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Conserved domains on  [gi|1958692215|gb|KAG1928960|]
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polyamine deacetylase HDAC10 [Pimephales promelas]

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 ...
20-356 0e+00

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


The actual alignment was detected with superfamily member cd11683:

Pssm-ID: 450134 [Multi-domain]  Cd Length: 337  Bit Score: 659.63  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   20 WTDPACEIEVPERLTASYEALERHGVAQRCTRVPVRQATEQEILLAHSEEYLEAVKQTPKMTVEELKAFSKKYNDVYFHQ 99
Cdd:cd11683      1 WDDPECEIEVPERLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRETQVMNKEELMAISGKYDAVYFHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  100 NIYGCAKLAVGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAIAALYAQKSYSVNRVLIVDWDVHHGQ 179
Cdd:cd11683     81 NTFHCARLAAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYAKKKYGLHRILIVDWDVHHGQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  180 GVQYCFEEDPSVLYFSWHRYEHQTFWPNLPESDYTSIGKGKGSGFNINVPWNKVGMTNSDYLAAFFHVLLPAAYEFDPEL 259
Cdd:cd11683    161 GIQYIFEEDPSVLYFSWHRYEHQRFWPFLRESDYDAVGRGKGLGFNINLPWNKVGMGNADYLAAFFHVLLPLAFEFDPEL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  260 VLVSAGFDSAIGDPEGEMCASPEIFAHLTQLLMPLAAGKMCLVLEGGYNLTCLAQSVCQTVQTLLGDPAPLLSGIGAACE 339
Cdd:cd11683    241 VLVSAGFDSAIGDPEGQMCATPECFAHLTHLLMVLAGGKLCAVLEGGYHLESLAESVCMTVQTLLGDPLPRLSGEMTPCQ 320
                          330
                   ....*....|....*..
gi 1958692215  340 SALESIQNVRKAQSSYW 356
Cdd:cd11683    321 SALESIQNVRAAQAPYW 337
CH_PARVB_rpt2 cd21338
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, ...
909-1038 2.24e-81

second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. It is involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia and also plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Beta-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


:

Pssm-ID: 409187  Cd Length: 130  Bit Score: 260.29  E-value: 2.24e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  909 GKSERDAFDTLLDHAPDKLNVVKTSLITFVNKHLNKLNLEVTELESQFADGVYLVLLMGLLENYFVPLYNFYLTPESFEQ 988
Cdd:cd21338      1 GRFERDAFDTLFDHAPDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHNFYLTPESFDQ 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958692215  989 KVHNVAFAFELMQDGGLQKPKARPEDVVNLNLKSTLRVLYNLFTNYKNSE 1038
Cdd:cd21338     81 KVHNVSFAFELMQDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKYKNVE 130
CH_PARVB_rpt1 cd21336
first calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is ...
761-866 8.48e-60

first calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. It is involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia and also plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Beta-parvin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


:

Pssm-ID: 409185  Cd Length: 106  Bit Score: 199.35  E-value: 8.48e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  761 DLQKVLIDWINSELEEDRIIVKDLEEDLYDGQVLQKLFEKLSGYKLNVAEVTQSEIGQKQKLQTVLEAVNGVLRPLEWHT 840
Cdd:cd21336      1 ELVKVLIDWINDVLVEERIIVKDLEEDLYDGQVLQKLLEKLAGRKLNVAEVTQSEIGQKQKLQTVLEAVNDLLRPQGWAI 80
                           90       100
                   ....*....|....*....|....*.
gi 1958692215  841 EWSVDAIHSKSLVSIVYLLLALAMYY 866
Cdd:cd21336     81 KWSVDSIHGKNLVAILHLLVALAMHF 106
Arginase_HDAC super family cl17011
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
554-660 1.95e-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.


The actual alignment was detected with superfamily member cd10002:

Pssm-ID: 450134 [Multi-domain]  Cd Length: 336  Bit Score: 57.32  E-value: 1.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  554 AGFMQAALGLILPLAYEFNPGLVL----------GVVGESGVKTHLapvWGHLTSLLQGVAQGRTLALLQGY--DKDL-- 619
Cdd:cd10002    219 ADYLAIFHHILLPLALEFQPELVLvsagfdasigDPEGEMAVTPAG---YAHLTRLLMGLAGGKLLLVLEGGylLESLae 295
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1958692215  620 -VEVTASALSGAPVPPLgVLGAPKPEDVQMIEKQRQRLQECW 660
Cdd:cd10002    296 sVSMTLRGLLGDPLPPL-APPIPIRSVLETILNAIAHLSPRW 336
 
Name Accession Description Interval E-value
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
20-356 0e+00

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: 659.63  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   20 WTDPACEIEVPERLTASYEALERHGVAQRCTRVPVRQATEQEILLAHSEEYLEAVKQTPKMTVEELKAFSKKYNDVYFHQ 99
Cdd:cd11683      1 WDDPECEIEVPERLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRETQVMNKEELMAISGKYDAVYFHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  100 NIYGCAKLAVGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAIAALYAQKSYSVNRVLIVDWDVHHGQ 179
Cdd:cd11683     81 NTFHCARLAAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYAKKKYGLHRILIVDWDVHHGQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  180 GVQYCFEEDPSVLYFSWHRYEHQTFWPNLPESDYTSIGKGKGSGFNINVPWNKVGMTNSDYLAAFFHVLLPAAYEFDPEL 259
Cdd:cd11683    161 GIQYIFEEDPSVLYFSWHRYEHQRFWPFLRESDYDAVGRGKGLGFNINLPWNKVGMGNADYLAAFFHVLLPLAFEFDPEL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  260 VLVSAGFDSAIGDPEGEMCASPEIFAHLTQLLMPLAAGKMCLVLEGGYNLTCLAQSVCQTVQTLLGDPAPLLSGIGAACE 339
Cdd:cd11683    241 VLVSAGFDSAIGDPEGQMCATPECFAHLTHLLMVLAGGKLCAVLEGGYHLESLAESVCMTVQTLLGDPLPRLSGEMTPCQ 320
                          330
                   ....*....|....*..
gi 1958692215  340 SALESIQNVRKAQSSYW 356
Cdd:cd11683    321 SALESIQNVRAAQAPYW 337
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
28-323 1.25e-121

Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. Regulation of transcription is caused in part by this mechanism. Histone deacetylases catalyze the removal of the acetyl group. Histone deacetylases are related to other proteins.


Pssm-ID: 425906 [Multi-domain]  Cd Length: 298  Bit Score: 373.88  E-value: 1.25e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   28 EVPERLTASYEALERHGVAQRCTRVPVRQATEQEILLAHSEEYLEAVKQT-PKMTVEELKAFSKKYNDVYFHQNIYGCAK 106
Cdd:pfam00850    3 ENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAaPEGGALLLLSYLSGDDDTPVSPGSYEAAL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  107 LAVGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAIAALYAQKSYSVNRVLIVDWDVHHGQGVQYCFE 186
Cdd:pfam00850   83 LAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLKRVAIVDFDVHHGNGTQEIFY 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  187 EDPSVLYFSWHRYEHQtFWPNlpESDYTSIGKGKGSGFNINVPWNKvGMTNSDYLAAFFHVLLPAAYEFDPELVLVSAGF 266
Cdd:pfam00850  163 DDPSVLTLSIHQYPGG-FYPG--TGFADETGEGKGKGYTLNVPLPP-GTGDAEYLAAFEEILLPALEEFQPDLILVSAGF 238
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  267 DSAIGDPEGEMCASPEIFAHLTQLLMPLA---AGKMCLVLEGGYNLTCLAQSVCQTVQTL 323
Cdd:pfam00850  239 DAHAGDPLGGLNLTTEGFAEITRILLELAdplCIRVVSVLEGGYNLDALARSATAVLAAL 298
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
6-325 3.29e-97

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 309.73  E-value: 3.29e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215    6 ALIFDEEMTRYKLLWTDPaceiEVPERLTASYEALERHGVAQRCTRVPVRQATEQEILLAHSEEYLEAVKQ-TPKMTVEE 84
Cdd:COG0123      2 ALIYHPDYLLHDLGPGHP----EPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAaSLDGGYGQ 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   85 LKAfskkynDVYFHQNIYGCAKLAVGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAIAALYAQKSYs 164
Cdd:COG0123     78 LDP------DTPVSPGTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGFCLFNNAAIAARYLLAKG- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  165 VNRVLIVDWDVHHGQGVQYCFEEDPSVLYFSWHRYehqtfwPNLPESDYTS-IGKGKGSGFNINVPWnKVGMTNSDYLAA 243
Cdd:COG0123    151 LERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD------PLYPGTGAADeTGEGAGEGSNLNVPL-PPGTGDAEYLAA 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  244 FFHVLLPAAYEFDPELVLVSAGFDSAIGDPEGEMCASPEIFAHLTQLLMPLAA---GKMCLVLEGGYNLTCLAQSVCQTV 320
Cdd:COG0123    224 LEEALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELADhcgGPVVSVLEGGYNLDALARSVAAHL 303

                   ....*
gi 1958692215  321 QTLLG 325
Cdd:COG0123    304 ETLLG 308
CH_PARVB_rpt2 cd21338
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, ...
909-1038 2.24e-81

second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. It is involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia and also plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Beta-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409187  Cd Length: 130  Bit Score: 260.29  E-value: 2.24e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  909 GKSERDAFDTLLDHAPDKLNVVKTSLITFVNKHLNKLNLEVTELESQFADGVYLVLLMGLLENYFVPLYNFYLTPESFEQ 988
Cdd:cd21338      1 GRFERDAFDTLFDHAPDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHNFYLTPESFDQ 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958692215  989 KVHNVAFAFELMQDGGLQKPKARPEDVVNLNLKSTLRVLYNLFTNYKNSE 1038
Cdd:cd21338     81 KVHNVSFAFELMQDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKYKNVE 130
CH_PARVB_rpt1 cd21336
first calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is ...
761-866 8.48e-60

first calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. It is involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia and also plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Beta-parvin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409185  Cd Length: 106  Bit Score: 199.35  E-value: 8.48e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  761 DLQKVLIDWINSELEEDRIIVKDLEEDLYDGQVLQKLFEKLSGYKLNVAEVTQSEIGQKQKLQTVLEAVNGVLRPLEWHT 840
Cdd:cd21336      1 ELVKVLIDWINDVLVEERIIVKDLEEDLYDGQVLQKLLEKLAGRKLNVAEVTQSEIGQKQKLQTVLEAVNDLLRPQGWAI 80
                           90       100
                   ....*....|....*....|....*.
gi 1958692215  841 EWSVDAIHSKSLVSIVYLLLALAMYY 866
Cdd:cd21336     81 KWSVDSIHGKNLVAILHLLVALAMHF 106
PTZ00063 PTZ00063
histone deacetylase; Provisional
56-306 1.19e-17

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 86.79  E-value: 1.19e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   56 QATEQEILLAHSEEYLEAVKQtpkMTVEELKAFS---KKYN-----DVYFHQNIYGCAKLAVGATLqlvDSVMKREVRNG 127
Cdd:PTZ00063    53 KSVEPELVLFHDEEYVDFLSS---ISPENYRDFTyqlKRFNvgeatDCPVFDGLFEFQQSCAGASI---DGAYKLNNHQA 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  128 MALVRPPG--HHSQRSAANGFCVFNNVAIAALYAQKSYSvnRVLIVDWDVHHGQGVQYCFEEDPSVLYFSWHRYEHqtFW 205
Cdd:PTZ00063   127 DICVNWSGglHHAKRSEASGFCYINDIVLGILELLKYHA--RVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKFGD--FF 202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  206 PNlpESDYTSIGKGKGSGFNINVPWNKvGMTNSDYLAAFFHVLLPAAYEFDPELVLVSAGFDSAIGDPEGEMCAS----P 281
Cdd:PTZ00063   203 PG--TGDVTDIGVAQGKYYSVNVPLND-GIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTikghA 279
                          250       260
                   ....*....|....*....|....*
gi 1958692215  282 EIFAHLTQLLMPLaagkmcLVLEGG 306
Cdd:PTZ00063   280 ACVEFVRSLNIPL------LVLGGG 298
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
760-868 4.05e-14

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 69.24  E-value: 4.05e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  760 KDLQKVLIDWINSELEED--RIIVKDLEEDLYDGQVLQKLFEKLSGYKLNVAEVTQSEIGQKQKLQTVLEAVN---GVLR 834
Cdd:pfam00307    1 LELEKELLRWINSHLAEYgpGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAEkklGVPK 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1958692215  835 PLewhtEWSVDAIHSKSLvSIVYLLLALAMYYAA 868
Cdd:pfam00307   81 VL----IEPEDLVEGDNK-SVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
928-1035 1.60e-10

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 59.22  E-value: 1.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  928 NVVKTSLITFVNKHLNKL--NLEVTELESQFADGVYLVLLMglleNYFVP-LYNFYLTPESFEQKVHNVAFAFELMQDG- 1003
Cdd:pfam00307    1 LELEKELLRWINSHLAEYgpGVRVTNFTTDLRDGLALCALL----NKLAPgLVDKKKLNKSEFDKLENINLALDVAEKKl 76
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1958692215 1004 GLQKPKARPEDVVNLNLKSTLRVLYNLFTNYK 1035
Cdd:pfam00307   77 GVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQ 108
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
554-660 1.95e-08

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: 57.32  E-value: 1.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  554 AGFMQAALGLILPLAYEFNPGLVL----------GVVGESGVKTHLapvWGHLTSLLQGVAQGRTLALLQGY--DKDL-- 619
Cdd:cd10002    219 ADYLAIFHHILLPLALEFQPELVLvsagfdasigDPEGEMAVTPAG---YAHLTRLLMGLAGGKLLLVLEGGylLESLae 295
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1958692215  620 -VEVTASALSGAPVPPLgVLGAPKPEDVQMIEKQRQRLQECW 660
Cdd:cd10002    296 sVSMTLRGLLGDPLPPL-APPIPIRSVLETILNAIAHLSPRW 336
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
764-828 1.60e-03

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 38.84  E-value: 1.60e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958692215   764 KVLIDWINSELEE-DRIIVKDLEEDLYDGQVLQKLFEKLSGYKLNVAEVTQ--SEIGQKQKLQTVLEA 828
Cdd:smart00033    1 KTLLRWVNSLLAEyDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAslSRFKKIENINLALSF 68
 
Name Accession Description Interval E-value
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
20-356 0e+00

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: 659.63  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   20 WTDPACEIEVPERLTASYEALERHGVAQRCTRVPVRQATEQEILLAHSEEYLEAVKQTPKMTVEELKAFSKKYNDVYFHQ 99
Cdd:cd11683      1 WDDPECEIEVPERLTASYERLRQYGLVQRCLRLPAREASEEEILLVHSPEYLSLVRETQVMNKEELMAISGKYDAVYFHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  100 NIYGCAKLAVGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAIAALYAQKSYSVNRVLIVDWDVHHGQ 179
Cdd:cd11683     81 NTFHCARLAAGATLQLVDAVLTGEVQNGMALVRPPGHHSQRNAANGFCVFNNVAIAAEYAKKKYGLHRILIVDWDVHHGQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  180 GVQYCFEEDPSVLYFSWHRYEHQTFWPNLPESDYTSIGKGKGSGFNINVPWNKVGMTNSDYLAAFFHVLLPAAYEFDPEL 259
Cdd:cd11683    161 GIQYIFEEDPSVLYFSWHRYEHQRFWPFLRESDYDAVGRGKGLGFNINLPWNKVGMGNADYLAAFFHVLLPLAFEFDPEL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  260 VLVSAGFDSAIGDPEGEMCASPEIFAHLTQLLMPLAAGKMCLVLEGGYNLTCLAQSVCQTVQTLLGDPAPLLSGIGAACE 339
Cdd:cd11683    241 VLVSAGFDSAIGDPEGQMCATPECFAHLTHLLMVLAGGKLCAVLEGGYHLESLAESVCMTVQTLLGDPLPRLSGEMTPCQ 320
                          330
                   ....*....|....*..
gi 1958692215  340 SALESIQNVRKAQSSYW 356
Cdd:cd11683    321 SALESIQNVRAAQAPYW 337
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
20-356 6.35e-175

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: 513.78  E-value: 6.35e-175
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   20 WTDPACEIEVPERLTASYEALERHGVAQRCTRVPVRQATEQEILLAHSEEYLEAVKQTPKMTVEELKAFSKKYNDVYFHQ 99
Cdd:cd10002      1 CNWDSNHIECPERLEAILERLTQDGLLERCVKIPAREAEEDEILLVHSQEYIDLVKSTETMEKEELESLCSGYDSVYLCP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  100 NIYGCAKLAVGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAIAALYAQKSYSVNRVLIVDWDVHHGQ 179
Cdd:cd10002     81 STYEAARLAAGSTIELVKAVMAGKIQNGFALIRPPGHHAMRNEANGYCIFNNVAIAAKYAIEKLGLKRILIVDWDVHHGQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  180 GVQYCFEEDPSVLYFSWHRYEHQTFWPNLPESDYTSIGKGKGSGFNINVPWNKVGMTNSDYLAAFFHVLLPAAYEFDPEL 259
Cdd:cd10002    161 GTQQGFYEDPRVLYFSIHRYEHGRFWPHLFESDYDYIGVGHGYGFNVNVPLNQTGLGDADYLAIFHHILLPLALEFQPEL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  260 VLVSAGFDSAIGDPEGEMCASPEIFAHLTQLLMPLAAGKMCLVLEGGYNLTCLAQSVCQTVQTLLGDPAPLLSgIGAACE 339
Cdd:cd10002    241 VLVSAGFDASIGDPEGEMAVTPAGYAHLTRLLMGLAGGKLLLVLEGGYLLESLAESVSMTLRGLLGDPLPPLA-PPIPIR 319
                          330
                   ....*....|....*..
gi 1958692215  340 SALESIQNVRKAQSSYW 356
Cdd:cd10002    320 SVLETILNAIAHLSPRW 336
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
9-360 3.87e-171

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: 504.57  E-value: 3.87e-171
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215    9 FDEEMTRYKLLWtDPAcEIEVPERLTASYEALERHGVAQRCTRVPVRQATEQEILLAHSEEYLEAVKQTPKMTVEELKAF 88
Cdd:cd10003      1 YDQRMMNHHNLW-DPG-HPECPQRISRIYERHNDLGLLERCLRLPSRLATEDELLLCHSEEHLDEMKSLEKMKPRELNRL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   89 SKKYNDVYFHQNIYGCAKLAVGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAIAALYAQKSYSVNRV 168
Cdd:cd10003     79 GKEYDSIYIHPDSYQCALLAAGCVLQVVEAVLTGESRNGVAIVRPPGHHAEQDTACGFCFFNNVAIAARYAQKKYGLKRI 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  169 LIVDWDVHHGQGVQYCFEEDPSVLYFSWHRYEHQTFWPNLPESDYTSIGKGKGSGFNINVPWNKVGMTNSDYLAAFFHVL 248
Cdd:cd10003    159 LIVDWDVHHGNGTQHMFESDPSVLYISLHRYDNGSFFPNSPEGNYDVVGKGKGEGFNVNIPWNKGGMGDAEYIAAFQQVV 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  249 LPAAYEFDPELVLVSAGFDSAIGDPEGEMCASPEIFAHLTQLLMPLAAGKMCLVLEGGYNLTCLAQSVCQTVQTLLGDPA 328
Cdd:cd10003    239 LPIAYEFNPELVLVSAGFDAARGDPLGGCKVTPEGYAHMTHMLMSLAGGRVIVILEGGYNLTSISESMSMCTKTLLGDPP 318
                          330       340       350
                   ....*....|....*....|....*....|..
gi 1958692215  329 PLLSGIGAACESALESIQNVRKAQSSYWSCFK 360
Cdd:cd10003    319 PVLDLPRPPCSSALKSINNVLQVHQKYWKSLR 350
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
19-356 1.58e-159

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: 473.95  E-value: 1.58e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   19 LWTD--PACeievPERLTASYEALERHGVAQRCTRVPVRQATEQEILLAHSEEYLEAVKQTPKMTVEELKAFSKKYNDVY 96
Cdd:cd11682      2 LWDEsfPEC----PERLHAIREKLIQEGLLERCVSVQAREASEEELLLVHSPEYVALMKSTQYMTEEELRTLADTYDSVY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   97 FHQNIYGCAKLAVGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAIAALYAQKSYSVNRVLIVDWDVH 176
Cdd:cd11682     78 LHPNSYSCACLAVGSVLQLVDKVLGGEIRNGLAIVRPPGHHAQHDKMDGYCMFNNVAIAARYAQQKHGVQRVLIVDWDVH 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  177 HGQGVQYCFEEDPSVLYFSWHRYEHQTFWPNLPESDYTSIGKGKGSGFNINVPWNKVGMTNSDYLAAFFHVLLPAAYEFD 256
Cdd:cd11682    158 HGQGTQFIFEQDPSVLYFSIHRYEQGRFWPHLKESDSSAVGFGRGEGYNINVPWNQVGMRDADYIAAFLHVLLPVALEFQ 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  257 PELVLVSAGFDSAIGDPEGEMCASPEIFAHLTQLLMPLAAGKMCLVLEGGYNLTCLAQSVCQTVQTLLGDPAPLLSGIGA 336
Cdd:cd11682    238 PQLVLVAAGFDAVIGDPKGEMAATPACFAHLTHLLMGLAGGKLILSLEGGYNLRSLAEGVCASLKALLGDPCPMLESPGA 317
                          330       340
                   ....*....|....*....|
gi 1958692215  337 ACESALESIQNVRKAQSSYW 356
Cdd:cd11682    318 PCRSALASVSCTISALEPFW 337
HDAC_classII cd09992
Histone deacetylases and histone-like deacetylases, classII; Class II histone deacetylases are ...
28-324 9.60e-128

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: 389.55  E-value: 9.60e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   28 EVPERLTASYEALERHGVAQRCTRVPVRQATEQEILLAHSEEYLEAVKQTPKMtveelkAFSKKYNDVYFHQNIYGCAKL 107
Cdd:cd09992      3 ERPERLLAILEALEEEGLLDRLVFVEPRPATEEELLRVHTPEYIERVEETCEA------GGGYLDPDTYVSPGSYEAALL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  108 AVGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAIAALYAQKSYSVNRVLIVDWDVHHGQGVQYCFEE 187
Cdd:cd09992     77 AAGAALAAVDAVLSGEAENAFALVRPPGHHAEPDRAMGFCLFNNVAIAARYAQKRYGLKRVLIVDWDVHHGNGTQDIFYD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  188 DPSVLYFSWHRYEhqtFWPNLPESDYTsiGKGKGSGFNINVPWNKvGMTNSDYLAAFFHVLLPAAYEFDPELVLVSAGFD 267
Cdd:cd09992    157 DPSVLYFSIHQYP---FYPGTGAAEET--GGGAGEGFTINVPLPP-GSGDAEYLAAFEEVLLPIAREFQPDLVLVSAGFD 230
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958692215  268 SAIGDPEGEMCASPEIFAHLTQLLMPLAA----GKMCLVLEGGYNLTCLAQSVCQTVQTLL 324
Cdd:cd09992    231 AHRGDPLGGMNLTPEGYARLTRLLKELADehcgGRLVFVLEGGYNLEALAESVLAVLEALL 291
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
28-332 1.40e-123

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: 379.77  E-value: 1.40e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   28 EVPERLTASYEALERHGVAQRCTRVPVRQATEQEILLAHSEEYLEAVKQTPKMTVEELKAFSKKYN--DVYFHQNIYGCA 105
Cdd:cd11600      5 EDPSRISRIFEKLKEAGLINRMLRIPIREATKEEILLVHSEEHWDRVEATEKMSDEQLKDRTEIFErdSLYVNNDTAFCA 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  106 KLAVGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAIAALYAQKSY--SVNRVLIVDWDVHHGQGVQY 183
Cdd:cd11600     85 RLSCGGAIEACRAVAEGRVKNAFAVVRPPGHHAEPDESMGFCFFNNVAVAAKWLQTEYpdKIKKILILDWDIHHGNGTQR 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  184 CFEEDPSVLYFSWHRYEHQTFWPNLPESDYTSIGKGKGSGFNINVPWNKVGMTNSDYLAAFFHVLLPAAYEFDPELVLVS 263
Cdd:cd11600    165 AFYDDPNVLYISLHRFENGGFYPGTPYGDYESVGEGAGLGFNVNIPWPQGGMGDADYIYAFQRIVMPIAYEFDPDLVIIS 244
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958692215  264 AGFDSAIGDPEGEMCASPEIFAHLTQLLMPLAAGKMCLVLEGGYNLTCLAQSVCQTVQTLLGDPAPLLS 332
Cdd:cd11600    245 AGFDAADGDELGQCHVTPAGYAHMTHMLMSLAGGKLVVALEGGYNLDAISDSALAVAKVLLGEAPPKLP 313
Hist_deacetyl pfam00850
Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. ...
28-323 1.25e-121

Histone deacetylase domain; Histones can be reversibly acetylated on several lysine residues. Regulation of transcription is caused in part by this mechanism. Histone deacetylases catalyze the removal of the acetyl group. Histone deacetylases are related to other proteins.


Pssm-ID: 425906 [Multi-domain]  Cd Length: 298  Bit Score: 373.88  E-value: 1.25e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   28 EVPERLTASYEALERHGVAQRCTRVPVRQATEQEILLAHSEEYLEAVKQT-PKMTVEELKAFSKKYNDVYFHQNIYGCAK 106
Cdd:pfam00850    3 ENPERLKAILEALREAGLLPDLEIIAPRPATEEELLLVHSPEYLEFLEEAaPEGGALLLLSYLSGDDDTPVSPGSYEAAL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  107 LAVGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAIAALYAQKSYSVNRVLIVDWDVHHGQGVQYCFE 186
Cdd:pfam00850   83 LAAGGTLAAADAVLSGEARNAFALVRPPGHHAERDRASGFCIFNNVAIAAKYLREKYGLKRVAIVDFDVHHGNGTQEIFY 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  187 EDPSVLYFSWHRYEHQtFWPNlpESDYTSIGKGKGSGFNINVPWNKvGMTNSDYLAAFFHVLLPAAYEFDPELVLVSAGF 266
Cdd:pfam00850  163 DDPSVLTLSIHQYPGG-FYPG--TGFADETGEGKGKGYTLNVPLPP-GTGDAEYLAAFEEILLPALEEFQPDLILVSAGF 238
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  267 DSAIGDPEGEMCASPEIFAHLTQLLMPLA---AGKMCLVLEGGYNLTCLAQSVCQTVQTL 323
Cdd:pfam00850  239 DAHAGDPLGGLNLTTEGFAEITRILLELAdplCIRVVSVLEGGYNLDALARSATAVLAAL 298
HDAC_classIIa cd11681
Histone deacetylases, class IIa; Class IIa histone deacetylases are Zn-dependent enzymes that ...
3-356 1.15e-105

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: 334.70  E-value: 1.15e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215    3 SGSALIFDEEMTRYKLLWTDPACEIEVPERLTASYEALERHGVAQRCTRVPVRQATEQEILLAHSEEY--LEAVKQT--P 78
Cdd:cd11681      1 FTTGLAYDPLMLKHQCICGNNSSHPEHGGRLQSIWSRLQETGLVNRCERLRGRKATLEELQLVHSEVHtlLYGTNPLsrL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   79 KMTVEELKAFSKKY------------NDVYFH-QNIYGCAKLAVGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANG 145
Cdd:cd11681     81 KLDPTKLAGLPQKSfvrlpcggigvdSDTVWNeLHTSNAARMAVGCVIDLAFKVATGELKNGFAVVRPPGHHAEPSQAMG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  146 FCVFNNVAIAALYAQKSYSVNRVLIVDWDVHHGQGVQYCFEEDPSVLYFSWHRYEHQTFWPNlpESDYTSIGKGKGSGFN 225
Cdd:cd11681    161 FCFFNSVAIAAKQLQQKLKLRKILIVDWDVHHGNGTQQIFYEDPNVLYISLHRYDDGNFFPG--TGAPTEVGSGAGEGFN 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  226 INVPWN---KVGMTNSDYLAAFFHVLLPAAYEFDPELVLVSAGFDSAIGDPE--GEMCASPEIFAHLTQLLMPLAAGKMC 300
Cdd:cd11681    239 VNIAWSgglDPPMGDAEYLAAFRTVVMPIAREFSPDIVLVSAGFDAAEGHPPplGGYKVSPACFGYMTRQLMNLAGGKVV 318
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958692215  301 LVLEGGYNLTCLAQSVCQTVQTLLGDPAPLLSGIGAA---CESALESIQNVRKAQSSYW 356
Cdd:cd11681    319 LALEGGYDLTAICDASEACVRALLGDELDPLSEEELErrpNPNAVTSLEKVIAIQSPYW 377
AcuC COG0123
Acetoin utilization deacetylase AcuC or a related deacetylase [Secondary metabolites ...
6-325 3.29e-97

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


Pssm-ID: 439893 [Multi-domain]  Cd Length: 308  Bit Score: 309.73  E-value: 3.29e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215    6 ALIFDEEMTRYKLLWTDPaceiEVPERLTASYEALERHGVAQRCTRVPVRQATEQEILLAHSEEYLEAVKQ-TPKMTVEE 84
Cdd:COG0123      2 ALIYHPDYLLHDLGPGHP----EPPERLRAILDALEASGLLDDLELVEPPPATEEDLLRVHTPDYVDALRAaSLDGGYGQ 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   85 LKAfskkynDVYFHQNIYGCAKLAVGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAIAALYAQKSYs 164
Cdd:COG0123     78 LDP------DTPVSPGTWEAALLAAGGALAAADAVLEGEARNAFALVRPPGHHAERDRAMGFCLFNNAAIAARYLLAKG- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  165 VNRVLIVDWDVHHGQGVQYCFEEDPSVLYFSWHRYehqtfwPNLPESDYTS-IGKGKGSGFNINVPWnKVGMTNSDYLAA 243
Cdd:COG0123    151 LERVAIVDFDVHHGNGTQDIFYDDPDVLTISIHQD------PLYPGTGAADeTGEGAGEGSNLNVPL-PPGTGDAEYLAA 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  244 FFHVLLPAAYEFDPELVLVSAGFDSAIGDPEGEMCASPEIFAHLTQLLMPLAA---GKMCLVLEGGYNLTCLAQSVCQTV 320
Cdd:COG0123    224 LEEALLPALEAFKPDLIVVSAGFDAHADDPLGRLNLTTEGYAWRTRRVLELADhcgGPVVSVLEGGYNLDALARSVAAHL 303

                   ....*
gi 1958692215  321 QTLLG 325
Cdd:COG0123    304 ETLLG 308
HDAC_classII_1 cd09996
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes bacterial ...
6-349 1.83e-84

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: 277.13  E-value: 1.83e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215    6 ALIFDEEM-----------TRYKLLWTDPACEIEVPERLTASYEALERHGVAQRCTRVPVRQATEQEILLAHSEEYLEAV 74
Cdd:cd09996      2 GFVWDERYlwhdtgtgalfLPVGGLLVQPGRHPENPETKRRIKNLLEVSGLSDHLVLITPRPATDEELLRVHTPEYIDRV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   75 KQTPKMTVEELKAFSkkyndvYFHQNIYGCAKLAVGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAI 154
Cdd:cd09996     82 KAASAAGGGEAGGGT------PFGPGSYEIALLAAGGAIAAVDAVLDGEVDNAYALVRPPGHHAEPDQGMGFCLFNNVAI 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  155 AALYAQKSYSVNRVLIVDWDVHHGQGVQYCFEEDPSVLYFSWHryEHQTFWPNLpeSDYTSIGKGKGSGFNINVPW-NKV 233
Cdd:cd09996    156 AARHALAVGGVKRVAVVDWDVHHGNGTQAIFYDDPDVLTISLH--QDRCFPPDS--GAVEERGEGAGEGYNLNIPLpPGS 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  234 GmtNSDYLAAFFHVLLPAAYEFDPELVLVSAGFDSAIGDPEGEMCASPEIFAHLTQLLMPLAA----GKMCLVLEGGYNL 309
Cdd:cd09996    232 G--DGAYLHAFERIVLPALRAFRPELIIVASGFDASAFDPLGRMMLTSDGFRALTRKLRDLADelcgGRLVMVHEGGYSE 309
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1958692215  310 TCLAQSVCQTVQTLLGDPA----PLLSGIGAACESAL-----ESIQNVR 349
Cdd:cd09996    310 AYVPFCGLAVLEELSGVRTgiadPLLYYPEAQGGQELqphqrAAIDAAA 358
CH_PARVB_rpt2 cd21338
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, ...
909-1038 2.24e-81

second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. It is involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia and also plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Beta-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409187  Cd Length: 130  Bit Score: 260.29  E-value: 2.24e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  909 GKSERDAFDTLLDHAPDKLNVVKTSLITFVNKHLNKLNLEVTELESQFADGVYLVLLMGLLENYFVPLYNFYLTPESFEQ 988
Cdd:cd21338      1 GRFERDAFDTLFDHAPDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHNFYLTPESFDQ 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958692215  989 KVHNVAFAFELMQDGGLQKPKARPEDVVNLNLKSTLRVLYNLFTNYKNSE 1038
Cdd:cd21338     81 KVHNVSFAFELMQDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKYKNVE 130
HDAC5 cd10007
Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes ...
5-377 2.59e-78

Histone deacetylase 5; Histone deacetylase 5 is a class IIa Zn-dependent enzyme that catalyzes hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. Class IIa histone deacetylases are signal-dependent co-repressors, having N-terminal regulatory domain with two or three conserved serine residues; phosphorylation of these residues is important for ability to shuttle between the nucleus and cytoplasm and act as transcriptional co-repressors. HDAC5 is involved in integration of chronic drug (cocaine) addiction and depression with changes in chromatin structure and gene expression; cocaine regulates HDAC5 function to antagonize the rewarding impact of cocaine, possibly by blocking drug-stimulated gene expression that supports drug-induced behavioral change. It is also involved in regulation of angiogenesis and cell cycle as well as immune system development. HDAC5 and HDAC9 have been found to be significantly up-regulated in high-risk medulloblastoma compared with low-risk and may potentially be novel drug targets.


Pssm-ID: 212531 [Multi-domain]  Cd Length: 420  Bit Score: 262.62  E-value: 2.59e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215    5 SALIFDEEMTRYKLLWTDPACEIEVPERLTASYEALERHGVAQRCTRVPVRQATEQEILLAHSEEYLEAVKQTP----KM 80
Cdd:cd10007      5 TGLVYDTFMLKHQCTCGNTNVHPEHAGRIQSVWSRLQETGLLGKCERVRGRKATLDEIQTVHSEHHTLLYGTSPlnrqKL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   81 TVEE-LKAFSKKY-------------NDVYFHQNIYGCAKLAVGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGF 146
Cdd:cd10007     85 DSKKlLGPLSQKMyavlpcggigvdsDTVWNEMHSSSAVRMAVGCLIELAFKVAAGELKNGFAVIRPPGHHAEESTAMGF 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  147 CVFNNVAIAALYAQKSYSVNRVLIVDWDVHHGQGVQYCFEEDPSVLYFSWHRYEHQTFWPNLPESDytSIGKGKGSGFNI 226
Cdd:cd10007    165 CFFNSVAIAAKLLQQKLNVGKILIVDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGNFFPGSGAPD--EVGAGPGVGFNV 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  227 NVPWN---KVGMTNSDYLAAFFHVLLPAAYEFDPELVLVSAGFDSAIG--DPEGEMCASPEIFAHLTQLLMPLAAGKMCL 301
Cdd:cd10007    243 NIAWTggvDPPIGDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGhqSPLGGYSVTAKCFGHLTKQLMTLAGGRVVL 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  302 VLEGGYNLT--CLAQSVCqtVQTLLGD-PAPLLSGI--GAACESALESIQNVRKAQSSYWSCFKHLEA---RSEMSTKRP 373
Cdd:cd10007    323 ALEGGHDLTaiCDASEAC--VSALLGMeLTPLDNTVlqQKPNDNAVATLERVIEIQSKHWSCLKRFAAtlgFSLLEAQRG 400

                   ....
gi 1958692215  374 RLDE 377
Cdd:cd10007    401 ELEE 404
CH_PARVA_B_rpt2 cd21306
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
914-1034 6.75e-78

second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409155  Cd Length: 121  Bit Score: 250.41  E-value: 6.75e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  914 DAFDTLLDHAPDKLNVVKTSLITFVNKHLNKLNLEVTELESQFADGVYLVLLMGLLENYFVPLYNFYLTPESFEQKVHNV 993
Cdd:cd21306      1 DAFDTLFDHAPDKLNVVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPTSFEQKVHNV 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1958692215  994 AFAFELMQDGGLQKPKARPEDVVNLNLKSTLRVLYNLFTNY 1034
Cdd:cd21306     81 QFAFELMQDAGLPKPKARPEDIVNLDLKSTLRVLYNLFTKY 121
HDAC_classII_2 cd11599
Histone deacetylases and histone-like deacetylases, classII; This subfamily includes ...
28-324 1.29e-77

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: 255.90  E-value: 1.29e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   28 EVPERLTASYEALERHGVAQRCTRVPVRQATEQEILLAHSEEYLEAVKQT-PKMTVEELKAfskkynDVYFHQNIYGCAK 106
Cdd:cd11599      3 ESPERLEAILDALIASGLDRLLRQLEAPPATREQLLRVHDAAYVDRLEAAaPEEGLVQLDP------DTAMSPGSLEAAL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  107 LAVGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAIAALYAQKSYSVNRVLIVDWDVHHGQGVQYCFE 186
Cdd:cd11599     77 RAAGAVVAAVDAVMAGEARNAFCAVRPPGHHAERDKAMGFCLFNNVAIAAAHALAHHGLERVAIVDFDVHHGNGTEDIFR 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  187 EDPSVLYFSWHRYEhqtFWPNLPESDYTSIGkgkgsgfNI-NVPWNKvGMTNSDYLAAFFHVLLPAAYEFDPELVLVSAG 265
Cdd:cd11599    157 DDPRVLFCSSHQHP---LYPGTGAPDETGHG-------NIvNVPLPA-GTGGAEFREAVEDRWLPALDAFKPDLILISAG 225
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958692215  266 FDSAIGDPEGEMCASPEIFAHLTQLLMPLAA----GKMCLVLEGGYNLTCLAQSVCQTVQTLL 324
Cdd:cd11599    226 FDAHRDDPLAQLNLTEEDYAWITEQLMDVADrycdGRIVSVLEGGYDLSALARSVAAHVRALM 288
HDAC7 cd10008
Histone deacetylase 7; Histone deacetylase 7 is a class IIa Zn-dependent enzyme that catalyzes ...
5-356 3.34e-75

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: 252.62  E-value: 3.34e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215    5 SALIFDEEMTRYKLLWTDPACEIEVPERLTASYEALERHGVAQRCTRVPVRQATEQEILLAHSEEYLEAVKQTPkmtVEE 84
Cdd:cd10008      3 TGLVYDSVMLKHQCSCGDNSNHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNP---LSR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   85 LKAFSKKYNDVyFHQNIY----------------------GCAKLAVGATLQLVDSVMKREVRNGMALVRPPGHHSQRSA 142
Cdd:cd10008     80 LKLDNGKLAGL-LAQRMFvmlpcggvgvdtdtiwnelhssNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHST 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  143 ANGFCVFNNVAIAALYAQKSYSVNRVLIVDWDVHHGQGVQYCFEEDPSVLYFSWHRYEHQTFWPNLPESDytSIGKGKGS 222
Cdd:cd10008    159 AMGFCFFNSVAIACRQLQQQGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVD--EVGAGSGE 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  223 GFNINVPWN---KVGMTNSDYLAAFFHVLLPAAYEFDPELVLVSAGFDSAIGDPE--GEMCASPEIFAHLTQLLMPLAAG 297
Cdd:cd10008    237 GFNVNVAWAgglDPPMGDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHPAplGGYHVSAKCFGYMTQQLMNLAGG 316
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958692215  298 KMCLVLEGGYNLT--CLAQSVCqtVQTLLG---DPAPLLSGIGAACESALESIQNVRKAQSSYW 356
Cdd:cd10008    317 AVVLALEGGHDLTaiCDASEAC--VAALLGnevDPLSEESWKQKPNLNAIRSLEAVIRVHSKYW 378
HDAC4 cd10006
Histone deacetylase 4; Histone deacetylase 4 is a class IIa Zn-dependent enzyme that catalyzes ...
5-360 4.07e-75

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: 253.81  E-value: 4.07e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215    5 SALIFDEEMTRYKLLWTDPACEIEVPERLTASYEALERHGVAQRCTRVPVRQATEQEILLAHSEEY--------LEAVKQ 76
Cdd:cd10006      6 TGLVYDTLMLKHQCTCGNSNSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHtllygtnpLNRQKL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   77 TPKMTVEELKAFSKK-------------YNDVyfHQNiyGCAKLAVGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAA 143
Cdd:cd10006     86 DSKKLLGSLASVFVRlpcggvgvdsdtiWNEV--HSS--GAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTP 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  144 NGFCVFNNVAIAALYAQKSYSVNRVLIVDWDVHHGQGVQYCFEEDPSVLYFSWHRYEHQTFWPNLPESDytSIGKGKGSG 223
Cdd:cd10006    162 MGFCYFNSVAIAAKLLQQRLNVSKILIVDWDVHHGNGTQQAFYSDPNVLYMSLHRYDDGNFFPGSGAPD--EVGTGPGVG 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  224 FNINVPWN---KVGMTNSDYLAAFFHVLLPAAYEFDPELVLVSAGFDSAIGDPE--GEMCASPEIFAHLTQLLMPLAAGK 298
Cdd:cd10006    240 FNVNMAFTgglDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTplGGYNLSAKCFGYLTKQLMGLAGGR 319
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958692215  299 MCLVLEGGYNLT--CLAQSVCqtVQTLLG---DPAPLLSGIGAACESALESIQNVRKAQSSYWSCFK 360
Cdd:cd10006    320 IVLALEGGHDLTaiCDASEAC--VSALLGnelDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQ 384
CH_PARVA_rpt2 cd21337
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ...
910-1038 3.17e-73

second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409186  Cd Length: 129  Bit Score: 237.97  E-value: 3.17e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  910 KSERDAFDTLLDHAPDKLNVVKTSLITFVNKHLNKLNLEVTELESQFADGVYLVLLMGLLENYFVPLYNFYLTPESFEQK 989
Cdd:cd21337      1 RHERDAFDTLFDHAPDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTPDSFEQK 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1958692215  990 VHNVAFAFELMQDGGLQKPKARPEDVVNLNLKSTLRVLYNLFTNYKNSE 1038
Cdd:cd21337     81 VLNVSFAFELMQDGGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKYRNVE 129
HDAC9 cd10009
Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes ...
3-356 1.12e-70

Histone deacetylase 9; Histone deacetylase 9 is a class IIa Zn-dependent enzyme that catalyzes hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. Class IIa histone deacetylases are signal-dependent co-repressors, they have N-terminal regulatory domain with two or three conserved serine residues, phosphorylation of these residues is important for ability to shuttle between the nucleus and cytoplasm and act as transcriptional co-repressors. HDAC9 is involved in regulation of gene expression and dendritic growth in developing cortical neurons. It also plays a role in hematopoiesis. Its deregulated expression may be associated with some human cancers. HDAC5 and HDAC9 have been found to be significantly up-regulated in high-risk medulloblastoma compared with low-risk and may potentially be novel drug targets.


Pssm-ID: 212533 [Multi-domain]  Cd Length: 379  Bit Score: 240.30  E-value: 1.12e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215    3 SGSALIFDEEMTRYKLLWTDPACEIEVPERLTASYEALERHGVAQRCTRVPVRQATEQEILLAHSEEY--------LEAV 74
Cdd:cd10009      1 SATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHsllygtnpLDGQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   75 KQTPKMTVEEL--KAFSK--------KYNDVYFHQNIYGCAKLAVGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAAN 144
Cdd:cd10009     81 KLDPRILLGDDsqKFFSSlpcgglgvDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAM 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  145 GFCVFNNVAIAALYAQKSYSVNRVLIVDWDVHHGQGVQYCFEEDPSVLYFSWHRYEHQTFWPNLPESDytSIGKGKGSGF 224
Cdd:cd10009    161 GFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPN--EVGTGLGEGY 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  225 NINVPWN---KVGMTNSDYLAAFFHVLLPAAYEFDPELVLVSAGFDSAIGD--PEGEMCASPEIFAHLTQLLMPLAAGKM 299
Cdd:cd10009    239 NINIAWTgglDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHtpPLGGYKVTAKCFGHLTKQLMTLADGRV 318
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  300 CLVLEGGYNLTCLAQSVCQTVQTLLGDP-APLLSGI--GAACESALESIQNVRKAQSSYW 356
Cdd:cd10009    319 VLALEGGHDLTAICDASEACVNALLGNElEPLAEDIlhQSPNMNAVISLQKIIEIQSKYW 378
HDAC cd09301
Histone deacetylase (HDAC) classes I, II, IV and related proteins; The HDAC/HDAC-like family ...
32-323 8.33e-63

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: 214.61  E-value: 8.33e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   32 RLTASYEALERHGVAQRCTRVPVRQATEQEILLAHSEEYLEAVKQ-TPKMTVEELKAFSKKYNDVYFHQnIYGCAKLAVG 110
Cdd:cd09301      1 RIRDLIEALKELGLRPKIELIECREATEELLLKVHTEEYLNELKAnFAVATITESKPVIFGPNFPVQRH-YFRGARLSTG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  111 ATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAIAALYAQKsYSVNRVLIVDWDVHHGQGVQYCFEEDPS 190
Cdd:cd09301     80 GVVEAAELVAKGELERAFAVVGAGGHHAGKSRAWGFCYFNDVVLAIKFLRE-RGISRILIIDTDAHHGDGTREAFYDDDR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  191 VLYFSWHRYehqtfwpnlpesDYTSIGKGKGSGFNINVPWNKvGMTNSDYLAAFFHVLLPAAYEFDPELVLVSAGFDSAI 270
Cdd:cd09301    159 VLHMSFHNY------------DIYPFGRGKGKGYKINVPLED-GLGDEEYLDAVERVISKVLEEFEPEVVVLQFGHDTHE 225
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958692215  271 GDPEGEMCASPEIFAHLTQLLMPLAAGK-MCLVLEGGYNLTCLAQSVCQTVQTL 323
Cdd:cd09301    226 GDRLGGFNLSEKGFVKLAEIVKEFARGGpILMVLGGGYNPEAAARIWTAIIKEL 279
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
914-1034 4.36e-61

second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409071  Cd Length: 121  Bit Score: 203.59  E-value: 4.36e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  914 DAFDTLLDHAPDKLNVVKTSLITFVNKHLNKLNLEVTELESQFADGVYLVLLMGLLENYFVPLYNFYLTPESFEQKVHNV 993
Cdd:cd21222      1 DAFDDLFDEAPEKLAEVKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPLHEYHLTPSTDDEKLHNV 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1958692215  994 AFAFELMQDGGLQKPKARPEDVVNLNLKSTLRVLYNLFTNY 1034
Cdd:cd21222     81 KLALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
HDAC_classII_APAH cd10001
Histone deacetylase class IIa; This subfamily includes bacterial acetylpolyamine ...
28-316 6.28e-60

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


Pssm-ID: 212525 [Multi-domain]  Cd Length: 298  Bit Score: 207.39  E-value: 6.28e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   28 EVPERLTASYEALERHGVAqrcTRVPVRQATEQEILLAHSEEYleavkqtpkmtVEELKAFSkkyNDVYFHQNIYGCAKL 107
Cdd:cd10001     27 ENPERAEAILDALKRAGLG---EVLPPRDFGLEPILAVHDPDY-----------VDFLETAD---TDTPISEGTWEAALA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  108 AVGATLQLVDSVMKREvRNGMALVRPPGHHSQRSAANGFCVFNNVAIAALYAQKSYSvnRVLIVDWDVHHGQGVQYCFEE 187
Cdd:cd10001     90 AADTALTAADLVLEGE-RAAYALCRPPGHHAGRDRAGGFCYFNNAAIAAQYLRDRAG--RVAILDVDVHHGNGTQEIFYE 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  188 DPSVLYFSWHRYEHqTFWPnlpesdYTS-----IGKGKGSGFNINVP--WnkvGMTNSDYLAAFFHVLLPAAyEFDPELV 260
Cdd:cd10001    167 RPDVLYVSIHGDPR-TFYP------FFLgfadeTGEGEGEGYNLNLPlpP---GTGDDDYLAALDEALAAIA-AFGPDAL 235
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958692215  261 LVSAGFDSAIGDPEGEMCASPEIFAHLTQLLMPLAAGKMcLVLEGGYNLTCLAQSV 316
Cdd:cd10001    236 VVSLGFDTHEGDPLSDFKLTTEDYARIGRRIAALGLPTV-FVQEGGYNVDALGRNA 290
CH_PARVB_rpt1 cd21336
first calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is ...
761-866 8.48e-60

first calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. It is involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia and also plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Beta-parvin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409185  Cd Length: 106  Bit Score: 199.35  E-value: 8.48e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  761 DLQKVLIDWINSELEEDRIIVKDLEEDLYDGQVLQKLFEKLSGYKLNVAEVTQSEIGQKQKLQTVLEAVNGVLRPLEWHT 840
Cdd:cd21336      1 ELVKVLIDWINDVLVEERIIVKDLEEDLYDGQVLQKLLEKLAGRKLNVAEVTQSEIGQKQKLQTVLEAVNDLLRPQGWAI 80
                           90       100
                   ....*....|....*....|....*.
gi 1958692215  841 EWSVDAIHSKSLVSIVYLLLALAMYY 866
Cdd:cd21336     81 KWSVDSIHGKNLVAILHLLVALAMHF 106
HDAC_AcuC_like cd09994
Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes; AcuC (Acetoin ...
6-309 5.99e-57

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: 199.32  E-value: 5.99e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215    6 ALIFDEEMTRYKLLWTDPAceieVPERLTASYEALERHGVAQRCTRVPVRQATEQEILLAHSEEYLEAVKQTPKMTVEEL 85
Cdd:cd09994      1 AFIYSEEYLRYSFGPNHPF----NPPRLSLTKDLLRALGLLPPVDLVPPRPATEEELLLFHTPDYIEAVKEASRGQEPEG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   86 kafSKKYN----DVYFHQNIYGCAKLAVGATLQLVDSVMKREVRNGmalVRPPG--HHSQRSAANGFCVFNNVAIAALYA 159
Cdd:cd09994     77 ---RGRLGlgteDNPVFPGMHEAAALVVGGTLLAARLVLEGEARRA---FNPAGglHHAMRGRASGFCVYNDAAVAIERL 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  160 QKSYsVNRVLIVDWDVHHGQGVQYCFEEDPSVLYFSWHRYeHQTFWPNlpESDYTSIGKGKGSGFNINVPWNKvGMTNSD 239
Cdd:cd09994    151 RDKG-GLRVAYVDIDAHHGDGVQAAFYDDPRVLTISLHES-GRYLFPG--TGFVDEIGEGEGYGYAVNIPLPP-GTGDDE 225
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958692215  240 YLAAFFHVLLPAAYEFDPELVLVSAGFDSAIGDPEGEMCASPEIFAHLTQLLMPLA----AGKMCLVLEGGYNL 309
Cdd:cd09994    226 FLRAFEAVVPPLLRAFRPDVIVSQHGADAHAGDPLTHLNLSNRAYRAAVRRIRELAdeycGGRWLALGGGGYNP 299
CH_PARVA_B_rpt1 cd21304
first calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
761-866 1.18e-54

first calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409153  Cd Length: 107  Bit Score: 184.82  E-value: 1.18e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  761 DLQKVLIDWINSELEEDRIIVKDLEEDLYDGQVLQKLFEKLSGYKLNVAEVTQSEIGQKQKLQTVLEAVNGVLRPLEWHT 840
Cdd:cd21304      1 ELIKVLIEWINDELAEQRIIVKDIEEDLYDGQVLQKLLEKLTGVKLEVAEVTQSEVGQKQKLRTVLDKINRILNLPRWSQ 80
                           90       100
                   ....*....|....*....|....*..
gi 1958692215  841 -EWSVDAIHSKSLVSIVYLLLALAMYY 866
Cdd:cd21304     81 qKWSVDSIHSKNLVAILHLLVALARHF 107
CH_PARVA_rpt1 cd21335
first calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, ...
756-870 2.93e-46

first calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409184  Cd Length: 115  Bit Score: 161.35  E-value: 2.93e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  756 DLNFKDLQKVLIDWINSELEEDRIIVKDLEEDLYDGQVLQKLFEKLSGYKLNVAEVTQSEIGQKQKLQTVLEAVNGVLRP 835
Cdd:cd21335      1 DPKLQELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFEKLEGEKLNVAEVTQSEIAQKQKLQTVLEKINETLKL 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1958692215  836 LEWHTEWSVDAIHSKSLVSIVYLLLALAMYYAAPI 870
Cdd:cd21335     81 PPRSIKWNVDSVHAKSLVAILHLLVALSQYFRAPI 115
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
761-866 8.94e-45

first calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409070  Cd Length: 106  Bit Score: 156.66  E-value: 8.94e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  761 DLQKVLIDWINSELEEDRIIVKDLEEDLYDGQVLQKLFEKLSGYKLNVAEVTQSEIGQKQKLQTVLEAVNGVLRPLEWHT 840
Cdd:cd21221      1 ELVRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEVAQSEEGQKQKLAVVLACVNFLLGLEEDEA 80
                           90       100
                   ....*....|....*....|....*.
gi 1958692215  841 EWSVDAIHSKSLVSIVYLLLALAMYY 866
Cdd:cd21221     81 RWTVDGIYNKDLVSILHLLVALAHHY 106
CH_PARVG_rpt2 cd21307
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
914-1035 2.17e-44

second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409156 [Multi-domain]  Cd Length: 122  Bit Score: 156.36  E-value: 2.17e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  914 DAFDTLLDHAPDKLNVVKTSLITFVNKHLNKLNLEVTELESQFADGVYLVLLMGLLENYFVPLYNFYLTPESFEQKVHNV 993
Cdd:cd21307      1 DAIDELFKLGPDKVNTVKKAILHFVNKHLGNLGLNVKDLDSQFADGVILLLLIGQLEGFFIHLSEFFLTPSSTSEMLHNV 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1958692215  994 AFAFELMQDGGLQKPKARPEDVVNLNLKSTLRVLYNLFTNYK 1035
Cdd:cd21307     81 TLALELLKEGGLLNFPVNPEDIVNGDSKATIRVLYCLFSKYK 122
HDAC8 cd10000
Histone deacetylase 8 (HDAC8); HDAC8 is a Zn-dependent class I histone deacetylase that ...
29-329 7.34e-40

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


Pssm-ID: 212524 [Multi-domain]  Cd Length: 364  Bit Score: 151.72  E-value: 7.34e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   29 VPERLTASYEALERHGVAQRCTRVPVRQATEQEILLAHSEEYLEAVKQ-TPKMTVEELKAFSKKYN---DVYFHQNIYGC 104
Cdd:cd10000     19 VPNRASMVHSLIEAYGLLKQLRVVKPRVATEEELASFHSDEYIQFLKKaSNEGDNDEEPSEQQEFGlgyDCPIFEGIYDY 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  105 AKLAVGATLQLVDSVMKREVRngMALVRPPG-HHSQRSAANGFCVFNNVAIAALYAQKSYSvnRVLIVDWDVHHGQGVQY 183
Cdd:cd10000     99 AAAVAGATLTAAQLLIDGKCK--VAINWFGGwHHAQRDEASGFCYVNDIVLGILKLREKFD--RVLYVDLDLHHGDGVED 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  184 CFEEDPSVLYFSWHRYEhQTFWPNlpESDYTSIGKGKGSGFNINVPWnKVGMTNSDYLAAFFHVLLPAAYEFDPELVLVS 263
Cdd:cd10000    175 AFSFTSKVMTVSLHKYS-PGFFPG--TGDVSDVGLGKGKYYTVNVPL-RDGIQDEQYLQIFTAVVPEIVAAFRPEAVVLQ 250
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958692215  264 AGFDSAIGDPEGEMCASPEIFAHLTQLLmpLAAGKMCLVL-EGGYNLTCLAQsvCQTVQT--LLGDPAP 329
Cdd:cd10000    251 CGADTLAGDPMGAFNLTPVGIGKCLKYV--LGWKLPTLILgGGGYNLANTAR--CWTYLTglILGEPLS 315
HDAC_classIV cd09993
Histone deacetylase class IV also known as histone deacetylase 11; Class IV histone ...
37-308 4.69e-37

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: 140.71  E-value: 4.69e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   37 YEALERHGVAQRCTRVPVRQATEQEILLAHSEEYLEAVKqTPKMTVEELKAFSKKYNDVYFHQniygcAKLAVGATLQLV 116
Cdd:cd09993     12 REALLEEGLVLPEDIVEPEPATREDLLRVHDPEYLESLK-SGELSREEIRRIGFPWSPELVER-----TRLAVGGTILAA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  117 DSVMKRevrnGMAlVRPPG--HHSQRSAANGFCVFNNVAIAALYAQKSYSVNRVLIVDWDVHHGQGVQYCFEEDPSVLYF 194
Cdd:cd09993     86 RLALEH----GLA-INLAGgtHHAFPDRGEGFCVFNDIAIAARVLLAEGLVRRVLIVDLDVHQGNGTAAIFADDPSVFTF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  195 SWHryeHQTFWPNLPEsdytsigkgkGSGFNINVPWnkvGMTNSDYLAAFFHVLLPAAYEFDPELVLVSAGFDSAIGDPE 274
Cdd:cd09993    161 SMH---GEKNYPFRKE----------PSDLDVPLPD---GTGDDEYLAALEEALPRLLAEFRPDLVFYNAGVDVLAGDRL 224
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1958692215  275 GEMCASPE--------IFAHLTQLLMPLAAgkmclVLEGGYN 308
Cdd:cd09993    225 GRLSLSLEglrerdrlVLRFARARGIPVAM-----VLGGGYS 261
HDAC_classI cd09991
Class I histone deacetylases; Class I histone deacetylases (HDACs) are Zn-dependent enzymes ...
30-322 2.64e-35

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: 136.94  E-value: 2.64e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   30 PERLTASYEALERHGVAQRCTRVPVRQATEQEILLAHSEEYLEAVKQTPKMTVEELKAFSKKYN---DVYFHQNIYGCAK 106
Cdd:cd09991     19 PHRIRMTHSLILSYGLYKKMEIYRPRPATAEELTKFHSDDYIDFLRSVSPDNMKEFKKQLERFNvgeDCPVFDGLYEYCQ 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  107 LAVGATLQLVdsvmkREVRNGMA--LVRPPG--HHSQRSAANGFCVFNNVAIAALYAQKSYSvnRVLIVDWDVHHGQGVQ 182
Cdd:cd09991     99 LYAGGSIAAA-----VKLNRGQAdiAINWAGglHHAKKSEASGFCYVNDIVLAILELLKYHQ--RVLYIDIDIHHGDGVE 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  183 YCFEEDPSVLYFSWHRYEHQTFwpnlPESDYTSIGKGKGSGFNINVPWNKvGMTNSDYLAAFFHVLLPAAYEFDPELVLV 262
Cdd:cd09991    172 EAFYTTDRVMTVSFHKFGEYFF----PGTGLRDIGAGKGKYYAVNVPLKD-GIDDESYLQIFEPVLSKVMEVFQPSAVVL 246
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958692215  263 SAGFDSAIGDPEGEMCASP----EIFAHLTQLLMPLaagkmcLVL-EGGYNLTCLAQsvCQTVQT 322
Cdd:cd09991    247 QCGADSLAGDRLGCFNLSIkghaKCVKFVKSFNIPL------LVLgGGGYTLRNVAR--CWTYET 303
CH_PARVG_rpt1 cd21305
first calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
761-866 1.89e-31

first calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. It contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409154  Cd Length: 106  Bit Score: 118.67  E-value: 1.89e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  761 DLQKVLIDWINSELEEDRIIVKDLEEDLYDGQVLQKLFEKLSGYKLNVAEVTQSEIGQKQKLQTVLEAVNGVLRPLEWHT 840
Cdd:cd21305      1 ELKEVLIDWINTTLKQEHIVVKSLEEDLYDGLVLHHLLVKLAGVKLEVEEIALTENAQKRKLTVILEAVNQSLQLEESQL 80
                           90       100
                   ....*....|....*....|....*.
gi 1958692215  841 EWSVDAIHSKSLVSIVYLLLALAMYY 866
Cdd:cd21305     81 KWSVELIHNKDLLATLHLLVAIAKHF 106
HDAC_Hos2 cd11598
Class I histone deacetylases including ScHos2 and SpPhd1; This subfamily includes Class I ...
30-286 1.46e-27

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: 114.47  E-value: 1.46e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   30 PERLTASYEALERHGVAQRCTRVPVRQATEQEILLAHSEEYLEAVKQTPKMTVEEL-KAFSKKYN---DVYFHQNIYGCA 105
Cdd:cd11598     22 PFRLTLTKHLVMGYGLHKAMDTYEARAATREELRQFHDADYLDFLSKVSPENANQLrFDKAEPFNigdDCPVFDGMYDYC 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  106 KLAVGATLQlvdsvMKREVRNG---MALVRPPG-HHSQRSAANGFCVFNNVAIAALYAQKSYSvnRVLIVDWDVHHGQGV 181
Cdd:cd11598    102 QLYAGASLD-----AARKLCSGqsdIAINWSGGlHHAKKSEASGFCYVNDIVLAILNLLRYFP--RVLYIDIDVHHGDGV 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  182 QYCFEEDPSVLYFSWHRYEHQtFWPNlpESDYTSIGKGKGSGFNINVPWNKvGMTNSDYLAAFFHVLLPAAYEFDPELVL 261
Cdd:cd11598    175 EEAFYRTDRVMTLSFHKYNGE-FFPG--TGDLDDNGGTPGKHFALNVPLED-GIDDEQYNLLFKSIIGPTIEKFQPSAIV 250
                          250       260
                   ....*....|....*....|....*
gi 1958692215  262 VSAGFDSAIGDPEGemCASPEIFAH 286
Cdd:cd11598    251 LQCGADSLGGDRLG--QFNLNIKAH 273
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
32-310 2.61e-25

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


Pssm-ID: 212543 [Multi-domain]  Cd Length: 294  Bit Score: 107.35  E-value: 2.61e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   32 RLTASYEALERHGVAQRCTRV-PVRQATEQEILLAHSEEYLEAVkqtpkmtveeLKAFSKKYnDVYFHQNIYGCAKLAVG 110
Cdd:cd11680     21 RSSLVHSLIRAYGLLQHFDEIiEPERATRKDLTKYHDKDYVDFL----------LKKYGLED-DCPVFPFLSMYVQLVAG 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  111 ATLQLVDSVmKREVRNGMALVRPPG-HHSQRSAANGFCVFNNVAIAALyAQKSYSVNRVLIVDWDVHHGQGVQYCFEEDP 189
Cdd:cd11680     90 SSLALAKHL-ITQVERDIAINWYGGrHHAQKSRASGFCYVNDIVLAIL-RLRRARFRRVFYLDLDLHHGDGVESAFFFSK 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  190 SVLYFSWHRYEhQTFWPNLPESDYTSigkgkgSGFNINVPwNKVGMTNSDYLAAFFHVLLPAAYEFDPELVLVSAGFDSA 269
Cdd:cd11680    168 NVLTCSIHRYD-PGFFPGTGSLKNSS------DKGMLNIP-LKRGLSDKTLLRIIDSIVRPLIEKFEPEVIVIQCGCDGL 239
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1958692215  270 IGDPEGEMCASPEIFAHLTQLLMPLAAGKMCLVL-EGGYNLT 310
Cdd:cd11680    240 SGDPHKEWNLTIRGYGSVIELLLKEFKDKPTLLLgGGGYNHT 281
HDAC_Hos3 cd09998
Class II histone deacetylases Hos3 and related proteins; Fungal histone deacetylase Hos3 from ...
9-316 1.91e-23

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


Pssm-ID: 212522 [Multi-domain]  Cd Length: 353  Bit Score: 103.30  E-value: 1.91e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215    9 FDEEMTRYKLLWTDPACEIEVPERLTAS--YEALERHGvaqrctrvpvrqateqeillahSEEYLEAVKQTPKMTVEELK 86
Cdd:cd09998      5 YKHRYSRSKTSKSYLSTIVERPERLRASvlGLSAAVHG----------------------SKWSAELIEMCDMAEAKLAK 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   87 AFSKKynDVYFHQN-IYGCAK------LAVGATLQLVDSVMKREV---RNGMALVRPPGHHSQRSAANGFCVFNNVAIAA 156
Cdd:cd09998     63 GESEI--PAHLPQGdLYLCPEsldaiqGALGAVCEAVDSVFKPESpgtKRAFVAIRPPGHHCSESTPSGFCWVNNVHVGA 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  157 LYAQKSYSVNRVLIVDWDVHHGQGVQ-YCFE-----------------------EDPSVLYFSWH---RYEHQTFWPNLP 209
Cdd:cd09998    141 AHAYLTHGITRVVILDIDLHHGNGTQdIAWRinaeankqalesssyddfkpagaPGLRIFYSSLHdinSFPCEDGDPAKV 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  210 ESDYTSIGKGKGSgfNI-NV---PWNkvgmTNSDY---LAAFFHVLLPAAYEF-------DPE--LVLVSAGFDSAIGDP 273
Cdd:cd09998    221 KDASVSIDGAHGQ--WIwNVhlqPWT----TEEDFwelYYPKYRILFEKAAEFlrlttaaTPFktLVFISAGFDASEHEY 294
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958692215  274 EG----EMCASPEIFAHLT----QLLMPLAAGKMCLVLEGGYNLTCLAQSV 316
Cdd:cd09998    295 ESmqrhGVNVPTSFYYRFArdavRFADAHAHGRLISVLEGGYSDRALCSGV 345
HDAC1 cd10010
Histone deacetylase 1 (HDAC1); Histone deacetylase 1 (HDAC1) is a Zn-dependent class I enzyme ...
30-322 1.60e-20

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


Pssm-ID: 212534 [Multi-domain]  Cd Length: 371  Bit Score: 94.75  E-value: 1.60e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   30 PERLTASYEALERHGVAQRCTRVPVRQATEQEILLAHSEEYLEAVKQTPKMTVEELKAFSKKYN---DVYFHQNIYGCAK 106
Cdd:cd10010     29 PHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNvgeDCPVFDGLFEFCQ 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  107 LAVGATlqlVDSVMKREVRNGMALVRPPG--HHSQRSAANGFCVFNNVAIAALYAQKSYsvNRVLIVDWDVHHGQGVQYC 184
Cdd:cd10010    109 LSAGGS---VASAVKLNKQQTDIAVNWAGglHHAKKSEASGFCYVNDIVLAILELLKYH--QRVLYIDIDIHHGDGVEEA 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  185 FEEDPSVLYFSWHRYEHqtFWPNlpESDYTSIGKGKGSGFNINVPWnKVGMTNSDYLAAFFHVLLPAAYEFDPELVLVSA 264
Cdd:cd10010    184 FYTTDRVMTVSFHKYGE--YFPG--TGDLRDIGAGKGKYYAVNYPL-RDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQC 258
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958692215  265 GFDSAIGDPEGemCASPEIFAH------LTQLLMPlaagkMCLVLEGGYNLTCLAQsvCQTVQT 322
Cdd:cd10010    259 GADSLSGDRLG--CFNLTIKGHakcvefVKSFNLP-----MLMLGGGGYTIRNVAR--CWTYET 313
HDAC3 cd10005
Histone deacetylase 3 (HDAC3); HDAC3 is a Zn-dependent class I histone deacetylase that ...
30-324 1.94e-18

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: 88.61  E-value: 1.94e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   30 PERLTASYEALERHGVAQRCTRVPVRQATEQEILLAHSEEYLEAVKQTPKMTVEELKAFSKKYN---DVYFHQNIYGCAK 106
Cdd:cd10005     24 PHRLALTHSLVLHYGLYKKMQVYKPYRASAHDMCRFHSEDYIDFLQRVTPQNIQGFTKSLNQFNvgdDCPVFPGLFDFCS 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  107 LAVGATLQLVDSVMKREVrnGMALVRPPG-HHSQRSAANGFCVFNNVAIAALYAQKSYsvNRVLIVDWDVHHGQGVQYCF 185
Cdd:cd10005    104 MYTGASLEGATKLNHKIC--DIAINWSGGlHHAKKFEASGFCYVNDIVIAILELLKYH--PRVLYIDIDIHHGDGVQEAF 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  186 EEDPSVLYFSWHRYEHQtFWPNlpESDYTSIGKGKGSGFNINVPWnKVGMTNSDYLAAFFHVLLPAAYEFDPELVLVSAG 265
Cdd:cd10005    180 YLTDRVMTVSFHKYGNY-FFPG--TGDMYEVGAESGRYYSVNVPL-KDGIDDQSYLQLFKPVIQQVIDFYQPTCIVLQCG 255
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958692215  266 FDSAIGDPEGemCASPEIFAH------LTQLLMPLaagkmcLVL-EGGYNLTCLAQsvCQTVQTLL 324
Cdd:cd10005    256 ADSLGCDRLG--CFNLSIKGHgecvefVKSFNIPL------LVLgGGGYTVRNVAR--CWTYETSL 311
RPD3-like cd10004
reduced potassium dependency-3 (RPD3)-like; Proteins of the Rpd3-like family are class I ...
30-326 2.87e-18

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: 87.94  E-value: 2.87e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   30 PERLTASYEALERHGVAQRCTRVPVRQATEQEILLAHSEEYLEAVKQTPKMTVEELKAFSKKYN---DVYFHQNIYGCAK 106
Cdd:cd10004     25 PHRIRMAHSLVMNYGLYKKMEIYRAKPATKNEMTQFHTDEYIDFLSRVTPDNMEKFQKEQVKYNvgdDCPVFDGLFEFCS 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  107 LAVGATLQLVDSVMKREVRngMALVRPPG-HHSQRSAANGFCVFNNVAIAALYAQKSYSvnRVLIVDWDVHHGQGVQYCF 185
Cdd:cd10004    105 ISAGGSMEGAARLNRGKCD--IAVNWAGGlHHAKKSEASGFCYVNDIVLGILELLRYHQ--RVLYIDIDVHHGDGVEEAF 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  186 EEDPSVLYFSWHRYEHqtFWPNLPESDYTSIGKGKgsGFNINVPWnKVGMTNSDYLAAFFHVLLPAAYEFDPELVLVSAG 265
Cdd:cd10004    181 YTTDRVMTCSFHKYGE--YFPGTGELRDIGIGTGK--NYAVNVPL-RDGIDDESYKSIFEPVIKHVMEWYQPEAVVLQCG 255
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958692215  266 FDSAIGDPEGEMCASPEIFAHLTQLLMPLAAGKMCLVlEGGYNLTCLAQSVCQTVQTLLGD 326
Cdd:cd10004    256 GDSLSGDRLGCFNLSMKGHANCVNFVKSFNLPMLVLG-GGGYTMRNVARTWAFETGLLAGE 315
HDAC2 cd10011
Histone deacetylase 2 (HDAC2); Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme ...
30-322 8.02e-18

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


Pssm-ID: 212535 [Multi-domain]  Cd Length: 366  Bit Score: 86.66  E-value: 8.02e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   30 PERLTASYEALERHGVAQRCTRVPVRQATEQEILLAHSEEYLEAVKQTPKMTVEELKAFSKKYN---DVYFHQNIYGCAK 106
Cdd:cd10011     25 PHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNvgeDCPVFDGLFEFCQ 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  107 LAVGATLqlVDSVMKREVRNGMALVRPPG-HHSQRSAANGFCVFNNVAIAALYAQKSYsvNRVLIVDWDVHHGQGVQYCF 185
Cdd:cd10011    105 LSTGGSV--AGAVKLNRQQTDMAVNWAGGlHHAKKSEASGFCYVNDIVLAILELLKYH--QRVLYIDIDIHHGDGVEEAF 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  186 EEDPSVLYFSwhryeHQTFWPNLPES-DYTSIGKGKGSGFNINVPWnKVGMTNSDYLAAFFHVLLPAAYEFDPELVLVSA 264
Cdd:cd10011    181 YTTDRVMTVS-----FHKYGEYFPGTgDLRDIGAGKGKYYAVNFPM-RDGIDDESYGQIFKPIISKVMEMYQPSAVVLQC 254
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958692215  265 GFDSAIGDPEGemCASPEIFAHlTQLLMPLAAGKMCLVLEGGYNLTCLAQSVCQTVQT 322
Cdd:cd10011    255 GADSLSGDRLG--CFNLTVKGH-AKCVEVVKTFNLPLLMLGGGGYTIRNVARCWTYET 309
PTZ00063 PTZ00063
histone deacetylase; Provisional
56-306 1.19e-17

histone deacetylase; Provisional


Pssm-ID: 240251  Cd Length: 436  Bit Score: 86.79  E-value: 1.19e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   56 QATEQEILLAHSEEYLEAVKQtpkMTVEELKAFS---KKYN-----DVYFHQNIYGCAKLAVGATLqlvDSVMKREVRNG 127
Cdd:PTZ00063    53 KSVEPELVLFHDEEYVDFLSS---ISPENYRDFTyqlKRFNvgeatDCPVFDGLFEFQQSCAGASI---DGAYKLNNHQA 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  128 MALVRPPG--HHSQRSAANGFCVFNNVAIAALYAQKSYSvnRVLIVDWDVHHGQGVQYCFEEDPSVLYFSWHRYEHqtFW 205
Cdd:PTZ00063   127 DICVNWSGglHHAKRSEASGFCYINDIVLGILELLKYHA--RVMYIDIDVHHGDGVEEAFYVTHRVMTVSFHKFGD--FF 202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  206 PNlpESDYTSIGKGKGSGFNINVPWNKvGMTNSDYLAAFFHVLLPAAYEFDPELVLVSAGFDSAIGDPEGEMCAS----P 281
Cdd:PTZ00063   203 PG--TGDVTDIGVAQGKYYSVNVPLND-GIDDDSFVDLFKPVISKCVEVYRPGAIVLQCGADSLTGDRLGRFNLTikghA 279
                          250       260
                   ....*....|....*....|....*
gi 1958692215  282 EIFAHLTQLLMPLaagkmcLVLEGG 306
Cdd:PTZ00063   280 ACVEFVRSLNIPL------LVLGGG 298
PTZ00346 PTZ00346
histone deacetylase; Provisional
136-330 1.55e-14

histone deacetylase; Provisional


Pssm-ID: 240374 [Multi-domain]  Cd Length: 429  Bit Score: 76.99  E-value: 1.55e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  136 HHSQRSAANGFCVFNNVAIAALYAQKSYsvNRVLIVDWDVHHGQGVQYCFEEDPSVLYFSWHRYeHQTFWPNLPESDYTS 215
Cdd:PTZ00346   154 HHSKCGECSGFCYVNDIVLGILELLKCH--DRVLYVDIDMHHGDGVDEAFCTSDRVFTLSLHKF-GESFFPGTGHPRDVG 230
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  216 IGKGKGSGFNINVpWNkvGMTNSDYLAAFFHVLLPAAYEFDPELVLVSAGFDSAIGDPEGEMCASPEIFAHLTQLLMPLA 295
Cdd:PTZ00346   231 YGRGRYYSMNLAV-WD--GITDFYYLGLFEHALHSIVRRYSPDAIVLQCGADSLAGDRLGLLNLSSFGHGQCVQAVRDLG 307
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1958692215  296 AgKMCLVLEGGYNLTCLAQSVCQTVQTLLGDPAPL 330
Cdd:PTZ00346   308 I-PMLALGGGGYTIRNVAKLWAYETSILTGHPLPP 341
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
760-868 4.05e-14

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 69.24  E-value: 4.05e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  760 KDLQKVLIDWINSELEED--RIIVKDLEEDLYDGQVLQKLFEKLSGYKLNVAEVTQSEIGQKQKLQTVLEAVN---GVLR 834
Cdd:pfam00307    1 LELEKELLRWINSHLAEYgpGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAEkklGVPK 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1958692215  835 PLewhtEWSVDAIHSKSLvSIVYLLLALAMYYAA 868
Cdd:pfam00307   81 VL----IEPEDLVEGDNK-SVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
928-1035 1.60e-10

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 59.22  E-value: 1.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  928 NVVKTSLITFVNKHLNKL--NLEVTELESQFADGVYLVLLMglleNYFVP-LYNFYLTPESFEQKVHNVAFAFELMQDG- 1003
Cdd:pfam00307    1 LELEKELLRWINSHLAEYgpGVRVTNFTTDLRDGLALCALL----NKLAPgLVDKKKLNKSEFDKLENINLALDVAEKKl 76
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1958692215 1004 GLQKPKARPEDVVNLNLKSTLRVLYNLFTNYK 1035
Cdd:pfam00307   77 GVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQ 108
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
930-1034 7.78e-10

first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409064  Cd Length: 107  Bit Score: 57.03  E-value: 7.78e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  930 VKTSLITF---VNKHLNKLNLEVTELESQFADGVYLVLLMGLLENYFVPLYNfyLTPESFEQKVHNVAFAFELMQDGGLQ 1006
Cdd:cd21215      2 VDVQKKTFtkwLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRYN--KNPKMRVQKLENVNKALEFIKSRGVK 79
                           90       100
                   ....*....|....*....|....*...
gi 1958692215 1007 KPKARPEDVVNLNLKSTLRVLYNLFTNY 1034
Cdd:cd21215     80 LTNIGAEDIVDGNLKLILGLLWTLILRF 107
HDAC10_HDAC6-dom1 cd10002
Histone deacetylase 6, domain 1 and histone deacetylase 10; Histone deacetylases 6 and 10 are ...
554-660 1.95e-08

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: 57.32  E-value: 1.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  554 AGFMQAALGLILPLAYEFNPGLVL----------GVVGESGVKTHLapvWGHLTSLLQGVAQGRTLALLQGY--DKDL-- 619
Cdd:cd10002    219 ADYLAIFHHILLPLALEFQPELVLvsagfdasigDPEGEMAVTPAG---YAHLTRLLMGLAGGKLLLVLEGGylLESLae 295
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1958692215  620 -VEVTASALSGAPVPPLgVLGAPKPEDVQMIEKQRQRLQECW 660
Cdd:cd10002    296 sVSMTLRGLLGDPLPPL-APPIPIRSVLETILNAIAHLSPRW 336
HDAC6-dom2 cd10003
Histone deacetylase 6, domain 2; Histone deacetylase 6 is a class IIb Zn-dependent enzyme that ...
554-664 3.69e-08

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: 56.58  E-value: 3.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  554 AGFMQAALGLILPLAYEFNPGLVLGVVG-ESGVKTHL------APVWGHLTSLLQGVAQGRTLALLQ-GYDKD-----LV 620
Cdd:cd10003    228 AEYIAAFQQVVLPIAYEFNPELVLVSAGfDAARGDPLggckvtPEGYAHMTHMLMSLAGGRVIVILEgGYNLTsisesMS 307
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1958692215  621 EVTaSALSGAPVPPLGVLGAPKPEDVQMIEKQRQRLQECWGLLR 664
Cdd:cd10003    308 MCT-KTLLGDPPPVLDLPRPPCSSALKSINNVLQVHQKYWKSLR 350
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
938-1030 3.01e-07

calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.


Pssm-ID: 409061  Cd Length: 105  Bit Score: 49.50  E-value: 3.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  938 VNKHLNKLNLE--VTELESQFADGVYLVLLMGLLENYFVPlyNFYLTPESFEQKVHNVAFAFELMQDGGLQKPKARPEDV 1015
Cdd:cd21212      9 ANHYLEKGGHKriITDLQKDLGDGLTLVNLIEAVAGEKVP--GIHSRPKTRAQKLENIQACLQFLAALGVDVQGITAEDI 86
                           90
                   ....*....|....*
gi 1958692215 1016 VNLNLKSTLRVLYNL 1030
Cdd:cd21212     87 VDGNLKAILGLFFSL 101
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
763-863 3.18e-07

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 49.64  E-value: 3.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  763 QKVLIDWINSELEEDRII-VKDLEEDLYDGQVLQKLFEKLSGYKLNVAEVTQ-SEIGQKQKLQTVLEAVNGVLRPLEWHT 840
Cdd:cd00014      1 EEELLKWINEVLGEELPVsITDLFESLRDGVLLCKLINKLSPGSIPKINKKPkSPFKKRENINLFLNACKKLGLPELDLF 80
                           90       100
                   ....*....|....*....|...
gi 1958692215  841 EwSVDAIHSKSLVSIVYLLLALA 863
Cdd:cd00014     81 E-PEDLYEKGNLKKVLGTLWALA 102
HDAC10 cd11683
Histone deacetylase 10; Histone deacetylases 10 are class IIb Zn-dependent enzymes that ...
554-660 3.23e-07

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: 53.71  E-value: 3.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  554 AGFMQAALGLILPLAYEFNPGLVL-------GVVGESGVKTHLAPVWGHLTSLLQGVAQGRTLALLQ-GYD-KDLVE--- 621
Cdd:cd11683    219 ADYLAAFFHVLLPLAFEFDPELVLvsagfdsAIGDPEGQMCATPECFAHLTHLLMVLAGGKLCAVLEgGYHlESLAEsvc 298
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1958692215  622 VTASALSGAPVPPLGVLGAPKPEDVQMIEKQRQRLQECW 660
Cdd:cd11683    299 MTVQTLLGDPLPRLSGEMTPCQSALESIQNVRAAQAPYW 337
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
912-1037 4.70e-07

first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409160  Cd Length: 124  Bit Score: 49.76  E-value: 4.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  912 ERDafdtLLDHAPDKLnVVKTSLITFVNKHLNKLNLEVTELESQFADGVYLVLLMGLLENYFVPLYNFYLTPESfeQKVH 991
Cdd:cd21311      3 ERD----LAEDAQWKR-IQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRS--QKLE 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1958692215  992 NVAFAFELMQ-DGGLQKPKARPEDVVNLNLKSTLRVLYNLFTNYKNS 1037
Cdd:cd21311     76 NVSVALKFLEeDEGIKIVNIDSSDIVDGKLKLILGLIWTLILHYSIS 122
HDAC6-dom1 cd11682
Histone deacetylase 6, domain 1; Histone deacetylases 6 are class IIb Zn-dependent enzymes ...
554-641 5.39e-07

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: 52.93  E-value: 5.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  554 AGFMQAALGLILPLAYEFNPGLVL------GVVGESGVKTHLAPV-WGHLTSLLQGVAQGR-TLALLQGYD-KDLVE-VT 623
Cdd:cd11682    219 ADYIAAFLHVLLPVALEFQPQLVLvaagfdAVIGDPKGEMAATPAcFAHLTHLLMGLAGGKlILSLEGGYNlRSLAEgVC 298
                           90       100
                   ....*....|....*....|
gi 1958692215  624 AS--ALSGAPVPPLGVLGAP 641
Cdd:cd11682    299 ASlkALLGDPCPMLESPGAP 318
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
931-1024 8.71e-07

first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409063  Cd Length: 105  Bit Score: 48.54  E-value: 8.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  931 KTSLITFVNKHLNKLNLEVTELESQFADGVYLVLLMGLLENYFVPLynfyltPESFEQKVH---NVAFAFELMQDGGLQK 1007
Cdd:cd21214      7 RKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPK------PERGKMRFHkiaNVNKALDFIASKGVKL 80
                           90
                   ....*....|....*..
gi 1958692215 1008 PKARPEDVVNLNLKSTL 1024
Cdd:cd21214     81 VSIGAEEIVDGNLKMTL 97
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
931-1030 9.75e-07

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 48.10  E-value: 9.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  931 KTSLITFVNKHLNK-LNLEVTELESQFADGVYLVLLMGLLENYFVPLYNfyLTPESFEQKVHNVAFAFELMQDGGLQKPK 1009
Cdd:cd00014      1 EEELLKWINEVLGEeLPVSITDLFESLRDGVLLCKLINKLSPGSIPKIN--KKPKSPFKKRENINLFLNACKKLGLPELD 78
                           90       100
                   ....*....|....*....|...
gi 1958692215 1010 -ARPEDVVNL-NLKSTLRVLYNL 1030
Cdd:cd00014     79 lFEPEDLYEKgNLKKVLGTLWAL 101
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
936-1034 1.95e-06

first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409076  Cd Length: 109  Bit Score: 47.67  E-value: 1.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  936 TF---VNKHLNKLNLEVTELESQFADGVYLVLLMGLLENYfvPLYNFYLTPESFEQKVHNVAFAFELMQDGGLQKPKARP 1012
Cdd:cd21227      8 TFtnwVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGR--KLGRVIKKPLNQHQKLENVTLALKAMAEDGIKLVNIGN 85
                           90       100
                   ....*....|....*....|..
gi 1958692215 1013 EDVVNLNLKSTLRVLYNLFTNY 1034
Cdd:cd21227     86 EDIVNGNLKLILGLIWHLILRY 107
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
938-1030 5.76e-06

first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409072  Cd Length: 113  Bit Score: 46.43  E-value: 5.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  938 VNKHLNKL--------------NLEVTELESQFADGVYLVLLMGLLENYFVPLYNFYLTPESFEQKVHNVAFAFELMQDG 1003
Cdd:cd21223      1 LTRHLGYLgyvlshvqtpldefDFAVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVPAISRLQKLHNVEVALKALKEA 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1958692215 1004 GLQKP----KARPEDVVNLNLKSTLRVLYNL 1030
Cdd:cd21223     81 GVLRGgdggGITAKDIVDGHREKTLALLWRI 111
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
763-806 2.43e-05

first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409042  Cd Length: 116  Bit Score: 44.59  E-value: 2.43e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958692215  763 QKVLIDWINSELEEDRIIVKDLEEDLYDGQVLQKLFEKLSGYKL 806
Cdd:cd21193     18 KKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKL 61
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
754-806 2.76e-05

first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409095  Cd Length: 117  Bit Score: 44.28  E-value: 2.76e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958692215  754 REDLNFKDLQKvlidWINSELEEDRIIVKDLEEDLYDGQVLQKLFEKLSGYKL 806
Cdd:cd21246     13 REAVQKKTFTK----WVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERL 61
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
767-866 3.19e-05

calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409062  Cd Length: 107  Bit Score: 43.83  E-value: 3.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  767 IDWINSEL--EEDRIIVKDLEEDLYDGQVLQKLFEKLSGYKLN-VAEVTQSEIGQKQKLQTVLEAVngVLRPLEWHtEWS 843
Cdd:cd21213      6 VAWVNSQLkkRPGIRPVQDLRRDLRDGVALAQLIEILAGEKLPgIDWNPTTDAERKENVEKVLQFM--ASKRIRMH-QTS 82
                           90       100
                   ....*....|....*....|...
gi 1958692215  844 VDAIHSKSLVSIVYLLLALAMYY 866
Cdd:cd21213     83 AKDIVDGNLKAIMRLILALAAHF 105
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
763-806 4.43e-05

first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409063  Cd Length: 105  Bit Score: 43.53  E-value: 4.43e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958692215  763 QKVLIDWINSELEEDRIIVKDLEEDLYDGQVLQKLFEKLSGYKL 806
Cdd:cd21214      7 RKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERL 50
HDAC_Clr3 cd11600
Class II Histone deacetylase Clr3 and similar proteins; Clr3 is a class II Histone ...
548-644 4.55e-05

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: 46.57  E-value: 4.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  548 EGESFTAGFMQAALG----------LILPLAYEFNPGLVLGVVG-------ESGvKTHLAPV-WGHLTSLLQGVAQGRTL 609
Cdd:cd11600    203 LGFNVNIPWPQGGMGdadyiyafqrIVMPIAYEFDPDLVIISAGfdaadgdELG-QCHVTPAgYAHMTHMLMSLAGGKLV 281
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1958692215  610 ALLQ-GYDKDlvEVTASALSGAPVpplgVLGAPKPE 644
Cdd:cd11600    282 VALEgGYNLD--AISDSALAVAKV----LLGEAPPK 311
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
761-839 8.52e-05

first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409035  Cd Length: 107  Bit Score: 42.75  E-value: 8.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  761 DLQK-VLIDWINSEL-EEDRIIVKDLEEDLYDGQVLQKLFEKLSGYKLNvaevtqSEIGQKQKLQtvLEAVNGVLRPLEW 838
Cdd:cd21186      1 DVQKkTFTKWINSQLsKANKPPIKDLFEDLRDGTRLLALLEVLTGKKLK------PEKGRMRVHH--LNNVNRALQVLEQ 72

                   .
gi 1958692215  839 H 839
Cdd:cd21186     73 N 73
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
935-1035 1.26e-04

calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409062  Cd Length: 107  Bit Score: 42.28  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  935 ITFVNKHLNKL--NLEVTELESQFADGVYLVLLMGLLENYFVPLYNFYltPESFEQKVHNVAFAFELMQDGGLQKPKARP 1012
Cdd:cd21213      6 VAWVNSQLKKRpgIRPVQDLRRDLRDGVALAQLIEILAGEKLPGIDWN--PTTDAERKENVEKVLQFMASKRIRMHQTSA 83
                           90       100
                   ....*....|....*....|...
gi 1958692215 1013 EDVVNLNLKSTLRVLYNLFTNYK 1035
Cdd:cd21213     84 KDIVDGNLKAIMRLILALAAHFK 106
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
929-1035 1.48e-04

first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409037  Cd Length: 105  Bit Score: 42.00  E-value: 1.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  929 VVKTSLITFVNKHLNKLNLEVTELESQFADGVYLVLLMGLLENYFVPLYNFYLtpeSFeQKVHNVAFAFELMQDGGLQKP 1008
Cdd:cd21188      3 VQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRM---RF-HRLQNVQTALDFLKYRKIKLV 78
                           90       100
                   ....*....|....*....|....*..
gi 1958692215 1009 KARPEDVVNLNLKSTLRVLYNLFTNYK 1035
Cdd:cd21188     79 NIRAEDIVDGNPKLTLGLIWTIILHFQ 105
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
937-1034 1.76e-04

first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409077  Cd Length: 108  Bit Score: 42.09  E-value: 1.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  937 FVNKHLNKLNLEVTELESQFADGVYLVLLMGLLENYFVPlYNFYLTPESFEQKVHNVAFAFELMQDGGLQKPKARPEDVV 1016
Cdd:cd21228     12 WCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMY-KKYNKRPTFRQMKLENVSVALEFLERESIKLVSIDSSAIV 90
                           90
                   ....*....|....*...
gi 1958692215 1017 NLNLKSTLRVLYNLFTNY 1034
Cdd:cd21228     91 DGNLKLILGLIWTLILHY 108
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
919-1037 3.05e-04

first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409159  Cd Length: 125  Bit Score: 41.55  E-value: 3.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  919 LLDHAPDKlNVVKTSLITFVNKHLNKLNLEVTELESQFADGVYLVLLMGLLENYfvPLYNFYLTPESFEQ-KVHNVAFAF 997
Cdd:cd21310      7 LAEDAPWK-KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQK--KMYRKYHPRPNFRQmKLENVSVAL 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958692215  998 ELMQDGGLQKPKARPEDVVNLNLKSTLRVLYNLFTNYKNS 1037
Cdd:cd21310     84 EFLDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 123
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
763-837 3.28e-04

first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409090  Cd Length: 113  Bit Score: 41.21  E-value: 3.28e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958692215  763 QKVLIDWINSELEEDR--IIVKDLEEDLYDGQVLQKLFEKLSGYKLnvaevtQSEIGQKQKLQTVLEAVNGVLRPLE 837
Cdd:cd21241      7 KKTFTNWINSYLAKRKppMKVEDLFEDIKDGTKLLALLEVLSGEKL------PCEKGRRLKRVHFLSNINTALKFLE 77
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
763-830 4.57e-04

first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409037  Cd Length: 105  Bit Score: 40.46  E-value: 4.57e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  763 QKVLIDWINSELEEDRIIVKDLEEDLYDGQVLQKLFEKLSGYKLnvaevtQSEIGQKQ--KLQTVLEAVN 830
Cdd:cd21188      5 KKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESL------PRERGRMRfhRLQNVQTALD 68
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
96-268 5.08e-04

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: 42.75  E-value: 5.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215   96 YFHQNIYGCaklavgatlqlVDSVMKReVRNGMALVrppGHHSQrsaANGfcvfNNVAIAALYaqksysvNRVLIVDWDV 175
Cdd:cd09987      9 EAHELLAGV-----------VVAVLKD-GKVPVVLG---GDHSI---ANG----AIRAVAELH-------PDLGVIDVDA 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  176 HHGQGVQY--------------CFEEDPSVLYFSWHRYEHQTFWPNlpesdytsiGKGKGSGFNINVPWNKVgmTNSDYL 241
Cdd:cd09987     60 HHDVRTPEafgkgnhhtprhllCEPLISDVHIVSIGIRGVSNGEAG---------GAYARKLGVVYFSMTEV--DKLGLG 128
                          170       180
                   ....*....|....*....|....*..
gi 1958692215  242 AAFfhVLLPAAYEFDPELVLVSAGFDS 268
Cdd:cd09987    129 DVF--EEIVSYLGDKGDNVYLSVDVDG 153
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
919-1037 5.61e-04

first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409158  Cd Length: 131  Bit Score: 41.22  E-value: 5.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  919 LLDHAPDKlNVVKTSLITFVNKHLNKLNLEVTELESQFADGVYLVLLMGLLENYfvPLYNFYLTPESFEQ-KVHNVAFAF 997
Cdd:cd21309      8 LAEDAPWK-KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQK--RMYRKYHQRPTFRQmQLENVSVAL 84
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958692215  998 ELMQDGGLQKPKARPEDVVNLNLKSTLRVLYNLFTNYKNS 1037
Cdd:cd21309     85 EFLDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSIS 124
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
754-848 6.19e-04

first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.


Pssm-ID: 409080  Cd Length: 111  Bit Score: 40.29  E-value: 6.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  754 REDLNFKDLQKvlidWINSELEE-DRIIVKDLEEDLYDGQVLQKLFEKLSGYKLnvaevtqseigQKQKLQTVLEAVNGV 832
Cdd:cd21231      3 REDVQKKTFTK----WINAQFAKfGKPPIEDLFTDLQDGRRLLELLEGLTGQKL-----------VKEKGSTRVHALNNV 67
                           90
                   ....*....|....*.
gi 1958692215  833 LRPLEWHTEWSVDAIH 848
Cdd:cd21231     68 NKALQVLQKNNVDLVN 83
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
919-1037 6.22e-04

first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409157  Cd Length: 129  Bit Score: 40.84  E-value: 6.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  919 LLDHAPDKlNVVKTSLITFVNKHLNKLNLEVTELESQFADGVYLVLLMGLLENYfvPLYNFYLTPESFEQ-KVHNVAFAF 997
Cdd:cd21308     11 LAEDAPWK-KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQK--KMHRKHNQRPTFRQmQLENVSVAL 87
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958692215  998 ELMQDGGLQKPKARPEDVVNLNLKSTLRVLYNLFTNYKNS 1037
Cdd:cd21308     88 EFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 127
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
763-806 6.93e-04

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409167  Cd Length: 139  Bit Score: 41.16  E-value: 6.93e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958692215  763 QKVLIDWINSELEEDRIIVKDLEEDLYDGQVLQKLFEKLSGYKL 806
Cdd:cd21318     40 KKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQL 83
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
764-828 1.60e-03

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 38.84  E-value: 1.60e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958692215   764 KVLIDWINSELEE-DRIIVKDLEEDLYDGQVLQKLFEKLSGYKLNVAEVTQ--SEIGQKQKLQTVLEA 828
Cdd:smart00033    1 KTLLRWVNSLLAEyDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAslSRFKKIENINLALSF 68
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
763-806 2.35e-03

first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409064  Cd Length: 107  Bit Score: 38.54  E-value: 2.35e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958692215  763 QKVLIDWINSELEEDRIIVKDLEEDLYDGQVLQKLFEKLSGYKL 806
Cdd:cd21215      6 KKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESL 49
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
763-806 2.40e-03

first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409040  Cd Length: 114  Bit Score: 38.71  E-value: 2.40e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1958692215  763 QKVLIDWINSELE--EDRIIVKDLEEDLYDGQVLQKLFEKLSGYKL 806
Cdd:cd21191      7 KRTFTRWINLHLEkcNPPLEVKDLFVDIQDGKILMALLEVLSGQNL 52
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
763-830 2.68e-03

first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409076  Cd Length: 109  Bit Score: 38.42  E-value: 2.68e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958692215  763 QKVLIDWINSELEEDRIIVKDLEEDLYDGQVLQKLFEKLSGYKLnvAEVTQSEIGQKQKLQTVLEAVN 830
Cdd:cd21227      6 KNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKL--GRVIKKPLNQHQKLENVTLALK 71
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
763-806 2.96e-03

first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409085  Cd Length: 128  Bit Score: 38.81  E-value: 2.96e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958692215  763 QKVLIDWINSELEEDRIIVKDLEEDLYDGQVLQKLFEKLSGYKL 806
Cdd:cd21236     19 KKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTL 62
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
937-1034 3.19e-03

first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409032  Cd Length: 108  Bit Score: 38.23  E-value: 3.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958692215  937 FVNKHLNKLNLEVTELESQFADGVYLVLLMGLLENYFV-PLYNfyLTPESFEQKVHNVAFAFELMQDGGLQKPKARPEDV 1015
Cdd:cd21183     12 WCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLkRSYN--RRPAFQQHYLENVSTALKFIEADHIKLVNIGSGDI 89
                           90
                   ....*....|....*....
gi 1958692215 1016 VNLNLKSTLRVLYNLFTNY 1034
Cdd:cd21183     90 VNGNIKLILGLIWTLILHY 108
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
768-806 3.47e-03

calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.


Pssm-ID: 409061  Cd Length: 105  Bit Score: 37.95  E-value: 3.47e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958692215  768 DWINSELEE--DRIIVKDLEEDLYDGQVLQKLFEKLSGYKL 806
Cdd:cd21212      7 DWANHYLEKggHKRIITDLQKDLGDGLTLVNLIEAVAGEKV 47
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
763-806 5.08e-03

first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409086  Cd Length: 118  Bit Score: 38.09  E-value: 5.08e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958692215  763 QKVLIDWINSELEEDRIIVKDLEEDLYDGQVLQKLFEKLSGYKL 806
Cdd:cd21237      8 KKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKL 51
 
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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