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Conserved domains on  [gi|967505306|ref|XP_014982810|]
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histone deacetylase 6 isoform X1 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
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: 665.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   99 CLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHP 178
Cdd:cd11682     1 CLWDESFPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYVALMKSTQYMTEEELRTLADTYDSVYLHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  179 NSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQ 258
Cdd:cd11682    81 NSYSCACLAVGSVLQLVDKVLGGEIRNGLAIVRPPGHHAQHDKMDGYCMFNNVAIAARYAQQKHGVQRVLIVDWDVHHGQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  259 GTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQL 338
Cdd:cd11682   161 GTQFIFEQDPSVLYFSIHRYEQGRFWPHLKESDSSAVGFGRGEGYNINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  339 VLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCR 418
Cdd:cd11682   241 VLVAAGFDAVIGDPKGEMAATPACFAHLTHLLMGLAGGKLILSLEGGYNLRSLAEGVCASLKALLGDPCPMLESPGAPCR 320
                         330
                  ....*....|....*..
gi 967505306  419 SAQASVSCALEALEPFW 435
Cdd:cd11682   321 SALASVSCTISALEPFW 337
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
489-839 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: 658.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  489 YDQSMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESS 568
Cdd:cd10003     1 YDQRMMNHHNLWDPGHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHLDEMKSLEKMKPRELNRLGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  569 NFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQAISGrALRIL 648
Cdd:cd10003    81 EYDSIYIHPDSYQCALLAAGCVLQVVEAVLTGESRNGVAIVRPPGHHAEQDTACGFCFFNNVAIAARYAQKKYG-LKRIL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  649 IVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVL 728
Cdd:cd10003   160 IVDWDVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSPEGNYDVVGKGKGEGFNVNIPWNKGGMGDAEYIAAFQQVVL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  729 PIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPP 808
Cdd:cd10003   240 PIAYEFNPELVLVSAGFDAARGDPLGGCKVTPEGYAHMTHMLMSLAGGRVIVILEGGYNLTSISESMSMCTKTLLGDPPP 319
                         330       340       350
                  ....*....|....*....|....*....|.
gi 967505306  809 LLTLPRPPLSGALASITETIQVHRRYWRSLR 839
Cdd:cd10003   320 VLDLPRPPCSSALKSINNVLQVHQKYWKSLR 350
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
1137-1199 1.70e-25

Zn-finger in ubiquitin-hydrolases and other protein;


:

Pssm-ID: 460464  Cd Length: 63  Bit Score: 100.41  E-value: 1.70e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 967505306  1137 CGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHENSGHPLVLSYIDLSTWCYYCQAYVHHQAL 1199
Cdd:pfam02148    1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPSL 63
DUF5585 super family cl39316
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
887-1049 2.11e-06

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


The actual alignment was detected with superfamily member pfam17823:

Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 51.88  E-value: 2.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   887 TSASSGEESTPGQTKSETAVVALTQDQSSEAATGGATLAQTISEAavggamlgQTTSEEAVGGATPDQTTSEKTVGGATL 966
Cdd:pfam17823  165 ASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPA--------RGISTAATATGHPAAGTALAAVGNSSP 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   967 DQTTSEDAVGgatlgqTTSEEAVGG-ATLAQTTSEAAMEGATLDQTTSEEAPGGTeliqTPLASSTDHQTPPTSP-VQGT 1044
Cdd:pfam17823  237 AAGTVTAAVG------TVTPAALATlAAAAGTVASAAGTINMGDPHARRLSPAKH----MPSDTMARNPAAPMGAqAQGP 306

                   ....*
gi 967505306  1045 TPQIS 1049
Cdd:pfam17823  307 IIQVS 311
 
Name Accession Description Interval E-value
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: 665.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   99 CLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHP 178
Cdd:cd11682     1 CLWDESFPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYVALMKSTQYMTEEELRTLADTYDSVYLHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  179 NSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQ 258
Cdd:cd11682    81 NSYSCACLAVGSVLQLVDKVLGGEIRNGLAIVRPPGHHAQHDKMDGYCMFNNVAIAARYAQQKHGVQRVLIVDWDVHHGQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  259 GTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQL 338
Cdd:cd11682   161 GTQFIFEQDPSVLYFSIHRYEQGRFWPHLKESDSSAVGFGRGEGYNINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  339 VLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCR 418
Cdd:cd11682   241 VLVAAGFDAVIGDPKGEMAATPACFAHLTHLLMGLAGGKLILSLEGGYNLRSLAEGVCASLKALLGDPCPMLESPGAPCR 320
                         330
                  ....*....|....*..
gi 967505306  419 SAQASVSCALEALEPFW 435
Cdd:cd11682   321 SALASVSCTISALEPFW 337
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
489-839 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: 658.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  489 YDQSMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESS 568
Cdd:cd10003     1 YDQRMMNHHNLWDPGHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHLDEMKSLEKMKPRELNRLGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  569 NFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQAISGrALRIL 648
Cdd:cd10003    81 EYDSIYIHPDSYQCALLAAGCVLQVVEAVLTGESRNGVAIVRPPGHHAEQDTACGFCFFNNVAIAARYAQKKYG-LKRIL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  649 IVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVL 728
Cdd:cd10003   160 IVDWDVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSPEGNYDVVGKGKGEGFNVNIPWNKGGMGDAEYIAAFQQVVL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  729 PIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPP 808
Cdd:cd10003   240 PIAYEFNPELVLVSAGFDAARGDPLGGCKVTPEGYAHMTHMLMSLAGGRVIVILEGGYNLTSISESMSMCTKTLLGDPPP 319
                         330       340       350
                  ....*....|....*....|....*....|.
gi 967505306  809 LLTLPRPPLSGALASITETIQVHRRYWRSLR 839
Cdd:cd10003   320 VLDLPRPPCSSALKSINNVLQVHQKYWKSLR 350
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
504-800 4.78e-130

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: 400.07  E-value: 4.78e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   504 HPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLR-ATEKMKTRELHRESSNFDSIYICPSTFAC 582
Cdd:pfam00850    1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEeAAPEGGALLLLSYLSGDDDTPVSPGSYEA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   583 AQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQAISGRAlRILIVDWDVHHGNGTQH 662
Cdd:pfam00850   81 ALLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLK-RVAIVDFDVHHGNGTQE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   663 MFEDDPSVLYVSLHRYdHGTFFPMgdEGASSQIGRAAGTGFTVNVAWNgPRMGDADYLAAWHRLVLPIAYEFNPELVLVS 742
Cdd:pfam00850  160 IFYDDPSVLTLSIHQY-PGGFYPG--TGFADETGEGKGKGYTLNVPLP-PGTGDAEYLAAFEEILLPALEEFQPDLILVS 235
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 967505306   743 AGFDAARGDPLGGCQVSPEGYAHLTHLLMGLA---SGRIILILEGGYNLTSISESMAACTR 800
Cdd:pfam00850  236 AGFDAHAGDPLGGLNLTTEGFAEITRILLELAdplCIRVVSVLEGGYNLDALARSATAVLA 296
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
106-402 1.67e-111

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: 350.77  E-value: 1.67e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   106 PEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYID-LMETTQYMNEGELRVLADTYDSVYLHPNSYSCA 184
Cdd:pfam00850    2 PENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEfLEEAAPEGGALLLLSYLSGDDDTPVSPGSYEAA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   185 CLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTF 264
Cdd:pfam00850   82 LLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLKRVAIVDFDVHHGNGTQEIF 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   265 DQDPSVLYFSIHRYEqGRFWPHLkaSNWSTTGFGQGQGYTINVPWNqVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAG 344
Cdd:pfam00850  162 YDDPSVLTLSIHQYP-GGFYPGT--GFADETGEGKGKGYTLNVPLP-PGTGDAEYLAAFEEILLPALEEFQPDLILVSAG 237
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 967505306   345 FDALQGDPKGEMAATPAGFAQLTHLLMGLA---GGKLILSLEGGYNLRALAEGVSASLHTL 402
Cdd:pfam00850  238 FDAHAGDPLGGLNLTTEGFAEITRILLELAdplCIRVVSVLEGGYNLDALARSATAVLAAL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
485-797 1.04e-103

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 330.15  E-value: 1.04e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  485 TGLVYDQSMMNHcNLWDsHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVghlratEKMKTRELH 564
Cdd:COG0123     1 TALIYHPDYLLH-DLGP-GHPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYV------DALRAASLD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  565 RESSNFDSI-YICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQAisGR 643
Cdd:COG0123    73 GGYGQLDPDtPVSPGTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGFCLFNNAAIAARYLLA--KG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  644 ALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDhgtFFPMgdEGASSQIGRAAGTGFTVNVAWnGPRMGDADYLAAW 723
Cdd:COG0123   151 LERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQDP---LYPG--TGAADETGEGAGEGSNLNVPL-PPGTGDAEYLAAL 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 967505306  724 HRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLA---SGRIILILEGGYNLTSISESMAA 797
Cdd:COG0123   225 EEALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELAdhcGGPVVSVLEGGYNLDALARSVAA 301
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
106-404 2.17e-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: 312.81  E-value: 2.17e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  106 PEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYmNEGELRVLADTYdsvyLHPNSYSCAC 185
Cdd:COG0123    19 PEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAASL-DGGYGQLDPDTP----VSPGTWEAAL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  186 LASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAqQKHRIRRVLIVDWDVHHGQGTQFTFD 265
Cdd:COG0123    94 LAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGFCLFNNAAIAARYL-LAKGLERVAIVDFDVHHGNGTQDIFY 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  266 QDPSVLYFSIHryeQGRFWPHLKASnwSTTGFGQGQGYTINVPwnqV--GMRDADYIAAFLHVLLPVALEFQPQLVLVAA 343
Cdd:COG0123   173 DDPDVLTISIH---QDPLYPGTGAA--DETGEGAGEGSNLNVP---LppGTGDAEYLAALEEALLPALEAFKPDLIVVSA 244
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 967505306  344 GFDALQGDPKGEMAATPAGFAQLTHLLMGLA---GGKLILSLEGGYNLRALAEGVSASLHTLLG 404
Cdd:COG0123   245 GFDAHADDPLGRLNLTTEGYAWRTRRVLELAdhcGGPVVSVLEGGYNLDALARSVAAHLETLLG 308
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
1137-1199 1.70e-25

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 100.41  E-value: 1.70e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 967505306  1137 CGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHENSGHPLVLSYIDLSTWCYYCQAYVHHQAL 1199
Cdd:pfam02148    1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPSL 63
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
1136-1185 2.07e-18

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 79.72  E-value: 2.07e-18
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 967505306   1136 PCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHENSGHPLVLSYIDLST 1185
Cdd:smart00290    1 RCSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
PTZ00063 PTZ00063
histone deacetylase; Provisional
504-796 1.81e-17

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 86.40  E-value: 1.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  504 HPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRE----LHR----ESSN---FDS 572
Cdd:PTZ00063   23 HPMKPQRIRMAHALILSYDLYKHMEIYRPHKSVEPELVLFHDEEYVDFLSSISPENYRDftyqLKRfnvgEATDcpvFDG 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  573 IYicpsTF--ACAQLATGAACRL------VEAVLSGEVlngaavvrppgHHAEQDAACGFCFFNSVAVA-----ARHAqa 639
Cdd:PTZ00063  103 LF----EFqqSCAGASIDGAYKLnnhqadICVNWSGGL-----------HHAKRSEASGFCYINDIVLGilellKYHA-- 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  640 isgralRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYdhGTFFPmgDEGASSQIGRAAGTGFTVNVAWNGPrMGDADY 719
Cdd:PTZ00063  166 ------RVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFP--GTGDVTDIGVAQGKYYSVNVPLNDG-IDDDSF 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 967505306  720 LAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILiLEGGYNLTSISESMA 796
Cdd:PTZ00063  235 VDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAACVEFVRSLNIPLLVL-GGGGYTIRNVARCWA 310
PTZ00063 PTZ00063
histone deacetylase; Provisional
215-409 9.36e-16

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 81.40  E-value: 9.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  215 HHAQHSLMDGYCMFNHVAVAARYAQQKHRirRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYeqGRFWPhlKASNWST 294
Cdd:PTZ00063  137 HHAKRSEASGFCYINDIVLGILELLKYHA--RVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFP--GTGDVTD 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  295 TGFGQGQGYTINVPWNQvGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLA 374
Cdd:PTZ00063  211 IGVAQGKYYSVNVPLND-GIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAACVEFVRSLN 289
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 967505306  375 GGKLILSlEGGYNLRALAE------GVSASLHTLLGDPCPM 409
Cdd:PTZ00063  290 IPLLVLG-GGGYTIRNVARcwayetGVILNKHDEMSDQISL 329
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
887-1049 2.11e-06

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 51.88  E-value: 2.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   887 TSASSGEESTPGQTKSETAVVALTQDQSSEAATGGATLAQTISEAavggamlgQTTSEEAVGGATPDQTTSEKTVGGATL 966
Cdd:pfam17823  165 ASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPA--------RGISTAATATGHPAAGTALAAVGNSSP 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   967 DQTTSEDAVGgatlgqTTSEEAVGG-ATLAQTTSEAAMEGATLDQTTSEEAPGGTeliqTPLASSTDHQTPPTSP-VQGT 1044
Cdd:pfam17823  237 AAGTVTAAVG------TVTPAALATlAAAAGTVASAAGTINMGDPHARRLSPAKH----MPSDTMARNPAAPMGAqAQGP 306

                   ....*
gi 967505306  1045 TPQIS 1049
Cdd:pfam17823  307 IIQVS 311
PRK11907 PRK11907
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
928-1045 2.01e-03

bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;


Pssm-ID: 237019 [Multi-domain]  Cd Length: 814  Bit Score: 42.53  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  928 ISEAAVGGAMLGQTTSEEAVGGATPDQTTSEKTvgGATLDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAmegat 1007
Cdd:PRK11907    6 FSKSAVALTLALLTASNPKLAQAEEIVTTTPAT--STEAEQTTPVESDATEEADNTETPVAATTAAEAPSSSETA----- 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 967505306 1008 ldqTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTT 1045
Cdd:PRK11907   79 ---ETSDPTSEATDTTTSEARTVTPAATETSKPVEGQT 113
 
Name Accession Description Interval E-value
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: 665.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   99 CLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHP 178
Cdd:cd11682     1 CLWDESFPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYVALMKSTQYMTEEELRTLADTYDSVYLHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  179 NSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQ 258
Cdd:cd11682    81 NSYSCACLAVGSVLQLVDKVLGGEIRNGLAIVRPPGHHAQHDKMDGYCMFNNVAIAARYAQQKHGVQRVLIVDWDVHHGQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  259 GTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQL 338
Cdd:cd11682   161 GTQFIFEQDPSVLYFSIHRYEQGRFWPHLKESDSSAVGFGRGEGYNINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  339 VLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCR 418
Cdd:cd11682   241 VLVAAGFDAVIGDPKGEMAATPACFAHLTHLLMGLAGGKLILSLEGGYNLRSLAEGVCASLKALLGDPCPMLESPGAPCR 320
                         330
                  ....*....|....*..
gi 967505306  419 SAQASVSCALEALEPFW 435
Cdd:cd11682   321 SALASVSCTISALEPFW 337
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
489-839 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: 658.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  489 YDQSMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESS 568
Cdd:cd10003     1 YDQRMMNHHNLWDPGHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHLDEMKSLEKMKPRELNRLGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  569 NFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQAISGrALRIL 648
Cdd:cd10003    81 EYDSIYIHPDSYQCALLAAGCVLQVVEAVLTGESRNGVAIVRPPGHHAEQDTACGFCFFNNVAIAARYAQKKYG-LKRIL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  649 IVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVL 728
Cdd:cd10003   160 IVDWDVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSPEGNYDVVGKGKGEGFNVNIPWNKGGMGDAEYIAAFQQVVL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  729 PIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPP 808
Cdd:cd10003   240 PIAYEFNPELVLVSAGFDAARGDPLGGCKVTPEGYAHMTHMLMSLAGGRVIVILEGGYNLTSISESMSMCTKTLLGDPPP 319
                         330       340       350
                  ....*....|....*....|....*....|.
gi 967505306  809 LLTLPRPPLSGALASITETIQVHRRYWRSLR 839
Cdd:cd10003   320 VLDLPRPPCSSALKSINNVLQVHQKYWKSLR 350
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: 580.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   99 CLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHP 178
Cdd:cd10002     1 CNWDSNHIECPERLEAILERLTQDGLLERCVKIPAREAEEDEILLVHSQEYIDLVKSTETMEKEELESLCSGYDSVYLCP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  179 NSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQ 258
Cdd:cd10002    81 STYEAARLAAGSTIELVKAVMAGKIQNGFALIRPPGHHAMRNEANGYCIFNNVAIAAKYAIEKLGLKRILIVDWDVHHGQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  259 GTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQL 338
Cdd:cd10002   161 GTQQGFYEDPRVLYFSIHRYEHGRFWPHLFESDYDYIGVGHGYGFNVNVPLNQTGLGDADYLAIFHHILLPLALEFQPEL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  339 VLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLEsPGAPCR 418
Cdd:cd10002   241 VLVSAGFDASIGDPEGEMAVTPAGYAHLTRLLMGLAGGKLLLVLEGGYLLESLAESVSMTLRGLLGDPLPPLA-PPIPIR 319
                         330
                  ....*....|....*..
gi 967505306  419 SAQASVSCALEALEPFW 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 ...
91-438 1.92e-161

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: 484.53  E-value: 1.92e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   91 DEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADT 170
Cdd:cd10003     2 DQRMMNHHNLWDPGHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHLDEMKSLEKMKPRELNRLGKE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  171 YDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIV 250
Cdd:cd10003    82 YDSIYIHPDSYQCALLAAGCVLQVVEAVLTGESRNGVAIVRPPGHHAEQDTACGFCFFNNVAIAARYAQKKYGLKRILIV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  251 DWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPV 330
Cdd:cd10003   162 DWDVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSPEGNYDVVGKGKGEGFNVNIPWNKGGMGDAEYIAAFQQVVLPI 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  331 ALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPML 410
Cdd:cd10003   242 AYEFNPELVLVSAGFDAARGDPLGGCKVTPEGYAHMTHMLMSLAGGRVIVILEGGYNLTSISESMSMCTKTLLGDPPPVL 321
                         330       340
                  ....*....|....*....|....*...
gi 967505306  411 ESPGAPCRSAQASVSCALEALEPFWEVL 438
Cdd:cd10003   322 DLPRPPCSSALKSINNVLQVHQKYWKSL 349
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
101-435 2.76e-147

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: 447.00  E-value: 2.76e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  101 WDDSF--PEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHP 178
Cdd:cd11683     1 WDDPEceIEVPERLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRETQVMNKEELMAISGKYDAVYFHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  179 NSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQ 258
Cdd:cd11683    81 NTFHCARLAAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYAKKKYGLHRILIVDWDVHHGQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  259 GTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQL 338
Cdd:cd11683   161 GIQYIFEEDPSVLYFSWHRYEHQRFWPFLRESDYDAVGRGKGLGFNINLPWNKVGMGNADYLAAFFHVLLPLAFEFDPEL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  339 VLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCR 418
Cdd:cd11683   241 VLVSAGFDSAIGDPEGQMCATPECFAHLTHLLMVLAGGKLCAVLEGGYHLESLAESVCMTVQTLLGDPLPRLSGEMTPCQ 320
                         330
                  ....*....|....*..
gi 967505306  419 SAQASVSCALEALEPFW 435
Cdd:cd11683   321 SALESIQNVRAAQAPYW 337
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
504-801 4.62e-141

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: 428.84  E-value: 4.62e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  504 HPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHressnfDSIYICPSTFACA 583
Cdd:cd09992     1 HPERPERLLAILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYIERVEETCEAGGGYLD------PDTYVSPGSYEAA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  584 QLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQAISGRAlRILIVDWDVHHGNGTQHM 663
Cdd:cd09992    75 LLAAGAALAAVDAVLSGEAENAFALVRPPGHHAEPDRAMGFCLFNNVAIAARYAQKRYGLK-RVLIVDWDVHHGNGTQDI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  664 FEDDPSVLYVSLHRYDhgtFFPMGdeGASSQIGRAAGTGFTVNVAWNgPRMGDADYLAAWHRLVLPIAYEFNPELVLVSA 743
Cdd:cd09992   154 FYDDPSVLYFSIHQYP---FYPGT--GAAEETGGGAGEGFTINVPLP-PGSGDAEYLAAFEEVLLPIAREFQPDLVLVSA 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 967505306  744 GFDAARGDPLGGCQVSPEGYAHLTHLLMGLAS----GRIILILEGGYNLTSISESMAACTRS 801
Cdd:cd09992   228 GFDAHRGDPLGGMNLTPEGYARLTRLLKELADehcgGRLVFVLEGGYNLEALAESVLAVLEA 289
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
503-801 1.41e-139

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: 425.60  E-value: 1.41e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  503 HHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNF--DSIYICPSTF 580
Cdd:cd11600     2 PHPEDPSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEHWDRVEATEKMSDEQLKDRTEIFerDSLYVNNDTA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  581 ACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQAI-SGRALRILIVDWDVHHGNG 659
Cdd:cd11600    82 FCARLSCGGAIEACRAVAEGRVKNAFAVVRPPGHHAEPDESMGFCFFNNVAVAAKWLQTEyPDKIKKILILDWDIHHGNG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  660 TQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELV 739
Cdd:cd11600   162 TQRAFYDDPNVLYISLHRFENGGFYPGTPYGDYESVGEGAGLGFNVNIPWPQGGMGDADYIYAFQRIVMPIAYEFDPDLV 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 967505306  740 LVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRS 801
Cdd:cd11600   242 IISAGFDAADGDELGQCHVTPAGYAHMTHMLMSLAGGKLVVALEGGYNLDAISDSALAVAKV 303
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
498-835 1.19e-137

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: 421.72  E-value: 1.19e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  498 NLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICP 577
Cdd:cd10002     1 CNWDSNHIECPERLEAILERLTQDGLLERCVKIPAREAEEDEILLVHSQEYIDLVKSTETMEKEELESLCSGYDSVYLCP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  578 STFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQAiSGRALRILIVDWDVHHG 657
Cdd:cd10002    81 STYEAARLAAGSTIELVKAVMAGKIQNGFALIRPPGHHAMRNEANGYCIFNNVAIAAKYAIE-KLGLKRILIVDWDVHHG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  658 NGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPE 737
Cdd:cd10002   160 QGTQQGFYEDPRVLYFSIHRYEHGRFWPHLFESDYDYIGVGHGYGFNVNVPLNQTGLGDADYLAIFHHILLPLALEFQPE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  738 LVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPL 817
Cdd:cd10002   240 LVLVSAGFDASIGDPEGEMAVTPAGYAHLTRLLMGLAGGKLLLVLEGGYLLESLAESVSMTLRGLLGDPLPPLAPPIPIR 319
                         330
                  ....*....|....*...
gi 967505306  818 SgALASITETIQVHRRYW 835
Cdd:cd10002   320 S-VLETILNAIAHLSPRW 336
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
106-403 1.40e-131

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


Pssm-ID: 212518 [Multi-domain]  Cd Length: 291  Bit Score: 403.80  E-value: 1.40e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  106 PEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELrvladtYDSVYLHPNSYSCAC 185
Cdd:cd09992     2 PERPERLLAILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYIERVEETCEAGGGYL------DPDTYVSPGSYEAAL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  186 LASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFD 265
Cdd:cd09992    76 LAAGAALAAVDAVLSGEAENAFALVRPPGHHAEPDRAMGFCLFNNVAIAARYAQKRYGLKRVLIVDWDVHHGNGTQDIFY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  266 QDPSVLYFSIHRYEqgrFWPHLKASNWstTGFGQGQGYTINVPWNQvGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGF 345
Cdd:cd09992   156 DDPSVLYFSIHQYP---FYPGTGAAEE--TGGGAGEGFTINVPLPP-GSGDAEYLAAFEEVLLPIAREFQPDLVLVSAGF 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 967505306  346 DALQGDPKGEMAATPAGFAQLTHLLMGLA----GGKLILSLEGGYNLRALAEGVSASLHTLL 403
Cdd:cd09992   230 DAHRGDPLGGMNLTPEGYARLTRLLKELAdehcGGRLVFVLEGGYNLEALAESVLAVLEALL 291
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
504-800 4.78e-130

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: 400.07  E-value: 4.78e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   504 HPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLR-ATEKMKTRELHRESSNFDSIYICPSTFAC 582
Cdd:pfam00850    1 HPENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEeAAPEGGALLLLSYLSGDDDTPVSPGSYEA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   583 AQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQAISGRAlRILIVDWDVHHGNGTQH 662
Cdd:pfam00850   81 ALLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLK-RVAIVDFDVHHGNGTQE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   663 MFEDDPSVLYVSLHRYdHGTFFPMgdEGASSQIGRAAGTGFTVNVAWNgPRMGDADYLAAWHRLVLPIAYEFNPELVLVS 742
Cdd:pfam00850  160 IFYDDPSVLTLSIHQY-PGGFYPG--TGFADETGEGKGKGYTLNVPLP-PGTGDAEYLAAFEEILLPALEEFQPDLILVS 235
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 967505306   743 AGFDAARGDPLGGCQVSPEGYAHLTHLLMGLA---SGRIILILEGGYNLTSISESMAACTR 800
Cdd:pfam00850  236 AGFDAHAGDPLGGLNLTTEGFAEITRILLELAdplCIRVVSVLEGGYNLDALARSATAVLA 296
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
499-835 4.55e-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: 380.35  E-value: 4.55e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  499 LWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPS 578
Cdd:cd11682     2 LWDESFPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYVALMKSTQYMTEEELRTLADTYDSVYLHPN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  579 TFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQAiSGRALRILIVDWDVHHGN 658
Cdd:cd11682    82 SYSCACLAVGSVLQLVDKVLGGEIRNGLAIVRPPGHHAQHDKMDGYCMFNNVAIAARYAQQ-KHGVQRVLIVDWDVHHGQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  659 GTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPEL 738
Cdd:cd11682   161 GTQFIFEQDPSVLYFSIHRYEQGRFWPHLKESDSSAVGFGRGEGYNINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  739 VLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLS 818
Cdd:cd11682   241 VLVAAGFDAVIGDPKGEMAATPACFAHLTHLLMGLAGGKLILSLEGGYNLRSLAEGVCASLKALLGDPCPMLESPGAPCR 320
                         330
                  ....*....|....*..
gi 967505306  819 GALASITETIQVHRRYW 835
Cdd:cd11682   321 SALASVSCTISALEPFW 337
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
485-835 5.26e-122

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: 381.69  E-value: 5.26e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  485 TGLVYDQSMMNH---CNLwDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYV----GHLRATEK 557
Cdd:cd11681     3 TGLAYDPLMLKHqciCGN-NSSHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTllygTNPLSRLK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  558 MKTRELHRES-SNF------------DSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGF 624
Cdd:cd11681    82 LDPTKLAGLPqKSFvrlpcggigvdsDTVWNELHTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQAMGF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  625 CFFNSVAVAARHAQAISGRAlRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPmgDEGASSQIGRAAGTGFT 704
Cdd:cd11681   162 CFFNSVAIAAKQLQQKLKLR-KILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFP--GTGAPTEVGSGAGEGFN 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  705 VNVAWNG---PRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDP--LGGCQVSPEGYAHLTHLLMGLASGRII 779
Cdd:cd11681   239 VNIAWSGgldPPMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPppLGGYKVSPACFGYMTRQLMNLAGGKVV 318
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 967505306  780 LILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLS---GALASITETIQVHRRYW 835
Cdd:cd11681   319 LALEGGYDLTAICDASEACVRALLGDELDPLSEEELERRpnpNAVTSLEKVIAIQSPYW 377
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
103-410 2.00e-119

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: 372.45  E-value: 2.00e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  103 DSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLAD--TYDSVYLHPNS 180
Cdd:cd11600     1 DPHPEDPSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEHWDRVEATEKMSDEQLKDRTEifERDSLYVNNDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  181 YSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKH--RIRRVLIVDWDVHHGQ 258
Cdd:cd11600    81 AFCARLSCGGAIEACRAVAEGRVKNAFAVVRPPGHHAEPDESMGFCFFNNVAVAAKWLQTEYpdKIKKILILDWDIHHGN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  259 GTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQL 338
Cdd:cd11600   161 GTQRAFYDDPNVLYISLHRFENGGFYPGTPYGDYESVGEGAGLGFNVNIPWPQGGMGDADYIYAFQRIVMPIAYEFDPDL 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 967505306  339 VLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPML 410
Cdd:cd11600   241 VIISAGFDAADGDELGQCHVTPAGYAHMTHMLMSLAGGKLVVALEGGYNLDAISDSALAVAKVLLGEAPPKL 312
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
506-835 8.62e-115

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: 361.10  E-value: 8.62e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  506 EVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQL 585
Cdd:cd11683     9 EVPERLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRETQVMNKEELMAISGKYDAVYFHPNTFHCARL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  586 ATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQAISGRAlRILIVDWDVHHGNGTQHMFE 665
Cdd:cd11683    89 AAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYAKKKYGLH-RILIVDWDVHHGQGIQYIFE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  666 DDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGF 745
Cdd:cd11683   168 EDPSVLYFSWHRYEHQRFWPFLRESDYDAVGRGKGLGFNINLPWNKVGMGNADYLAAFFHVLLPLAFEFDPELVLVSAGF 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  746 DAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASIT 825
Cdd:cd11683   248 DSAIGDPEGQMCATPECFAHLTHLLMVLAGGKLCAVLEGGYHLESLAESVCMTVQTLLGDPLPRLSGEMTPCQSALESIQ 327
                         330
                  ....*....|
gi 967505306  826 ETIQVHRRYW 835
Cdd:cd11683   328 NVRAAQAPYW 337
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
106-402 1.67e-111

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: 350.77  E-value: 1.67e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   106 PEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYID-LMETTQYMNEGELRVLADTYDSVYLHPNSYSCA 184
Cdd:pfam00850    2 PENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEfLEEAAPEGGALLLLSYLSGDDDTPVSPGSYEAA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   185 CLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTF 264
Cdd:pfam00850   82 LLAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLKRVAIVDFDVHHGNGTQEIF 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   265 DQDPSVLYFSIHRYEqGRFWPHLkaSNWSTTGFGQGQGYTINVPWNqVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAG 344
Cdd:pfam00850  162 YDDPSVLTLSIHQYP-GGFYPGT--GFADETGEGKGKGYTLNVPLP-PGTGDAEYLAAFEEILLPALEEFQPDLILVSAG 237
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 967505306   345 FDALQGDPKGEMAATPAGFAQLTHLLMGLA---GGKLILSLEGGYNLRALAEGVSASLHTL 402
Cdd:pfam00850  238 FDAHAGDPLGGLNLTTEGFAEITRILLELAdplCIRVVSVLEGGYNLDALARSATAVLAAL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
485-797 1.04e-103

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 330.15  E-value: 1.04e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  485 TGLVYDQSMMNHcNLWDsHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVghlratEKMKTRELH 564
Cdd:COG0123     1 TALIYHPDYLLH-DLGP-GHPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYV------DALRAASLD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  565 RESSNFDSI-YICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQAisGR 643
Cdd:COG0123    73 GGYGQLDPDtPVSPGTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGFCLFNNAAIAARYLLA--KG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  644 ALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDhgtFFPMgdEGASSQIGRAAGTGFTVNVAWnGPRMGDADYLAAW 723
Cdd:COG0123   151 LERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQDP---LYPG--TGAADETGEGAGEGSNLNVPL-PPGTGDAEYLAAL 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 967505306  724 HRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLA---SGRIILILEGGYNLTSISESMAA 797
Cdd:COG0123   225 EEALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELAdhcGGPVVSVLEGGYNLDALARSVAA 301
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
485-839 7.57e-100

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: 323.53  E-value: 7.57e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  485 TGLVYDQSMMNH-CNLWDSH-HPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVgHLRATEKMKTRE 562
Cdd:cd10006     6 TGLVYDTLMLKHqCTCGNSNsHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHT-LLYGTNPLNRQK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  563 LHRE------SSNF------------DSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGF 624
Cdd:cd10006    85 LDSKkllgslASVFvrlpcggvgvdsDTIWNEVHSSGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  625 CFFNSVAVAARHAQAISGRAlRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPmgDEGASSQIGRAAGTGFT 704
Cdd:cd10006   165 CYFNSVAIAAKLLQQRLNVS-KILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYDDGNFFP--GSGAPDEVGTGPGVGFN 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  705 VNVAWNG---PRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGD--PLGGCQVSPEGYAHLTHLLMGLASGRII 779
Cdd:cd10006   242 VNMAFTGgldPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHptPLGGYNLSAKCFGYLTKQLMGLAGGRIV 321
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 967505306  780 LILEGGYNLTSISESMAACTRSLLGDPPP---LLTLPRPPLSGALASITETIQVHRRYWRSLR 839
Cdd:cd10006   322 LALEGGHDLTAICDASEACVSALLGNELDplpEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQ 384
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
85-435 2.89e-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: 2.89e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   85 GTGLVLDEQLNEFHCLWDDS--FPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQ----- 157
Cdd:cd11681     2 TTGLAYDPLMLKHQCICGNNssHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHTLLYGTNPlsrlk 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  158 ---------------YMNEGELRVLADTYDSVyLHpnSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLM 222
Cdd:cd11681    82 ldptklaglpqksfvRLPCGGIGVDSDTVWNE-LH--TSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  223 DGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNwsTTGFGQGQG 302
Cdd:cd11681   159 MGFCFFNSVAIAAKQLQQKLKLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFPGTGAPT--EVGSGAGEG 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  303 YTINVPWN---QVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPK--GEMAATPAGFAQLTHLLMGLAGGK 377
Cdd:cd11681   237 FNVNIAWSgglDPPMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPPplGGYKVSPACFGYMTRQLMNLAGGK 316
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 967505306  378 LILSLEGGYNLRALAEGVSASLHTLLGD---PCPMLESPGAPCRSAQASVSCALEALEPFW 435
Cdd:cd11681   317 VVLALEGGYDLTAICDASEACVRALLGDeldPLSEEELERRPNPNAVTSLEKVIAIQSPYW 377
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
485-835 4.38e-99

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: 320.42  E-value: 4.38e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  485 TGLVYDQSMMNH-CNLWD-SHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVgHLRATE-----K 557
Cdd:cd10008     3 TGLVYDSVMLKHqCSCGDnSNHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHV-LLYGTNplsrlK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  558 MKTRELHRESS--------------NFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACG 623
Cdd:cd10008    82 LDNGKLAGLLAqrmfvmlpcggvgvDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  624 FCFFNSVAVAARHAQaISGRALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPmgDEGASSQIGRAAGTGF 703
Cdd:cd10008   162 FCFFNSVAIACRQLQ-QQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFP--GSGAVDEVGAGSGEGF 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  704 TVNVAWNG---PRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGD--PLGGCQVSPEGYAHLTHLLMGLASGRI 778
Cdd:cd10008   239 NVNVAWAGgldPPMGDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHpaPLGGYHVSAKCFGYMTQQLMNLAGGAV 318
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  779 ILILEGGYNLTSISESMAACTRSLLGDPP---PLLTLPRPPLSGALASITETIQVHRRYW 835
Cdd:cd10008   319 VLALEGGHDLTAICDASEACVAALLGNEVdplSEESWKQKPNLNAIRSLEAVIRVHSKYW 378
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
106-404 2.17e-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: 312.81  E-value: 2.17e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  106 PEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYmNEGELRVLADTYdsvyLHPNSYSCAC 185
Cdd:COG0123    19 PEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAASL-DGGYGQLDPDTP----VSPGTWEAAL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  186 LASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAqQKHRIRRVLIVDWDVHHGQGTQFTFD 265
Cdd:COG0123    94 LAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGFCLFNNAAIAARYL-LAKGLERVAIVDFDVHHGNGTQDIFY 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  266 QDPSVLYFSIHryeQGRFWPHLKASnwSTTGFGQGQGYTINVPwnqV--GMRDADYIAAFLHVLLPVALEFQPQLVLVAA 343
Cdd:COG0123   173 DDPDVLTISIH---QDPLYPGTGAA--DETGEGAGEGSNLNVP---LppGTGDAEYLAALEEALLPALEAFKPDLIVVSA 244
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 967505306  344 GFDALQGDPKGEMAATPAGFAQLTHLLMGLA---GGKLILSLEGGYNLRALAEGVSASLHTLLG 404
Cdd:COG0123   245 GFDAHADDPLGRLNLTTEGYAWRTRRVLELAdhcGGPVVSVLEGGYNLDALARSVAAHLETLLG 308
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
485-839 1.72e-96

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: 315.00  E-value: 1.72e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  485 TGLVYDQSMMNH-CNLWDSH-HPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSaEYVGHLRATEKMKTRE 562
Cdd:cd10007     5 TGLVYDTFMLKHqCTCGNTNvHPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHS-EHHTLLYGTSPLNRQK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  563 LhrESSNF---------------------DSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAA 621
Cdd:cd10007    84 L--DSKKLlgplsqkmyavlpcggigvdsDTVWNEMHSSSAVRMAVGCLIELAFKVAAGELKNGFAVIRPPGHHAEESTA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  622 CGFCFFNSVAVAARHAQAISGRAlRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPmgDEGASSQIGRAAGT 701
Cdd:cd10007   162 MGFCFFNSVAIAAKLLQQKLNVG-KILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGNFFP--GSGAPDEVGAGPGV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  702 GFTVNVAWNG---PRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARG--DPLGGCQVSPEGYAHLTHLLMGLASG 776
Cdd:cd10007   239 GFNVNIAWTGgvdPPIGDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGhqSPLGGYSVTAKCFGHLTKQLMTLAGG 318
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967505306  777 RIILILEGGYNLTSISESMAACTR---SLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLR 839
Cdd:cd10007   319 RVVLALEGGHDLTAICDASEACVSallGMELTPLDNTVLQQKPNDNAVATLERVIEIQSKHWSCLK 384
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
485-789 4.27e-91

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: 297.55  E-value: 4.27e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  485 TGLVYDQSMMNH-------------CNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGH 551
Cdd:cd09996     1 TGFVWDERYLWHdtgtgalflpvggLLVQPGRHPENPETKRRIKNLLEVSGLSDHLVLITPRPATDEELLRVHTPEYIDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  552 LRATEKMKTRELHRESsnfdsiYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVA 631
Cdd:cd09996    81 VKAASAAGGGEAGGGT------PFGPGSYEIALLAAGGAIAAVDAVLDGEVDNAYALVRPPGHHAEPDQGMGFCLFNNVA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  632 VAARHAQAiSGRALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRyDHgtFFPMgDEGASSQIGRAAGTGFTVNVawng 711
Cdd:cd09996   155 IAARHALA-VGGVKRVAVVDWDVHHGNGTQAIFYDDPDVLTISLHQ-DR--CFPP-DSGAVEERGEGAGEGYNLNI---- 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  712 PRM---GDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLA----SGRIILILEG 784
Cdd:cd09996   226 PLPpgsGDGAYLHAFERIVLPALRAFRPELIIVASGFDASAFDPLGRMMLTSDGFRALTRKLRDLAdelcGGRLVMVHEG 305

                  ....*
gi 967505306  785 GYNLT 789
Cdd:cd09996   306 GYSEA 310
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
504-797 6.06e-88

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: 286.33  E-value: 6.06e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  504 HPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATekmktRELHRESSNFDSIYICPSTFACA 583
Cdd:cd11599     1 HPESPERLEAILDALIASGLDRLLRQLEAPPATREQLLRVHDAAYVDRLEAA-----APEEGLVQLDPDTAMSPGSLEAA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  584 QLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQAISGrALRILIVDWDVHHGNGTQHM 663
Cdd:cd11599    76 LRAAGAVVAAVDAVMAGEARNAFCAVRPPGHHAERDKAMGFCLFNNVAIAAAHALAHHG-LERVAIVDFDVHHGNGTEDI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  664 FEDDPSVLYVSLHRYdhgTFFPmgDEGASSQIGR--------AAGTGFtvnvawngprmgdADYLAAWHRLVLPIAYEFN 735
Cdd:cd11599   155 FRDDPRVLFCSSHQH---PLYP--GTGAPDETGHgnivnvplPAGTGG-------------AEFREAVEDRWLPALDAFK 216
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967505306  736 PELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLAS----GRIILILEGGYNLTSISESMAA 797
Cdd:cd11599   217 PDLILISAGFDAHRDDPLAQLNLTEEDYAWITEQLMDVADrycdGRIVSVLEGGYDLSALARSVAA 282
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
106-403 1.58e-82

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: 271.31  E-value: 1.58e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  106 PEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQyMNEGELRVLADTYDSvylhPNSYSCAC 185
Cdd:cd11599     2 PESPERLEAILDALIASGLDRLLRQLEAPPATREQLLRVHDAAYVDRLEAAA-PEEGLVQLDPDTAMS----PGSLEAAL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  186 LASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFD 265
Cdd:cd11599    77 RAAGAVVAAVDAVMAGEARNAFCAVRPPGHHAERDKAMGFCLFNNVAIAAAHALAHHGLERVAIVDFDVHHGNGTEDIFR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  266 QDPSVLYFSIHRYeqgRFWPHlkasnwstTGFGQ--GQGYTINVPWNQvGMRDADYIAAFLHVLLPVALEFQPQLVLVAA 343
Cdd:cd11599   157 DDPRVLFCSSHQH---PLYPG--------TGAPDetGHGNIVNVPLPA-GTGGAEFREAVEDRWLPALDAFKPDLILISA 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 967505306  344 GFDALQGDPKGEMAATPAGFAQLTHLLMGLA----GGKLILSLEGGYNLRALAEGVSASLHTLL 403
Cdd:cd11599   225 GFDAHRDDPLAQLNLTEEDYAWITEQLMDVAdrycDGRIVSVLEGGYDLSALARSVAAHVRALM 288
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
483-836 1.94e-81

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: 271.89  E-value: 1.94e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  483 SRTGLVYDQSMMNH-CNLWDS-HHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSaEYVGHLRAT----- 555
Cdd:cd10009     1 SATGIAYDPLMLKHqCVCGNStTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHS-EHHSLLYGTnpldg 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  556 EKMKTRELHRESS--------------NFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAA 621
Cdd:cd10009    80 QKLDPRILLGDDSqkffsslpcgglgvDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  622 CGFCFFNSVAVAARHAQAISGRAlRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPmgDEGASSQIGRAAGT 701
Cdd:cd10009   160 MGFCFFNSVAITAKYLRDQLNIS-KILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFP--GSGAPNEVGTGLGE 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  702 GFTVNVAWNG---PRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGD--PLGGCQVSPEGYAHLTHLLMGLASG 776
Cdd:cd10009   237 GYNINIAWTGgldPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLADG 316
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 967505306  777 RIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLS---GALASITETIQVHRRYWR 836
Cdd:cd10009   317 RVVLALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSpnmNAVISLQKIIEIQSKYWK 379
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
86-442 8.59e-81

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: 271.14  E-value: 8.59e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   86 TGLVLDEQLNEFHCLW--DDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSlEYIDLMETTQYMNEGE 163
Cdd:cd10006     6 TGLVYDTLMLKHQCTCgnSNSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHS-EAHTLLYGTNPLNRQK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  164 L------RVLADTY------------DSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGY 225
Cdd:cd10006    85 LdskkllGSLASVFvrlpcggvgvdsDTIWNEVHSSGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  226 CMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNwsTTGFGQGQGYTI 305
Cdd:cd10006   165 CYFNSVAIAAKLLQQRLNVSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYDDGNFFPGSGAPD--EVGTGPGVGFNV 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  306 NVPWN---QVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPK--GEMAATPAGFAQLTHLLMGLAGGKLIL 380
Cdd:cd10006   243 NMAFTgglDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTplGGYNLSAKCFGYLTKQLMGLAGGRIVL 322
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 967505306  381 SLEGGYNLRALAEGVSASLHTLLG---DPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSS 442
Cdd:cd10006   323 ALEGGHDLTAICDASEACVSALLGnelDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTT 387
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
86-435 1.19e-80

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: 269.57  E-value: 1.19e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   86 TGLVLDEQLNEFHCLWDDS--FPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQY----M 159
Cdd:cd10008     3 TGLVYDSVMLKHQCSCGDNsnHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLsrlkL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  160 NEGELR---------------VLADTyDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDG 224
Cdd:cd10008    83 DNGKLAgllaqrmfvmlpcggVGVDT-DTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  225 YCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNwsTTGFGQGQGYT 304
Cdd:cd10008   162 FCFFNSVAIACRQLQQQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVD--EVGAGSGEGFN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  305 INVPWN---QVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPK--GEMAATPAGFAQLTHLLMGLAGGKLI 379
Cdd:cd10008   240 VNVAWAgglDPPMGDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHPAplGGYHVSAKCFGYMTQQLMNLAGGAVV 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 967505306  380 LSLEGGYNLRALAEGVSASLHTLLG---DPCPMLESPGAPCRSAQASVSCALEALEPFW 435
Cdd:cd10008   320 LALEGGHDLTAICDASEACVAALLGnevDPLSEESWKQKPNLNAIRSLEAVIRVHSKYW 378
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
83-442 1.86e-78

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: 264.93  E-value: 1.86e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   83 LAGTGLVLDEQLNEFHCLWDDS--FPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSlEYIDLMETTQYMN 160
Cdd:cd10007     2 LFTTGLVYDTFMLKHQCTCGNTnvHPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHS-EHHTLLYGTSPLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  161 EGELR--------------VL------ADTyDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHS 220
Cdd:cd10007    81 RQKLDskkllgplsqkmyaVLpcggigVDS-DTVWNEMHSSSAVRMAVGCLIELAFKVAAGELKNGFAVIRPPGHHAEES 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  221 LMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNwsTTGFGQG 300
Cdd:cd10007   160 TAMGFCFFNSVAIAAKLLQQKLNVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGNFFPGSGAPD--EVGAGPG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  301 QGYTINVPWN---QVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQG--DPKGEMAATPAGFAQLTHLLMGLAG 375
Cdd:cd10007   238 VGFNVNIAWTggvDPPIGDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGhqSPLGGYSVTAKCFGHLTKQLMTLAG 317
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  376 GKLILSLEGGYNLRALAEGVSASLHTLLGD---PCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSS 442
Cdd:cd10007   318 GRVVLALEGGHDLTAICDASEACVSALLGMeltPLDNTVLQQKPNDNAVATLERVIEIQSKHWSCLKRFA 387
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
86-431 1.03e-75

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: 255.18  E-value: 1.03e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   86 TGLVLDEqlnefHCLWDDS------------------FPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSL 147
Cdd:cd09996     1 TGFVWDE-----RYLWHDTgtgalflpvggllvqpgrHPENPETKRRIKNLLEVSGLSDHLVLITPRPATDEELLRVHTP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  148 EYIDLMETTQYMNEGELRVLAdtydsvYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCM 227
Cdd:cd09996    76 EYIDRVKAASAAGGGEAGGGT------PFGPGSYEIALLAAGGAIAAVDAVLDGEVDNAYALVRPPGHHAEPDQGMGFCL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  228 FNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHryeQGRFWPHlkasNWST---TGFGQGQGYT 304
Cdd:cd09996   150 FNNVAIAARHALAVGGVKRVAVVDWDVHHGNGTQAIFYDDPDVLTISLH---QDRCFPP----DSGAveeRGEGAGEGYN 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  305 INVPW-NQVGmrDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLA----GGKLI 379
Cdd:cd09996   223 LNIPLpPGSG--DGAYLHAFERIVLPALRAFRPELIIVASGFDASAFDPLGRMMLTSDGFRALTRKLRDLAdelcGGRLV 300
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 967505306  380 LSLEGGYNLRALAEGVSASLHTLLGDPC----PMLESPGA-PCRSAQASVSCALEAL 431
Cdd:cd09996   301 MVHEGGYSEAYVPFCGLAVLEELSGVRTgiadPLLYYPEAqGGQELQPHQRAAIDAA 357
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
503-797 1.16e-75

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: 252.46  E-value: 1.16e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  503 HHPEVPQRILRIMCRLEELGLAgrcLTLTPRPATEAELLTCHSAEYVGHLRatekmktrelhressNFD-SIYICPSTFA 581
Cdd:cd10001    24 PHPENPERAEAILDALKRAGLG---EVLPPRDFGLEPILAVHDPDYVDFLE---------------TADtDTPISEGTWE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  582 CAQLATGAACRLVEAVLSGEVLngA-AVVRPPGHHAEQDAACGFCFFNSVAVAARHAQAisgRALRILIVDWDVHHGNGT 660
Cdd:cd10001    86 AALAAADTALTAADLVLEGERA--AyALCRPPGHHAGRDRAGGFCYFNNAAIAAQYLRD---RAGRVAILDVDVHHGNGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  661 QHMFEDDPSVLYVSLHRYDHgTFFPmGDEGASSQIGRAAGTGFTVNV--AWNgprMGDADYLAAWHRLVLPIAyEFNPEL 738
Cdd:cd10001   161 QEIFYERPDVLYVSIHGDPR-TFYP-FFLGFADETGEGEGEGYNLNLplPPG---TGDDDYLAALDEALAAIA-AFGPDA 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 967505306  739 VLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLAsGRIILILEGGYNLTSISESMAA 797
Cdd:cd10001   235 LVVSLGFDTHEGDPLSDFKLTTEDYARIGRRIAALG-LPTVFVQEGGYNVDALGRNAVA 292
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
86-436 7.74e-70

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: 239.15  E-value: 7.74e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   86 TGLVLDEQLNEFHCLWDDS--FPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSlEYIDLMETTQYMNEGE 163
Cdd:cd10009     3 TGIAYDPLMLKHQCVCGNSttHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHS-EHHSLLYGTNPLDGQK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  164 L---RVLADTY----------------DSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDG 224
Cdd:cd10009    82 LdprILLGDDSqkffsslpcgglgvdsDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  225 YCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNwsTTGFGQGQGYT 304
Cdd:cd10009   162 FCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPN--EVGTGLGEGYN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  305 INVPWN---QVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGD--PKGEMAATPAGFAQLTHLLMGLAGGKLI 379
Cdd:cd10009   240 INIAWTgglDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLADGRVV 319
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  380 LSLEGGYNLRALAEGVSASLHTLLG---DPCPMLESPGAPCRSAQASVSCALEALEPFWE 436
Cdd:cd10009   320 LALEGGHDLTAICDASEACVNALLGnelEPLAEDILHQSPNMNAVISLQKIIEIQSKYWK 379
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
510-799 4.65e-68

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: 230.40  E-value: 4.65e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  510 RILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGA 589
Cdd:cd09301     1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKANFAVATITESKPVIFGPNFPVQRHYFRGARLSTGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  590 ACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQAISGRalRILIVDWDVHHGNGTQHMFEDDPS 669
Cdd:cd09301    81 VVEAAELVAKGELERAFAVVGAGGHHAGKSRAWGFCYFNDVVLAIKFLRERGIS--RILIIDTDAHHGDGTREAFYDDDR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  670 VLYVSLHRYDHGTFfpmgdegassqiGRAAGTGFTVNVAWNGPrMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAAR 749
Cdd:cd09301   159 VLHMSFHNYDIYPF------------GRGKGKGYKINVPLEDG-LGDEEYLDAVERVISKVLEEFEPEVVVLQFGHDTHE 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 967505306  750 GDPLGGCQVSPEGYAHLTHLLMGLAS-GRIILILEGGYNLTSISESMAACT 799
Cdd:cd09301   226 GDRLGGFNLSEKGFVKLAEIVKEFARgGPILMVLGGGYNPEAAARIWTAII 276
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
106-403 7.45e-62

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: 213.55  E-value: 7.45e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  106 PEGPERLHAIKEQLIQEGLLDRCVsfQARFAEkEELMLVHSLEYIDLMETtqymnegelrvlADTydSVYLHPNSYSCAC 185
Cdd:cd10001    26 PENPERAEAILDALKRAGLGEVLP--PRDFGL-EPILAVHDPDYVDFLET------------ADT--DTPISEGTWEAAL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  186 LASGSVLRLVDAVLGAEiRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHriRRVLIVDWDVHHGQGTQFTFD 265
Cdd:cd10001    89 AAADTALTAADLVLEGE-RAAYALCRPPGHHAGRDRAGGFCYFNNAAIAAQYLRDRA--GRVAILDVDVHHGNGTQEIFY 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  266 QDPSVLYFSIHRYEQGrFWPHlkasnwsTTGF------GQGQGYTINVPWnQVGMRDADYIAAFLHVLLPVAlEFQPQLV 339
Cdd:cd10001   166 ERPDVLYVSIHGDPRT-FYPF-------FLGFadetgeGEGEGYNLNLPL-PPGTGDDDYLAALDEALAAIA-AFGPDAL 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 967505306  340 LVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILsLEGGYNLRALAEGVSASLHTLL 403
Cdd:cd10001   236 VVSLGFDTHEGDPLSDFKLTTEDYARIGRRIAALGLPTVFV-QEGGYNVDALGRNAVAFLAGFE 298
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
111-402 2.00e-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: 205.75  E-value: 2.00e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  111 RLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGS 190
Cdd:cd09301     1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKANFAVATITESKPVIFGPNFPVQRHYFRGARLSTGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  191 VLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHrIRRVLIVDWDVHHGQGTQFTFDQDPSV 270
Cdd:cd09301    81 VVEAAELVAKGELERAFAVVGAGGHHAGKSRAWGFCYFNDVVLAIKFLRERG-ISRILIIDTDAHHGDGTREAFYDDDRV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  271 LYFSIHRYeqgrfwphlkasNWSTTGFGQGQGYTINVPWNQvGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQG 350
Cdd:cd09301   160 LHMSFHNY------------DIYPFGRGKGKGYKINVPLED-GLGDEEYLDAVERVISKVLEEFEPEVVVLQFGHDTHEG 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 967505306  351 DPKGEMAATPAGFAQLTHLLMGLA-GGKLILSLEGGYNLRALAEGVSASLHTL 402
Cdd:cd09301   227 DRLGGFNLSEKGFVKLAEIVKEFArGGPILMVLGGGYNPEAAARIWTAIIKEL 279
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
503-788 4.07e-56

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: 197.40  E-value: 4.07e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  503 HHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEK-MKTRELHR------ESSNFDSIYi 575
Cdd:cd09994    16 NHPFNPPRLSLTKDLLRALGLLPPVDLVPPRPATEEELLLFHTPDYIEAVKEASRgQEPEGRGRlglgteDNPVFPGMH- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  576 cpstfACAQLATGAACRLVEAVLSGEVLNgaaVVRPPG--HHAEQDAACGFCFFNSVAVAARHAQAISGRalRILIVDWD 653
Cdd:cd09994    95 -----EAAALVVGGTLLAARLVLEGEARR---AFNPAGglHHAMRGRASGFCVYNDAAVAIERLRDKGGL--RVAYVDID 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  654 VHHGNGTQHMFEDDPSVLYVSLHRyDHGTFFPmGdEGASSQIGRAAGTGFTVNVAWNgPRMGDADYLAAWHRLVLPIAYE 733
Cdd:cd09994   165 AHHGDGVQAAFYDDPRVLTISLHE-SGRYLFP-G-TGFVDEIGEGEGYGYAVNIPLP-PGTGDDEFLRAFEAVVPPLLRA 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 967505306  734 FNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLA----SGRIILILEGGYNL 788
Cdd:cd09994   241 FRPDVIVSQHGADAHAGDPLTHLNLSNRAYRAAVRRIRELAdeycGGRWLALGGGGYNP 299
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
100-402 9.38e-46

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: 167.35  E-value: 9.38e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  100 LWDDSF---------PEGPERLHAIKEqLIQE-GLLDRCVSFQARFAEKEELMLVHSLEYIDLME--TTQYMNEGELRVL 167
Cdd:cd09994     3 IYSEEYlrysfgpnhPFNPPRLSLTKD-LLRAlGLLPPVDLVPPRPATEEELLLFHTPDYIEAVKeaSRGQEPEGRGRLG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  168 ADTYDSVYlHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIrppG--HHAQHSLMDGYCMFNHVAVAARYAQqKHRIR 245
Cdd:cd09994    82 LGTEDNPV-FPGMHEAAALVVGGTLLAARLVLEGEARRAFNPA---GglHHAMRGRASGFCVYNDAAVAIERLR-DKGGL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  246 RVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHryEQGR-FWPHLKASNwsTTGFGQGQGYTINVPWNQvGMRDADYIAAFL 324
Cdd:cd09994   157 RVAYVDIDAHHGDGVQAAFYDDPRVLTISLH--ESGRyLFPGTGFVD--EIGEGEGYGYAVNIPLPP-GTGDDEFLRAFE 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  325 HVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLA----GGKLILSLEGGYNLRALAEGVSASLH 400
Cdd:cd09994   232 AVVPPLLRAFRPDVIVSQHGADAHAGDPLTHLNLSNRAYRAAVRRIRELAdeycGGRWLALGGGGYNPDVVARAWALLWA 311

                  ..
gi 967505306  401 TL 402
Cdd:cd09994   312 VL 313
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
487-792 8.38e-43

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: 160.58  E-value: 8.38e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  487 LVYDQSMMNHCNlwdsHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLR-ATEKMKTRELHR 565
Cdd:cd10000     3 YIHSPEYVNLCD----RLPKVPNRASMVHSLIEAYGLLKQLRVVKPRVATEEELASFHSDEYIQFLKkASNEGDNDEEPS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  566 ESSNFDSIYICPST---FACAQLATGAACRLVEAVLSGEVlngAAVVRPPG--HHAEQDAACGFCFFNSVAVAArhaQAI 640
Cdd:cd10000    79 EQQEFGLGYDCPIFegiYDYAAAVAGATLTAAQLLIDGKC---KVAINWFGgwHHAQRDEASGFCYVNDIVLGI---LKL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  641 SGRALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGtFFPmgDEGASSQIGRAAGTGFTVNVAWngpRMG--DAD 718
Cdd:cd10000   153 REKFDRVLYVDLDLHHGDGVEDAFSFTSKVMTVSLHKYSPG-FFP--GTGDVSDVGLGKGKYYTVNVPL---RDGiqDEQ 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 967505306  719 YLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLasGRIILIL-EGGYNLTSIS 792
Cdd:cd10000   227 YLQIFTAVVPEIVAAFRPEAVVLQCGADTLAGDPMGAFNLTPVGIGKCLKYVLGW--KLPTLILgGGGYNLANTA 299
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
513-762 1.51e-40

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: 151.11  E-value: 1.51e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  513 RIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRatEKMKTRELHRES--SNFDSI-----YICPSTFACAQL 585
Cdd:cd09993    10 LLREALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLESLK--SGELSREEIRRIgfPWSPELvertrLAVGGTILAARL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  586 A--TGAACRLveavlSGevlngaavvrppG-HHAEQDAACGFCFFNSVAVAARHAQAiSGRALRILIVDWDVHHGNGTQH 662
Cdd:cd09993    88 AleHGLAINL-----AG------------GtHHAFPDRGEGFCVFNDIAIAARVLLA-EGLVRRVLIVDLDVHQGNGTAA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  663 MFEDDPSVLYVSLHrydHGTFFPmGDEGASSqigraagtgFTVNVAWNgprMGDADYLAAWHRLVLPIAYEFNPELVLVS 742
Cdd:cd09993   150 IFADDPSVFTFSMH---GEKNYP-FRKEPSD---------LDVPLPDG---TGDDEYLAALEEALPRLLAEFRPDLVFYN 213
                         250       260
                  ....*....|....*....|
gi 967505306  743 AGFDAARGDPLGGCQVSPEG 762
Cdd:cd09993   214 AGVDVLAGDRLGRLSLSLEG 233
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
503-792 3.67e-36

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: 139.64  E-value: 3.67e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  503 HHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPST--- 579
Cdd:cd09991    14 GHPMKPHRIRMTHSLILSYGLYKKMEIYRPRPATAEELTKFHSDDYIDFLRSVSPDNMKEFKKQLERFNVGEDCPVFdgl 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  580 FACAQLATGAACRLVEAVLSGevlNGAAVVRPPG--HHAEQDAACGFCFFNSVAVA-----ARHAqaisgralRILIVDW 652
Cdd:cd09991    94 YEYCQLYAGGSIAAAVKLNRG---QADIAINWAGglHHAKKSEASGFCYVNDIVLAilellKYHQ--------RVLYIDI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  653 DVHHGNGTQHMFEDDPSVLYVSLHRYDHGtFFPMGDEgasSQIGRAAGTGFTVNVAWNgPRMGDADYLAAWHRLVLPIAY 732
Cdd:cd09991   163 DIHHGDGVEEAFYTTDRVMTVSFHKFGEY-FFPGTGL---RDIGAGKGKYYAVNVPLK-DGIDDESYLQIFEPVLSKVME 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 967505306  733 EFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLasGRIILIL-EGGYNLTSIS 792
Cdd:cd09991   238 VFQPSAVVLQCGADSLAGDRLGCFNLSIKGHAKCVKFVKSF--NIPLLVLgGGGYTLRNVA 296
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
115-402 2.24e-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: 2.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  115 IKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEgELRVLadtydsvyLHPNSyscACLasgsVLRL 194
Cdd:cd09993    11 LREALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLESLKSGELSRE-EIRRI--------GFPWS---PEL----VERT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  195 VDAV----LGAE--IRNGMAIiRPPG--HHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQ 266
Cdd:cd09993    75 RLAVggtiLAARlaLEHGLAI-NLAGgtHHAFPDRGEGFCVFNDIAIAARVLLAEGLVRRVLIVDLDVHQGNGTAAIFAD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  267 DPSVLYFSIHryeQGRFWPHLK-ASNWSttgfgqgqgytINVPWnqvGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGF 345
Cdd:cd09993   154 DPSVFTFSMH---GEKNYPFRKePSDLD-----------VPLPD---GTGDDEYLAALEEALPRLLAEFRPDLVFYNAGV 216
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  346 DALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLI---LSLEGGYNlRALAEGVSASLHTL 402
Cdd:cd09993   217 DVLAGDRLGRLSLSLEGLRERDRLVLRFARARGIpvaMVLGGGYS-RDIARLVARHAQTL 275
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
103-388 1.11e-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: 1.11e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  103 DSFPEGPERLHAIkEQLIQE-GLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYM--NEGELRVLAD---TYDSVYL 176
Cdd:cd10000    14 DRLPKVPNRASMV-HSLIEAyGLLKQLRVVKPRVATEEELASFHSDEYIQFLKKASNEgdNDEEPSEQQEfglGYDCPIF 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  177 hPNSYSCACLASGSVLRLVDAVLGAEIRngMAIIRPPG-HHAQHSLMDGYCMFNHVAVAARYAqqKHRIRRVLIVDWDVH 255
Cdd:cd10000    93 -EGIYDYAAAVAGATLTAAQLLIDGKCK--VAINWFGGwHHAQRDEASGFCYVNDIVLGILKL--REKFDRVLYVDLDLH 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  256 HGQGTQFTFDQDPSVLYFSIHRYEQGrFWPhlKASNWSTTGFGQGQGYTINVPWNQvGMRDADYIAAFLHVLLPVALEFQ 335
Cdd:cd10000   168 HGDGVEDAFSFTSKVMTVSLHKYSPG-FFP--GTGDVSDVGLGKGKYYTVNVPLRD-GIQDEQYLQIFTAVVPEIVAAFR 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 967505306  336 PQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSlEGGYNL 388
Cdd:cd10000   244 PEAVVLQCGADTLAGDPMGAFNLTPVGIGKCLKYVLGWKLPTLILG-GGGYNL 295
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
106-392 6.53e-29

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


Pssm-ID: 212517 [Multi-domain]  Cd Length: 306  Bit Score: 118.45  E-value: 6.53e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  106 PEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYID-LMETTQ-YMNE--GELRVLADTYDSvYLHPNSY 181
Cdd:cd09991    16 PMKPHRIRMTHSLILSYGLYKKMEIYRPRPATAEELTKFHSDDYIDfLRSVSPdNMKEfkKQLERFNVGEDC-PVFDGLY 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  182 SCACLASGSvlrlvdAVLGAE-IRNGMA--IIRPPG--HHAQHSLMDGYCMFNHVAVAARYAQQKHRirRVLIVDWDVHH 256
Cdd:cd09991    95 EYCQLYAGG------SIAAAVkLNRGQAdiAINWAGglHHAKKSEASGFCYVNDIVLAILELLKYHQ--RVLYIDIDIHH 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  257 GQGTQFTFDQDPSVLYFSIHRYEQGRFwphlkasnwSTTGF-----GQGQGYTINVPWNQvGMRDADYIAAFLHVLLPVA 331
Cdd:cd09991   167 GDGVEEAFYTTDRVMTVSFHKFGEYFF---------PGTGLrdigaGKGKYYAVNVPLKD-GIDDESYLQIFEPVLSKVM 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 967505306  332 LEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLaGGKLILSLEGGYNLRALA 392
Cdd:cd09991   237 EVFQPSAVVLQCGADSLAGDRLGCFNLSIKGHAKCVKFVKSF-NIPLLVLGGGGYTLRNVA 296
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
1137-1199 1.70e-25

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 100.41  E-value: 1.70e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 967505306  1137 CGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHENSGHPLVLSYIDLSTWCYYCQAYVHHQAL 1199
Cdd:pfam02148    1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPSL 63
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
526-789 1.91e-25

Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is responsible for Smc3 deacetylation. Smc3 is an important player during the establishment of sister chromatid cohesion. Hos1 belongs to the class I histone deacetylases (HDACs). HDACs are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues in histone amino termini to yield a deacetylated histone (EC 3.5.1.98). Enzymes belonging to this group participate in regulation of a number of processes through protein (mostly different histones) modification (deacetylation). Class I histone deacetylases in general act via the formation of large multiprotein complexes. Other class I HDACs are animal HDAC1, HDAC2, HDAC3, HDAC8, fungal RPD3 and HOS2, plant HDA9, protist, archaeal and bacterial (AcuC) deacetylases. Members of this class are involved in cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and in posttranslational control of the acetyl coenzyme A synthetase.


Pssm-ID: 212543 [Multi-domain]  Cd Length: 294  Bit Score: 107.74  E-value: 1.91e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  526 RCLTLTPRPATEAELLTCHSAEYVGHLratekmktreLHRESSNFDSiYICPSTFACAQLATGAACRLVEAVLSGEvlnG 605
Cdd:cd11680    38 FDEIIEPERATRKDLTKYHDKDYVDFL----------LKKYGLEDDC-PVFPFLSMYVQLVAGSSLALAKHLITQV---E 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  606 AAVV------RppgHHAEQDAACGFCFFNSVAVAARHAQaiSGRALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYD 679
Cdd:cd11680   104 RDIAinwyggR---HHAQKSRASGFCYVNDIVLAILRLR--RARFRRVFYLDLDLHHGDGVESAFFFSKNVLTCSIHRYD 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  680 HGtFFPMGdeGASSQigraAGTGFTVNVAWNgPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVS 759
Cdd:cd11680   179 PG-FFPGT--GSLKN----SSDKGMLNIPLK-RGLSDKTLLRIIDSIVRPLIEKFEPEVIVIQCGCDGLSGDPHKEWNLT 250
                         250       260       270
                  ....*....|....*....|....*....|.
gi 967505306  760 PEGYAHLTHLLMGLASGRIILIL-EGGYNLT 789
Cdd:cd11680   251 IRGYGSVIELLLKEFKDKPTLLLgGGGYNHT 281
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
175-399 9.97e-23

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: 101.37  E-value: 9.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  175 YLHPNSYSCACLASGSVLRLVDAVLGAEI---RNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVD 251
Cdd:cd09998    77 YLCPESLDAIQGALGAVCEAVDSVFKPESpgtKRAFVAIRPPGHHCSESTPSGFCWVNNVHVGAAHAYLTHGITRVVILD 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  252 WDVHHGQGTQ--------FTFDQD----------------PSVLYFSIHRY-----EQGrFWPHLKASNWSTTGfGQGQg 302
Cdd:cd09998   157 IDLHHGNGTQdiawrinaEANKQAlesssyddfkpagapgLRIFYSSLHDInsfpcEDG-DPAKVKDASVSIDG-AHGQ- 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  303 YTINV---PWNQVGMRDADYIAAFlHVLLPVALEF-------QPQ--LVLVAAGFDALQGDPKGeMA----ATPAGF-AQ 365
Cdd:cd09998   234 WIWNVhlqPWTTEEDFWELYYPKY-RILFEKAAEFlrlttaaTPFktLVFISAGFDASEHEYES-MQrhgvNVPTSFyYR 311
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 967505306  366 LT----HLLMGLAGGKLILSLEGGYNLRALAEGVSASL 399
Cdd:cd09998   312 FArdavRFADAHAHGRLISVLEGGYSDRALCSGVLAHL 349
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
116-387 1.00e-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: 100.03  E-value: 1.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  116 KEQLIQE-----GLLDRCV-SFQARFAEKEELMLVHSLEYIDLMeTTQYMNEGelrvlaDTYDSVYLHpnSYscACLASG 189
Cdd:cd11680    21 RSSLVHSlirayGLLQHFDeIIEPERATRKDLTKYHDKDYVDFL-LKKYGLED------DCPVFPFLS--MY--VQLVAG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  190 SVLRLVDAVLGAEIRNgMAIIRPPG-HHAQHSLMDGYCMFNHVaVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDP 268
Cdd:cd11680    90 SSLALAKHLITQVERD-IAINWYGGrHHAQKSRASGFCYVNDI-VLAILRLRRARFRRVFYLDLDLHHGDGVESAFFFSK 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  269 SVLYFSIHRYEQGrFWPHLKASNWSTTGFgqgqgyTINVPWNQvGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDAL 348
Cdd:cd11680   168 NVLTCSIHRYDPG-FFPGTGSLKNSSDKG------MLNIPLKR-GLSDKTLLRIIDSIVRPLIEKFEPEVIVIQCGCDGL 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 967505306  349 QGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSL-EGGYN 387
Cdd:cd11680   240 SGDPHKEWNLTIRGYGSVIELLLKEFKDKPTLLLgGGGYN 279
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
504-792 2.33e-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: 99.45  E-value: 2.33e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  504 HPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHL-RATEKMKTRELHRESSNFDSIYICP---ST 579
Cdd:cd11598    18 HPMKPFRLTLTKHLVMGYGLHKAMDTYEARAATREELRQFHDADYLDFLsKVSPENANQLRFDKAEPFNIGDDCPvfdGM 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  580 FACAQLATGAACRLVEAVLSGEvlNGAAVVRPPG-HHAEQDAACGFCFFNSVAVAARHAQAISGRalrILIVDWDVHHGN 658
Cdd:cd11598    98 YDYCQLYAGASLDAARKLCSGQ--SDIAINWSGGlHHAKKSEASGFCYVNDIVLAILNLLRYFPR---VLYIDIDVHHGD 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  659 GTQHMFEDDPSVLYVSLHRYDhGTFFPmgDEGASSQIGRAAGTGFTVNVAWNGPrMGDADYLAAWHRLVLPIAYEFNPEL 738
Cdd:cd11598   173 GVEEAFYRTDRVMTLSFHKYN-GEFFP--GTGDLDDNGGTPGKHFALNVPLEDG-IDDEQYNLLFKSIIGPTIEKFQPSA 248
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 967505306  739 VLVSAGFDAARGDPLGGCQVSPEGYAHLTHLlmgLASGRIILIL--EGGYNLTSIS 792
Cdd:cd11598   249 IVLQCGADSLGGDRLGQFNLNIKAHGACVKF---VKSFGIPMLVvgGGGYTPRNVA 301
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
573-796 5.61e-22

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


Pssm-ID: 212522 [Multi-domain]  Cd Length: 353  Bit Score: 99.06  E-value: 5.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  573 IYICPSTFACAQLATGAACRLVEAVLSGEVL--NGAAV-VRPPGHHAEQDAACGFCFFNSVAVAARHAqAISGRALRILI 649
Cdd:cd09998    76 LYLCPESLDAIQGALGAVCEAVDSVFKPESPgtKRAFVaIRPPGHHCSESTPSGFCWVNNVHVGAAHA-YLTHGITRVVI 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  650 VDWDVHHGNGTQHM------------------------FEDDPSVLYVSLHryDHGTF-----FPMGDEGASSQIGRAAG 700
Cdd:cd09998   155 LDIDLHHGNGTQDIawrinaeankqalesssyddfkpaGAPGLRIFYSSLH--DINSFpcedgDPAKVKDASVSIDGAHG 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  701 TgftvNVaWN---GPRMGDADY---LAAWHRLVLPIAYEF-------NPE--LVLVSAGFDAARGDPLG----GCQVSPE 761
Cdd:cd09998   233 Q----WI-WNvhlQPWTTEEDFwelYYPKYRILFEKAAEFlrlttaaTPFktLVFISAGFDASEHEYESmqrhGVNVPTS 307
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 967505306  762 GYAHLT----HLLMGLASGRIILILEGGYNLTSI-SESMA 796
Cdd:cd09998   308 FYYRFArdavRFADAHAHGRLISVLEGGYSDRALcSGVLA 347
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
489-792 6.07e-22

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


Pssm-ID: 212534 [Multi-domain]  Cd Length: 371  Bit Score: 99.37  E-value: 6.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  489 YDQSMMNHcnLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESS 568
Cdd:cd10010    12 YDGDVGNY--YYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQ 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  569 NFDSIYICP---STFACAQLATGAAcrLVEAVLSGEVLNGAAVVRPPG-HHAEQDAACGFCFFNSVAVAA----RHAQai 640
Cdd:cd10010    90 RFNVGEDCPvfdGLFEFCQLSAGGS--VASAVKLNKQQTDIAVNWAGGlHHAKKSEASGFCYVNDIVLAIlellKYHQ-- 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  641 sgralRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYdhGTFFPmgDEGASSQIGRAAGTGFTVNVAWNGPrMGDADYL 720
Cdd:cd10010   166 -----RVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKY--GEYFP--GTGDLRDIGAGKGKYYAVNYPLRDG-IDDESYE 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 967505306  721 AAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLaSGRIILILEGGYNLTSIS 792
Cdd:cd10010   236 AIFKPVMSKVMEMFQPSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEFVKSF-NLPMLMLGGGGYTIRNVA 306
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
484-796 1.31e-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: 98.34  E-value: 1.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  484 RTGLVYDQSMMNHCnlWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTREL 563
Cdd:cd10004     3 KVAYFYDSDVGNYA--YGPGHPMKPHRIRMAHSLVMNYGLYKKMEIYRAKPATKNEMTQFHTDEYIDFLSRVTPDNMEKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  564 HRESSNFDSIYICP---STFACAQLATGAACRLVEAVLSGE---VLNGAAVVrppgHHAEQDAACGFCFFNSVAVAA--- 634
Cdd:cd10004    81 QKEQVKYNVGDDCPvfdGLFEFCSISAGGSMEGAARLNRGKcdiAVNWAGGL----HHAKKSEASGFCYVNDIVLGIlel 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  635 -RHAQaisgralRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYdhGTFFPmgDEGASSQIGRAAGTGFTVNVAWngpR 713
Cdd:cd10004   157 lRYHQ-------RVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKY--GEYFP--GTGELRDIGIGTGKNYAVNVPL---R 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  714 MG--DADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLL--MGLAsgrIILILEGGYNLT 789
Cdd:cd10004   223 DGidDESYKSIFEPVIKHVMEWYQPEAVVLQCGGDSLSGDRLGCFNLSMKGHANCVNFVksFNLP---MLVLGGGGYTMR 299

                  ....*..
gi 967505306  790 SISESMA 796
Cdd:cd10004   300 NVARTWA 306
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
90-392 4.56e-21

Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I histone deacetylase (HDAC) Hos2 from Saccharomyces cerevisiae as well as a histone deacetylase Phd1 from Schizosaccharomyces pombe. Hos2 binds to the coding regions of genes during gene activation, specifically it deacetylates the lysines in H3 and H4 histone tails. It is preferentially associated with genes of high activity genome-wide and is shown to be necessary for efficient transcription. Thus, Hos2 is directly required for gene activation in contrast to other class I histone deacetylases. Protein encoded by phd1 is inhibited by trichostatin A (TSA), a specific inhibitor of histone deacetylase, and is involved in the meiotic cell cycle in S. pombe. Class 1 HDACs are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues in histone amino termini to yield a deacetylated histone (EC 3.5.1.98).


Pssm-ID: 212540 [Multi-domain]  Cd Length: 311  Bit Score: 95.60  E-value: 4.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   90 LDEQLNEFHclWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLM-----ETTQYMNEGEL 164
Cdd:cd11598     5 FNSRVEDYH--FGRTHPMKPFRLTLTKHLVMGYGLHKAMDTYEARAATREELRQFHDADYLDFLskvspENANQLRFDKA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  165 RVLADTYDSVYLHpNSYSCACLASGSVLrlvDAVlgAEIRNG---MAIIRPPG-HHAQHSLMDGYCMFNHVAVAA----R 236
Cdd:cd11598    83 EPFNIGDDCPVFD-GMYDYCQLYAGASL---DAA--RKLCSGqsdIAINWSGGlHHAKKSEASGFCYVNDIVLAIlnllR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  237 YaqqkhrIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYeQGRFWPhlKASNWSTTGFGQGQGYTINVPWNQvGMRD 316
Cdd:cd11598   157 Y------FPRVLYIDIDVHHGDGVEEAFYRTDRVMTLSFHKY-NGEFFP--GTGDLDDNGGTPGKHFALNVPLED-GIDD 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  317 ADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKG----EMAATPA--GFAQLTHLLMGLAGGklilsleGGYNLRA 390
Cdd:cd11598   227 EQYNLLFKSIIGPTIEKFQPSAIVLQCGADSLGGDRLGqfnlNIKAHGAcvKFVKSFGIPMLVVGG-------GGYTPRN 299

                  ..
gi 967505306  391 LA 392
Cdd:cd11598   300 VA 301
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
106-392 2.19e-20

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


Pssm-ID: 212534 [Multi-domain]  Cd Length: 371  Bit Score: 94.75  E-value: 2.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  106 PEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGE-------LRVLAD--TYDSVYL 176
Cdd:cd10010    26 PMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEyskqmqrFNVGEDcpVFDGLFE 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  177 HPNSYSCACLASGSVLRLVDAVLGAEIRNGMaiirppgHHAQHSLMDGYCMFNHVAVAARYAQQKHRirRVLIVDWDVHH 256
Cdd:cd10010   106 FCQLSAGGSVASAVKLNKQQTDIAVNWAGGL-------HHAKKSEASGFCYVNDIVLAILELLKYHQ--RVLYIDIDIHH 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  257 GQGTQFTFDQDPSVLYFSIHRYeqGRFWPhlKASNWSTTGFGQGQGYTINVPWNQvGMRDADYIAAFLHVLLPVALEFQP 336
Cdd:cd10010   177 GDGVEEAFYTTDRVMTVSFHKY--GEYFP--GTGDLRDIGAGKGKYYAVNYPLRD-GIDDESYEAIFKPVMSKVMEMFQP 251
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 967505306  337 QLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSlEGGYNLRALA 392
Cdd:cd10010   252 SAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLG-GGGYTIRNVA 306
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
106-392 8.53e-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: 92.95  E-value: 8.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  106 PEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMEttqymnegelRVLADTYDSVYLHPNSYS--- 182
Cdd:cd10004    22 PMKPHRIRMAHSLVMNYGLYKKMEIYRAKPATKNEMTQFHTDEYIDFLS----------RVTPDNMEKFQKEQVKYNvgd 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  183 -----------CACLASGSVLRlvdavlGAEIRNG---MAIIRPPG-HHAQHSLMDGYCMFNHVAVAA----RYAQqkhr 243
Cdd:cd10004    92 dcpvfdglfefCSISAGGSMEG------AARLNRGkcdIAVNWAGGlHHAKKSEASGFCYVNDIVLGIlellRYHQ---- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  244 irRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYeqGRFWP---HLKasnwsTTGFGQGQGYTINVPWNQvGMRDADYI 320
Cdd:cd10004   162 --RVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKY--GEYFPgtgELR-----DIGIGTGKNYAVNVPLRD-GIDDESYK 231
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 967505306  321 AAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKG------EMAATPAGFAQLTHLLMGLAGGklilsleGGYNLRALA 392
Cdd:cd10004   232 SIFEPVIKHVMEWYQPEAVVLQCGGDSLSGDRLGcfnlsmKGHANCVNFVKSFNLPMLVLGG-------GGYTMRNVA 302
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
1136-1185 2.07e-18

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 79.72  E-value: 2.07e-18
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 967505306   1136 PCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHENSGHPLVLSYIDLST 1185
Cdd:smart00290    1 RCSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
489-792 1.17e-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: 86.27  E-value: 1.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  489 YDQSMMNHcnLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESS 568
Cdd:cd10011     8 YDGDIGNY--YYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQ 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  569 NFDSIYICP---STFACAQLATGAAcrLVEAVLSGEVLNGAAVVRPPG-HHAEQDAACGFCFFNSVAVAA----RHAQai 640
Cdd:cd10011    86 RFNVGEDCPvfdGLFEFCQLSTGGS--VAGAVKLNRQQTDMAVNWAGGlHHAKKSEASGFCYVNDIVLAIlellKYHQ-- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  641 sgralRILIVDWDVHHGNGTQHMFEDDPSVLYVSlhRYDHGTFFPmgDEGASSQIGRAAGTGFTVNVAWNGPrMGDADYL 720
Cdd:cd10011   162 -----RVLYIDIDIHHGDGVEEAFYTTDRVMTVS--FHKYGEYFP--GTGDLRDIGAGKGKYYAVNFPMRDG-IDDESYG 231
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 967505306  721 AAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLaSGRIILILEGGYNLTSIS 792
Cdd:cd10011   232 QIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTF-NLPLLMLGGGGYTIRNVA 302
PTZ00063 PTZ00063
histone deacetylase; Provisional
504-796 1.81e-17

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 86.40  E-value: 1.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  504 HPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRE----LHR----ESSN---FDS 572
Cdd:PTZ00063   23 HPMKPQRIRMAHALILSYDLYKHMEIYRPHKSVEPELVLFHDEEYVDFLSSISPENYRDftyqLKRfnvgEATDcpvFDG 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  573 IYicpsTF--ACAQLATGAACRL------VEAVLSGEVlngaavvrppgHHAEQDAACGFCFFNSVAVA-----ARHAqa 639
Cdd:PTZ00063  103 LF----EFqqSCAGASIDGAYKLnnhqadICVNWSGGL-----------HHAKRSEASGFCYINDIVLGilellKYHA-- 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  640 isgralRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYdhGTFFPmgDEGASSQIGRAAGTGFTVNVAWNGPrMGDADY 719
Cdd:PTZ00063  166 ------RVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFP--GTGDVTDIGVAQGKYYSVNVPLNDG-IDDDSF 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 967505306  720 LAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILiLEGGYNLTSISESMA 796
Cdd:PTZ00063  235 VDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAACVEFVRSLNIPLLVL-GGGGYTIRNVARCWA 310
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
504-785 8.94e-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: 83.99  E-value: 8.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  504 HPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICP---STF 580
Cdd:cd10005    20 HPMKPHRLALTHSLVLHYGLYKKMQVYKPYRASAHDMCRFHSEDYIDFLQRVTPQNIQGFTKSLNQFNVGDDCPvfpGLF 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  581 ACAQLATGAAcrlveavLSGEV-LNGA----AVVRPPG-HHAEQDAACGFCFFNSVAVA-----ARHAqaisgralRILI 649
Cdd:cd10005   100 DFCSMYTGAS-------LEGATkLNHKicdiAINWSGGlHHAKKFEASGFCYVNDIVIAilellKYHP--------RVLY 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  650 VDWDVHHGNGTQHMFEDDPSVLYVSLHRYDhGTFFPmgDEGASSQIGRAAGTGFTVNVAW-NGprMGDADYLAAWHRLVL 728
Cdd:cd10005   165 IDIDIHHGDGVQEAFYLTDRVMTVSFHKYG-NYFFP--GTGDMYEVGAESGRYYSVNVPLkDG--IDDQSYLQLFKPVIQ 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 967505306  729 PIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLasGRIILILEGG 785
Cdd:cd10005   240 QVIDFYQPTCIVLQCGADSLGCDRLGCFNLSIKGHGECVEFVKSF--NIPLLVLGGG 294
PTZ00063 PTZ00063
histone deacetylase; Provisional
215-409 9.36e-16

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 81.40  E-value: 9.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  215 HHAQHSLMDGYCMFNHVAVAARYAQQKHRirRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYeqGRFWPhlKASNWST 294
Cdd:PTZ00063  137 HHAKRSEASGFCYINDIVLGILELLKYHA--RVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKF--GDFFP--GTGDVTD 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  295 TGFGQGQGYTINVPWNQvGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLA 374
Cdd:PTZ00063  211 IGVAQGKYYSVNVPLND-GIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAACVEFVRSLN 289
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 967505306  375 GGKLILSlEGGYNLRALAE------GVSASLHTLLGDPCPM 409
Cdd:PTZ00063  290 IPLLVLG-GGGYTIRNVARcwayetGVILNKHDEMSDQISL 329
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
106-392 1.89e-15

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


Pssm-ID: 212535 [Multi-domain]  Cd Length: 366  Bit Score: 79.72  E-value: 1.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  106 PEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGE-------LRVLAD--TYDSVYL 176
Cdd:cd10011    22 PMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEyskqmqrFNVGEDcpVFDGLFE 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  177 HpnsysCACLASGSVlrlVDAVLGAEIRNGMAIIRPPG-HHAQHSLMDGYCMFNHVAVAARYAQQKHriRRVLIVDWDVH 255
Cdd:cd10011   102 F-----CQLSTGGSV---AGAVKLNRQQTDMAVNWAGGlHHAKKSEASGFCYVNDIVLAILELLKYH--QRVLYIDIDIH 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  256 HGQGTQFTFDQDPSVLyfSIHRYEQGRFWPhlKASNWSTTGFGQGQGYTINVPWNQvGMRDADYIAAFLHVLLPVALEFQ 335
Cdd:cd10011   172 HGDGVEEAFYTTDRVM--TVSFHKYGEYFP--GTGDLRDIGAGKGKYYAVNFPMRD-GIDDESYGQIFKPIISKVMEMYQ 246
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 967505306  336 PQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSlEGGYNLRALA 392
Cdd:cd10011   247 PSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLG-GGGYTIRNVA 302
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
91-392 6.73e-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: 78.21  E-value: 6.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   91 DEQLNEFHclWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLME--TTQYMNE-----GE 163
Cdd:cd10005     8 DPDVGNFH--YGPGHPMKPHRLALTHSLVLHYGLYKKMQVYKPYRASAHDMCRFHSEDYIDFLQrvTPQNIQGftkslNQ 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  164 LRVLAD--TYDSVYLHPNSYSCACLaSGSVlrlvdavlgaEIRNGM---AIIRPPG-HHAQHSLMDGYCMFNHVAVAARY 237
Cdd:cd10005    86 FNVGDDcpVFPGLFDFCSMYTGASL-EGAT----------KLNHKIcdiAINWSGGlHHAKKFEASGFCYVNDIVIAILE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  238 AQQKHRirRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYeQGRFWPhlKASNWSTTGFGQGQGYTINVPWNQvGMRDA 317
Cdd:cd10005   155 LLKYHP--RVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKY-GNYFFP--GTGDMYEVGAESGRYYSVNVPLKD-GIDDQ 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 967505306  318 DYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSlEGGYNLRALA 392
Cdd:cd10005   229 SYLQLFKPVIQQVIDFYQPTCIVLQCGADSLGCDRLGCFNLSIKGHGECVEFVKSFNIPLLVLG-GGGYTVRNVA 302
PTZ00346 PTZ00346
histone deacetylase; Provisional
503-796 2.24e-13

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 73.91  E-value: 2.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  503 HHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLrATEKMKTRELHRESSNFDSIYICPSTFAC 582
Cdd:PTZ00346   42 QHAMKPYRVLAAMEIVRSLKIDAHCRTVVPPLVKVEELMAYHTDTYLANL-GLHSCRSWLWNAETSKVFFSGDCPPVEGL 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  583 AQLATGAAC-RLVEAVL--SGEVlnGAAVVRPPG-HHAEQDAACGFCFFNSVAVAARHAQAISGRalrILIVDWDVHHGN 658
Cdd:PTZ00346  121 MEHSIATASgTLMGAVLlnSGQV--DVAVHWGGGmHHSKCGECSGFCYVNDIVLGILELLKCHDR---VLYVDIDMHHGD 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  659 GTQHMFEDDPSVLYVSLHRYDHgTFFPmgDEGASSQIGRAAGTGFTVNVA-WNGprMGDADYLAAWHRLVLPIAYEFNPE 737
Cdd:PTZ00346  196 GVDEAFCTSDRVFTLSLHKFGE-SFFP--GTGHPRDVGYGRGRYYSMNLAvWDG--ITDFYYLGLFEHALHSIVRRYSPD 270
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  738 LVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLasGRIILIL-EGGYNLTSISESMA 796
Cdd:PTZ00346  271 AIVLQCGADSLAGDRLGLLNLSSFGHGQCVQAVRDL--GIPMLALgGGGYTIRNVAKLWA 328
PTZ00346 PTZ00346
histone deacetylase; Provisional
215-409 4.09e-13

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 73.14  E-value: 4.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  215 HHAQHSLMDGYCMFNHVAVAARYAQQKHRirRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGrFWPhlKASNWST 294
Cdd:PTZ00346  154 HHSKCGECSGFCYVNDIVLGILELLKCHD--RVLYVDIDMHHGDGVDEAFCTSDRVFTLSLHKFGES-FFP--GTGHPRD 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  295 TGFGQGQGYTINVP-WNqvGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGL 373
Cdd:PTZ00346  229 VGYGRGRYYSMNLAvWD--GITDFYYLGLFEHALHSIVRRYSPDAIVLQCGADSLAGDRLGLLNLSSFGHGQCVQAVRDL 306
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 967505306  374 AGGKLILSlEGGYNLRALAEGVSASLHTLLGDPCPM 409
Cdd:PTZ00346  307 GIPMLALG-GGGYTIRNVAKLWAYETSILTGHPLPP 341
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
590-801 1.03e-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: 59.70  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  590 ACRLVEAVLSGEVLNGAAVVRPPGHHAEqdaacgfcfFNSVAVAarHAQAISgralRILIVDWDVHHGNGTQHMF----- 664
Cdd:cd09987    10 AHELLAGVVVAVLKDGKVPVVLGGDHSI---------ANGAIRA--VAELHP----DLGVIDVDAHHDVRTPEAFgkgnh 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  665 ---------EDDPSVLYVSLHRYDHGTFFPMGDegassqigrAAGTGFTVNVAWNGPRmgDADYLAAWHRLVLPIayEFN 735
Cdd:cd09987    75 htprhllcePLISDVHIVSIGIRGVSNGEAGGA---------YARKLGVVYFSMTEVD--KLGLGDVFEEIVSYL--GDK 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967505306  736 PELVLVSAGFDAARGDPLGGCQ------VSPEGYAHLTHLLMGLAsGRIILILEGGYNL----TSISESMAACTRS 801
Cdd:cd09987   142 GDNVYLSVDVDGLDPSFAPGTGtpgpggLSYREGLYITERIAKTN-LVVGLDIVEVNPLldetGRTARLAAALTLE 216
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
214-405 1.63e-07

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


Pssm-ID: 212513  Cd Length: 217  Bit Score: 53.53  E-value: 1.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  214 GHHAqhslmdgycMFNHVAVAARYAQQkhrirRVLIVDWDVHHGQGTQFTF--------------DQDPSVLYFSIHRYE 279
Cdd:cd09987    33 GDHS---------IANGAIRAVAELHP-----DLGVIDVDAHHDVRTPEAFgkgnhhtprhllcePLISDVHIVSIGIRG 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  280 QGRFWPHlkasnwsttGFGQGQGYTINVPWNQVgmRDADYIAAFLHVLLPValEFQPQLVLVAAGFDALQGDPkGEMAAT 359
Cdd:cd09987    99 VSNGEAG---------GAYARKLGVVYFSMTEV--DKLGLGDVFEEIVSYL--GDKGDNVYLSVDVDGLDPSF-APGTGT 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 967505306  360 PAGFaqlthllmGLA--GGKLILSLEGGYNLRALAEGVsaSLHTLLGD 405
Cdd:cd09987   165 PGPG--------GLSyrEGLYITERIAKTNLVVGLDIV--EVNPLLDE 202
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
887-1049 2.11e-06

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 51.88  E-value: 2.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   887 TSASSGEESTPGQTKSETAVVALTQDQSSEAATGGATLAQTISEAavggamlgQTTSEEAVGGATPDQTTSEKTVGGATL 966
Cdd:pfam17823  165 ASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPA--------RGISTAATATGHPAAGTALAAVGNSSP 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306   967 DQTTSEDAVGgatlgqTTSEEAVGG-ATLAQTTSEAAMEGATLDQTTSEEAPGGTeliqTPLASSTDHQTPPTSP-VQGT 1044
Cdd:pfam17823  237 AAGTVTAAVG------TVTPAALATlAAAAGTVASAAGTINMGDPHARRLSPAKH----MPSDTMARNPAAPMGAqAQGP 306

                   ....*
gi 967505306  1045 TPQIS 1049
Cdd:pfam17823  307 IIQVS 311
PRK11907 PRK11907
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
928-1045 2.01e-03

bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;


Pssm-ID: 237019 [Multi-domain]  Cd Length: 814  Bit Score: 42.53  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505306  928 ISEAAVGGAMLGQTTSEEAVGGATPDQTTSEKTvgGATLDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAmegat 1007
Cdd:PRK11907    6 FSKSAVALTLALLTASNPKLAQAEEIVTTTPAT--STEAEQTTPVESDATEEADNTETPVAATTAAEAPSSSETA----- 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 967505306 1008 ldqTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTT 1045
Cdd:PRK11907   79 ---ETSDPTSEATDTTTSEARTVTPAATETSKPVEGQT 113
zf-UBP_var pfam17807
Variant UBP zinc finger; This domain is found in ubiquitin C-terminal hydrolase enzymes and is ...
1148-1178 6.81e-03

Variant UBP zinc finger; This domain is found in ubiquitin C-terminal hydrolase enzymes and is related to the pfam02148 domain. However, it has an altered pattern of zinc binding residues.


Pssm-ID: 407678  Cd Length: 64  Bit Score: 36.42  E-value: 6.81e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 967505306  1148 VCLSCYQVYCGRyingHMLQHHENSGHPLVL 1178
Cdd:pfam17807   30 VCLKCFLGFCKK----HAQLHFERTGHPVYL 56
 
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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