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Conserved domains on  [gi|1370521764|ref|XP_016885129|]
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histone deacetylase 8 isoform X1 [Homo sapiens]

Protein Classification

histone deacetylase 8( domain architecture ID 10177994)

histone deacetylase 8 (HD8) 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)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 16-345 0e+00

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: 642.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  16 PVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHP--DS 93
Cdd:cd10000     1 VVYIHSPEYVNLCDRLPKVPNRASMVHSLIEAYGLLKQLRVVKPRVATEEELASFHSDEYIQFLKKASNEGDNDEEpsEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  94 IEYGLGYDCPATEGIFDYAAAIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERIL 173
Cdd:cd10000    81 QEFGLGYDCPIFEGIYDYAAAVAGATLTAAQLLIDGKCKVAINWFGGWHHAQRDEASGFCYVNDIVLGILKLREKFDRVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 174 YVDLDLHHGDG--------------------------TGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQ 227
Cdd:cd10000   161 YVDLDLHHGDGvedafsftskvmtvslhkyspgffpgTGDVSDVGLGKGKYYTVNVPLRDGIQDEQYLQIFTAVVPEIVA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 228 AFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPD 307
Cdd:cd10000   241 AFRPEAVVLQCGADTLAGDPMGAFNLTPVGIGKCLKYVLGWKLPTLILGGGGYNLANTARCWTYLTGLILGEPLSSDIPD 320

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1370521764 308 HEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKE 345
Cdd:cd10000   321 HEFFTSYGPDYELEISPSLRPDLNEDQYIEKILETIKG 358
 
Name Accession Description Interval E-value
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 16-345 0e+00

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: 642.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  16 PVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHP--DS 93
Cdd:cd10000     1 VVYIHSPEYVNLCDRLPKVPNRASMVHSLIEAYGLLKQLRVVKPRVATEEELASFHSDEYIQFLKKASNEGDNDEEpsEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  94 IEYGLGYDCPATEGIFDYAAAIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERIL 173
Cdd:cd10000    81 QEFGLGYDCPIFEGIYDYAAAVAGATLTAAQLLIDGKCKVAINWFGGWHHAQRDEASGFCYVNDIVLGILKLREKFDRVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 174 YVDLDLHHGDG--------------------------TGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQ 227
Cdd:cd10000   161 YVDLDLHHGDGvedafsftskvmtvslhkyspgffpgTGDVSDVGLGKGKYYTVNVPLRDGIQDEQYLQIFTAVVPEIVA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 228 AFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPD 307
Cdd:cd10000   241 AFRPEAVVLQCGADTLAGDPMGAFNLTPVGIGKCLKYVLGWKLPTLILGGGGYNLANTARCWTYLTGLILGEPLSSDIPD 320

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1370521764 308 HEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKE 345
Cdd:cd10000   321 HEFFTSYGPDYELEISPSLRPDLNEDQYIEKILETIKG 358
PTZ00063 PTZ00063
histone deacetylase; Provisional
 35-339 7.42e-94

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 287.48  E-value: 7.42e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIE---YGLGYDCPATEGIFDY 111
Cdd:PTZ00063   27 PQRIRMAHALILSYDLYKHMEIYRPHKSVEPELVLFHDEEYVDFLSSISPENYRDFTYQLKrfnVGEATDCPVFDGLFEF 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 112 AAAIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDG------- 184
Cdd:PTZ00063  107 QQSCAGASIDGAYKLNNHQADICVNWSGGLHHAKRSEASGFCYINDIVLGILELLKYHARVMYIDIDVHHGDGveeafyv 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 185 ------------------TGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGD 246
Cdd:PTZ00063  187 thrvmtvsfhkfgdffpgTGDVTDIGVAQGKYYSVNVPLNDGIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGD 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 247 PMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKT--LSSEIPDHEFFTAYGPDYVLEITP 324
Cdd:PTZ00063  267 RLGRFNLTIKGHAACVEFVRSLNIPLLVLGGGGYTIRNVARCWAYETGVILNKHdeMSDQISLNDYYDYYAPDFQLHLQP 346

                         330
                  ....*....|....*
gi 1370521764 325 SCRPDRNEPHRIQQI 339
Cdd:PTZ00063  347 SNIPNYNSPEHLEKI 361
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 35-296 5.89e-84

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: 257.16  E-value: 5.89e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIEYGlGYDCPATEGIFDYAAA 114
Cdd:pfam00850   5 PERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAAPEGGALLLLSYLSG-DDDTPVSPGSYEAALL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 115 IGGATITAAQCLIDGMCK--VAINWsGGWHHAKKDEASGFCYLNDAVLGILRLRRK--FERILYVDLDLHHGDGT----- 185
Cdd:pfam00850  84 AAGGTLAAADAVLSGEARnaFALVR-PPGHHAERDRASGFCIFNNVAIAAKYLREKygLKRVAIVDFDVHHGNGTqeify 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 186 ---------------------GDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIA 244
Cdd:pfam00850 163 ddpsvltlsihqypggfypgtGFADETGEGKGKGYTLNVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAGFDAHA 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370521764 245 GDPMCSFNMTPVGIGKCLKYILQWQLAT----LILGGGGYNLANTARCWTYLTGVI 296
Cdd:pfam00850 243 GDPLGGLNLTTEGFAEITRILLELADPLcirvVSVLEGGYNLDALARSATAVLAAL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 18-298 2.78e-65

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 209.58  E-value: 2.78e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  18 YIYSPEYVS--------MCdslakiPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGddd 89
Cdd:COG0123     3 LIYHPDYLLhdlgpghpEP------PERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAASLDG--- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  90 hpdsiEYG-LGYDCPATEGIFDYAAAIGGATITAAQCLIDGMCKVA-INWSGGWHHAKKDEASGFCYLNDAVLGILRLRR 167
Cdd:COG0123    74 -----GYGqLDPDTPVSPGTWEAALLAAGGALAAADAVLEGEARNAfALVRPPGHHAERDRAMGFCLFNNAAIAARYLLA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 168 K-FERILYVDLDLHHGDGT------------------------GDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVL 222
Cdd:COG0123   149 KgLERVAIVDFDVHHGNGTqdifyddpdvltisihqdplypgtGAADETGEGAGEGSNLNVPLPPGTGDAEYLAALEEAL 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 223 KEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQW----QLATLILGGGGYNLANTARCWTYLTGVILG 298
Cdd:COG0123   229 LPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELadhcGGPVVSVLEGGYNLDALARSVAAHLETLLG 308
 
Name Accession Description Interval E-value
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 16-345 0e+00

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: 642.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  16 PVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHP--DS 93
Cdd:cd10000     1 VVYIHSPEYVNLCDRLPKVPNRASMVHSLIEAYGLLKQLRVVKPRVATEEELASFHSDEYIQFLKKASNEGDNDEEpsEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  94 IEYGLGYDCPATEGIFDYAAAIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERIL 173
Cdd:cd10000    81 QEFGLGYDCPIFEGIYDYAAAVAGATLTAAQLLIDGKCKVAINWFGGWHHAQRDEASGFCYVNDIVLGILKLREKFDRVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 174 YVDLDLHHGDG--------------------------TGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQ 227
Cdd:cd10000   161 YVDLDLHHGDGvedafsftskvmtvslhkyspgffpgTGDVSDVGLGKGKYYTVNVPLRDGIQDEQYLQIFTAVVPEIVA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 228 AFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPD 307
Cdd:cd10000   241 AFRPEAVVLQCGADTLAGDPMGAFNLTPVGIGKCLKYVLGWKLPTLILGGGGYNLANTARCWTYLTGLILGEPLSSDIPD 320

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1370521764 308 HEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKE 345
Cdd:cd10000   321 HEFFTSYGPDYELEISPSLRPDLNEDQYIEKILETIKG 358
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
 19-296 1.74e-150

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: 427.00  E-value: 1.74e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  19 IYSPEYVSMCDSL--AKIPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDD-HPDSIE 95
Cdd:cd09991     1 FYDPDVGNYYYGQghPMKPHRIRMTHSLILSYGLYKKMEIYRPRPATAEELTKFHSDDYIDFLRSVSPDNMKEfKKQLER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  96 YGLGYDCPATEGIFDYAAAIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYV 175
Cdd:cd09991    81 FNVGEDCPVFDGLYEYCQLYAGGSIAAAVKLNRGQADIAINWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 176 DLDLHHGDG-------------------------TGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFN 230
Cdd:cd09991   161 DIDIHHGDGveeafyttdrvmtvsfhkfgeyffpGTGLRDIGAGKGKYYAVNVPLKDGIDDESYLQIFEPVLSKVMEVFQ 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370521764 231 PKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVI 296
Cdd:cd09991   241 PSAVVLQCGADSLAGDRLGCFNLSIKGHAKCVKFVKSFNIPLLVLGGGGYTLRNVARCWTYETAVL 306
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
 35-345 7.84e-103

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: 308.56  E-value: 7.84e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSI-EYGLGYDCPATEGIFDYAA 113
Cdd:cd10005    24 PHRLALTHSLVLHYGLYKKMQVYKPYRASAHDMCRFHSEDYIDFLQRVTPQNIQGFTKSLnQFNVGDDCPVFPGLFDFCS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 114 AIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDG--------- 184
Cdd:cd10005   104 MYTGASLEGATKLNHKICDIAINWSGGLHHAKKFEASGFCYVNDIVIAILELLKYHPRVLYIDIDIHHGDGvqeafyltd 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 185 -----------------TGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDP 247
Cdd:cd10005   184 rvmtvsfhkygnyffpgTGDMYEVGAESGRYYSVNVPLKDGIDDQSYLQLFKPVIQQVIDFYQPTCIVLQCGADSLGCDR 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 248 MCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCR 327
Cdd:cd10005   264 LGCFNLSIKGHGECVEFVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVDEEISNELPYNEYFEYFAPDFTLHPDVSTR 343

                         330
                  ....*....|....*....
gi 1370521764 328 PD-RNEPHRIQQILNYIKE 345
Cdd:cd10005   344 IEnQNSKQYLDQIRQTVFE 362
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
 35-345 3.04e-101

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: 304.42  E-value: 3.04e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDH-PDSIEYGLGYDCPATEGIFDYAA 113
Cdd:cd10004    25 PHRIRMAHSLVMNYGLYKKMEIYRAKPATKNEMTQFHTDEYIDFLSRVTPDNMEKFqKEQVKYNVGDDCPVFDGLFEFCS 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 114 AIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDG--------- 184
Cdd:cd10004   105 ISAGGSMEGAARLNRGKCDIAVNWAGGLHHAKKSEASGFCYVNDIVLGILELLRYHQRVLYIDIDVHHGDGveeafyttd 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 185 ----------------TGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPM 248
Cdd:cd10004   185 rvmtcsfhkygeyfpgTGELRDIGIGTGKNYAVNVPLRDGIDDESYKSIFEPVIKHVMEWYQPEAVVLQCGGDSLSGDRL 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 249 CSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRP 328
Cdd:cd10004   265 GCFNLSMKGHANCVNFVKSFNLPMLVLGGGGYTMRNVARTWAFETGLLAGEELDKDLPYNEYYEYYGPDYELNVRPSNME 344

                         330
                  ....*....|....*..
gi 1370521764 329 DRNEPHRIQQILNYIKE 345
Cdd:cd10004   345 NHNTPEYLDKITTAVIE 361
PTZ00063 PTZ00063
histone deacetylase; Provisional
 35-339 7.42e-94

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 287.48  E-value: 7.42e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIE---YGLGYDCPATEGIFDY 111
Cdd:PTZ00063   27 PQRIRMAHALILSYDLYKHMEIYRPHKSVEPELVLFHDEEYVDFLSSISPENYRDFTYQLKrfnVGEATDCPVFDGLFEF 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 112 AAAIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDG------- 184
Cdd:PTZ00063  107 QQSCAGASIDGAYKLNNHQADICVNWSGGLHHAKRSEASGFCYINDIVLGILELLKYHARVMYIDIDVHHGDGveeafyv 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 185 ------------------TGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGD 246
Cdd:PTZ00063  187 thrvmtvsfhkfgdffpgTGDVTDIGVAQGKYYSVNVPLNDGIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGD 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 247 PMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKT--LSSEIPDHEFFTAYGPDYVLEITP 324
Cdd:PTZ00063  267 RLGRFNLTIKGHAACVEFVRSLNIPLLVLGGGGYTIRNVARCWAYETGVILNKHdeMSDQISLNDYYDYYAPDFQLHLQP 346

                         330
                  ....*....|....*
gi 1370521764 325 SCRPDRNEPHRIQQI 339
Cdd:PTZ00063  347 SNIPNYNSPEHLEKI 361
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
 35-339 2.96e-93

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: 283.88  E-value: 2.96e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIE-YGLGYDCPATEGIFDYAA 113
Cdd:cd10010    29 PHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQrFNVGEDCPVFDGLFEFCQ 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 114 AIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDG--------- 184
Cdd:cd10010   109 LSAGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGveeafyttd 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 185 ----------------TGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPM 248
Cdd:cd10010   189 rvmtvsfhkygeyfpgTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGADSLSGDRL 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 249 CSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRP 328
Cdd:cd10010   269 GCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDSEIPNELPYNDYFEYFGPDFKLHISPSNMT 348

                         330
                  ....*....|.
gi 1370521764 329 DRNEPHRIQQI 339
Cdd:cd10010   349 NQNTNEYLEKI 359
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
 35-339 1.12e-92

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: 282.34  E-value: 1.12e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIE-YGLGYDCPATEGIFDYAA 113
Cdd:cd10011    25 PHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQrFNVGEDCPVFDGLFEFCQ 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 114 AIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDG--------- 184
Cdd:cd10011   105 LSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGveeafyttd 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 185 ----------------TGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPM 248
Cdd:cd10011   185 rvmtvsfhkygeyfpgTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRL 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 249 CSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRP 328
Cdd:cd10011   265 GCFNLTVKGHAKCVEVVKTFNLPLLMLGGGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMT 344

                         330
                  ....*....|.
gi 1370521764 329 DRNEPHRIQQI 339
Cdd:cd10011   345 NQNTPEYMEKI 355
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
 35-295 1.98e-89

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: 272.02  E-value: 1.98e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVS-QEGDDDHPDSIE-YGLGYDCPATEGIFDYA 112
Cdd:cd11598    22 PFRLTLTKHLVMGYGLHKAMDTYEARAATREELRQFHDADYLDFLSKVSpENANQLRFDKAEpFNIGDDCPVFDGMYDYC 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 113 AAIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDG-------- 184
Cdd:cd11598   102 QLYAGASLDAARKLCSGQSDIAINWSGGLHHAKKSEASGFCYVNDIVLAILNLLRYFPRVLYIDIDVHHGDGveeafyrt 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 185 ------------------TGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGD 246
Cdd:cd11598   182 drvmtlsfhkyngeffpgTGDLDDNGGTPGKHFALNVPLEDGIDDEQYNLLFKSIIGPTIEKFQPSAIVLQCGADSLGGD 261

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1370521764 247 PMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGV 295
Cdd:cd11598   262 RLGQFNLNIKAHGACVKFVKSFGIPMLVVGGGGYTPRNVARAWCYETAV 310
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
 17-296 3.10e-87

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: 265.67  E-value: 3.10e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  17 VYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQM-RIVKPKVASMEEMATFHTDAYLQHLQKvsqegdddhpdsiE 95
Cdd:cd11680     1 ILSVSEELTKIADLLPSNKGRSSLVHSLIRAYGLLQHFdEIIEPERATRKDLTKYHDKDYVDFLLK-------------K 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  96 YGLGYDCPATEGIFDYAAAIGGATITAAQCLIDGMCK-VAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRK-FERIL 173
Cdd:cd11680    68 YGLEDDCPVFPFLSMYVQLVAGSSLALAKHLITQVERdIAINWYGGRHHAQKSRASGFCYVNDIVLAILRLRRArFRRVF 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 174 YVDLDLHHGDG--------------------------TGDVSDvglgKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQ 227
Cdd:cd11680   148 YLDLDLHHGDGvesafffsknvltcsihrydpgffpgTGSLKN----SSDKGMLNIPLKRGLSDKTLLRIIDSIVRPLIE 223

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370521764 228 AFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQW--QLATLILGGGGYNLANTARCWTYLTGVI 296
Cdd:cd11680   224 KFEPEVIVIQCGCDGLSGDPHKEWNLTIRGYGSVIELLLKEfkDKPTLLLGGGGYNHTEAARAWTYLTSMV 294
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
 35-296 2.47e-84

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: 258.64  E-value: 2.47e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDhpDSIEYGLG-YDCPATEGIFDYAA 113
Cdd:cd09994    21 PPRLSLTKDLLRALGLLPPVDLVPPRPATEEELLLFHTPDYIEAVKEASRGQEPE--GRGRLGLGtEDNPVFPGMHEAAA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 114 AIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRK-FERILYVDLDLHHGDG-------- 184
Cdd:cd09994    99 LVVGGTLLAARLVLEGEARRAFNPAGGLHHAMRGRASGFCVYNDAAVAIERLRDKgGLRVAYVDIDAHHGDGvqaafydd 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 185 ------------------TGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGD 246
Cdd:cd09994   179 prvltislhesgrylfpgTGFVDEIGEGEGYGYAVNIPLPPGTGDDEFLRAFEAVVPPLLRAFRPDVIVSQHGADAHAGD 258

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370521764 247 PMCSFNMTPVGIGKCLKYILQW-----QLATLILGGGGYNLANTARCWTYLTGVI 296
Cdd:cd09994   259 PLTHLNLSNRAYRAAVRRIRELadeycGGRWLALGGGGYNPDVVARAWALLWAVL 313
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 35-296 5.89e-84

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: 257.16  E-value: 5.89e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIEYGlGYDCPATEGIFDYAAA 114
Cdd:pfam00850   5 PERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAAPEGGALLLLSYLSG-DDDTPVSPGSYEAALL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 115 IGGATITAAQCLIDGMCK--VAINWsGGWHHAKKDEASGFCYLNDAVLGILRLRRK--FERILYVDLDLHHGDGT----- 185
Cdd:pfam00850  84 AAGGTLAAADAVLSGEARnaFALVR-PPGHHAERDRASGFCIFNNVAIAAKYLREKygLKRVAIVDFDVHHGNGTqeify 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 186 ---------------------GDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIA 244
Cdd:pfam00850 163 ddpsvltlsihqypggfypgtGFADETGEGKGKGYTLNVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAGFDAHA 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370521764 245 GDPMCSFNMTPVGIGKCLKYILQWQLAT----LILGGGGYNLANTARCWTYLTGVI 296
Cdd:pfam00850 243 GDPLGGLNLTTEGFAEITRILLELADPLcirvVSVLEGGYNLDALARSATAVLAAL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 18-298 2.78e-65

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 209.58  E-value: 2.78e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  18 YIYSPEYVS--------MCdslakiPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGddd 89
Cdd:COG0123     3 LIYHPDYLLhdlgpghpEP------PERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAASLDG--- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  90 hpdsiEYG-LGYDCPATEGIFDYAAAIGGATITAAQCLIDGMCKVA-INWSGGWHHAKKDEASGFCYLNDAVLGILRLRR 167
Cdd:COG0123    74 -----GYGqLDPDTPVSPGTWEAALLAAGGALAAADAVLEGEARNAfALVRPPGHHAERDRAMGFCLFNNAAIAARYLLA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 168 K-FERILYVDLDLHHGDGT------------------------GDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVL 222
Cdd:COG0123   149 KgLERVAIVDFDVHHGNGTqdifyddpdvltisihqdplypgtGAADETGEGAGEGSNLNVPLPPGTGDAEYLAALEEAL 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 223 KEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQW----QLATLILGGGGYNLANTARCWTYLTGVILG 298
Cdd:COG0123   229 LPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELadhcGGPVVSVLEGGYNLDALARSVAAHLETLLG 308
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
 37-296 1.94e-61

Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family includes Zn-dependent histone deacetylase classes I, II and IV (class III HDACs, also called sirtuins, are NAD-dependent and structurally unrelated, and therefore not part of this family). Histone deacetylases catalyze hydrolysis of N(6)-acetyl-lysine residues in histone amino termini to yield a deacetylated histone (EC 3.5.1.98), as opposed to the acetylation reaction by some histone acetyltransferases (EC 2.3.1.48). Deacetylases of this family are involved in signal transduction through histone and other protein modification, and can repress/activate transcription of a number of different genes. They usually act via the formation of large multiprotein complexes. They are involved in various cellular processes, including cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and post-translational control of the acetyl coenzyme A synthetase. In mammals, they are known to be involved in progression of different tumors. Specific inhibitors of mammalian histone deacetylases are an emerging class of promising novel anticancer drugs.


Pssm-ID: 212512 [Multi-domain]  Cd Length: 279  Bit Score: 198.81  E-value: 1.94e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  37 RASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKvsQEGDDDHPDSIEYGLGYDCPATEGIFDYAAAIG 116
Cdd:cd09301     1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKA--NFAVATITESKPVIFGPNFPVQRHYFRGARLST 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 117 GATITAAQCLIDGMCKVAINW-SGGWHHAKKDEASGFCYLNDAVLGILRLRRK-FERILYVDLDLHHGDGT--------- 185
Cdd:cd09301    79 GGVVEAAELVAKGELERAFAVvGAGGHHAGKSRAWGFCYFNDVVLAIKFLRERgISRILIIDTDAHHGDGTreafydddr 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 186 --------GDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVG 257
Cdd:cd09301   159 vlhmsfhnYDIYPFGRGKGKGYKINVPLEDGLGDEEYLDAVERVISKVLEEFEPEVVVLQFGHDTHEGDRLGGFNLSEKG 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1370521764 258 IGKCLKYI--LQWQLATLILGGGGYNLANTARCWTYLTGVI 296
Cdd:cd09301   239 FVKLAEIVkeFARGGPILMVLGGGYNPEAAARIWTAIIKEL 279
PTZ00346 PTZ00346
histone deacetylase; Provisional
 35-301 1.18e-58

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 196.41  E-value: 1.18e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIEYGLGYDCPATEGIFDYAAA 114
Cdd:PTZ00346   47 PYRVLAAMEIVRSLKIDAHCRTVVPPLVKVEELMAYHTDTYLANLGLHSCRSWLWNAETSKVFFSGDCPPVEGLMEHSIA 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 115 IGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDG---------- 184
Cdd:PTZ00346  127 TASGTLMGAVLLNSGQVDVAVHWGGGMHHSKCGECSGFCYVNDIVLGILELLKCHDRVLYVDIDMHHGDGvdeafctsdr 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 185 ----------------TGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPM 248
Cdd:PTZ00346  207 vftlslhkfgesffpgTGHPRDVGYGRGRYYSMNLAVWDGITDFYYLGLFEHALHSIVRRYSPDAIVLQCGADSLAGDRL 286

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370521764 249 CSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTL 301
Cdd:PTZ00346  287 GLLNLSSFGHGQCVQAVRDLGIPMLALGGGGYTIRNVAKLWAYETSILTGHPL 339
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
 35-288 9.08e-37

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: 134.55  E-value: 9.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDD-DHPDsieyglgydCPATEGIFD--Y 111
Cdd:cd09992     5 PERLLAILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYIERVEETCEAGGGyLDPD---------TYVSPGSYEaaL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 112 AAAigGATITAAQCLIDGMCK---VAINWSGgwHHAKKDEASGFCYLNDAVLGI--LRLRRKFERILYVDLDLHHGDGT- 185
Cdd:cd09992    76 LAA--GAALAAVDAVLSGEAEnafALVRPPG--HHAEPDRAMGFCLFNNVAIAAryAQKRYGLKRVLIVDWDVHHGNGTq 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 186 -----------------------GDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADT 242
Cdd:cd09992   152 difyddpsvlyfsihqypfypgtGAAEETGGGAGEGFTINVPLPPGSGDAEYLAAFEEVLLPIAREFQPDLVLVSAGFDA 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370521764 243 IAGDPMCSFNMTPVGIGKCLKYILqwQLATLILGG-------GGYNLANTARC 288
Cdd:cd09992   232 HRGDPLGGMNLTPEGYARLTRLLK--ELADEHCGGrlvfvleGGYNLEALAES 282
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
 34-283 2.81e-33

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: 125.73  E-value: 2.81e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  34 IPKRASMVHSLIEAYALhkqMRIVKPKVASMEEMATFHTDAYLQHLQKVSQegdddhpdsieyglgyDCPATEGIFDYAA 113
Cdd:cd10001    28 NPERAEAILDALKRAGL---GEVLPPRDFGLEPILAVHDPDYVDFLETADT----------------DTPISEGTWEAAL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 114 AIGGATITAAQCLIDGmCKVAINWS---GgwHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDGT----- 185
Cdd:cd10001    89 AAADTALTAADLVLEG-ERAAYALCrppG--HHAGRDRAGGFCYFNNAAIAAQYLRDRAGRVAILDVDVHHGNGTqeify 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 186 ----------------------GDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVyQAFNPKAVVLQLGADTI 243
Cdd:cd10001   166 erpdvlyvsihgdprtfypfflGFADETGEGEGEGYNLNLPLPPGTGDDDYLAALDEALAAI-AAFGPDALVVSLGFDTH 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1370521764 244 AGDPMCSFNMTPVG---IGKClkyILQWQLATLILGGGGYNLA 283
Cdd:cd10001   245 EGDPLSDFKLTTEDyarIGRR---IAALGLPTVFVQEGGYNVD 284
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
 23-303 1.00e-32

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: 125.53  E-value: 1.00e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  23 EYVSMCDS-LAKIPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDD-HPDSIEYGLGY 100
Cdd:cd10003     7 NHHNLWDPgHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHLDEMKSLEKMKPRElNRLGKEYDSIY 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 101 DCPATegiFDYAAAIGGATITAAQCLIDGMCK--VAINWSGGwHHAKKDEASGFCYLNDAVLGILRLRRKF--ERILYVD 176
Cdd:cd10003    87 IHPDS---YQCALLAAGCVLQVVEAVLTGESRngVAIVRPPG-HHAEQDTACGFCFFNNVAIAARYAQKKYglKRILIVD 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 177 LDLHHGDGT-----------------------------GDVSDVGLGKGRYYSVNVPI-QDGIQDEKYYQICESVLKEVY 226
Cdd:cd10003   163 WDVHHGNGTqhmfesdpsvlyislhrydngsffpnspeGNYDVVGKGKGEGFNVNIPWnKGGMGDAEYIAAFQQVVLPIA 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 227 QAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKclkyiLQWQLATLILGG------GGYNLANTARCWTYLTGVILGKT 300
Cdd:cd10003   243 YEFNPELVLVSAGFDAARGDPLGGCKVTPEGYAH-----MTHMLMSLAGGRvivileGGYNLTSISESMSMCTKTLLGDP 317


                  ...
gi 1370521764 301 LSS 303
Cdd:cd10003   318 PPV 320
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 37-281 1.22e-32

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


Pssm-ID: 212519 [Multi-domain]  Cd Length: 275  Bit Score: 123.38  E-value: 1.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  37 RASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLqkVSQEGDDDHPDSIEYglgydcPATEGIFDYAAAIG 116
Cdd:cd09993     7 KYGLLREALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLESL--KSGELSREEIRRIGF------PWSPELVERTRLAV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 117 GATITAAQ-CLIDGmckVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRK--FERILYVDLDLHHGDGT-------G 186
Cdd:cd09993    79 GGTILAARlALEHG---LAINLAGGTHHAFPDRGEGFCVFNDIAIAARVLLAEglVRRVLIVDLDVHQGNGTaaifaddP 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 187 DV-------SDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIG 259
Cdd:cd09993   156 SVftfsmhgEKNYPFRKEPSDLDVPLPDGTGDDEYLAALEEALPRLLAEFRPDLVFYNAGVDVLAGDRLGRLSLSLEGLR 235

                         250       260
                  ....*....|....*....|....*.
gi 1370521764 260 KCLKYILQWQLA----TLILGGGGYN 281
Cdd:cd09993   236 ERDRLVLRFARArgipVAMVLGGGYS 261
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
 41-288 1.36e-30

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: 119.59  E-value: 1.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  41 VHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDhpdsieygLGYDCPATEGIFDYAAAIGGATI 120
Cdd:cd09996    43 IKNLLEVSGLSDHLVLITPRPATDEELLRVHTPEYIDRVKAASAAGGGE--------AGGGTPFGPGSYEIALLAAGGAI 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 121 TAAQCLIDGMCKVA---INWSGgwHHAKKDEASGFCYLNDAVLGILRLRRKF--ERILYVDLDLHHGDGT---------- 185
Cdd:cd09996   115 AAVDAVLDGEVDNAyalVRPPG--HHAEPDQGMGFCLFNNVAIAARHALAVGgvKRVAVVDWDVHHGNGTqaifyddpdv 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 186 ---------------GDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCS 250
Cdd:cd09996   193 ltislhqdrcfppdsGAVEERGEGAGEGYNLNIPLPPGSGDGAYLHAFERIVLPALRAFRPELIIVASGFDASAFDPLGR 272

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1370521764 251 FNMTPVG---IGKCLKyilqwQLATLILGG-------GGYNLANTARC 288
Cdd:cd09996   273 MMLTSDGfraLTRKLR-----DLADELCGGrlvmvheGGYSEAYVPFC 315
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 35-298 1.07e-21

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: 94.68  E-value: 1.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPD-SIEYGLGYDCPATegiFDYAA 113
Cdd:cd10002    11 PERLEAILERLTQDGLLERCVKIPAREAEEDEILLVHSQEYIDLVKSTETMEKEELESlCSGYDSVYLCPST---YEAAR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 114 AIGGATITAAQCLIDGMCK--VAINWSGGwHHAKKDEASGFCYLNDAVLGILRLRRKF--ERILYVDLDLHHGDGTG--- 186
Cdd:cd10002    88 LAAGSTIELVKAVMAGKIQngFALIRPPG-HHAMRNEANGYCIFNNVAIAAKYAIEKLglKRILIVDWDVHHGQGTQqgf 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 187 --DVSD------------------------VGLGKGRYYSVNVPI-QDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLG 239
Cdd:cd10002   167 yeDPRVlyfsihryehgrfwphlfesdydyIGVGHGYGFNVNVPLnQTGLGDADYLAIFHHILLPLALEFQPELVLVSAG 246

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370521764 240 ADTIAGDPMCSFNMTPVGIGKcLKYIL--QWQLATLILGGGGYNLANTARCWTYLTGVILG 298
Cdd:cd10002   247 FDASIGDPEGEMAVTPAGYAH-LTRLLmgLAGGKLLLVLEGGYLLESLAESVSMTLRGLLG 306
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 35-298 1.04e-19

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: 88.56  E-value: 1.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  35 PKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIEYGLG---YDCPATegiFDY 111
Cdd:cd11600     7 PSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEHWDRVEATEKMSDEQLKDRTEIFERdslYVNNDT---AFC 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 112 AAAIGGATITAAQCLIDGMCK--VAINWSGGwHHAKKDEASGFCYLNDAVLG--ILRLRR--KFERILYVDLDLHHGDGT 185
Cdd:cd11600    84 ARLSCGGAIEACRAVAEGRVKnaFAVVRPPG-HHAEPDESMGFCFFNNVAVAakWLQTEYpdKIKKILILDWDIHHGNGT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 186 -----------------------------GDVSDVGLGKGRYYSVNVP-IQDGIQDEKYYQICESVLKEVYQAFNPKAVV 235
Cdd:cd11600   163 qrafyddpnvlyislhrfenggfypgtpyGDYESVGEGAGLGFNVNIPwPQGGMGDADYIYAFQRIVMPIAYEFDPDLVI 242

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370521764 236 LQLGADTIAGDPMCSFNMTPVGIGKclkyiLQWQLATLILGG------GGYNLANTARCWTYLTGVILG 298
Cdd:cd11600   243 ISAGFDAADGDELGQCHVTPAGYAH-----MTHMLMSLAGGKlvvaleGGYNLDAISDSALAVAKVLLG 306
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
 44-288 8.12e-19

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: 87.02  E-value: 8.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  44 LIEAYALHKQMRIvKPKVASMEEMATFHTDAY-------LQHLQKVSQEGDDDHPDSIEY-----GLGYDcpaTEGIFDY 111
Cdd:cd11681    38 LQETGLVNRCERL-RGRKATLEELQLVHSEVHtllygtnPLSRLKLDPTKLAGLPQKSFVrlpcgGIGVD---SDTVWNE 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 112 AAAIGGATItAAQCLIDGMCKVAIN-WSGGW-------HHAKKDEASGFCYLNDAVLG--ILRLRRKFERILYVDLDLHH 181
Cdd:cd11681   114 LHTSNAARM-AVGCVIDLAFKVATGeLKNGFavvrppgHHAEPSQAMGFCFFNSVAIAakQLQQKLKLRKILIVDWDVHH 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 182 GDGT---------------------------GDVSDVGLGKGRYYSVNVPIQDGIQ----DEKYYQICESVLKEVYQAFN 230
Cdd:cd11681   193 GNGTqqifyedpnvlyislhryddgnffpgtGAPTEVGSGAGEGFNVNIAWSGGLDppmgDAEYLAAFRTVVMPIAREFS 272

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370521764 231 PKAVVLQLGADTIAGDP--MCSFNMTPvgigKCLKYILQwQLATLILGG------GGYNLanTARC 288
Cdd:cd11681   273 PDIVLVSAGFDAAEGHPppLGGYKVSP----ACFGYMTR-QLMNLAGGKvvlaleGGYDL--TAIC 331
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
 27-348 1.09e-18

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: 87.01  E-value: 1.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  27 MCDSLAKIPKRASMVHSL---IEAYALHKQMRIVKPKVASMEEMATFHTDAYLQ-------HLQKVSQEGDDDHPDSIEY 96
Cdd:cd10006    20 TCGNSNSHPEHAGRIQSIwsrLQETGLRGKCECIRGRKATLEELQTVHSEAHTLlygtnplNRQKLDSKKLLGSLASVFV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  97 -----GLGYDcpaTEGIFDYAAAIGGATItAAQCLIDGMCKVAI-NWSGGW-------HHAKKDEASGFCYLNDAVLG-- 161
Cdd:cd10006   100 rlpcgGVGVD---SDTIWNEVHSSGAARL-AVGCVVELVFKVATgELKNGFavvrppgHHAEESTPMGFCYFNSVAIAak 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 162 ILRLRRKFERILYVDLDLHHGDGT---------------------------GDVSDVGLGKGRYYSVNVPIQDGIQ---- 210
Cdd:cd10006   176 LLQQRLNVSKILIVDWDVHHGNGTqqafysdpnvlymslhryddgnffpgsGAPDEVGTGPGVGFNVNMAFTGGLDppmg 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 211 DEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPmcsfnmTPVG----IGKCLKYILQwQLATLIlGG-------GG 279
Cdd:cd10006   256 DAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHP------TPLGgynlSAKCFGYLTK-QLMGLA-GGrivlaleGG 327

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370521764 280 YNLANTARCWTYLTGVILGKTLSSEipdhefftaygPDYVLEItpscRPDRNEPHRIQQILNYIKEKWP 348
Cdd:cd10006   328 HDLTAICDASEACVSALLGNELDPL-----------PEKVLQQ----RPNANAVRSMEKVMEIHSKYWR 381
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
 29-286 2.64e-16

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: 79.12  E-value: 2.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  29 DSLAKIPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQhLQKVSQEGDDDHPDSI--EYGLGYDCPate 106
Cdd:cd11682     5 ESFPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYVA-LMKSTQYMTEEELRTLadTYDSVYLHP--- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 107 GIFDYAAAIGGATITAAQCLIDGMCK--VAINWSGGwHHAKKDEASGFCYLNDAVLGI--LRLRRKFERILYVDLDLHHG 182
Cdd:cd11682    81 NSYSCACLAVGSVLQLVDKVLGGEIRngLAIVRPPG-HHAQHDKMDGYCMFNNVAIAAryAQQKHGVQRVLIVDWDVHHG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 183 DGT-----------------------------GDVSDVGLGKGRYYSVNVPI-QDGIQDEKYYQICESVLKEVYQAFNPK 232
Cdd:cd11682   160 QGTqfifeqdpsvlyfsihryeqgrfwphlkeSDSSAVGFGRGEGYNINVPWnQVGMRDADYIAAFLHVLLPVALEFQPQ 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370521764 233 AVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLILG-GGGYNLANTA 286
Cdd:cd11682   240 LVLVAAGFDAVIGDPKGEMAATPACFAHLTHLLMGLAGGKLILSlEGGYNLRSLA 294
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 33-293 7.38e-15

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: 74.90  E-value: 7.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  33 KIPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQ-----------HLQKVSQEGDDD--HPDSieyglg 99
Cdd:cd11683     9 EVPERLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSlvretqvmnkeELMAISGKYDAVyfHPNT------ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 100 YDCpategifdyAAAIGGATITAAQCLIDGMCK--VAINWSGGwHHAKKDEASGFCYLNDAVLGILRLRRKF--ERILYV 175
Cdd:cd11683    83 FHC---------ARLAAGATLQLVDAVLTGEVQngMALVRPPG-HHSQRNAANGFCVFNNVAIAAEYAKKKYglHRILIV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 176 DLDLHHGDGT-----------------------------GDVSDVGLGKGRYYSVNVPI-QDGIQDEKYYQICESVLKEV 225
Cdd:cd11683   153 DWDVHHGQGIqyifeedpsvlyfswhryehqrfwpflreSDYDAVGRGKGLGFNINLPWnKVGMGNADYLAAFFHVLLPL 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370521764 226 YQAFNPKAVVLQLGADTIAGDPMCSFNMTPvgigKCLKYILqwQLATLILGG-------GGYNLANTAR--CWTYLT 293
Cdd:cd11683   233 AFEFDPELVLVSAGFDSAIGDPEGQMCATP----ECFAHLT--HLLMVLAGGklcavleGGYHLESLAEsvCMTVQT 303
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
 142-288 1.28e-14

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: 74.28  E-value: 1.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 142 HHAKKDEASGFCYLNDAVLGI--LRLRRKFERILYVDLDLHHGDGT---------------------------GDVSDVG 192
Cdd:cd10008   152 HHADHSTAMGFCFFNSVAIACrqLQQQGKASKILIVDWDVHHGNGTqqtfyqdpsvlyislhrhddgnffpgsGAVDEVG 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 193 LGKGRYYSVNVPIQDGIQ----DEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPmcsfnmTPVG----IGKCLKY 264
Cdd:cd10008   232 AGSGEGFNVNVAWAGGLDppmgDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHP------APLGgyhvSAKCFGY 305

                         170       180       190
                  ....*....|....*....|....*....|
gi 1370521764 265 ILQwQLATLILGG------GGYNLanTARC 288
Cdd:cd10008   306 MTQ-QLMNLAGGAvvlaleGGHDL--TAIC 332
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
 117-288 5.78e-14

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: 72.71  E-value: 5.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 117 GATITAAQCLIDGMCKVAI-NWSGGW-------HHAKKDEASGFCYLNDAVLGILRLRRKFE--RILYVDLDLHHGDGT- 185
Cdd:cd10007   121 SAVRMAVGCLIELAFKVAAgELKNGFavirppgHHAEESTAMGFCFFNSVAIAAKLLQQKLNvgKILIVDWDIHHGNGTq 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 186 --------------------------GDVSDVGLGKGRYYSVNVPIQDGIQ----DEKYYQICESVLKEVYQAFNPKAVV 235
Cdd:cd10007   201 qafyndpnvlyislhryddgnffpgsGAPDEVGAGPGVGFNVNIAWTGGVDppigDVEYLTAFRTVVMPIANEFSPDVVL 280

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370521764 236 LQLGADTIAG--DPMCSFNMTpvgiGKCLKYILQwQLATLIlGG-------GGYNLanTARC 288
Cdd:cd10007   281 VSAGFDAVEGhqSPLGGYSVT----AKCFGHLTK-QLMTLA-GGrvvlaleGGHDL--TAIC 334
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
 27-288 8.15e-14

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: 71.97  E-value: 8.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  27 MCDSLAKIPKRASMVHS----LIEAYALHKQMRIvKPKVASMEEMATFHTDAYL----------QHLQKVSQEGDDDHP- 91
Cdd:cd10009    17 VCGNSTTHPEHAGRIQSiwsrLQETGLLNKCERI-QGRKASLEEIQLVHSEHHSllygtnpldgQKLDPRILLGDDSQKf 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  92 -DSIEYG-LGYDcpaTEGIFDYAAAIGGATItAAQCLIDGMCKVAI-NWSGGW-------HHAKKDEASGFCYLNDAVLG 161
Cdd:cd10009    96 fSSLPCGgLGVD---SDTIWNELHSSGAARM-AVGCVIELASKVASgELKNGFavvrppgHHAEESTAMGFCFFNSVAIT 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 162 ILRLRRKFE--RILYVDLDLHHGDGT---------------------------GDVSDVGLGKGRYYSVNVPIQDGIQ-- 210
Cdd:cd10009   172 AKYLRDQLNisKILIVDLDVHHGNGTqqafyadpsilyislhrydegnffpgsGAPNEVGTGLGEGYNINIAWTGGLDpp 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 211 --DEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGD--PMCSFNMTPVGIGKCLKYILQWQLATLILG-GGGYNLanT 285
Cdd:cd10009   252 mgDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLADGRVVLAlEGGHDL--T 329


                  ...
gi 1370521764 286 ARC 288
Cdd:cd10009   330 AIC 332
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
 55-254 7.32e-13

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: 68.31  E-value: 7.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  55 RIVKPKVASMEEMATFHTDAYLQHL-QKVSQEG----DDD---HPDSIEYGLgydcpategifdYAAaigGATITAAQCL 126
Cdd:cd11599    25 RQLEAPPATREQLLRVHDAAYVDRLeAAAPEEGlvqlDPDtamSPGSLEAAL------------RAA---GAVVAAVDAV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 127 IDGMCK---VAINWSGgwHHAKKDEASGFCYLNDAVLGIL--RLRRKFERILYVDLDLHHGDGT---------------- 185
Cdd:cd11599    90 MAGEARnafCAVRPPG--HHAERDKAMGFCLFNNVAIAAAhaLAHHGLERVAIVDFDVHHGNGTedifrddprvlfcssh 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370521764 186 --------GDVSDVGLGkgryYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMT 254
Cdd:cd11599   168 qhplypgtGAPDETGHG----NIVNVPLPAGTGGAEFREAVEDRWLPALDAFKPDLILISAGFDAHRDDPLAQLNLT 240
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
 86-188 2.89e-09

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: 57.85  E-value: 2.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764  86 GDDDHPDSIEYGLGYDCPATEGIFDYAAaigGATITAAQCLIDGMCK------VAINWSGgwHHAKKDEASGFCYLNDAV 159
Cdd:cd09998    63 GESEIPAHLPQGDLYLCPESLDAIQGAL---GAVCEAVDSVFKPESPgtkrafVAIRPPG--HHCSESTPSGFCWVNNVH 137

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1370521764 160 LGILR--LRRKFERILYVDLDLHHGDGTGDV 188
Cdd:cd09998   138 VGAAHayLTHGITRVVILDIDLHHGNGTQDI 168
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 131-296 2.34e-08

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: 53.92  E-value: 2.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 131 CKVAINWSGgwHHAKKdeasgfcylNDAVLGILRLrrkFERILYVDLDLHHGDGT---------------------GDVS 189
Cdd:cd09987    25 GKVPVVLGG--DHSIA---------NGAIRAVAEL---HPDLGVIDVDAHHDVRTpeafgkgnhhtprhllcepliSDVH 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370521764 190 DVGLG-------------KGRYYSVNVPIQDGIqDEKYYQICESVLKevYQAFNPKAVVLQLGADTIAGDPM--CS---- 250
Cdd:cd09987    91 IVSIGirgvsngeaggayARKLGVVYFSMTEVD-KLGLGDVFEEIVS--YLGDKGDNVYLSVDVDGLDPSFApgTGtpgp 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370521764 251 FNMTPVGIGKCLKYILQWQLATLILGGGGYNLA----NTARCWTYLTGVI 296
Cdd:cd09987   168 GGLSYREGLYITERIAKTNLVVGLDIVEVNPLLdetgRTARLAAALTLEL 217
 
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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