSlEGGYNLHSLAE------GVSATLHTLLGDPCPV 409
Cdd:PTZ00063   290 IPLLVLG-GGGYTIRNVARcwayetGVILNKHDEMSDQISL 329
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
1046-1094 1.43e-15

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 71.63  E-value: 1.43e-15
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 1387293808  1046 PCQDCGTLQENWVCLSCYQVYCGRYINAHMLQHHEGSGHPLVLSYADLS 1094
Cdd:smart00290    1 RCSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLGTQR 49
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
 865-989 4.58e-03

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 40.15  E-value: 4.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  865 ANVTTTVEGNILETGMGQAAS--EASVKESTPDQTESATAPVELTQGQSSDTATQGAALDQTISEGATGGAELIQNPPAS 942
Cdd:cd06917    130 ANILVTNTGNVKLCDFGVAASlnQNSSKRSTFVGTPYWMAPEVITEGKYYDTKADIWSLGITTYEMATGNPPYSDVDALR 209

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1387293808  943 C---INNRIPPALPVQGAtaqtspSKLMANLRILDLDSTTQEPSEEEGLL 989
Cdd:cd06917    210 AvmlIPKSKPPRLEGNGY------SPLLKEFVAACLDEEPKDRLSADELL 253
 
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 ...
 486-836 0e+00

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: 643.24  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  486 YDQQMMDHHNLWDNYHPEMPQRIHFIMHHLDELGLAKRCHSLPARPATDAELLTCHSAEHLERLRATEKMKTRELRREGA 565
Cdd:cd10003      1 YDQRMMNHHNLWDPGHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHLDEMKSLEKMKPRELNRLGK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  566 NYDSIYICSSTFACAQLAAGAACRLVEAVLAGEVLNGVAVVRPPGHHAEPDAACGFCFFNSVAVAARHAQAISGhALRIL 645
Cdd:cd10003     81 EYDSIYIHPDSYQCALLAAGCVLQVVEAVLTGESRNGVAIVRPPGHHAEQDTACGFCFFNNVAIAARYAQKKYG-LKRIL 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  646 IVDWDIHHGNGTQHIFEEDPSVLYISLHRYDHGTFFPMGNEGACTRIGKATGTGFTVNVAWNGPRMGDADYLAAWHRLVL 725
Cdd:cd10003    160 IVDWDVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSPEGNYDVVGKGKGEGFNVNIPWNKGGMGDAEYIAAFQQVVL 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  726 PVAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHQLMGLANGHIILILEGGYNLTSISESMAACTRSLLGDPLP 805
Cdd:cd10003    240 PIAYEFNPELVLVSAGFDAARGDPLGGCKVTPEGYAHMTHMLMSLAGGRVIVILEGGYNLTSISESMSMCTKTLLGDPPP 319

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1387293808  806 LLTRLRPPLSGAQASITKTIQVHRRYWRSLR 836
Cdd:cd10003    320 VLDLPRPPCSSALKSINNVLQVHQKYWKSLR 350
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
 99-435 0e+00

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: 641.90  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808   99 CLWDDSFPERPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEEELHVLADTYDSVYLHP 178
Cdd:cd11682      1 CLWDESFPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYVALMKSTQYMTEEELRTLADTYDSVYLHP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  179 NSYTCACLASGSVLRLVDAVLEAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHDIQRVLIVDWDVHHGQ 258
Cdd:cd11682     81 NSYSCACLAVGSVLQLVDKVLGGEIRNGLAIVRPPGHHAQHDKMDGYCMFNNVAIAARYAQQKHGVQRVLIVDWDVHHGQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  259 GIQFAFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGLGQGQGYTINVPWNQVGMQDADYIAAFLHVLLPVAFEFQPQL 338
Cdd:cd11682    161 GTQFIFEQDPSVLYFSIHRYEQGRFWPHLKESDSSAVGFGRGEGYNINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQL 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  339 VLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAEGKLILSLEGGYNLHSLAEGVSATLHTLLGDPCPVLESPGAPCP 418
Cdd:cd11682    241 VLVAAGFDAVIGDPKGEMAATPACFAHLTHLLMGLAGGKLILSLEGGYNLRSLAEGVCASLKALLGDPCPMLESPGAPCR 320

                          330
                   ....*....|....*..
gi 1387293808  419 SAQASLSCTLEALEPFW 435
Cdd:cd11682    321 SALASVSCTISALEPFW 337
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 99-435 0e+00

Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are class IIb Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. HDACs usually act via association with DNA binding proteins to target specific chromatin regions. HDAC6 is the only histone deacetylase with internal duplication of two catalytic domains which appear to function independently of each other, and also has a C-terminal ubiquitin-binding domain. It is located in the cytoplasm and associates with microtubule motor complex, functioning as the tubulin deacetylase and regulating microtubule-dependent cell motility. HDAC10 has an N-terminal deacetylase domain and a C-terminal pseudo-repeat that shares significant similarity with its catalytic domain. It is located in the nucleus and cytoplasm, and is involved in regulation of melanogenesis. It transcriptionally down-regulates thioredoxin-interacting protein (TXNIP), leading to altered reactive oxygen species (ROS) signaling in human gastric cancer cells. Known interaction partners of HDAC6 are alpha tubulin (substrate) and ubiquitin-like modifier FAT10 (also known as Ubiquitin D or UBD) while interaction partners of HDAC10 are Pax3, KAP1, hsc70 and HDAC3 proteins.


Pssm-ID: 212526 [Multi-domain]  Cd Length: 336  Bit Score: 563.86  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808   99 CLWDDSFPERPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEEELHVLADTYDSVYLHP 178
Cdd:cd10002      1 CNWDSNHIECPERLEAILERLTQDGLLERCVKIPAREAEEDEILLVHSQEYIDLVKSTETMEKEELESLCSGYDSVYLCP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  179 NSYTCACLASGSVLRLVDAVLEAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHDIQRVLIVDWDVHHGQ 258
Cdd:cd10002     81 STYEAARLAAGSTIELVKAVMAGKIQNGFALIRPPGHHAMRNEANGYCIFNNVAIAAKYAIEKLGLKRILIVDWDVHHGQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  259 GIQFAFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGLGQGQGYTINVPWNQVGMQDADYIAAFLHVLLPVAFEFQPQL 338
Cdd:cd10002    161 GTQQGFYEDPRVLYFSIHRYEHGRFWPHLFESDYDYIGVGHGYGFNVNVPLNQTGLGDADYLAIFHHILLPLALEFQPEL 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  339 VLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAEGKLILSLEGGYNLHSLAEGVSATLHTLLGDPCPVLEsPGAPCP 418
Cdd:cd10002    241 VLVSAGFDASIGDPEGEMAVTPAGYAHLTRLLMGLAGGKLLLVLEGGYLLESLAESVSMTLRGLLGDPLPPLA-PPIPIR 319

                          330
                   ....*....|....*..
gi 1387293808  419 SAQASLSCTLEALEPFW 435
Cdd:cd10002    320 SVLETILNAIAHLSPRW 336
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
 90-438 5.57e-168

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: 499.17  E-value: 5.57e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808   90 FDEQLNEFHCLWDDSFPERPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEEELHVLAD 169
Cdd:cd10003      1 YDQRMMNHHNLWDPGHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHLDEMKSLEKMKPRELNRLGK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  170 TYDSVYLHPNSYTCACLASGSVLRLVDAVLEAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHDIQRVLI 249
Cdd:cd10003     81 EYDSIYIHPDSYQCALLAAGCVLQVVEAVLTGESRNGVAIVRPPGHHAEQDTACGFCFFNNVAIAARYAQKKYGLKRILI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  250 VDWDVHHGQGIQFAFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGLGQGQGYTINVPWNQVGMQDADYIAAFLHVLLP 329
Cdd:cd10003    161 VDWDVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSPEGNYDVVGKGKGEGFNVNIPWNKGGMGDAEYIAAFQQVVLP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  330 VAFEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAEGKLILSLEGGYNLHSLAEGVSATLHTLLGDPCPV 409
Cdd:cd10003    241 IAYEFNPELVLVSAGFDAARGDPLGGCKVTPEGYAHMTHMLMSLAGGRVIVILEGGYNLTSISESMSMCTKTLLGDPPPV 320

                          330       340
                   ....*....|....*....|....*....
gi 1387293808  410 LESPGAPCPSAQASLSCTLEALEPFWESL 438
Cdd:cd10003    321 LDLPRPPCSSALKSINNVLQVHQKYWKSL 349
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 101-435 3.01e-150

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: 452.39  E-value: 3.01e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  101 WDDSF--PERPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEEELHVLADTYDSVYLHP 178
Cdd:cd11683      1 WDDPEceIEVPERLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRETQVMNKEELMAISGKYDAVYFHP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  179 NSYTCACLASGSVLRLVDAVLEAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHDIQRVLIVDWDVHHGQ 258
Cdd:cd11683     81 NTFHCARLAAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYAKKKYGLHRILIVDWDVHHGQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  259 GIQFAFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGLGQGQGYTINVPWNQVGMQDADYIAAFLHVLLPVAFEFQPQL 338
Cdd:cd11683    161 GIQYIFEEDPSVLYFSWHRYEHQRFWPFLRESDYDAVGRGKGLGFNINLPWNKVGMGNADYLAAFFHVLLPLAFEFDPEL 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  339 VLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAEGKLILSLEGGYNLHSLAEGVSATLHTLLGDPCPVLESPGAPCP 418
Cdd:cd11683    241 VLVSAGFDSAIGDPEGQMCATPECFAHLTHLLMVLAGGKLCAVLEGGYHLESLAESVCMTVQTLLGDPLPRLSGEMTPCQ 320

                          330
                   ....*....|....*..
gi 1387293808  419 SAQASLSCTLEALEPFW 435
Cdd:cd11683    321 SALESIQNVRAAQAPYW 337
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 501-807 6.08e-140

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: 424.45  E-value: 6.08e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  501 HPEMPQRIHFIMHHLDELGLAKRCHSLPARPATDAELLTCHSAEHLERLRATEKMKTRELRREGA--NYDSIYICSSTFA 578
Cdd:cd11600      3 HPEDPSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEHWDRVEATEKMSDEQLKDRTEifERDSLYVNNDTAF 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  579 CAQLAAGAACRLVEAVLAGEVLNGVAVVRPPGHHAEPDAACGFCFFNSVAVAARHAQAI-SGHALRILIVDWDIHHGNGT 657
Cdd:cd11600     83 CARLSCGGAIEACRAVAEGRVKNAFAVVRPPGHHAEPDESMGFCFFNNVAVAAKWLQTEyPDKIKKILILDWDIHHGNGT 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  658 QHIFEEDPSVLYISLHRYDHGTFFPMGNEGACTRIGKATGTGFTVNVAWNGPRMGDADYLAAWHRLVLPVAYEFNPELVL 737
Cdd:cd11600    163 QRAFYDDPNVLYISLHRFENGGFYPGTPYGDYESVGEGAGLGFNVNIPWPQGGMGDADYIYAFQRIVMPIAYEFDPDLVI 242

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  738 VSAGFDAARGDPLGGCQVSPEGYAHLTHQLMGLANGHIILILEGGYNLTSISESMAACTRSLLGDPLPLL 807
Cdd:cd11600    243 ISAGFDAADGDELGQCHVTPAGYAHMTHMLMSLAGGKLVVALEGGYNLDAISDSALAVAKVLLGEAPPKL 312
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 495-832 1.70e-135

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: 414.01  E-value: 1.70e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  495 NLWDNYHPEMPQRIHFIMHHLDELGLAKRCHSLPARPATDAELLTCHSAEHLERLRATEKMKTRELRREGANYDSIYICS 574
Cdd:cd10002      1 CNWDSNHIECPERLEAILERLTQDGLLERCVKIPAREAEEDEILLVHSQEYIDLVKSTETMEKEELESLCSGYDSVYLCP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  575 STFACAQLAAGAACRLVEAVLAGEVLNGVAVVRPPGHHAEPDAACGFCFFNSVAVAARHAQAiSGHALRILIVDWDIHHG 654
Cdd:cd10002     81 STYEAARLAAGSTIELVKAVMAGKIQNGFALIRPPGHHAMRNEANGYCIFNNVAIAAKYAIE-KLGLKRILIVDWDVHHG 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  655 NGTQHIFEEDPSVLYISLHRYDHGTFFPMGNEGACTRIGKATGTGFTVNVAWNGPRMGDADYLAAWHRLVLPVAYEFNPE 734
Cdd:cd10002    160 QGTQQGFYEDPRVLYFSIHRYEHGRFWPHLFESDYDYIGVGHGYGFNVNVPLNQTGLGDADYLAIFHHILLPLALEFQPE 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  735 LVLVSAGFDAARGDPLGGCQVSPEGYAHLTHQLMGLANGHIILILEGGYNLTSISESMAACTRSLLGDPLPLLTRLRpPL 814
Cdd:cd10002    240 LVLVSAGFDASIGDPEGEMAVTPAGYAHLTRLLMGLAGGKLLLVLEGGYLLESLAESVSMTLRGLLGDPLPPLAPPI-PI 318

                          330
                   ....*....|....*...
gi 1387293808  815 SGAQASITKTIQVHRRYW 832
Cdd:cd10002    319 RSVLETILNAIAHLSPRW 336
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
 106-403 2.76e-131

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


Pssm-ID: 212518 [Multi-domain]  Cd Length: 291  Bit Score: 401.11  E-value: 2.76e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  106 PERPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEEELHvlADTYdsvyLHPNSYTCAC 185
Cdd:cd09992      2 PERPERLLAILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYIERVEETCEAGGGYLD--PDTY----VSPGSYEAAL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  186 LASGSVLRLVDAVLEAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHDIQRVLIVDWDVHHGQGIQFAFD 265
Cdd:cd09992     76 LAAGAALAAVDAVLSGEAENAFALVRPPGHHAEPDRAMGFCLFNNVAIAARYAQKRYGLKRVLIVDWDVHHGNGTQDIFY 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  266 QDPSVLYFSIHRYEqgrFWPHLKASNWstTGLGQGQGYTINVPWNQvGMQDADYIAAFLHVLLPVAFEFQPQLVLVAAGF 345
Cdd:cd09992    156 DDPSVLYFSIHQYP---FYPGTGAAEE--TGGGAGEGFTINVPLPP-GSGDAEYLAAFEEVLLPIAREFQPDLVLVSAGF 229

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387293808  346 DALQGDPKGEMAATPAGFAQLTHLLMGLAE----GKLILSLEGGYNLHSLAEGVSATLHTLL 403
Cdd:cd09992    230 DAHRGDPLGGMNLTPEGYARLTRLLKELADehcgGRLVFVLEGGYNLEALAESVLAVLEALL 291
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
 501-800 4.96e-129

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: 394.94  E-value: 4.96e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  501 HPEMPQRIHFIMHHLDELGLAKRCHSLPARPATDAELLTCHSAEHLERLRATEKMKTRELrreganYDSIYICSSTFACA 580
Cdd:cd09992      1 HPERPERLLAILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYIERVEETCEAGGGYL------DPDTYVSPGSYEAA 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  581 QLAAGAACRLVEAVLAGEVLNGVAVVRPPGHHAEPDAACGFCFFNSVAVAARHAQAISGHAlRILIVDWDIHHGNGTQHI 660
Cdd:cd09992     75 LLAAGAALAAVDAVLSGEAENAFALVRPPGHHAEPDRAMGFCLFNNVAIAARYAQKRYGLK-RVLIVDWDVHHGNGTQDI 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  661 FEEDPSVLYISLHRYDhgtFFPMGneGACTRIGKATGTGFTVNVAWNgPRMGDADYLAAWHRLVLPVAYEFNPELVLVSA 740
Cdd:cd09992    154 FYDDPSVLYFSIHQYP---FYPGT--GAAEETGGGAGEGFTINVPLP-PGSGDAEYLAAFEEVLLPIAREFQPDLVLVSA 227

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387293808  741 GFDAARGDPLGGCQVSPEGYAHLTHQLMGLA----NGHIILILEGGYNLTSISESMAACTRSLL 800
Cdd:cd09992    228 GFDAHRGDPLGGMNLTPEGYARLTRLLKELAdehcGGRLVFVLEGGYNLEALAESVLAVLEALL 291
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 482-832 1.89e-128

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: 397.10  E-value: 1.89e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  482 TGLVYDQQMMDHHNLW--DNYHPEMPQRIHFIMHHLDELGLAKRCHSLPARPATDAELLTCHSAEH--------LERLRA 551
Cdd:cd11681      3 TGLAYDPLMLKHQCICgnNSSHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHtllygtnpLSRLKL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  552 TEKMKTRELRRE---------GANYDSIYICSSTFACAQLAAGAACRLVEAVLAGEVLNGVAVVRPPGHHAEPDAACGFC 622
Cdd:cd11681     83 DPTKLAGLPQKSfvrlpcggiGVDSDTVWNELHTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQAMGFC 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  623 FFNSVAVAARHAQAISGHAlRILIVDWDIHHGNGTQHIFEEDPSVLYISLHRYDHGTFFPmgNEGACTRIGKATGTGFTV 702
Cdd:cd11681    163 FFNSVAIAAKQLQQKLKLR-KILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFP--GTGAPTEVGSGAGEGFNV 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  703 NVAWNG---PRMGDADYLAAWHRLVLPVAYEFNPELVLVSAGFDAARGDP--LGGCQVSPEGYAHLTHQLMGLANGHIIL 777
Cdd:cd11681    240 NIAWSGgldPPMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPppLGGYKVSPACFGYMTRQLMNLAGGKVVL 319

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1387293808  778 ILEGGYNLTSISESMAACTRSLLGD---PLPLLTRLRPPLSGAQASITKTIQVHRRYW 832
Cdd:cd11681    320 ALEGGYDLTAICDASEACVRALLGDeldPLSEEELERRPNPNAVTSLEKVIAIQSPYW 377
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 103-410 2.80e-122

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: 378.23  E-value: 2.80e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  103 DSFPERPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEEELHVLAD--TYDSVYLHPNS 180
Cdd:cd11600      1 DPHPEDPSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEHWDRVEATEKMSDEQLKDRTEifERDSLYVNNDT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  181 YTCACLASGSVLRLVDAVLEAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKH--DIQRVLIVDWDVHHGQ 258
Cdd:cd11600     81 AFCARLSCGGAIEACRAVAEGRVKNAFAVVRPPGHHAEPDESMGFCFFNNVAVAAKWLQTEYpdKIKKILILDWDIHHGN 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  259 GIQFAFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGLGQGQGYTINVPWNQVGMQDADYIAAFLHVLLPVAFEFQPQL 338
Cdd:cd11600    161 GTQRAFYDDPNVLYISLHRFENGGFYPGTPYGDYESVGEGAGLGFNVNIPWPQGGMGDADYIYAFQRIVMPIAYEFDPDL 240

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387293808  339 VLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAEGKLILSLEGGYNLHSLAEGVSATLHTLLGDPCPVL 410
Cdd:cd11600    241 VIISAGFDAADGDELGQCHVTPAGYAHMTHMLMSLAGGKLVVALEGGYNLDAISDSALAVAKVLLGEAPPKL 312
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
 496-832 2.97e-122

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: 379.20  E-value: 2.97e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  496 LWDNYHPEMPQRIHFIMHHLDELGLAKRCHSLPARPATDAELLTCHSAEHLERLRATEKMKTRELRREGANYDSIYICSS 575
Cdd:cd11682      2 LWDESFPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYVALMKSTQYMTEEELRTLADTYDSVYLHPN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  576 TFACAQLAAGAACRLVEAVLAGEVLNGVAVVRPPGHHAEPDAACGFCFFNSVAVAARHAQAISGhALRILIVDWDIHHGN 655
Cdd:cd11682     82 SYSCACLAVGSVLQLVDKVLGGEIRNGLAIVRPPGHHAQHDKMDGYCMFNNVAIAARYAQQKHG-VQRVLIVDWDVHHGQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  656 GTQHIFEEDPSVLYISLHRYDHGTFFPMGNEGACTRIGKATGTGFTVNVAWNGPRMGDADYLAAWHRLVLPVAYEFNPEL 735
Cdd:cd11682    161 GTQFIFEQDPSVLYFSIHRYEQGRFWPHLKESDSSAVGFGRGEGYNINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQL 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  736 VLVSAGFDAARGDPLGGCQVSPEGYAHLTHQLMGLANGHIILILEGGYNLTSISESMAACTRSLLGDPLPLLTRLRPPLS 815
Cdd:cd11682    241 VLVAAGFDAVIGDPKGEMAATPACFAHLTHLLMGLAGGKLILSLEGGYNLRSLAEGVCASLKALLGDPCPMLESPGAPCR 320

                          330
                   ....*....|....*..
gi 1387293808  816 GAQASITKTIQVHRRYW 832
Cdd:cd11682    321 SALASVSCTISALEPFW 337
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 501-799 5.91e-121

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: 374.27  E-value: 5.91e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  501 HPEMPQRIHFIMHHLDELGLAKRCHSLPARPATDAELLTCHSAEHLERLR-ATEKMKTRELRREGANYDSIYICSSTFAC 579
Cdd:pfam00850    1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEeAAPEGGALLLLSYLSGDDDTPVSPGSYEA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  580 AQLAAGAACRLVEAVLAGEVLNGVAVVRPPGHHAEPDAACGFCFFNSVAVAARHAQAISGHAlRILIVDWDIHHGNGTQH 659
Cdd:pfam00850   81 ALLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLK-RVAIVDFDVHHGNGTQE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  660 IFEEDPSVLYISLHRYdHGTFFPMgnEGACTRIGKATGTGFTVNVAWNgPRMGDADYLAAWHRLVLPVAYEFNPELVLVS 739
Cdd:pfam00850  160 IFYDDPSVLTLSIHQY-PGGFYPG--TGFADETGEGKGKGYTLNVPLP-PGTGDAEYLAAFEEILLPALEEFQPDLILVS 235

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387293808  740 AGFDAARGDPLGGCQVSPEGYAHLTHQLMGLANGH---IILILEGGYNLTSISESMAACTRSL 799
Cdd:pfam00850  236 AGFDAHAGDPLGGLNLTTEGFAEITRILLELADPLcirVVSVLEGGYNLDALARSATAVLAAL 298
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 503-832 1.50e-113

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: 356.09  E-value: 1.50e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  503 EMPQRIHFIMHHLDELGLAKRCHSLPARPATDAELLTCHSAEHLERLRATEKMKTRELRREGANYDSIYICSSTFACAQL 582
Cdd:cd11683      9 EVPERLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRETQVMNKEELMAISGKYDAVYFHPNTFHCARL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  583 AAGAACRLVEAVLAGEVLNGVAVVRPPGHHAEPDAACGFCFFNSVAVAARHAQaiSGHAL-RILIVDWDIHHGNGTQHIF 661
Cdd:cd11683     89 AAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYAK--KKYGLhRILIVDWDVHHGQGIQYIF 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  662 EEDPSVLYISLHRYDHGTFFPMGNEGACTRIGKATGTGFTVNVAWNGPRMGDADYLAAWHRLVLPVAYEFNPELVLVSAG 741
Cdd:cd11683    167 EEDPSVLYFSWHRYEHQRFWPFLRESDYDAVGRGKGLGFNINLPWNKVGMGNADYLAAFFHVLLPLAFEFDPELVLVSAG 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  742 FDAARGDPLGGCQVSPEGYAHLTHQLMGLANGHIILILEGGYNLTSISESMAACTRSLLGDPLPLLTRLRPPLSGAQASI 821
Cdd:cd11683    247 FDSAIGDPEGQMCATPECFAHLTHLLMVLAGGKLCAVLEGGYHLESLAESVCMTVQTLLGDPLPRLSGEMTPCQSALESI 326

                          330
                   ....*....|.
gi 1387293808  822 TKTIQVHRRYW 832
Cdd:cd11683    327 QNVRAAQAPYW 337
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 106-402 7.71e-112

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: 350.00  E-value: 7.71e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  106 PERPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYID-LMETTQYMNEEELHVLADTYDSVYLHPNSYTCA 184
Cdd:pfam00850    2 PENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEfLEEAAPEGGALLLLSYLSGDDDTPVSPGSYEAA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  185 CLASGSVLRLVDAVLEAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHDIQRVLIVDWDVHHGQGIQFAF 264
Cdd:pfam00850   82 LLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLKRVAIVDFDVHHGNGTQEIF 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  265 DQDPSVLYFSIHRYEqGRFWPHLkaSNWSTTGLGQGQGYTINVPWNqVGMQDADYIAAFLHVLLPVAFEFQPQLVLVAAG 344
Cdd:pfam00850  162 YDDPSVLTLSIHQYP-GGFYPGT--GFADETGEGKGKGYTLNVPLP-PGTGDAEYLAAFEEILLPALEEFQPDLILVSAG 237

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387293808  345 FDALQGDPKGEMAATPAGFAQLTHLLMGLAE---GKLILSLEGGYNLHSLAEGVSATLHTL 402
Cdd:pfam00850  238 FDAHAGDPLGGLNLTTEGFAEITRILLELADplcIRVVSVLEGGYNLDALARSATAVLAAL 298
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
 482-832 2.51e-105

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: 335.83  E-value: 2.51e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  482 TGLVYDQQMMDHH-NLWDNY-HPEMPQRIHFIMHHLDELGLAKRCHSLPARPATDAELLTCHSAEH--------LERLRA 551
Cdd:cd10008      3 TGLVYDSVMLKHQcSCGDNSnHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHvllygtnpLSRLKL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  552 TEKMKTRELRRE----------GANYDSIYICSSTFACAQLAAGAACRLVEAVLAGEVLNGVAVVRPPGHHAEPDAACGF 621
Cdd:cd10008     83 DNGKLAGLLAQRmfvmlpcggvGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGF 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  622 CFFNSVAVAARHAQaISGHALRILIVDWDIHHGNGTQHIFEEDPSVLYISLHRYDHGTFFPmgNEGACTRIGKATGTGFT 701
Cdd:cd10008    163 CFFNSVAIACRQLQ-QQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFP--GSGAVDEVGAGSGEGFN 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  702 VNVAWNG---PRMGDADYLAAWHRLVLPVAYEFNPELVLVSAGFDAARGD--PLGGCQVSPEGYAHLTHQLMGLANGHII 776
Cdd:cd10008    240 VNVAWAGgldPPMGDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHpaPLGGYHVSAKCFGYMTQQLMNLAGGAVV 319

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1387293808  777 LILEGGYNLTSISESMAACTRSLLG---DPLPLLTRLRPPLSGAQASITKTIQVHRRYW 832
Cdd:cd10008    320 LALEGGHDLTAICDASEACVAALLGnevDPLSEESWKQKPNLNAIRSLEAVIRVHSKYW 378
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
 482-836 1.43e-102

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: 329.69  E-value: 1.43e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  482 TGLVYDQQMMDHHNLW--DNYHPEMPQRIHFIMHHLDELGLAKRCHSLPARPATDAELLTCHSAEHLeRLRATEKMKTRE 559
Cdd:cd10006      6 TGLVYDTLMLKHQCTCgnSNSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHT-LLYGTNPLNRQK 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  560 LRRE----------------GANYDSIYICSSTFACAQLAAGAAC--RLVEAVLAGEVLNGVAVVRPPGHHAEPDAACGF 621
Cdd:cd10006     85 LDSKkllgslasvfvrlpcgGVGVDSDTIWNEVHSSGAARLAVGCvvELVFKVATGELKNGFAVVRPPGHHAEESTPMGF 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  622 CFFNSVAVAARHAQAiSGHALRILIVDWDIHHGNGTQHIFEEDPSVLYISLHRYDHGTFFPmgNEGACTRIGKATGTGFT 701
Cdd:cd10006    165 CYFNSVAIAAKLLQQ-RLNVSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYDDGNFFP--GSGAPDEVGTGPGVGFN 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  702 VNVAWNG---PRMGDADYLAAWHRLVLPVAYEFNPELVLVSAGFDAARGD--PLGGCQVSPEGYAHLTHQLMGLANGHII 776
Cdd:cd10006    242 VNMAFTGgldPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHptPLGGYNLSAKCFGYLTKQLMGLAGGRIV 321

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387293808  777 LILEGGYNLTSISESMAACTRSLLG---DPLPLLTRLRPPLSGAQASITKTIQVHRRYWRSLR 836
Cdd:cd10006    322 LALEGGHDLTAICDASEACVSALLGnelDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQ 384
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
 482-836 5.80e-101

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: 325.79  E-value: 5.80e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  482 TGLVYDQQMMDHHNLW--DNYHPEMPQRIHFIMHHLDELGLAKRCHSLPARPATDAELLTCHSaEHLERLRATEKMKTRE 559
Cdd:cd10007      5 TGLVYDTFMLKHQCTCgnTNVHPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHS-EHHTLLYGTSPLNRQK 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  560 LRRE-----------------GANYDSIYICSSTFACAQLAAGAAC--RLVEAVLAGEVLNGVAVVRPPGHHAEPDAACG 620
Cdd:cd10007     84 LDSKkllgplsqkmyavlpcgGIGVDSDTVWNEMHSSSAVRMAVGCliELAFKVAAGELKNGFAVIRPPGHHAEESTAMG 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  621 FCFFNSVAVAARHAQAISGHAlRILIVDWDIHHGNGTQHIFEEDPSVLYISLHRYDHGTFFPmgNEGACTRIGKATGTGF 700
Cdd:cd10007    164 FCFFNSVAIAAKLLQQKLNVG-KILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGNFFP--GSGAPDEVGAGPGVGF 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  701 TVNVAWNG---PRMGDADYLAAWHRLVLPVAYEFNPELVLVSAGFDAARG--DPLGGCQVSPEGYAHLTHQLMGLANGHI 775
Cdd:cd10007    241 NVNIAWTGgvdPPIGDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGhqSPLGGYSVTAKCFGHLTKQLMTLAGGRV 320

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387293808  776 ILILEGGYNLTSISESMAACTRSLLGD---PLPLLTRLRPPLSGAQASITKTIQVHRRYWRSLR 836
Cdd:cd10007    321 VLALEGGHDLTAICDASEACVSALLGMeltPLDNTVLQQKPNDNAVATLERVIEIQSKHWSCLK 384
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 84-435 1.00e-99

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: 320.83  E-value: 1.00e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808   84 SGTGLVFDEQLNEFHCLWDDS--FPERPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMET----TQ 157
Cdd:cd11681      1 FTTGLAYDPLMLKHQCICGNNssHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTLLYGTnplsRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  158 YMNEEELHVLA--------------DTyDSVYLHPNSYTCACLASGSVLRLVDAVLEAEIRNGMAIIRPPGHHAQHSLMD 223
Cdd:cd11681     81 KLDPTKLAGLPqksfvrlpcggigvDS-DTVWNELHTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQAM 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  224 GYCMFNHVAVAARYAQQKHDIQRVLIVDWDVHHGQGIQFAFDQDPSVLYFSIHRYEQGRFWPHLKASNwsTTGLGQGQGY 303
Cdd:cd11681    160 GFCFFNSVAIAAKQLQQKLKLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFPGTGAPT--EVGSGAGEGF 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  304 TINVPWN---QVGMQDADYIAAFLHVLLPVAFEFQPQLVLVAAGFDALQGDPK--GEMAATPAGFAQLTHLLMGLAEGKL 378
Cdd:cd11681    238 NVNIAWSgglDPPMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPPplGGYKVSPACFGYMTRQLMNLAGGKV 317

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  379 ILSLEGGYNLHSLAEGVSATLHTLLGDPCPVLESPG---APCPSAQASLSCTLEALEPFW 435
Cdd:cd11681    318 VLALEGGYDLTAICDASEACVRALLGDELDPLSEEElerRPNPNAVTSLEKVIAIQSPYW 377
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 86-404 3.42e-98

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 313.97  E-value: 3.42e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808   86 TGLVFDEQLNEfHCLWDDSfPERPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYmnEEELH 165
Cdd:COG0123      1 TALIYHPDYLL-HDLGPGH-PEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAASL--DGGYG 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  166 VL-ADTYdsvyLHPNSYTCACLASGSVLRLVDAVLEAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAqQKHDI 244
Cdd:COG0123     77 QLdPDTP----VSPGTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGFCLFNNAAIAARYL-LAKGL 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  245 QRVLIVDWDVHHGQGIQFAFDQDPSVLYFSIHryeQGRFWPHLKASnwSTTGLGQGQGYTINVPwnqV--GMQDADYIAA 322
Cdd:COG0123    152 ERVAIVDFDVHHGNGTQDIFYDDPDVLTISIH---QDPLYPGTGAA--DETGEGAGEGSNLNVP---LppGTGDAEYLAA 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  323 FLHVLLPVAFEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAE---GKLILSLEGGYNLHSLAEGVSATL 399
Cdd:COG0123    224 LEEALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELADhcgGPVVSVLEGGYNLDALARSVAAHL 303


                   ....*
gi 1387293808  400 HTLLG 404
Cdd:COG0123    304 ETLLG 308
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 482-801 7.20e-97

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 310.12  E-value: 7.20e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  482 TGLVYDQQMMDHHnlWDNYHPEMPQRIHFIMHHLDELGLAKRCHSLPARPATDAELLTCHSAEHLERLRATEkmktreLR 561
Cdd:COG0123      1 TALIYHPDYLLHD--LGPGHPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAAS------LD 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  562 REGANYDSI-YICSSTFACAQLAAGAACRLVEAVLAGEVLNGVAVVRPPGHHAEPDAACGFCFFNSVAVAARHAQAisGH 640
Cdd:COG0123     73 GGYGQLDPDtPVSPGTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGFCLFNNAAIAARYLLA--KG 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  641 ALRILIVDWDIHHGNGTQHIFEEDPSVLYISLHRYDhgtFFPMgnEGACTRIGKATGTGFTVNVAWnGPRMGDADYLAAW 720
Cdd:COG0123    151 LERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQDP---LYPG--TGAADETGEGAGEGSNLNVPL-PPGTGDAEYLAAL 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  721 HRLVLPVAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHQLMGLA---NGHIILILEGGYNLTSISESMAACTR 797
Cdd:COG0123    225 EEALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELAdhcGGPVVSVLEGGYNLDALARSVAAHLE 304


                   ....
gi 1387293808  798 SLLG 801
Cdd:COG0123    305 TLLG 308
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
 482-833 3.22e-86

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: 284.22  E-value: 3.22e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  482 TGLVYDQQMMDHHNLWDNY--HPEMPQRIHFIMHHLDELGLAKRCHSLPARPATDAELLTCHSaEHLERLRAT-----EK 554
Cdd:cd10009      3 TGIAYDPLMLKHQCVCGNSttHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHS-EHHSLLYGTnpldgQK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  555 MKTRELRRE------------GANYDSIYICSSTFACAQLAAGAAC--RLVEAVLAGEVLNGVAVVRPPGHHAEPDAACG 620
Cdd:cd10009     82 LDPRILLGDdsqkffsslpcgGLGVDSDTIWNELHSSGAARMAVGCviELASKVASGELKNGFAVVRPPGHHAEESTAMG 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  621 FCFFNSVAVAARHAQAiSGHALRILIVDWDIHHGNGTQHIFEEDPSVLYISLHRYDHGTFFPmgNEGACTRIGKATGTGF 700
Cdd:cd10009    162 FCFFNSVAITAKYLRD-QLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFP--GSGAPNEVGTGLGEGY 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  701 TVNVAWNG---PRMGDADYLAAWHRLVLPVAYEFNPELVLVSAGFDAARGD--PLGGCQVSPEGYAHLTHQLMGLANGHI 775
Cdd:cd10009    239 NINIAWTGgldPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLADGRV 318

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387293808  776 ILILEGGYNLTSISESMAACTRSLLG---DPLPLLTRLRPPLSGAQASITKTIQVHRRYWR 833
Cdd:cd10009    319 VLALEGGHDLTAICDASEACVNALLGnelEPLAEDILHQSPNMNAVISLQKIIEIQSKYWK 379
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
 86-445 3.09e-82

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: 274.22  E-value: 3.09e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808   86 TGLVFDEQLNEFHCLW--DDSFPERPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSlEYIDLMETTQYMNEEE 163
Cdd:cd10006      6 TGLVYDTLMLKHQCTCgnSNSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHS-EAHTLLYGTNPLNRQK 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  164 L------HVLADTY------------DSVYLHPNSYTCACLASGSVLRLVDAVLEAEIRNGMAIIRPPGHHAQHSLMDGY 225
Cdd:cd10006     85 LdskkllGSLASVFvrlpcggvgvdsDTIWNEVHSSGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGF 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  226 CMFNHVAVAARYAQQKHDIQRVLIVDWDVHHGQGIQFAFDQDPSVLYFSIHRYEQGRFWPHLKASNwsTTGLGQGQGYTI 305
Cdd:cd10006    165 CYFNSVAIAAKLLQQRLNVSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYDDGNFFPGSGAPD--EVGTGPGVGFNV 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  306 NVPWN---QVGMQDADYIAAFLHVLLPVAFEFQPQLVLVAAGFDALQGDPK--GEMAATPAGFAQLTHLLMGLAEGKLIL 380
Cdd:cd10006    243 NMAFTgglDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTplGGYNLSAKCFGYLTKQLMGLAGGRIVL 322

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  381 SLEGGYNLHSLAEGVSATLHTLLG---DPCP--VLESpgAPCPSAQASLSCTLEALEPFWESLVRSVESL 445
Cdd:cd10006    323 ALEGGHDLTAICDASEACVSALLGnelDPLPekVLQQ--RPNANAVRSMEKVMEIHSKYWRCLQRTTSTA 390
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
 83-445 2.08e-81

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: 272.25  E-value: 2.08e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808   83 LSGTGLVFDEQLNEFHCLWDDS--FPERPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSlEYIDLMETTQYMN 160
Cdd:cd10007      2 LFTTGLVYDTFMLKHQCTCGNTnvHPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHS-EHHTLLYGTSPLN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  161 EEELH--------------VL------ADTyDSVYLHPNSYTCACLASGSVLRLVDAVLEAEIRNGMAIIRPPGHHAQHS 220
Cdd:cd10007     81 RQKLDskkllgplsqkmyaVLpcggigVDS-DTVWNEMHSSSAVRMAVGCLIELAFKVAAGELKNGFAVIRPPGHHAEES 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  221 LMDGYCMFNHVAVAARYAQQKHDIQRVLIVDWDVHHGQGIQFAFDQDPSVLYFSIHRYEQGRFWPHLKASNwsTTGLGQG 300
Cdd:cd10007    160 TAMGFCFFNSVAIAAKLLQQKLNVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGNFFPGSGAPD--EVGAGPG 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  301 QGYTINVPWN---QVGMQDADYIAAFLHVLLPVAFEFQPQLVLVAAGFDALQG--DPKGEMAATPAGFAQLTHLLMGLAE 375
Cdd:cd10007    238 VGFNVNIAWTggvDPPIGDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGhqSPLGGYSVTAKCFGHLTKQLMTLAG 317

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387293808  376 GKLILSLEGGYNLHSLAEGVSATLHTLLGD---PCPVLESPGAPCPSAQASLSCTLEALEPFWESLVRSVESL 445
Cdd:cd10007    318 GRVVLALEGGHDLTAICDASEACVSALLGMeltPLDNTVLQQKPNDNAVATLERVIEIQSKHWSCLKRFAATL 390
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
 501-800 3.14e-80

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: 263.99  E-value: 3.14e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  501 HPEMPQRIHFIMHHLDELGLAKRCHSLPARPATDAELLTCHSAEHLERLRAteKMKTRELRREGAnyDSiYICSSTFACA 580
Cdd:cd11599      1 HPESPERLEAILDALIASGLDRLLRQLEAPPATREQLLRVHDAAYVDRLEA--AAPEEGLVQLDP--DT-AMSPGSLEAA 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  581 QLAAGAACRLVEAVLAGEVLNGVAVVRPPGHHAEPDAACGFCFFNSVAVAARHAQAISGhALRILIVDWDIHHGNGTQHI 660
Cdd:cd11599     76 LRAAGAVVAAVDAVMAGEARNAFCAVRPPGHHAERDKAMGFCLFNNVAIAAAHALAHHG-LERVAIVDFDVHHGNGTEDI 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  661 FEEDPSVLYISLHRYdhgTFFPmgnegaCTRIGKATGTGFTVNVAWNgPRMGDADYLAAWHRLVLPVAYEFNPELVLVSA 740
Cdd:cd11599    155 FRDDPRVLFCSSHQH---PLYP------GTGAPDETGHGNIVNVPLP-AGTGGAEFREAVEDRWLPALDAFKPDLILISA 224

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387293808  741 GFDAARGDPLGGCQVSPEGYAHLTHQLMGLAN----GHIILILEGGYNLTSISESMAACTRSLL 800
Cdd:cd11599    225 GFDAHRDDPLAQLNLTEEDYAWITEQLMDVADrycdGRIVSVLEGGYDLSALARSVAAHVRALM 288
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
 106-403 8.75e-80

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: 262.83  E-value: 8.75e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  106 PERPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQymNEEELHVL-ADTYDSvylhPNSYTCA 184
Cdd:cd11599      2 PESPERLEAILDALIASGLDRLLRQLEAPPATREQLLRVHDAAYVDRLEAAA--PEEGLVQLdPDTAMS----PGSLEAA 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  185 CLASGSVLRLVDAVLEAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHDIQRVLIVDWDVHHGQGIQFAF 264
Cdd:cd11599     76 LRAAGAVVAAVDAVMAGEARNAFCAVRPPGHHAERDKAMGFCLFNNVAIAAAHALAHHGLERVAIVDFDVHHGNGTEDIF 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  265 DQDPSVLYFSIHRYeqgRFWPHlkasnwstTGLGQ--GQGYTINVPWNQvGMQDADYIAAFLHVLLPVAFEFQPQLVLVA 342
Cdd:cd11599    156 RDDPRVLFCSSHQH---PLYPG--------TGAPDetGHGNIVNVPLPA-GTGGAEFREAVEDRWLPALDAFKPDLILIS 223

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387293808  343 AGFDALQGDPKGEMAATPAGFAQLTHLLMGLA----EGKLILSLEGGYNLHSLAEGVSATLHTLL 403
Cdd:cd11599    224 AGFDAHRDDPLAQLNLTEEDYAWITEQLMDVAdrycDGRIVSVLEGGYDLSALARSVAAHVRALM 288
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
 482-786 1.02e-79

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: 265.58  E-value: 1.02e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  482 TGLVYDQQMMDHHNlwDNY---------------HPEMPQRIHFIMHHLDELGLAKRCHSLPARPATDAELLTCHSAEHL 546
Cdd:cd09996      1 TGFVWDERYLWHDT--GTGalflpvggllvqpgrHPENPETKRRIKNLLEVSGLSDHLVLITPRPATDEELLRVHTPEYI 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  547 ERLRATEKMKTREL-RREGANYDSIYICSstfacaqLAAGAACRLVEAVLAGEVLNGVAVVRPPGHHAEPDAACGFCFFN 625
Cdd:cd09996     79 DRVKAASAAGGGEAgGGTPFGPGSYEIAL-------LAAGGAIAAVDAVLDGEVDNAYALVRPPGHHAEPDQGMGFCLFN 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  626 SVAVAARHAQAiSGHALRILIVDWDIHHGNGTQHIFEEDPSVLYISLHRyDHgtFFPMGNeGACTRIGKATGTGFTVNVa 705
Cdd:cd09996    152 NVAIAARHALA-VGGVKRVAVVDWDVHHGNGTQAIFYDDPDVLTISLHQ-DR--CFPPDS-GAVEERGEGAGEGYNLNI- 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  706 wngPRM---GDADYLAAWHRLVLPVAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHQLMGLAN----GHIILI 778
Cdd:cd09996    226 ---PLPpgsGDGAYLHAFERIVLPALRAFRPELIIVASGFDASAFDPLGRMMLTSDGFRALTRKLRDLADelcgGRLVMV 302


                   ....*...
gi 1387293808  779 LEGGYNLT 786
Cdd:cd09996    303 HEGGYSEA 310
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
 86-435 3.02e-79

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: 264.95  E-value: 3.02e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808   86 TGLVFDEQLNEFHCLWDDS--FPERPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIdLMETTQYMNEEE 163
Cdd:cd10008      3 TGLVYDSVMLKHQCSCGDNsnHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHV-LLYGTNPLSRLK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  164 LH--------------------VLADTyDSVYLHPNSYTCACLASGSVLRLVDAVLEAEIRNGMAIIRPPGHHAQHSLMD 223
Cdd:cd10008     82 LDngklagllaqrmfvmlpcggVGVDT-DTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAM 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  224 GYCMFNHVAVAARYAQQKHDIQRVLIVDWDVHHGQGIQFAFDQDPSVLYFSIHRYEQGRFWPHLKASNwsTTGLGQGQGY 303
Cdd:cd10008    161 GFCFFNSVAIACRQLQQQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVD--EVGAGSGEGF 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  304 TINVPWN---QVGMQDADYIAAFLHVLLPVAFEFQPQLVLVAAGFDALQGDPK--GEMAATPAGFAQLTHLLMGLAEGKL 378
Cdd:cd10008    239 NVNVAWAgglDPPMGDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHPAplGGYHVSAKCFGYMTQQLMNLAGGAV 318

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  379 ILSLEGGYNLHSLAEGVSATLHTLLG---DPCPVLESPGAPCPSAQASLSCTLEALEPFW 435
Cdd:cd10008    319 VLALEGGHDLTAICDASEACVAALLGnevDPLSEESWKQKPNLNAIRSLEAVIRVHSKYW 378
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
 86-404 5.50e-79

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: 263.27  E-value: 5.50e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808   86 TGLVFDEqlnefHCLWDDS------------------FPERPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSL 147
Cdd:cd09996      1 TGFVWDE-----RYLWHDTgtgalflpvggllvqpgrHPENPETKRRIKNLLEVSGLSDHLVLITPRPATDEELLRVHTP 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  148 EYIDLMETTQYMNEEELHVLAdtydsvYLHPNSYTCACLASGSVLRLVDAVLEAEIRNGMAIIRPPGHHAQHSLMDGYCM 227
Cdd:cd09996     76 EYIDRVKAASAAGGGEAGGGT------PFGPGSYEIALLAAGGAIAAVDAVLDGEVDNAYALVRPPGHHAEPDQGMGFCL 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  228 FNHVAVAARYAQQKHDIQRVLIVDWDVHHGQGIQFAFDQDPSVLYFSIHryeQGRFWPHlkasNWST---TGLGQGQGYT 304
Cdd:cd09996    150 FNNVAIAARHALAVGGVKRVAVVDWDVHHGNGTQAIFYDDPDVLTISLH---QDRCFPP----DSGAveeRGEGAGEGYN 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  305 INVPW-NQVGmqDADYIAAFLHVLLPVAFEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAE----GKLI 379
Cdd:cd09996    223 LNIPLpPGSG--DGAYLHAFERIVLPALRAFRPELIIVASGFDASAFDPLGRMMLTSDGFRALTRKLRDLADelcgGRLV 300

                          330       340
                   ....*....|....*....|....*
gi 1387293808  380 LSLEGGYNLHSLAEGVSATLHTLLG 404
Cdd:cd09996    301 MVHEGGYSEAYVPFCGLAVLEELSG 325
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
 84-436 2.11e-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: 246.08  E-value: 2.11e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808   84 SGTGLVFDEQLNEFHCLWDDS--FPERPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSlEYIDLMETTQYMNE 161
Cdd:cd10009      1 SATGIAYDPLMLKHQCVCGNSttHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHS-EHHSLLYGTNPLDG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  162 EELH---VLADTY----------------DSVYLHPNSYTCACLASGSVLRLVDAVLEAEIRNGMAIIRPPGHHAQHSLM 222
Cdd:cd10009     80 QKLDpriLLGDDSqkffsslpcgglgvdsDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTA 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  223 DGYCMFNHVAVAARYAQQKHDIQRVLIVDWDVHHGQGIQFAFDQDPSVLYFSIHRYEQGRFWPHLKASNwsTTGLGQGQG 302
Cdd:cd10009    160 MGFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPN--EVGTGLGEG 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  303 YTINVPWN---QVGMQDADYIAAFLHVLLPVAFEFQPQLVLVAAGFDALQGD--PKGEMAATPAGFAQLTHLLMGLAEGK 377
Cdd:cd10009    238 YNINIAWTgglDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLADGR 317

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387293808  378 LILSLEGGYNLHSLAEGVSATLHTLLG---DPCPVLESPGAPCPSAQASLSCTLEALEPFWE 436
Cdd:cd10009    318 VVLALEGGHDLTAICDASEACVNALLGnelEPLAEDILHQSPNMNAVISLQKIIEIQSKYWK 379
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
 487-794 9.38e-67

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: 227.04  E-value: 9.38e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  487 DQQMMDHHNLWDN----YHPEMPQRIHFIMHHLDELGLAKRchsLPARPATDAELLTCHSAEHLERLRatekmktrelrr 562
Cdd:cd10001      7 DHLLHHPKTELSRgklvPHPENPERAEAILDALKRAGLGEV---LPPRDFGLEPILAVHDPDYVDFLE------------ 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  563 eGANYDSiYICSSTFACAQLAAGAACRLVEAVLAGEVLNgVAVVRPPGHHAEPDAACGFCFFNSVAVAARHAQAISGhal 642
Cdd:cd10001     72 -TADTDT-PISEGTWEAALAAADTALTAADLVLEGERAA-YALCRPPGHHAGRDRAGGFCYFNNAAIAAQYLRDRAG--- 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  643 RILIVDWDIHHGNGTQHIFEEDPSVLYISLHRYDHgTFFPmGNEGACTRIGKATGTGFTVNV--AWNgprMGDADYLAAW 720
Cdd:cd10001    146 RVAILDVDVHHGNGTQEIFYERPDVLYVSIHGDPR-TFYP-FFLGFADETGEGEGEGYNLNLplPPG---TGDDDYLAAL 220

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387293808  721 HRLVLPVAyEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHQLMGLaNGHIILILEGGYNLTSISESMAA 794
Cdd:cd10001    221 DEALAAIA-AFGPDALVVSLGFDTHEGDPLSDFKLTTEDYARIGRRIAAL-GLPTVFVQEGGYNVDALGRNAVA 292
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
 507-799 4.44e-61

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: 210.37  E-value: 4.44e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  507 RIHFIMHHLDELGLAKRCHSLPARPATDAELLTCHSAEHLERLRATEKMKTRELRREGANYDSIYICSSTFACAQLAAGA 586
Cdd:cd09301      1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKANFAVATITESKPVIFGPNFPVQRHYFRGARLSTGG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  587 ACRLVEAVLAGEVLNGVAVVRPPGHHAEPDAACGFCFFNSVAVAARHAQAIsGHAlRILIVDWDIHHGNGTQHIFEEDPS 666
Cdd:cd09301     81 VVEAAELVAKGELERAFAVVGAGGHHAGKSRAWGFCYFNDVVLAIKFLRER-GIS-RILIIDTDAHHGDGTREAFYDDDR 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  667 VLYISLHRYDHGTFfpmgnegactriGKATGTGFTVNVAWNGPrMGDADYLAAWHRLVLPVAYEFNPELVLVSAGFDAAR 746
Cdd:cd09301    159 VLHMSFHNYDIYPF------------GRGKGKGYKINVPLEDG-LGDEEYLDAVERVISKVLEEFEPEVVVLQFGHDTHE 225

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1387293808  747 GDPLGGCQVSPEGYAHLTHQLMGLAN-GHIILILEGGYNLTSISESMAACTRSL 799
Cdd:cd09301    226 GDRLGGFNLSEKGFVKLAEIVKEFARgGPILMVLGGGYNPEAAARIWTAIIKEL 279
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
 106-403 6.14e-60

Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine amidohydrolase (APAH) as well as other Class II histone deacetylase (HDAC) and related proteins. Deacetylases of class II are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues of histones (EC 3.5.1.98) and possibly other proteins to yield deacetylated histones/other proteins. Mycoplana ramosa APAH exhibits broad substrate specificity and catalyzes the deacetylation of polyamines such as putrescine, spermidine, and spermine by cleavage of a non-peptide amide bond.


Pssm-ID: 212525 [Multi-domain]  Cd Length: 298  Bit Score: 207.78  E-value: 6.14e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  106 PERPERLHAIKEQLIQEGLLDRCVsfQARFAEkEELMLVHSLEYIDLMETtqymneeelhvlADTydSVYLHPNSYTCAC 185
Cdd:cd10001     26 PENPERAEAILDALKRAGLGEVLP--PRDFGL-EPILAVHDPDYVDFLET------------ADT--DTPISEGTWEAAL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  186 LASGSVLRLVDAVLEAEiRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHDiqRVLIVDWDVHHGQGIQFAFD 265
Cdd:cd10001     89 AAADTALTAADLVLEGE-RAAYALCRPPGHHAGRDRAGGFCYFNNAAIAAQYLRDRAG--RVAILDVDVHHGNGTQEIFY 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  266 QDPSVLYFSIHRYEQGrFWPHlKASNWSTTGLGQGQGYTINVPWnQVGMQDADYIAAFLHVLLPVAfEFQPQLVLVAAGF 345
Cdd:cd10001    166 ERPDVLYVSIHGDPRT-FYPF-FLGFADETGEGEGEGYNLNLPL-PPGTGDDDYLAALDEALAAIA-AFGPDALVVSLGF 241

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1387293808  346 DALQGDPKGEMAATPAGFAQLTHLLMGLAEGKLILsLEGGYNLHSLAEGVSATLHTLL 403
Cdd:cd10001    242 DTHEGDPLSDFKLTTEDYARIGRRIAALGLPTVFV-QEGGYNVDALGRNAVAFLAGFE 298
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
 111-402 4.30e-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: 204.59  E-value: 4.30e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  111 RLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEEELHVLADTYDSVYLHPNSYTCACLASGS 190
Cdd:cd09301      1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKANFAVATITESKPVIFGPNFPVQRHYFRGARLSTGG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  191 VLRLVDAVLEAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKhDIQRVLIVDWDVHHGQGIQFAFDQDPSV 270
Cdd:cd09301     81 VVEAAELVAKGELERAFAVVGAGGHHAGKSRAWGFCYFNDVVLAIKFLRER-GISRILIIDTDAHHGDGTREAFYDDDRV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  271 LYFSIHRYeqgrfwphlkasNWSTTGLGQGQGYTINVPWNQvGMQDADYIAAFLHVLLPVAFEFQPQLVLVAAGFDALQG 350
Cdd:cd09301    160 LHMSFHNY------------DIYPFGRGKGKGYKINVPLED-GLGDEEYLDAVERVISKVLEEFEPEVVVLQFGHDTHEG 226

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1387293808  351 DPKGEMAATPAGFAQLTHLLMGLAEGK-LILSLEGGYNLHSLAEGVSATLHTL 402
Cdd:cd09301    227 DRLGGFNLSEKGFVKLAEIVKEFARGGpILMVLGGGYNPEAAARIWTAIIKEL 279
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
 500-785 1.13e-52

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


Pssm-ID: 212520 [Multi-domain]  Cd Length: 313  Bit Score: 187.38  E-value: 1.13e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  500 YHPEMPQRIHFIMHHLDELGLAKRCHSLPARPATDAELLTCHSAEHLERLRATEK-MKTRELRREGANYD---------- 568
Cdd:cd09994     16 NHPFNPPRLSLTKDLLRALGLLPPVDLVPPRPATEEELLLFHTPDYIEAVKEASRgQEPEGRGRLGLGTEdnpvfpgmhe 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  569 -SIYICSSTFacaqlaagaacRLVEAVLAGEVlngVAVVRPPG--HHAEPDAACGFCFFNSVAVAARHAQAISGhaLRIL 645
Cdd:cd09994     96 aAALVVGGTL-----------LAARLVLEGEA---RRAFNPAGglHHAMRGRASGFCVYNDAAVAIERLRDKGG--LRVA 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  646 IVDWDIHHGNGTQHIFEEDPSVLYISLHRyDHGTFFPmgNEGACTRIGKATGTGFTVNVAWNgPRMGDADYLAAWHRLVL 725
Cdd:cd09994    160 YVDIDAHHGDGVQAAFYDDPRVLTISLHE-SGRYLFP--GTGFVDEIGEGEGYGYAVNIPLP-PGTGDDEFLRAFEAVVP 235

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387293808  726 PVAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHQLMGLA----NGHIILILEGGYNL 785
Cdd:cd09994    236 PLLRAFRPDVIVSQHGADAHAGDPLTHLNLSNRAYRAAVRRIRELAdeycGGRWLALGGGGYNP 299
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
 88-392 1.01e-47

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: 173.13  E-value: 1.01e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808   88 LVFDEQLNEFHclWDDSFPERPERLHAIKEqLIQE-GLLDRCVSFQARFAEKEELMLVHSLEYIDLM---ETTQYMNEEE 163
Cdd:cd09994      2 FIYSEEYLRYS--FGPNHPFNPPRLSLTKD-LLRAlGLLPPVDLVPPRPATEEELLLFHTPDYIEAVkeaSRGQEPEGRG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  164 LHVLaDTYDSVYlHPNSYTCACLASGSVLRLVDAVLEAEIRNGMAIIrppG--HHAQHSLMDGYCMFNHVAVAARYAQqK 241
Cdd:cd09994     79 RLGL-GTEDNPV-FPGMHEAAALVVGGTLLAARLVLEGEARRAFNPA---GglHHAMRGRASGFCVYNDAAVAIERLR-D 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  242 HDIQRVLIVDWDVHHGQGIQFAFDQDPSVLYFSIHryEQGR-FWPHLKASNwsTTGLGQGQGYTINVPWNQvGMQDADYI 320
Cdd:cd09994    153 KGGLRVAYVDIDAHHGDGVQAAFYDDPRVLTISLH--ESGRyLFPGTGFVD--EIGEGEGYGYAVNIPLPP-GTGDDEFL 227

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387293808  321 AAFLHVLLPVAFEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAE----GKLILSLEGGYNLHSLA 392
Cdd:cd09994    228 RAFEAVVPPLLRAFRPDVIVSQHGADAHAGDPLTHLNLSNRAYRAAVRRIRELADeycgGRWLALGGGGYNPDVVA 303
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 103-408 7.78e-40

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: 151.72  E-value: 7.78e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  103 DSFPERPERLHAIkEQLIQE-GLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYM--NEEELHVLAD---TYDSVYL 176
Cdd:cd10000     14 DRLPKVPNRASMV-HSLIEAyGLLKQLRVVKPRVATEEELASFHSDEYIQFLKKASNEgdNDEEPSEQQEfglGYDCPIF 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  177 hPNSYTCACLASGSVLRLVDAVLEAEIRngMAIIRPPG-HHAQHSLMDGYCMFNHVAVAARYAQQKHDiqRVLIVDWDVH 255
Cdd:cd10000     93 -EGIYDYAAAVAGATLTAAQLLIDGKCK--VAINWFGGwHHAQRDEASGFCYVNDIVLGILKLREKFD--RVLYVDLDLH 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  256 HGQGIQFAFDQDPSVLYFSIHRYEQGrFWPhlKASNWSTTGLGQGQGYTINVPWNQvGMQDADYIAAFLHVLLPVAFEFQ 335
Cdd:cd10000    168 HGDGVEDAFSFTSKVMTVSLHKYSPG-FFP--GTGDVSDVGLGKGKYYTVNVPLRD-GIQDEQYLQIFTAVVPEIVAAFR 243

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387293808  336 PQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAEGKLILSlEGGYNLHSLAEGVSATLHTLLGDPCP 408
Cdd:cd10000    244 PEAVVLQCGADTLAGDPMGAFNLTPVGIGKCLKYVLGWKLPTLILG-GGGYNLANTARCWTYLTGLILGEPLS 315
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 511-759 2.08e-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: 136.09  E-value: 2.08e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  511 IMHHLDELGLAKRCHSLPARPATDAELLTCHSAEHLERLRaTEKMKTRELRREGANYDSiyicsstfacaqlaagaacRL 590
Cdd:cd09993     11 LREALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLESLK-SGELSREEIRRIGFPWSP-------------------EL 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  591 VEAVL---AGEVL-------NGVAVvRPPG--HHAEPDAACGFCFFNSVAVAARHAQAiSGHALRILIVDWDIHHGNGTQ 658
Cdd:cd09993     71 VERTRlavGGTILaarlaleHGLAI-NLAGgtHHAFPDRGEGFCVFNDIAIAARVLLA-EGLVRRVLIVDLDVHQGNGTA 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  659 HIFEEDPSVLYISLHrydHGTFFPMGNEGACTRIGKATGTgftvnvawngprmGDADYLAAWHRLVLPVAYEFNPELVLV 738
Cdd:cd09993    149 AIFADDPSVFTFSMH---GEKNYPFRKEPSDLDVPLPDGT-------------GDDEYLAALEEALPRLLAEFRPDLVFY 212

                          250       260
                   ....*....|....*....|.
gi 1387293808  739 SAGFDAARGDPLGGCQVSPEG 759
Cdd:cd09993    213 NAGVDVLAGDRLGRLSLSLEG 233
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 484-805 1.08e-34

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


Pssm-ID: 212524 [Multi-domain]  Cd Length: 364  Bit Score: 136.70  E-value: 1.08e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  484 LVYDQqmmDHHNLWDNYhPEMPQRIHFIMHHLDELGLAKRCHSLPARPATDAELLTCHSAEHLERLRA------TEKMKT 557
Cdd:cd10000      3 YIHSP---EYVNLCDRL-PKVPNRASMVHSLIEAYGLLKQLRVVKPRVATEEELASFHSDEYIQFLKKasnegdNDEEPS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  558 rELRREGANYD-----SIYICSSTFACAqlaagaacrlveAVLAGEVL----NGVAVVRPPG-HHAEPDAACGFCFFNSV 627
Cdd:cd10000     79 -EQQEFGLGYDcpifeGIYDYAAAVAGA------------TLTAAQLLidgkCKVAINWFGGwHHAQRDEASGFCYVNDI 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  628 AVAArhaQAISGHALRILIVDWDIHHGNGTQHIFEEDPSVLYISLHRYDHGtFFPmgNEGACTRIGKATGTGFTVNVAWn 707
Cdd:cd10000    146 VLGI---LKLREKFDRVLYVDLDLHHGDGVEDAFSFTSKVMTVSLHKYSPG-FFP--GTGDVSDVGLGKGKYYTVNVPL- 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  708 gpRMG--DADYLAAWHRLVLPVAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHQLMGLANGHIILiLEGGYNL 785
Cdd:cd10000    219 --RDGiqDEQYLQIFTAVVPEIVAAFRPEAVVLQCGADTLAGDPMGAFNLTPVGIGKCLKYVLGWKLPTLIL-GGGGYNL 295

                          330       340
                   ....*....|....*....|
gi 1387293808  786 TSISESMAACTRSLLGDPLP 805
Cdd:cd10000    296 ANTARCWTYLTGLILGEPLS 315
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 115-362 4.45e-33

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


Pssm-ID: 212519 [Multi-domain]  Cd Length: 275  Bit Score: 129.54  E-value: 4.45e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  115 IKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEEELhvladtydsVYLHPNSytcACL-------A 187
Cdd:cd09993     11 LREALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLESLKSGELSREEIR---------RIGFPWS---PELvertrlaV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  188 SGSVLrlvdAVLEAeIRNGMAIiRPPG--HHAQHSLMDGYCMFNHVAVAARYAQQKHDIQRVLIVDWDVHHGQGIQFAFD 265
Cdd:cd09993     79 GGTIL----AARLA-LEHGLAI-NLAGgtHHAFPDRGEGFCVFNDIAIAARVLLAEGLVRRVLIVDLDVHQGNGTAAIFA 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  266 QDPSVLYFSIHryeQGRFWPHLK-ASNWSttglgqgqgytINVPWnqvGMQDADYIAAfLHVLLPVAF-EFQPQLVLVAA 343
Cdd:cd09993    153 DDPSVFTFSMH---GEKNYPFRKePSDLD-----------VPLPD---GTGDDEYLAA-LEEALPRLLaEFRPDLVFYNA 214

                          250
                   ....*....|....*....
gi 1387293808  344 GFDALQGDPKGEMAATPAG 362
Cdd:cd09993    215 GVDVLAGDRLGRLSLSLEG 233
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
 106-392 1.30e-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: 126.16  E-value: 1.30e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  106 PERPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYID-LMETTQYMNEE---ELHVLADTYDSvYLHPNSY 181
Cdd:cd09991     16 PMKPHRIRMTHSLILSYGLYKKMEIYRPRPATAEELTKFHSDDYIDfLRSVSPDNMKEfkkQLERFNVGEDC-PVFDGLY 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  182 T-CACLASGSVlrlvDAVleAEIRNGMA--IIRPPG--HHAQHSLMDGYCMFNHVAVAARYAQQKHdiQRVLIVDWDVHH 256
Cdd:cd09991     95 EyCQLYAGGSI----AAA--VKLNRGQAdiAINWAGglHHAKKSEASGFCYVNDIVLAILELLKYH--QRVLYIDIDIHH 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  257 GQGIQFAFDQDPSVLYFSIHRYEQGRFwphlKASNWSTTGLGQGQGYTINVPWNQvGMQDADYIAAFLHVLLPVAFEFQP 336
Cdd:cd09991    167 GDGVEEAFYTTDRVMTVSFHKFGEYFF----PGTGLRDIGAGKGKYYAVNVPLKD-GIDDESYLQIFEPVLSKVMEVFQP 241

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1387293808  337 QLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLaEGKLILSLEGGYNLHSLA 392
Cdd:cd09991    242 SAVVLQCGADSLAGDRLGCFNLSIKGHAKCVKFVKSF-NIPLLVLGGGGYTLRNVA 296
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
 501-789 3.92e-28

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


Pssm-ID: 212517 [Multi-domain]  Cd Length: 306  Bit Score: 116.14  E-value: 3.92e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  501 HPEMPQRIHFIMHHLDELGLAKRCHSLPARPATDAELLTCHSAEHLERLRATEKMKTRELRREGANYDSIYICSS----- 575
Cdd:cd09991     15 HPMKPHRIRMTHSLILSYGLYKKMEIYRPRPATAEELTKFHSDDYIDFLRSVSPDNMKEFKKQLERFNVGEDCPVfdgly 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  576 TFacaqlaagaaCRLVEA--VLAGEVLN-GVA--VVRPPG--HHAEPDAACGFCFFNSVAVA-----ARHAqaisghalR 643
Cdd:cd09991     95 EY----------CQLYAGgsIAAAVKLNrGQAdiAINWAGglHHAKKSEASGFCYVNDIVLAilellKYHQ--------R 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  644 ILIVDWDIHHGNGTQHIFEEDPSVLYISLHRYdhGTFFPMGneGACTRIGKATGTGFTVNVAWNgPRMGDADYLAAWHRL 723
Cdd:cd09991    157 VLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKF--GEYFFPG--TGLRDIGAGKGKYYAVNVPLK-DGIDDESYLQIFEPV 231

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387293808  724 VLPVAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLThQLMGLANGHIILILEGGYNLTSIS 789
Cdd:cd09991    232 LSKVMEVFQPSAVVLQCGADSLAGDRLGCFNLSIKGHAKCV-KFVKSFNIPLLVLGGGGYTLRNVA 296
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
1047-1109 1.26e-23

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 95.02  E-value: 1.26e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387293808 1047 CQDCGTLQENWVCLSCYQVYCGRYINAHMLQHHEGSGHPLVLSYADLSAWCYHCQAYVHHKDL 1109
Cdd:pfam02148    1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPSL 63
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
 116-387 3.20e-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: 101.19  E-value: 3.20e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  116 KEQLIQE-----GLLDRCV-SFQARFAEKEELMLVHSLEYIDLMeTTQYMNEEELHVLAdtYDSVYLHpnsytcacLASG 189
Cdd:cd11680     21 RSSLVHSlirayGLLQHFDeIIEPERATRKDLTKYHDKDYVDFL-LKKYGLEDDCPVFP--FLSMYVQ--------LVAG 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  190 SVLRLVDAVLEAEIRNgMAIIRPPG-HHAQHSLMDGYCMFNHVaVAARYAQQKHDIQRVLIVDWDVHHGQGIQFAFDQDP 268
Cdd:cd11680     90 SSLALAKHLITQVERD-IAINWYGGrHHAQKSRASGFCYVNDI-VLAILRLRRARFRRVFYLDLDLHHGDGVESAFFFSK 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  269 SVLYFSIHRYEQGrFWPhlkasnwSTTGL-GQGQGYTINVPWNQvGMQDADYIAAFLHVLLPVAFEFQPQLVLVAAGFDA 347
Cdd:cd11680    168 NVLTCSIHRYDPG-FFP-------GTGSLkNSSDKGMLNIPLKR-GLSDKTLLRIIDSIVRPLIEKFEPEVIVIQCGCDG 238

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1387293808  348 LQGDPKGEMAATPAGFAQLTHLLMGLAEGKLILSL-EGGYN 387
Cdd:cd11680    239 LSGDPHKEWNLTIRGYGSVIELLLKEFKDKPTLLLgGGGYN 279
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
 90-354 4.38e-23

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: 101.38  E-value: 4.38e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808   90 FDEQLNEFHclWDDSFPERPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDL--METTQYMN-----EE 162
Cdd:cd11598      5 FNSRVEDYH--FGRTHPMKPFRLTLTKHLVMGYGLHKAMDTYEARAATREELRQFHDADYLDFlsKVSPENANqlrfdKA 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  163 ELHVLAD---TYDSVYLHPNSYTCACLASGSvlRLVDAvleaeiRNGMAIIRPPG-HHAQHSLMDGYCMFNHVAVAA--- 235
Cdd:cd11598     83 EPFNIGDdcpVFDGMYDYCQLYAGASLDAAR--KLCSG------QSDIAINWSGGlHHAKKSEASGFCYVNDIVLAIlnl 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  236 -RYaqqkhdIQRVLIVDWDVHHGQGIQFAFDQDPSVLYFSIHRYeQGRFWPhlKASNWSTTGLGQGQGYTINVPWNQvGM 314
Cdd:cd11598    155 lRY------FPRVLYIDIDVHHGDGVEEAFYRTDRVMTLSFHKY-NGEFFP--GTGDLDDNGGTPGKHFALNVPLED-GI 224

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1387293808  315 QDADYIAAFLHVLLPVAFEFQPQLVLVAAGFDALQGDPKG 354
Cdd:cd11598    225 DDEQYNLLFKSIIGPTIEKFQPSAIVLQCGADSLGGDRLG 264
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
 106-392 6.20e-23

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: 102.07  E-value: 6.20e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  106 PERPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEEE-------LHVLAD--TYDSVYL 176
Cdd:cd10010     26 PMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEyskqmqrFNVGEDcpVFDGLFE 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  177 HPNSYTCACLASGSVLRLVDAVLEAEIRNGMaiirppgHHAQHSLMDGYCMFNHVAVAARYAQQKHdiQRVLIVDWDVHH 256
Cdd:cd10010    106 FCQLSAGGSVASAVKLNKQQTDIAVNWAGGL-------HHAKKSEASGFCYVNDIVLAILELLKYH--QRVLYIDIDIHH 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  257 GQGIQFAFDQDPSVLYFSIHRYeqGRFWPhlKASNWSTTGLGQGQGYTINVPWNQvGMQDADYIAAFLHVLLPVAFEFQP 336
Cdd:cd10010    177 GDGVEEAFYTTDRVMTVSFHKY--GEYFP--GTGDLRDIGAGKGKYYAVNYPLRD-GIDDESYEAIFKPVMSKVMEMFQP 251

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1387293808  337 QLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAEGKLILSlEGGYNLHSLA 392
Cdd:cd10010    252 SAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLG-GGGYTIRNVA 306
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
 523-786 1.17e-22

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: 99.65  E-value: 1.17e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  523 RCHSLPARPATDAELLTCHSAEHLERLratekmktreLRREGANYDSIYICSstfacaqlaAGAACRLVEA---VLAGEV 599
Cdd:cd11680     38 FDEIIEPERATRKDLTKYHDKDYVDFL----------LKKYGLEDDCPVFPF---------LSMYVQLVAGsslALAKHL 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  600 LNG----VAVVRPPG-HHAEPDAACGFCFFNSVAVAARHAQaiSGHALRILIVDWDIHHGNGTQHIFEEDPSVLYISLHR 674
Cdd:cd11680     99 ITQverdIAINWYGGrHHAQKSRASGFCYVNDIVLAILRLR--RARFRRVFYLDLDLHHGDGVESAFFFSKNVLTCSIHR 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  675 YDHGtFFPMGneGACtrigKATGTGFTVNVAWNgPRMGDADYLAAWHRLVLPVAYEFNPELVLVSAGFDAARGDPLGGCQ 754
Cdd:cd11680    177 YDPG-FFPGT--GSL----KNSSDKGMLNIPLK-RGLSDKTLLRIIDSIVRPLIEKFEPEVIVIQCGCDGLSGDPHKEWN 248

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1387293808  755 VSPEGYAHLTHQLMGLANGHIILIL-EGGYNLT 786
Cdd:cd11680    249 LTIRGYGSVIELLLKEFKDKPTLLLgGGGYNHT 281
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
 486-762 7.67e-22

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: 97.53  E-value: 7.67e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  486 YDQQMMDHHnlWDNYHPEMPQRIHFIMHHLDELGLAKRCHSLPARPATDAELLTCHSAEHLERLRATEKMKTRELRREGA 565
Cdd:cd11598      5 FNSRVEDYH--FGRTHPMKPFRLTLTKHLVMGYGLHKAMDTYEARAATREELRQFHDADYLDFLSKVSPENANQLRFDKA 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  566 ---NYDS---IYICSSTFACaqlaagaacRLVEAVLAG--EVLNG---VAVVRPPG-HHAEPDAACGFCFFNSVAVAArh 633
Cdd:cd11598     83 epfNIGDdcpVFDGMYDYCQ---------LYAGASLDAarKLCSGqsdIAINWSGGlHHAKKSEASGFCYVNDIVLAI-- 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  634 AQAISGHAlRILIVDWDIHHGNGTQHIFEEDPSVLYISLHRYDhGTFFPmgNEGACTRIGKATGTGFTVNVAWNGPrMGD 713
Cdd:cd11598    152 LNLLRYFP-RVLYIDIDVHHGDGVEEAFYRTDRVMTLSFHKYN-GEFFP--GTGDLDDNGGTPGKHFALNVPLEDG-IDD 226

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1387293808  714 ADYLAAWHRLVLPVAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAH 762
Cdd:cd11598    227 EQYNLLFKSIIGPTIEKFQPSAIVLQCGADSLGGDRLGQFNLNIKAHGA 275
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
 90-392 4.86e-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: 96.42  E-value: 4.86e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808   90 FDEQLNEFHclWDDSFPERPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETT------QYMNEEE 163
Cdd:cd10004      8 YDSDVGNYA--YGPGHPMKPHRIRMAHSLVMNYGLYKKMEIYRAKPATKNEMTQFHTDEYIDFLSRVtpdnmeKFQKEQV 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  164 LHVLAD---TYDSVYLHpnsytCACLASGSVlrlvDAVLEAEIRNGMAIIRPPG--HHAQHSLMDGYCMFNHVAVAARYA 238
Cdd:cd10004     86 KYNVGDdcpVFDGLFEF-----CSISAGGSM----EGAARLNRGKCDIAVNWAGglHHAKKSEASGFCYVNDIVLGILEL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  239 QQKHdiQRVLIVDWDVHHGQGIQFAFDQDPSVLYFSIHRYeqGRFWP---HLKasnwsTTGLGQGQGYTINVPWNQvGMQ 315
Cdd:cd10004    157 LRYH--QRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKY--GEYFPgtgELR-----DIGIGTGKNYAVNVPLRD-GID 226

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387293808  316 DADYIAAFLHVLLPVAFEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAEGKLILSlEGGYNLHSLA 392
Cdd:cd10004    227 DESYKSIFEPVIKHVMEWYQPEAVVLQCGGDSLSGDRLGCFNLSMKGHANCVNFVKSFNLPMLVLG-GGGYTMRNVA 302
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
 107-399 1.89e-20

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


Pssm-ID: 212522 [Multi-domain]  Cd Length: 353  Bit Score: 94.44  E-value: 1.89e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  107 ERPERLHAIKeqliqeglldrcVSFQARFAEKEElmlvhSLEYIDLMETTQYMNEEELHVLADTYDS--VYLHPNSYTCA 184
Cdd:cd09998     24 ERPERLRASV------------LGLSAAVHGSKW-----SAELIEMCDMAEAKLAKGESEIPAHLPQgdLYLCPESLDAI 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  185 CLASGSVLRLVDAVLEAEI---RNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHDIQRVLIVDWDVHHGQGIQ 261
Cdd:cd09998     87 QGALGAVCEAVDSVFKPESpgtKRAFVAIRPPGHHCSESTPSGFCWVNNVHVGAAHAYLTHGITRVVILDIDLHHGNGTQ 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  262 --------FAFDQD----------------PSVLYFSIHRY-----EQGrFWPHLKASNWSTTGLgQGQgytiNVpWNqV 312
Cdd:cd09998    167 diawrinaEANKQAlesssyddfkpagapgLRIFYSSLHDInsfpcEDG-DPAKVKDASVSIDGA-HGQ----WI-WN-V 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  313 GMQ----DADYIAAF---LHVLLPVAFEF-------QPQ--LVLVAAGFDALQGDPKGeMA----ATPAGF-AQLT---- 367
Cdd:cd09998    239 HLQpwttEEDFWELYypkYRILFEKAAEFlrlttaaTPFktLVFISAGFDASEHEYES-MQrhgvNVPTSFyYRFArdav 317

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1387293808  368 HLLMGLAEGKLILSLEGGYNLHSLAEGVSATL 399
Cdd:cd09998    318 RFADAHAHGRLISVLEGGYSDRALCSGVLAHL 349
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
 481-805 4.14e-20

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: 93.72  E-value: 4.14e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  481 RTGLVYDQQMMDHHnlWDNYHPEMPQRIHFIMHHLDELGLAKRCHSLPARPATDAELLTCHSAEHLERLRATEKMKTREL 560
Cdd:cd10004      3 KVAYFYDSDVGNYA--YGPGHPMKPHRIRMAHSLVMNYGLYKKMEIYRAKPATKNEMTQFHTDEYIDFLSRVTPDNMEKF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  561 RREGANY---------DSIY-ICSstfacaqlaagaacrlveaVLAGEVLNG----------VAVVRPPG-HHAEPDAAC 619
Cdd:cd10004     81 QKEQVKYnvgddcpvfDGLFeFCS-------------------ISAGGSMEGaarlnrgkcdIAVNWAGGlHHAKKSEAS 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  620 GFCFFNSVAVAA----RHAQaisghalRILIVDWDIHHGNGTQHIFEEDPSVLYISLHRYdhGTFFPmgNEGACTRIGKA 695
Cdd:cd10004    142 GFCYVNDIVLGIlellRYHQ-------RVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKY--GEYFP--GTGELRDIGIG 210

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  696 TGTGFTVNVAWngpRMG--DADYLAAWHRLVLPVAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLThQLMGLANG 773
Cdd:cd10004    211 TGKNYAVNVPL---RDGidDESYKSIFEPVIKHVMEWYQPEAVVLQCGGDSLSGDRLGCFNLSMKGHANCV-NFVKSFNL 286

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1387293808  774 HIILILEGGYNLTSISESMAACTRSLLGDPLP 805
Cdd:cd10004    287 PMLVLGGGGYTMRNVARTWAFETGLLAGEELD 318
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
 501-805 6.68e-18

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: 87.04  E-value: 6.68e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  501 HPEMPQRIHFIMHHLDELGLAKRCHSLPARPATDAELLTCHSAEHLERLRATEKMKTRELRREGANYDSIYICSstfacA 580
Cdd:cd10010     25 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCP-----V 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  581 QLAAGAACRL------VEAVLAGEVLNGVAVVRPPG-HHAEPDAACGFCFFNSVAVAArhAQAISGHAlRILIVDWDIHH 653
Cdd:cd10010    100 FDGLFEFCQLsaggsvASAVKLNKQQTDIAVNWAGGlHHAKKSEASGFCYVNDIVLAI--LELLKYHQ-RVLYIDIDIHH 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  654 GNGTQHIFEEDPSVLYISLHRYdhGTFFPmgNEGACTRIGKATGTGFTVNVAWNGPrMGDADYLAAWHRLVLPVAYEFNP 733
Cdd:cd10010    177 GDGVEEAFYTTDRVMTVSFHKY--GEYFP--GTGDLRDIGAGKGKYYAVNYPLRDG-IDDESYEAIFKPVMSKVMEMFQP 251

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387293808  734 ELVLVSAGFDAARGDPLGGCQVSPEGYAHLThQLMGLANGHIILILEGGYNLTSISESMAACTRSLLGDPLP 805
Cdd:cd10010    252 SAVVLQCGADSLSGDRLGCFNLTIKGHAKCV-EFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDSEIP 322
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
 570-793 1.09e-17

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: 85.97  E-value: 1.09e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  570 IYICSSTFACAQLAAGAACRLVEAVLAGEVL---NGVAVVRPPGHHAEPDAACGFCFFNSVAVAARHaqAISGHAL-RIL 645
Cdd:cd09998     76 LYLCPESLDAIQGALGAVCEAVDSVFKPESPgtkRAFVAIRPPGHHCSESTPSGFCWVNNVHVGAAH--AYLTHGItRVV 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  646 IVDWDIHHGNGTQHI------------------------FEEDPSVLYISLHryDHGTF-----FPMGNEGACTRIGKAT 696
Cdd:cd09998    154 ILDIDLHHGNGTQDIawrinaeankqalesssyddfkpaGAPGLRIFYSSLH--DINSFpcedgDPAKVKDASVSIDGAH 231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  697 GTgftvNVaWN---GPRMGDADY---LAAWHRLVLPVAYEF-------NPE--LVLVSAGFDAARGDPLG----GCQVSP 757
Cdd:cd09998    232 GQ----WI-WNvhlQPWTTEEDFwelYYPKYRILFEKAAEFlrlttaaTPFktLVFISAGFDASEHEYESmqrhGVNVPT 306

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1387293808  758 EGYAHLTHQLMGLA----NGHIILILEGGYNLTSI-SESMA 793
Cdd:cd09998    307 SFYYRFARDAVRFAdahaHGRLISVLEGGYSDRALcSGVLA 347
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
 106-392 1.29e-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: 1.29e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  106 PERPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEEE-------LHVLAD--TYDSVYL 176
Cdd:cd10011     22 PMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEyskqmqrFNVGEDcpVFDGLFE 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  177 HpnsytCACLASGSVlrlVDAVLEAEIRNGMAIIRPPG-HHAQHSLMDGYCMFNHVAVAARYAQQKHdiQRVLIVDWDVH 255
Cdd:cd10011    102 F-----CQLSTGGSV---AGAVKLNRQQTDMAVNWAGGlHHAKKSEASGFCYVNDIVLAILELLKYH--QRVLYIDIDIH 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  256 HGQGIQFAFDQDPSVLyfSIHRYEQGRFWPhlKASNWSTTGLGQGQGYTINVPWNQvGMQDADYIAAFLHVLLPVAFEFQ 335
Cdd:cd10011    172 HGDGVEEAFYTTDRVM--TVSFHKYGEYFP--GTGDLRDIGAGKGKYYAVNFPMRD-GIDDESYGQIFKPIISKVMEMYQ 246

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1387293808  336 PQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAEGKLILSlEGGYNLHSLA 392
Cdd:cd10011    247 PSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLG-GGGYTIRNVA 302
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
 90-392 1.70e-17

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: 85.91  E-value: 1.70e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808   90 FDEQLNEFHclWDDSFPERPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLME--TTQYMNE-----E 162
Cdd:cd10005      7 YDPDVGNFH--YGPGHPMKPHRLALTHSLVLHYGLYKKMQVYKPYRASAHDMCRFHSEDYIDFLQrvTPQNIQGftkslN 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  163 ELHVLAD--TYDSVYLHPNSYTCACLASGSVL--RLVDavleaeirngMAIIRPPG-HHAQHSLMDGYCMFNHVAVAARY 237
Cdd:cd10005     85 QFNVGDDcpVFPGLFDFCSMYTGASLEGATKLnhKICD----------IAINWSGGlHHAKKFEASGFCYVNDIVIAILE 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  238 AQQKHdiQRVLIVDWDVHHGQGIQFAFDQDPSVLYFSIHRYeQGRFWPhlKASNWSTTGLGQGQGYTINVPWNQvGMQDA 317
Cdd:cd10005    155 LLKYH--PRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKY-GNYFFP--GTGDMYEVGAESGRYYSVNVPLKD-GIDDQ 228

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387293808  318 DYIAAFLHVLLPVAFEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAEGKLILSlEGGYNLHSLA 392
Cdd:cd10005    229 SYLQLFKPVIQQVIDFYQPTCIVLQCGADSLGCDRLGCFNLSIKGHGECVEFVKSFNIPLLVLG-GGGYTVRNVA 302
PTZ00063 PTZ00063
histone deacetylase; Provisional
 611-801 3.15e-16

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 82.55  E-value: 3.15e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  611 HHAEPDAACGFCFFNSVAVAArhAQAISGHAlRILIVDWDIHHGNGTQHIFEEDPSVLYISLHRYdhGTFFPmgNEGACT 690
Cdd:PTZ00063   137 HHAKRSEASGFCYINDIVLGI--LELLKYHA-RVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFP--GTGDVT 209

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  691 RIGKATGTGFTVNVAWNGPrMGDADYLAAWHRLVLPVAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHQLMGL 770
Cdd:PTZ00063   210 DIGVAQGKYYSVNVPLNDG-IDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAACVEFVRSL 288

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1387293808  771 aNGHIILILEGGYNLTSISESMAACTRSLLG 801
Cdd:PTZ00063   289 -NIPLLVLGGGGYTIRNVARCWAYETGVILN 318
PTZ00063 PTZ00063
histone deacetylase; Provisional
 215-409 3.86e-16

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 82.17  E-value: 3.86e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  215 HHAQHSLMDGYCMFNHVAVAARYAQQKHdiQRVLIVDWDVHHGQGIQFAFDQDPSVLYFSIHRYeqGRFWPhlKASNWST 294
Cdd:PTZ00063   137 HHAKRSEASGFCYINDIVLGILELLKYH--ARVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFP--GTGDVTD 210

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  295 TGLGQGQGYTINVPWNQvGMQDADYIAAFLHVLLPVAFEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLA 374
Cdd:PTZ00063   211 IGVAQGKYYSVNVPLND-GIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAACVEFVRSLN 289

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1387293808  375 EGKLILSlEGGYNLHSLAE------GVSATLHTLLGDPCPV 409
Cdd:PTZ00063   290 IPLLVLG-GGGYTIRNVARcwayetGVILNKHDEMSDQISL 329
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
1046-1094 1.43e-15

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 71.63  E-value: 1.43e-15
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 1387293808  1046 PCQDCGTLQENWVCLSCYQVYCGRYINAHMLQHHEGSGHPLVLSYADLS 1094
Cdd:smart00290    1 RCSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLGTQR 49
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
 481-805 6.68e-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: 77.82  E-value: 6.68e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  481 RTGLVYDQQMMDHHnlWDNYHPEMPQRIHFIMHHLDELGLAKRCHSLPARPATDAELLTCHSAEHLERLRATEKMKTREL 560
Cdd:cd10005      2 RVAYFYDPDVGNFH--YGPGHPMKPHRLALTHSLVLHYGLYKKMQVYKPYRASAHDMCRFHSEDYIDFLQRVTPQNIQGF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  561 RREGANY---------DSIY-ICSstfacaqlaagaacRLVEAVLAGEV-LNG----VAVVRPPG-HHAEPDAACGFCFF 624
Cdd:cd10005     80 TKSLNQFnvgddcpvfPGLFdFCS--------------MYTGASLEGATkLNHkicdIAINWSGGlHHAKKFEASGFCYV 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  625 NSVAVAArhAQAISGHAlRILIVDWDIHHGNGTQHIFEEDPSVLYISLHRYDhGTFFPmgNEGACTRIGKATGTGFTVNV 704
Cdd:cd10005    146 NDIVIAI--LELLKYHP-RVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYG-NYFFP--GTGDMYEVGAESGRYYSVNV 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  705 AW-NGprMGDADYLAAWHRLVLPVAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHQLMGLaNGHIILILEGGY 783
Cdd:cd10005    220 PLkDG--IDDQSYLQLFKPVIQQVIDFYQPTCIVLQCGADSLGCDRLGCFNLSIKGHGECVEFVKSF-NIPLLVLGGGGY 296

                          330       340
                   ....*....|....*....|..
gi 1387293808  784 NLTSISESMAACTRSLLGDPLP 805
Cdd:cd10005    297 TVRNVARCWTYETSLLVDEEIS 318
PTZ00346 PTZ00346
histone deacetylase; Provisional
 215-425 2.59e-14

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 76.61  E-value: 2.59e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  215 HHAQHSLMDGYCMFNHVAVAARYAQQKHDiqRVLIVDWDVHHGQGIQFAFDQDPSVLYFSIHRYEQGrFWPhlKASNWST 294
Cdd:PTZ00346   154 HHSKCGECSGFCYVNDIVLGILELLKCHD--RVLYVDIDMHHGDGVDEAFCTSDRVFTLSLHKFGES-FFP--GTGHPRD 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  295 TGLGQGQGYTINVP-WNqvGMQDADYIAAFLHVLLPVAFEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGL 373
Cdd:PTZ00346   229 VGYGRGRYYSMNLAvWD--GITDFYYLGLFEHALHSIVRRYSPDAIVLQCGADSLAGDRLGLLNLSSFGHGQCVQAVRDL 306

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1387293808  374 AEGKLILSlEGGYNLHSLAEGVSATLHTLLGDPCPvlesPGAPCPSAQASLS 425
Cdd:PTZ00346   307 GIPMLALG-GGGYTIRNVAKLWAYETSILTGHPLP----PNTVLPVAEMPLS 353
PTZ00346 PTZ00346
histone deacetylase; Provisional
 611-816 3.23e-14

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 76.22  E-value: 3.23e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  611 HHAEPDAACGFCFFNSVAVAArhAQAISGHAlRILIVDWDIHHGNGTQHIFEEDPSVLYISLHRYDHgTFFPmgNEGACT 690
Cdd:PTZ00346   154 HHSKCGECSGFCYVNDIVLGI--LELLKCHD-RVLYVDIDMHHGDGVDEAFCTSDRVFTLSLHKFGE-SFFP--GTGHPR 227

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  691 RIGKATGTGFTVNVA-WNGprMGDADYLAAWHRLVLPVAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHQLMG 769
Cdd:PTZ00346   228 DVGYGRGRYYSMNLAvWDG--ITDFYYLGLFEHALHSIVRRYSPDAIVLQCGADSLAGDRLGLLNLSSFGHGQCVQAVRD 305

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1387293808  770 LanGHIILIL-EGGYNLTSISESMAACTRSLLGDPLPLLTRL---RPPLSG 816
Cdd:PTZ00346   306 L--GIPMLALgGGGYTIRNVAKLWAYETSILTGHPLPPNTVLpvaEMPLSG 354
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
 501-789 2.15e-13

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: 73.17  E-value: 2.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  501 HPEMPQRIHFIMHHLDELGLAKRCHSLPARPATDAELLTCHSAEHLERLRATEKMKTRELRREGANYDSIYICSstfacA 580
Cdd:cd10011     21 HPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNVGEDCP-----V 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  581 QLAAGAACRL-VEAVLAGEV-LN----GVAVVRPPG-HHAEPDAACGFCFFNSVAVAArhAQAISGHAlRILIVDWDIHH 653
Cdd:cd10011     96 FDGLFEFCQLsTGGSVAGAVkLNrqqtDMAVNWAGGlHHAKKSEASGFCYVNDIVLAI--LELLKYHQ-RVLYIDIDIHH 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  654 GNGTQHIFEEDPSVLYISlhRYDHGTFFPmgNEGACTRIGKATGTGFTVNVAWNGPrMGDADYLAAWHRLVLPVAYEFNP 733
Cdd:cd10011    173 GDGVEEAFYTTDRVMTVS--FHKYGEYFP--GTGDLRDIGAGKGKYYAVNFPMRDG-IDDESYGQIFKPIISKVMEMYQP 247

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1387293808  734 ELVLVSAGFDAARGDPLGGCQVSPEGYAHLThQLMGLANGHIILILEGGYNLTSIS 789
Cdd:cd10011    248 SAVVLQCGADSLSGDRLGCFNLTVKGHAKCV-EVVKTFNLPLLMLGGGGYTIRNVA 302
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 625-799 2.33e-09

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: 58.54  E-value: 2.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  625 NSVAVAArhAQAISGHALRILIVDWDIHHGNGTQ------------HIFEED--PSVLYISLHRYDHGTFFPMgnegact 690
Cdd:cd09987     35 HSIANGA--IRAVAELHPDLGVIDVDAHHDVRTPeafgkgnhhtprHLLCEPliSDVHIVSIGIRGVSNGEAG------- 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  691 riGKATGTGFTVNVAWNGPRmgDADYLAAWHRLVLPVayEFNPELVLVSAGFDAARGDPLGGCQ------VSPEGYAHLT 764
Cdd:cd09987    106 --GAYARKLGVVYFSMTEVD--KLGLGDVFEEIVSYL--GDKGDNVYLSVDVDGLDPSFAPGTGtpgpggLSYREGLYIT 179

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1387293808  765 HQLMGLANGHIILILEGGYNL---TSISESMAACTRSL 799
Cdd:cd09987    180 ERIAKTNLVVGLDIVEVNPLLdetGRTARLAAALTLEL 217
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 214-405 5.03e-06

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


Pssm-ID: 212513  Cd Length: 217  Bit Score: 48.91  E-value: 5.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  214 GHHAqhslmdgycMFNHVAVAAryAQQKhdiQRVLIVDWDVHHGQGIQFAF--------------DQDPSVLYFSIHRYE 279
Cdd:cd09987     33 GDHS---------IANGAIRAV--AELH---PDLGVIDVDAHHDVRTPEAFgkgnhhtprhllcePLISDVHIVSIGIRG 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  280 QGRFWPHLKasnwsttglGQGQGYTINVPWNQVGmqDADYIAAFLHVLLPVafEFQPQLVLVAAGFDALQGDPkGEMAAT 359
Cdd:cd09987     99 VSNGEAGGA---------YARKLGVVYFSMTEVD--KLGLGDVFEEIVSYL--GDKGDNVYLSVDVDGLDPSF-APGTGT 164

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1387293808  360 PAGFaqlthllmGLA--EGKLILSLEGGYNLHSLAEGVSatLHTLLGD 405
Cdd:cd09987    165 PGPG--------GLSyrEGLYITERIAKTNLVVGLDIVE--VNPLLDE 202
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
 865-989 4.58e-03

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 40.15  E-value: 4.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387293808  865 ANVTTTVEGNILETGMGQAAS--EASVKESTPDQTESATAPVELTQGQSSDTATQGAALDQTISEGATGGAELIQNPPAS 942
Cdd:cd06917    130 ANILVTNTGNVKLCDFGVAASlnQNSSKRSTFVGTPYWMAPEVITEGKYYDTKADIWSLGITTYEMATGNPPYSDVDALR 209

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1387293808  943 C---INNRIPPALPVQGAtaqtspSKLMANLRILDLDSTTQEPSEEEGLL 989
Cdd:cd06917    210 AvmlIPKSKPPRLEGNGY------SPLLKEFVAACLDEEPKDRLSADELL 253
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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