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Conserved domains on  [gi|1007392892|ref|NP_001308160|]
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histone deacetylase 6 isoform c [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Arginase_HDAC super family cl17011
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
99-145 2.99e-23

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


The actual alignment was detected with superfamily member cd11682:

Pssm-ID: 450134 [Multi-domain]  Cd Length: 337  Bit Score: 92.61  E-value: 2.99e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1007392892  99 CLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVH 145
Cdd:cd11682     1 CLWDESFPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVH 47
 
Name Accession Description Interval E-value
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
99-145 2.99e-23

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: 92.61  E-value: 2.99e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1007392892  99 CLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVH 145
Cdd:cd11682     1 CLWDESFPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVH 47
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
101-145 1.41e-07

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 48.95  E-value: 1.41e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1007392892 101 WDDSF---------PEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVH 145
Cdd:COG0123     5 YHPDYllhdlgpghPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVH 58
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
106-145 5.50e-06

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: 44.53  E-value: 5.50e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1007392892 106 PEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVH 145
Cdd:pfam00850   2 PENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVH 41
PLN02481 PLN02481
Omega-hydroxypalmitate O-feruloyl transferase
104-133 5.61e-03

Omega-hydroxypalmitate O-feruloyl transferase


Pssm-ID: 215266 [Multi-domain]  Cd Length: 436  Bit Score: 35.81  E-value: 5.61e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1007392892 104 SFPEGPERLHAIKEQLIQEGLLDRCVSFQA 133
Cdd:PLN02481  238 SFCFDPEKLEKLKSMALEDGVIKKCSTFEA 267
 
Name Accession Description Interval E-value
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
99-145 2.99e-23

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: 92.61  E-value: 2.99e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1007392892  99 CLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVH 145
Cdd:cd11682     1 CLWDESFPECPERLHAIREKLIQEGLLERCVSVQAREASEEELLLVH 47
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
99-145 1.49e-19

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: 82.74  E-value: 1.49e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1007392892  99 CLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVH 145
Cdd:cd10002     1 CNWDSNHIECPERLEAILERLTQDGLLERCVKIPAREAEEDEILLVH 47
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
91-145 1.28e-11

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: 60.82  E-value: 1.28e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1007392892  91 DEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVH 145
Cdd:cd10003     2 DQRMMNHHNLWDPGHPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCH 56
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
106-145 6.69e-10

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: 55.58  E-value: 6.69e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1007392892 106 PEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVH 145
Cdd:cd09992     2 PERPERLLAILEALEEEGLLDRLVFVEPRPATEEELLRVH 41
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
101-145 1.41e-07

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 48.95  E-value: 1.41e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1007392892 101 WDDSF---------PEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVH 145
Cdd:COG0123     5 YHPDYllhdlgpghPEPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVH 58
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
106-145 5.50e-06

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: 44.53  E-value: 5.50e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1007392892 106 PEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVH 145
Cdd:pfam00850   2 PENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVH 41
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
106-145 9.17e-06

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: 43.65  E-value: 9.17e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1007392892 106 PEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVH 145
Cdd:cd11599     2 PESPERLEAILDALIASGLDRLLRQLEAPPATREQLLRVH 41
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
101-145 9.38e-06

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: 43.70  E-value: 9.38e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1007392892 101 WDDsfP----EGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVH 145
Cdd:cd11683     1 WDD--PeceiEVPERLTASYERLRQYGLVQRCLRLPAREASEEEILLVH 47
PLN02481 PLN02481
Omega-hydroxypalmitate O-feruloyl transferase
104-133 5.61e-03

Omega-hydroxypalmitate O-feruloyl transferase


Pssm-ID: 215266 [Multi-domain]  Cd Length: 436  Bit Score: 35.81  E-value: 5.61e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1007392892 104 SFPEGPERLHAIKEQLIQEGLLDRCVSFQA 133
Cdd:PLN02481  238 SFCFDPEKLEKLKSMALEDGVIKKCSTFEA 267
 
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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