NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2217393211|ref|XP_047298211|]
View 

histone deacetylase 8 isoform X6 [Homo sapiens]

Protein Classification

arginase family protein( domain architecture ID 98571)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Arginase_HDAC super family cl17011
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 16-260 1.42e-157

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


The actual alignment was detected with superfamily member cd10000:

Pssm-ID: 450134 [Multi-domain]  Cd Length: 364  Bit Score: 442.16  E-value: 1.42e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  16 PVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQM----------------------------------------- 54
Cdd:cd10000     1 VVYIHSPEYVNLCDRLPKVPNRASMVHSLIEAYGLLKQLrvvkprvateeelasfhsdeyiqflkkasnegdndeepseq 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  55 ----------------------------------------------------RDEASGFCYLNDAVLGILRLRRKFERIL 82
Cdd:cd10000    81 qefglgydcpifegiydyaaavagatltaaqllidgkckvainwfggwhhaqRDEASGFCYVNDIVLGILKLREKFDRVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  83 YVDLDLHHGDG--------------------------TGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQ 136
Cdd:cd10000   161 YVDLDLHHGDGvedafsftskvmtvslhkyspgffpgTGDVSDVGLGKGKYYTVNVPLRDGIQDEQYLQIFTAVVPEIVA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211 137 AFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPD 216
Cdd:cd10000   241 AFRPEAVVLQCGADTLAGDPMGAFNLTPVGIGKCLKYVLGWKLPTLILGGGGYNLANTARCWTYLTGLILGEPLSSDIPD 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 2217393211 217 HEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLKHVV 260
Cdd:cd10000   321 HEFFTSYGPDYELEISPSLRPDLNEDQYIEKILETIKGNLKNVV 364
 
Name Accession Description Interval E-value
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 16-260 1.42e-157

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: 442.16  E-value: 1.42e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  16 PVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQM----------------------------------------- 54
Cdd:cd10000     1 VVYIHSPEYVNLCDRLPKVPNRASMVHSLIEAYGLLKQLrvvkprvateeelasfhsdeyiqflkkasnegdndeepseq 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  55 ----------------------------------------------------RDEASGFCYLNDAVLGILRLRRKFERIL 82
Cdd:cd10000    81 qefglgydcpifegiydyaaavagatltaaqllidgkckvainwfggwhhaqRDEASGFCYVNDIVLGILKLREKFDRVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  83 YVDLDLHHGDG--------------------------TGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQ 136
Cdd:cd10000   161 YVDLDLHHGDGvedafsftskvmtvslhkyspgffpgTGDVSDVGLGKGKYYTVNVPLRDGIQDEQYLQIFTAVVPEIVA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211 137 AFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPD 216
Cdd:cd10000   241 AFRPEAVVLQCGADTLAGDPMGAFNLTPVGIGKCLKYVLGWKLPTLILGGGGYNLANTARCWTYLTGLILGEPLSSDIPD 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 2217393211 217 HEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLKHVV 260
Cdd:cd10000   321 HEFFTSYGPDYELEISPSLRPDLNEDQYIEKILETIKGNLKNVV 364
PTZ00063 PTZ00063
histone deacetylase; Provisional
 50-259 1.14e-67

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 215.44  E-value: 1.14e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  50 LHKQMRDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDG-------------------------TGDVSDVGLGK 104
Cdd:PTZ00063  136 LHHAKRSEASGFCYINDIVLGILELLKYHARVMYIDIDVHHGDGveeafyvthrvmtvsfhkfgdffpgTGDVTDIGVAQ 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211 105 GRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLIL 184
Cdd:PTZ00063  216 GKYYSVNVPLNDGIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAACVEFVRSLNIPLLVL 295

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217393211 185 GGGGYNLANTARCWTYLTGVILGKT--LSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLKHV 259
Cdd:PTZ00063  296 GGGGYTIRNVARCWAYETGVILNKHdeMSDQISLNDYYDYYAPDFQLHLQPSNIPNYNSPEHLEKIKVKILENLRYL 372
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 51-205 7.64e-55

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: 178.58  E-value: 7.64e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  51 HKQMRDEASGFCYLNDAVLGILRLRRK--FERILYVDLDLHHGDGT--------------------------GDVSDVGL 102
Cdd:pfam00850 112 HHAERDRASGFCIFNNVAIAAKYLREKygLKRVAIVDFDVHHGNGTqeifyddpsvltlsihqypggfypgtGFADETGE 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211 103 GKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLAT- 181
Cdd:pfam00850 192 GKGKGYTLNVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAGFDAHAGDPLGGLNLTTEGFAEITRILLELADPLc 271

                         170       180
                  ....*....|....*....|....*..
gi 2217393211 182 ---LILGGGGYNLANTARCWTYLTGVI 205
Cdd:pfam00850 272 irvVSVLEGGYNLDALARSATAVLAAL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 54-207 1.99e-41

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 144.09  E-value: 1.99e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  54 MRDEASGFCYLNDAVLGILRLRRK-FERILYVDLDLHHGDGT------------------------GDVSDVGLGKGRYY 108
Cdd:COG0123   126 ERDRAMGFCLFNNAAIAARYLLAKgLERVAIVDFDVHHGNGTqdifyddpdvltisihqdplypgtGAADETGEGAGEGS 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211 109 SVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQW----QLATLIL 184
Cdd:COG0123   206 NLNVPLPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELadhcGGPVVSV 285

                         170       180
                  ....*....|....*....|...
gi 2217393211 185 GGGGYNLANTARCWTYLTGVILG 207
Cdd:COG0123   286 LEGGYNLDALARSVAAHLETLLG 308
 
Name Accession Description Interval E-value
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
 16-260 1.42e-157

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: 442.16  E-value: 1.42e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  16 PVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQM----------------------------------------- 54
Cdd:cd10000     1 VVYIHSPEYVNLCDRLPKVPNRASMVHSLIEAYGLLKQLrvvkprvateeelasfhsdeyiqflkkasnegdndeepseq 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  55 ----------------------------------------------------RDEASGFCYLNDAVLGILRLRRKFERIL 82
Cdd:cd10000    81 qefglgydcpifegiydyaaavagatltaaqllidgkckvainwfggwhhaqRDEASGFCYVNDIVLGILKLREKFDRVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  83 YVDLDLHHGDG--------------------------TGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQ 136
Cdd:cd10000   161 YVDLDLHHGDGvedafsftskvmtvslhkyspgffpgTGDVSDVGLGKGKYYTVNVPLRDGIQDEQYLQIFTAVVPEIVA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211 137 AFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPD 216
Cdd:cd10000   241 AFRPEAVVLQCGADTLAGDPMGAFNLTPVGIGKCLKYVLGWKLPTLILGGGGYNLANTARCWTYLTGLILGEPLSSDIPD 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 2217393211 217 HEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLKHVV 260
Cdd:cd10000   321 HEFFTSYGPDYELEISPSLRPDLNEDQYIEKILETIKGNLKNVV 364
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
 50-205 4.75e-87

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: 260.98  E-value: 4.75e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  50 LHKQMRDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDG-------------------------TGDVSDVGLGK 104
Cdd:cd09991   126 LHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGveeafyttdrvmtvsfhkfgeyffpGTGLRDIGAGK 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211 105 GRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLIL 184
Cdd:cd09991   206 GKYYAVNVPLKDGIDDESYLQIFEPVLSKVMEVFQPSAVVLQCGADSLAGDRLGCFNLSIKGHAKCVKFVKSFNIPLLVL 285

                         170       180
                  ....*....|....*....|.
gi 2217393211 185 GGGGYNLANTARCWTYLTGVI 205
Cdd:cd09991   286 GGGGYTLRNVARCWTYETAVL 306
PTZ00063 PTZ00063
histone deacetylase; Provisional
 50-259 1.14e-67

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 215.44  E-value: 1.14e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  50 LHKQMRDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDG-------------------------TGDVSDVGLGK 104
Cdd:PTZ00063  136 LHHAKRSEASGFCYINDIVLGILELLKYHARVMYIDIDVHHGDGveeafyvthrvmtvsfhkfgdffpgTGDVTDIGVAQ 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211 105 GRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLIL 184
Cdd:PTZ00063  216 GKYYSVNVPLNDGIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTIKGHAACVEFVRSLNIPLLVL 295

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217393211 185 GGGGYNLANTARCWTYLTGVILGKT--LSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLKHV 259
Cdd:PTZ00063  296 GGGGYTIRNVARCWAYETGVILNKHdeMSDQISLNDYYDYYAPDFQLHLQPSNIPNYNSPEHLEKIKVKILENLRYL 372
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
 47-258 1.04e-65

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: 208.89  E-value: 1.04e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  47 AYALHKQMRDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDG-------------------------TGDVSDVG 101
Cdd:cd10004   129 AGGLHHAKKSEASGFCYVNDIVLGILELLRYHQRVLYIDIDVHHGDGveeafyttdrvmtcsfhkygeyfpgTGELRDIG 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211 102 LGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLAT 181
Cdd:cd10004   209 IGTGKNYAVNVPLRDGIDDESYKSIFEPVIKHVMEWYQPEAVVLQCGGDSLSGDRLGCFNLSMKGHANCVNFVKSFNLPM 288

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217393211 182 LILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLKH 258
Cdd:cd10004   289 LVLGGGGYTMRNVARTWAFETGLLAGEELDKDLPYNEYYEYYGPDYELNVRPSNMENHNTPEYLDKITTAVIENLRN 365
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
 50-257 3.05e-65

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: 207.63  E-value: 3.05e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  50 LHKQMRDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDG--------------------------TGDVSDVGLG 103
Cdd:cd10005   131 LHHAKKFEASGFCYVNDIVIAILELLKYHPRVLYIDIDIHHGDGvqeafyltdrvmtvsfhkygnyffpgTGDMYEVGAE 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211 104 KGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLI 183
Cdd:cd10005   211 SGRYYSVNVPLKDGIDDQSYLQLFKPVIQQVIDFYQPTCIVLQCGADSLGCDRLGCFNLSIKGHGECVEFVKSFNIPLLV 290

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217393211 184 LGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRPD-RNEPHRIQQILNYIKGNLK 257
Cdd:cd10005   291 LGGGGYTVRNVARCWTYETSLLVDEEISNELPYNEYFEYFAPDFTLHPDVSTRIEnQNSKQYLDQIRQTVFENLK 365
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
 47-257 1.08e-64

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: 206.07  E-value: 1.08e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  47 AYALHKQMRDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDG-------------------------TGDVSDVG 101
Cdd:cd10011   129 AGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGveeafyttdrvmtvsfhkygeyfpgTGDLRDIG 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211 102 LGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLAT 181
Cdd:cd10011   209 AGKGKYYAVNFPMRDGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPL 288

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217393211 182 LILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLK 257
Cdd:cd10011   289 LMLGGGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYMEKIKQRLFENLR 364
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
 49-257 4.04e-64

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: 204.53  E-value: 4.04e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  49 ALHKQMRDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDG-------------------------TGDVSDVGLG 103
Cdd:cd10010   135 GLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGveeafyttdrvmtvsfhkygeyfpgTGDLRDIGAG 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211 104 KGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLI 183
Cdd:cd10010   215 KGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLM 294

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217393211 184 LGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLK 257
Cdd:cd10010   295 LGGGGYTIRNVARCWTYETAVALDSEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLR 368
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
 50-204 3.02e-55

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: 179.96  E-value: 3.02e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  50 LHKQMRDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDG--------------------------TGDVSDVGLG 103
Cdd:cd11598   130 LHHAKKSEASGFCYVNDIVLAILNLLRYFPRVLYIDIDVHHGDGveeafyrtdrvmtlsfhkyngeffpgTGDLDDNGGT 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211 104 KGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLI 183
Cdd:cd11598   210 PGKHFALNVPLEDGIDDEQYNLLFKSIIGPTIEKFQPSAIVLQCGADSLGGDRLGQFNLNIKAHGACVKFVKSFGIPMLV 289

                         170       180
                  ....*....|....*....|.
gi 2217393211 184 LGGGGYNLANTARCWTYLTGV 204
Cdd:cd11598   290 VGGGGYTPRNVARAWCYETAV 310
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
 51-205 7.64e-55

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: 178.58  E-value: 7.64e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  51 HKQMRDEASGFCYLNDAVLGILRLRRK--FERILYVDLDLHHGDGT--------------------------GDVSDVGL 102
Cdd:pfam00850 112 HHAERDRASGFCIFNNVAIAAKYLREKygLKRVAIVDFDVHHGNGTqeifyddpsvltlsihqypggfypgtGFADETGE 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211 103 GKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLAT- 181
Cdd:pfam00850 192 GKGKGYTLNVPLPPGTGDAEYLAAFEEILLPALEEFQPDLILVSAGFDAHAGDPLGGLNLTTEGFAEITRILLELADPLc 271

                         170       180
                  ....*....|....*....|....*..
gi 2217393211 182 ---LILGGGGYNLANTARCWTYLTGVI 205
Cdd:pfam00850 272 irvVSVLEGGYNLDALARSATAVLAAL 298
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
 50-205 3.00e-51

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: 169.66  E-value: 3.00e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  50 LHKQMRDEASGFCYLNDAVLGILRLRRK-FERILYVDLDLHHGDG--------------------------TGDVSDVGL 102
Cdd:cd09994   126 LHHAMRGRASGFCVYNDAAVAIERLRDKgGLRVAYVDIDAHHGDGvqaafyddprvltislhesgrylfpgTGFVDEIGE 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211 103 GKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQW--QLA 180
Cdd:cd09994   206 GEGYGYAVNIPLPPGTGDDEFLRAFEAVVPPLLRAFRPDVIVSQHGADAHAGDPLTHLNLSNRAYRAAVRRIRELadEYC 285

                         170       180
                  ....*....|....*....|....*...
gi 2217393211 181 T---LILGGGGYNLANTARCWTYLTGVI 205
Cdd:cd09994   286 GgrwLALGGGGYNPDVVARAWALLWAVL 313
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
 51-205 2.32e-48

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: 161.66  E-value: 2.32e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  51 HKQMRDEASGFCYLNDAVLGILRLRRK-FERILYVDLDLHHGDG--------------------------TGDVSDvglg 103
Cdd:cd11680   115 HHAQKSRASGFCYVNDIVLAILRLRRArFRRVFYLDLDLHHGDGvesafffsknvltcsihrydpgffpgTGSLKN---- 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211 104 KGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQW--QLAT 181
Cdd:cd11680   191 SSDKGMLNIPLKRGLSDKTLLRIIDSIVRPLIEKFEPEVIVIQCGCDGLSGDPHKEWNLTIRGYGSVIELLLKEfkDKPT 270

                         170       180
                  ....*....|....*....|....
gi 2217393211 182 LILGGGGYNLANTARCWTYLTGVI 205
Cdd:cd11680   271 LLLGGGGYNHTEAARAWTYLTSMV 294
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
 49-205 7.49e-43

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: 146.81  E-value: 7.49e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  49 ALHKQMRDEASGFCYLNDAVLGILRLRRK-FERILYVDLDLHHGDGT-----------------GDVSDVGLGKGRYYSV 110
Cdd:cd09301   103 GGHHAGKSRAWGFCYFNDVVLAIKFLRERgISRILIIDTDAHHGDGTreafydddrvlhmsfhnYDIYPFGRGKGKGYKI 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211 111 NVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYI--LQWQLATLILGGGG 188
Cdd:cd09301   183 NVPLEDGLGDEEYLDAVERVISKVLEEFEPEVVVLQFGHDTHEGDRLGGFNLSEKGFVKLAEIVkeFARGGPILMVLGGG 262

                         170
                  ....*....|....*..
gi 2217393211 189 YNLANTARCWTYLTGVI 205
Cdd:cd09301   263 YNPEAAARIWTAIIKEL 279
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
 54-207 1.99e-41

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 144.09  E-value: 1.99e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  54 MRDEASGFCYLNDAVLGILRLRRK-FERILYVDLDLHHGDGT------------------------GDVSDVGLGKGRYY 108
Cdd:COG0123   126 ERDRAMGFCLFNNAAIAARYLLAKgLERVAIVDFDVHHGNGTqdifyddpdvltisihqdplypgtGAADETGEGAGEGS 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211 109 SVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQW----QLATLIL 184
Cdd:COG0123   206 NLNVPLPPGTGDAEYLAALEEALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELadhcGGPVVSV 285

                         170       180
                  ....*....|....*....|...
gi 2217393211 185 GGGGYNLANTARCWTYLTGVILG 207
Cdd:COG0123   286 LEGGYNLDALARSVAAHLETLLG 308
PTZ00346 PTZ00346
histone deacetylase; Provisional
 49-210 4.98e-40

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 143.25  E-value: 4.98e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  49 ALHKQMRDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDG--------------------------TGDVSDVGL 102
Cdd:PTZ00346  152 GMHHSKCGECSGFCYVNDIVLGILELLKCHDRVLYVDIDMHHGDGvdeafctsdrvftlslhkfgesffpgTGHPRDVGY 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211 103 GKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATL 182
Cdd:PTZ00346  232 GRGRYYSMNLAVWDGITDFYYLGLFEHALHSIVRRYSPDAIVLQCGADSLAGDRLGLLNLSSFGHGQCVQAVRDLGIPML 311

                         170       180
                  ....*....|....*....|....*...
gi 2217393211 183 ILGGGGYNLANTARCWTYLTGVILGKTL 210
Cdd:PTZ00346  312 ALGGGGYTIRNVAKLWAYETSILTGHPL 339
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
 47-192 7.52e-28

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: 108.01  E-value: 7.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  47 AYAL-----HKQMRDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDGT--------------------------- 94
Cdd:cd10001   108 AYALcrppgHHAGRDRAGGFCYFNNAAIAAQYLRDRAGRVAILDVDVHHGNGTqeifyerpdvlyvsihgdprtfypffl 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  95 GDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVyQAFNPKAVVLQLGADTIAGDPMCSFNMTPVG---IGKCl 171
Cdd:cd10001   188 GFADETGEGEGEGYNLNLPLPPGTGDDDYLAALDEALAAI-AAFGPDALVVSLGFDTHEGDPLSDFKLTTEDyarIGRR- 265

                         170       180
                  ....*....|....*....|.
gi 2217393211 172 kyILQWQLATLILGGGGYNLA 192
Cdd:cd10001   266 --IAALGLPTVFVQEGGYNVD 284
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
 47-197 1.82e-24

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: 98.72  E-value: 1.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  47 AYAL-----HKQMRDEASGFCYLNDAVLGI--LRLRRKFERILYVDLDLHHGDGT------------------------G 95
Cdd:cd09992    96 AFALvrppgHHAEPDRAMGFCLFNNVAIAAryAQKRYGLKRVLIVDWDVHHGNGTqdifyddpsvlyfsihqypfypgtG 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  96 DVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYIL 175
Cdd:cd09992   176 AAEETGGGAGEGFTINVPLPPGSGDAEYLAAFEEVLLPIAREFQPDLVLVSAGFDAHRGDPLGGMNLTPEGYARLTRLLK 255

                         170       180
                  ....*....|....*....|....*....
gi 2217393211 176 qwQLATLILGG-------GGYNLANTARC 197
Cdd:cd09992   256 --ELADEHCGGrlvfvleGGYNLEALAES 282
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
 51-190 7.07e-22

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


Pssm-ID: 212519 [Multi-domain]  Cd Length: 275  Bit Score: 91.41  E-value: 7.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  51 HKQMRDEASGFCYLNDAVLGILRLRRK--FERILYVDLDLHHGDGT-------GDV-------SDVGLGKGRYYSVNVPI 114
Cdd:cd09993   102 HHAFPDRGEGFCVFNDIAIAARVLLAEglVRRVLIVDLDVHQGNGTaaifaddPSVftfsmhgEKNYPFRKEPSDLDVPL 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211 115 QDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLA----TLILGGGGYN 190
Cdd:cd09993   182 PDGTGDDEYLAALEEALPRLLAEFRPDLVFYNAGVDVLAGDRLGRLSLSLEGLRERDRLVLRFARArgipVAMVLGGGYS 261
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
 51-212 3.99e-18

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: 82.39  E-value: 3.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  51 HKQMRDEASGFCYLNDAVLGILRLRRKF--ERILYVDLDLHHGDGT-----------------------------GDVSD 99
Cdd:cd10003   126 HHAEQDTACGFCFFNNVAIAARYAQKKYglKRILIVDWDVHHGNGTqhmfesdpsvlyislhrydngsffpnspeGNYDV 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211 100 VGLGKGRYYSVNVPI-QDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKclkyiLQWQ 178
Cdd:cd10003   206 VGKGKGEGFNVNIPWnKGGMGDAEYIAAFQQVVLPIAYEFNPELVLVSAGFDAARGDPLGGCKVTPEGYAH-----MTHM 280

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2217393211 179 LATLILGG------GGYNLANTARCWTYLTGVILGKTLSS 212
Cdd:cd10003   281 LMSLAGGRvivileGGYNLTSISESMSMCTKTLLGDPPPV 320
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
 56-207 4.88e-16

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: 76.23  E-value: 4.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  56 DEASGFCYLNDAVLG--ILRLRR--KFERILYVDLDLHHGDGT-----------------------------GDVSDVGL 102
Cdd:cd11600   120 DESMGFCFFNNVAVAakWLQTEYpdKIKKILILDWDIHHGNGTqrafyddpnvlyislhrfenggfypgtpyGDYESVGE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211 103 GKGRYYSVNVP-IQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKclkyiLQWQLAT 181
Cdd:cd11600   200 GAGLGFNVNIPwPQGGMGDADYIYAFQRIVMPIAYEFDPDLVIISAGFDAADGDELGQCHVTPAGYAH-----MTHMLMS 274

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2217393211 182 LILGG------GGYNLANTARCWTYLTGVILG 207
Cdd:cd11600   275 LAGGKlvvaleGGYNLDAISDSALAVAKVLLG 306
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
 51-207 1.01e-15

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: 75.42  E-value: 1.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  51 HKQMRDEASGFCYLNDAVLGILRLRRKF--ERILYVDLDLHHGDGTG-----DVSD------------------------ 99
Cdd:cd10002   117 HHAMRNEANGYCIFNNVAIAAKYAIEKLglKRILIVDWDVHHGQGTQqgfyeDPRVlyfsihryehgrfwphlfesdydy 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211 100 VGLGKGRYYSVNVPI-QDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKcLKYIL--Q 176
Cdd:cd10002   197 IGVGHGYGFNVNVPLnQTGLGDADYLAIFHHILLPLALEFQPELVLVSAGFDASIGDPEGEMAVTPAGYAH-LTRLLmgL 275

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2217393211 177 WQLATLILGGGGYNLANTARCWTYLTGVILG 207
Cdd:cd10002   276 AGGKLLLVLEGGYLLESLAESVSMTLRGLLG 306
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
 60-207 5.95e-13

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: 67.75  E-value: 5.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  60 GFCYLNDAVLG--ILRLRRKFERILYVDLDLHHGDGT---------------------------GDVSDVGLGKGRYYSV 110
Cdd:cd10006   163 GFCYFNSVAIAakLLQQRLNVSKILIVDWDVHHGNGTqqafysdpnvlymslhryddgnffpgsGAPDEVGTGPGVGFNV 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211 111 NVPIQDGIQ----DEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPmcsfnmTPVGigkclkyilqwqlatlilgg 186
Cdd:cd10006   243 NMAFTGGLDppmgDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHP------TPLG-------------------- 296

                         170       180
                  ....*....|....*....|.
gi 2217393211 187 gGYNLanTARCWTYLTGVILG 207
Cdd:cd10006   297 -GYNL--SAKCFGYLTKQLMG 314
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
 51-202 2.18e-12

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: 66.04  E-value: 2.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  51 HKQMRDEASGFCYLNDAVLGILRLRRKF--ERILYVDLDLHHGDGT-----------------------------GDVSD 99
Cdd:cd11683   117 HHSQRNAANGFCVFNNVAIAAEYAKKKYglHRILIVDWDVHHGQGIqyifeedpsvlyfswhryehqrfwpflreSDYDA 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211 100 VGLGKGRYYSVNVPI-QDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPvgigKCLKYILqwQ 178
Cdd:cd11683   197 VGRGKGLGFNINLPWnKVGMGNADYLAAFFHVLLPLAFEFDPELVLVSAGFDSAIGDPEGQMCATP----ECFAHLT--H 270

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2217393211 179 LATLILGG-------GGYNLANTAR--CWTYLT 202
Cdd:cd11683   271 LLMVLAGGklcavleGGYHLESLAEsvCMTVQT 303
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
 51-197 2.24e-10

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: 60.03  E-value: 2.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  51 HKQMRDEASGFCYLNDAVLGILRLRRKFE--RILYVDLDLHHGDGT---------------------------GDVSDVG 101
Cdd:cd10009   152 HHAEESTAMGFCFFNSVAITAKYLRDQLNisKILIVDLDVHHGNGTqqafyadpsilyislhrydegnffpgsGAPNEVG 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211 102 LGKGRYYSVNVPIQDGIQ----DEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGD--PMCSFNMTPVGIGKCLKYIL 175
Cdd:cd10009   232 TGLGEGYNINIAWTGGLDppmgDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLM 311

                         170       180
                  ....*....|....*....|...
gi 2217393211 176 QWQLATLILG-GGGYNLanTARC 197
Cdd:cd10009   312 TLADGRVVLAlEGGHDL--TAIC 332
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
 56-97 2.48e-07

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: 50.91  E-value: 2.48e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2217393211  56 DEASGFCYLNDAVLGILR--LRRKFERILYVDLDLHHGDGTGDV 97
Cdd:cd09998   125 STPSGFCWVNNVHVGAAHayLTHGITRVVILDIDLHHGNGTQDI 168
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 65-205 3.06e-07

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


Pssm-ID: 212513  Cd Length: 217  Bit Score: 49.68  E-value: 3.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211  65 NDAVLGILRLrrkFERILYVDLDLHHGDGT---------------------GDVSDVGLG-------------KGRYYSV 110
Cdd:cd09987    39 NGAIRAVAEL---HPDLGVIDVDAHHDVRTpeafgkgnhhtprhllcepliSDVHIVSIGirgvsngeaggayARKLGVV 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393211 111 NVPIQDGIqDEKYYQICESVLKevYQAFNPKAVVLQLGADTIAGDPM--CS----FNMTPVGIGKCLKYILQWQLATLIL 184
Cdd:cd09987   116 YFSMTEVD-KLGLGDVFEEIVS--YLGDKGDNVYLSVDVDGLDPSFApgTGtpgpGGLSYREGLYITERIAKTNLVVGLD 192

                         170       180
                  ....*....|....*....|....*
gi 2217393211 185 GGGGYNLA----NTARCWTYLTGVI 205
Cdd:cd09987   193 IVEVNPLLdetgRTARLAAALTLEL 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH