NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|21312790|ref|NP_080646|]
View 

histone acetyltransferase KAT8 isoform 1 [Mus musculus]

Protein Classification

MYST family histone acetyltransferase( domain architecture ID 11476376)

MYST (SAS/MOZ) family histone acetyltransferase (HAT) is involved in the regulation of gene expression by adding acetyl groups to histone proteins which facilitates the binding of transcription factors to DNA

Gene Ontology:  GO:0004402|GO:0006281|GO:0046872|GO:0010224

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PLN00104 PLN00104
MYST -like histone acetyltransferase; Provisional
 21-449 0e+00

MYST -like histone acetyltransferase; Provisional


:

Pssm-ID: 215056 [Multi-domain]  Cd Length: 450  Bit Score: 563.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790   21 GEPGPGENAAVEGPARSPGRVSPPTPARGEPEVTVEIGETYLCR-RPDSTWHSAEVIQSRVNDQEGRE--EFYVHYVGFN 97
Cdd:PLN00104  20 DDAAATDGAGANAAAPAAPAESDPSKKRPGVMLPLEVGTRVMCRwRFDGKYHPVKVIERRRGGSGGPNdyEYYVHYTEFN 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790   98 RRLDEWVDKNRLALTKTVKDAVQKNSEKYLSelaeqpeRKITRNQKRKHDEINHVQKtYAEMDPttaALEKEHEAITKVK 177
Cdd:PLN00104 100 RRLDEWVKLEQLDLDTVETVGDEKVEDKVAS-------LKMTRHQKRKIDETHVEEG-HEELDA---ASLREHEEFTKVK 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790  178 YVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKYMKFEKSYRFHLGQCQWRQPPGKEIYRK----SNISVYEVDG 253
Cdd:PLN00104 169 NIATIELGRYEIDTWYFSPFPPEYNDCSKLYFCEFCLKFMKRKEQLQRHMKKCDLKHPPGDEIYRHptrqEGLSMFEVDG 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790  254 KDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNVACILTLPPYQRRGYGKFLI 333
Cdd:PLN00104 249 KKNKVYCQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEKHSEEDYNLACILTLPPYQRKGYGKFLI 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790  334 AFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDFRGTLSIKDLSQMTSITQNDIISTLQSLNMVKYWKGQH 413
Cdd:PLN00104 329 AFSYELSKREGKVGTPERPLSDLGLVSYRGYWTRVLLEILKKHKGNISIKELSDMTAIKAEDIVSTLQSLNLIQYRKGQH 408

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 21312790  414 VICVTPKLVEEHLKSAqyKKPPITVDSVCLKWAPPK 449
Cdd:PLN00104 409 VICADPKVLEEHLKAA--GRGGLEVDPSKLIWTPYK 442
 
Name Accession Description Interval E-value
PLN00104 PLN00104
MYST -like histone acetyltransferase; Provisional
 21-449 0e+00

MYST -like histone acetyltransferase; Provisional


Pssm-ID: 215056 [Multi-domain]  Cd Length: 450  Bit Score: 563.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790   21 GEPGPGENAAVEGPARSPGRVSPPTPARGEPEVTVEIGETYLCR-RPDSTWHSAEVIQSRVNDQEGRE--EFYVHYVGFN 97
Cdd:PLN00104  20 DDAAATDGAGANAAAPAAPAESDPSKKRPGVMLPLEVGTRVMCRwRFDGKYHPVKVIERRRGGSGGPNdyEYYVHYTEFN 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790   98 RRLDEWVDKNRLALTKTVKDAVQKNSEKYLSelaeqpeRKITRNQKRKHDEINHVQKtYAEMDPttaALEKEHEAITKVK 177
Cdd:PLN00104 100 RRLDEWVKLEQLDLDTVETVGDEKVEDKVAS-------LKMTRHQKRKIDETHVEEG-HEELDA---ASLREHEEFTKVK 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790  178 YVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKYMKFEKSYRFHLGQCQWRQPPGKEIYRK----SNISVYEVDG 253
Cdd:PLN00104 169 NIATIELGRYEIDTWYFSPFPPEYNDCSKLYFCEFCLKFMKRKEQLQRHMKKCDLKHPPGDEIYRHptrqEGLSMFEVDG 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790  254 KDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNVACILTLPPYQRRGYGKFLI 333
Cdd:PLN00104 249 KKNKVYCQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEKHSEEDYNLACILTLPPYQRKGYGKFLI 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790  334 AFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDFRGTLSIKDLSQMTSITQNDIISTLQSLNMVKYWKGQH 413
Cdd:PLN00104 329 AFSYELSKREGKVGTPERPLSDLGLVSYRGYWTRVLLEILKKHKGNISIKELSDMTAIKAEDIVSTLQSLNLIQYRKGQH 408

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 21312790  414 VICVTPKLVEEHLKSAqyKKPPITVDSVCLKWAPPK 449
Cdd:PLN00104 409 VICADPKVLEEHLKAA--GRGGLEVDPSKLIWTPYK 442
MOZ_SAS pfam01853
MOZ/SAS family; This region of these proteins has been suggested to be homologous to ...
 235-412 1.17e-137

MOZ/SAS family; This region of these proteins has been suggested to be homologous to acetyltransferases.


Pssm-ID: 460362 [Multi-domain]  Cd Length: 179  Bit Score: 392.56  E-value: 1.17e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790   235 PPGKEIYRKSNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNV 314
Cdd:pfam01853   1 PPGNEIYRKGNISIFEVDGRKQKLYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTETDETGCHIVGYFSKEKESSDNYNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790   315 ACILTLPPYQRRGYGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDFR-GTLSIKDLSQMTSITQ 393
Cdd:pfam01853  81 ACILTLPPYQRKGYGKLLIEFSYELSKREGKIGGPEKPLSDLGLLSYRSYWSEVILEYLLKHRkEGISIEDISKATGITP 160

                         170
                  ....*....|....*....
gi 21312790   394 NDIISTLQSLNMVKYWKGQ 412
Cdd:pfam01853 161 EDIISTLQSLNMLKYYKGQ 179
SAS2 COG5027
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics];
65-445 4.74e-132

Histone acetyltransferase (MYST family) [Chromatin structure and dynamics];


Pssm-ID: 227360 [Multi-domain]  Cd Length: 395  Bit Score: 386.82  E-value: 4.74e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790  65 RPDSTWHSAEVIQSRVNdqEGREEFYVHYVGFNRRLDEWVDKNRLALT--------KTVKDAVQKNSEKYLSELAEQPER 136
Cdd:COG5027  15 EKDGEARKAEILEINTR--KSRIKFYVHYVELNRRLDEWITADLINLGaaisipkrKKQTEKGKKEKKPKVSDRMDLDNE 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790 137 KItrnQKRKHDEINHVQKTYAEMDPTTAALEKEHEAitKVKYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKY 216
Cdd:COG5027  93 NV---QLEMLYSISNEREIRQLRFGGSKVQNPHEGA--RVKNINEIKLGNYEIEPWYFSPYPEEFSDLDIVYICEFCLKY 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790 217 MKFEKSYRFHLGQCQWRQPPGKEIYRKSNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGA 296
Cdd:COG5027 168 YGSQTSLVRHRKKCSLQHPPGNEIYRDKYISFFEIDGRKQRLYCRNLCLLSKLFLDHKTLYYDVDPFLFYVLTERGDTGC 247

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790 297 HIVGYFSKEKESPDGNNVACILTLPPYQRRGYGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDF 376
Cdd:COG5027 248 HLVGYFSKEKESEQDYNLACILTLPPYQRRGYGKLLIDFSYLLSQKEGKVGSPEKPLSDLGLLSYRAYWSEIVAKLLLKM 327

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790 377 RG-TLSIKDLSQMTSITQNDIISTLQSLNMVKYWKGQHVICVTPKLVEEHLKSAQYKKPPITVDSvcLKW 445
Cdd:COG5027 328 DKeITDINEISKETGMSTDDVIHTLEALNILREYKGQYIISLNSDKLHNYLRLWSKKRRRINPDL--LLW 395
CBD_MOF_like cd18984
chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar ...
 58-124 2.02e-31

chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar proteins; This subgroup includes the chromo barrel domain of Drosophila melanogaster males-absent on the first (MOF) protein. The histone H4 lysine 16 (H4K16)-specific acetyltransferase MOF is part of two distinct complexes involved in X chromosome dosage compensation and autosomal transcription regulation. Its chromobarrel domain is essential for H4K16 acetylation throughout the Drosophila genome and controls spreading of the male-specific lethal (MSL) complex on the X chromosome. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains, and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromodomain. The MOF-like chromo barrels may be may be auto-inhibited, i.e. they seem to have occluded peptide binding sites.


Pssm-ID: 350847 [Multi-domain]  Cd Length: 70  Bit Score: 114.96  E-value: 2.02e-31
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790  58 GETYLCRRPDSTWHSAEVIQSRVNDQEGREEFYVHYVGFNRRLDEWVDKNRLALT---KTVKDAVQKNSE 124
Cdd:cd18984   1 GSTYYCRRSDDTVHRAEVIQSRTTKQAGREEYYVHYVGLNRRLDEWVDKSRLSLNdlgKIVKTPAPPNAE 70
CHROMO smart00298
Chromatin organization modifier domain;
71-111 6.32e-05

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 40.66  E-value: 6.32e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 21312790     71 HSAEVIQSRVNDQEGREEFYVHYVGFNRRLDEWVDKNRLAL 111
Cdd:smart00298   2 YEVEKILDHRWKKKGELEYLVKWKGYSYSEDTWEPEENLLN 42
 
Name Accession Description Interval E-value
PLN00104 PLN00104
MYST -like histone acetyltransferase; Provisional
 21-449 0e+00

MYST -like histone acetyltransferase; Provisional


Pssm-ID: 215056 [Multi-domain]  Cd Length: 450  Bit Score: 563.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790   21 GEPGPGENAAVEGPARSPGRVSPPTPARGEPEVTVEIGETYLCR-RPDSTWHSAEVIQSRVNDQEGRE--EFYVHYVGFN 97
Cdd:PLN00104  20 DDAAATDGAGANAAAPAAPAESDPSKKRPGVMLPLEVGTRVMCRwRFDGKYHPVKVIERRRGGSGGPNdyEYYVHYTEFN 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790   98 RRLDEWVDKNRLALTKTVKDAVQKNSEKYLSelaeqpeRKITRNQKRKHDEINHVQKtYAEMDPttaALEKEHEAITKVK 177
Cdd:PLN00104 100 RRLDEWVKLEQLDLDTVETVGDEKVEDKVAS-------LKMTRHQKRKIDETHVEEG-HEELDA---ASLREHEEFTKVK 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790  178 YVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKYMKFEKSYRFHLGQCQWRQPPGKEIYRK----SNISVYEVDG 253
Cdd:PLN00104 169 NIATIELGRYEIDTWYFSPFPPEYNDCSKLYFCEFCLKFMKRKEQLQRHMKKCDLKHPPGDEIYRHptrqEGLSMFEVDG 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790  254 KDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNVACILTLPPYQRRGYGKFLI 333
Cdd:PLN00104 249 KKNKVYCQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEKHSEEDYNLACILTLPPYQRKGYGKFLI 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790  334 AFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDFRGTLSIKDLSQMTSITQNDIISTLQSLNMVKYWKGQH 413
Cdd:PLN00104 329 AFSYELSKREGKVGTPERPLSDLGLVSYRGYWTRVLLEILKKHKGNISIKELSDMTAIKAEDIVSTLQSLNLIQYRKGQH 408

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 21312790  414 VICVTPKLVEEHLKSAqyKKPPITVDSVCLKWAPPK 449
Cdd:PLN00104 409 VICADPKVLEEHLKAA--GRGGLEVDPSKLIWTPYK 442
PLN03238 PLN03238
probable histone acetyltransferase MYST; Provisional
 160-427 4.45e-149

probable histone acetyltransferase MYST; Provisional


Pssm-ID: 215642 [Multi-domain]  Cd Length: 290  Bit Score: 426.19  E-value: 4.45e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790  160 DPTTAALEKEHEAITKVKYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKYMKFEKSYRFHLGQCQWRQPPGKE 239
Cdd:PLN03238   1 DPVLAELEREHEETTKVKNIEMIELGKYEMDTWYYSPYPEPYASCTKLYICEYCLKYMRKKKSLLRHLAKCDIRQPPGGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790  240 IYR---KSNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNVAC 316
Cdd:PLN03238  81 IYGavtEGPLSVFEVDGKKAKVYCQNLCLLAKLFLDHKTLYYDVDPFLFYVMTEVDDHGSHIVGYFSKEKVSAEDYNLAC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790  317 ILTLPPYQRRGYGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDFRGTLSIKDLSQMTSITQNDI 396
Cdd:PLN03238 161 ILTLPPYQRKGYGKFLISFAYELSKREGKVGTPERPLSDLGKVSFRSYWTRVLLEQLRDVKGDVSIKDLSLATGIRGEDI 240

                        250       260       270
                 ....*....|....*....|....*....|.
gi 21312790  397 ISTLQSLNMVKYWKGQHVICVTPKLVEEHLK 427
Cdd:PLN03238 241 VSTLQSLNLIKYWKGQHVIHVDQRVLDEHWA 271
MOZ_SAS pfam01853
MOZ/SAS family; This region of these proteins has been suggested to be homologous to ...
 235-412 1.17e-137

MOZ/SAS family; This region of these proteins has been suggested to be homologous to acetyltransferases.


Pssm-ID: 460362 [Multi-domain]  Cd Length: 179  Bit Score: 392.56  E-value: 1.17e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790   235 PPGKEIYRKSNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNV 314
Cdd:pfam01853   1 PPGNEIYRKGNISIFEVDGRKQKLYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTETDETGCHIVGYFSKEKESSDNYNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790   315 ACILTLPPYQRRGYGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDFR-GTLSIKDLSQMTSITQ 393
Cdd:pfam01853  81 ACILTLPPYQRKGYGKLLIEFSYELSKREGKIGGPEKPLSDLGLLSYRSYWSEVILEYLLKHRkEGISIEDISKATGITP 160

                         170
                  ....*....|....*....
gi 21312790   394 NDIISTLQSLNMVKYWKGQ 412
Cdd:pfam01853 161 EDIISTLQSLNMLKYYKGQ 179
SAS2 COG5027
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics];
65-445 4.74e-132

Histone acetyltransferase (MYST family) [Chromatin structure and dynamics];


Pssm-ID: 227360 [Multi-domain]  Cd Length: 395  Bit Score: 386.82  E-value: 4.74e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790  65 RPDSTWHSAEVIQSRVNdqEGREEFYVHYVGFNRRLDEWVDKNRLALT--------KTVKDAVQKNSEKYLSELAEQPER 136
Cdd:COG5027  15 EKDGEARKAEILEINTR--KSRIKFYVHYVELNRRLDEWITADLINLGaaisipkrKKQTEKGKKEKKPKVSDRMDLDNE 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790 137 KItrnQKRKHDEINHVQKTYAEMDPTTAALEKEHEAitKVKYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKY 216
Cdd:COG5027  93 NV---QLEMLYSISNEREIRQLRFGGSKVQNPHEGA--RVKNINEIKLGNYEIEPWYFSPYPEEFSDLDIVYICEFCLKY 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790 217 MKFEKSYRFHLGQCQWRQPPGKEIYRKSNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGA 296
Cdd:COG5027 168 YGSQTSLVRHRKKCSLQHPPGNEIYRDKYISFFEIDGRKQRLYCRNLCLLSKLFLDHKTLYYDVDPFLFYVLTERGDTGC 247

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790 297 HIVGYFSKEKESPDGNNVACILTLPPYQRRGYGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDF 376
Cdd:COG5027 248 HLVGYFSKEKESEQDYNLACILTLPPYQRRGYGKLLIDFSYLLSQKEGKVGSPEKPLSDLGLLSYRAYWSEIVAKLLLKM 327

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790 377 RG-TLSIKDLSQMTSITQNDIISTLQSLNMVKYWKGQHVICVTPKLVEEHLKSAQYKKPPITVDSvcLKW 445
Cdd:COG5027 328 DKeITDINEISKETGMSTDDVIHTLEALNILREYKGQYIISLNSDKLHNYLRLWSKKRRRINPDL--LLW 395
PLN03239 PLN03239
histone acetyltransferase; Provisional
 89-447 9.08e-110

histone acetyltransferase; Provisional


Pssm-ID: 178777 [Multi-domain]  Cd Length: 351  Bit Score: 328.15  E-value: 9.08e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790   89 FYVHYVGFNRRLDEWVDKnrlaltktvkdavqknsEKYLSELAEQPERKITRNQKRKHDEINHVQKTYAEMDPTTAALEK 168
Cdd:PLN03239   1 YYVHYKDFNRRMDEWISK-----------------DKSNEEILALPSDHLATHTVGEDVVATIAAPELDEHEGLDDAALK 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790  169 EHEAITKVKYVDKIHIGNYEIDAWYFSPFPE----DYGKQPKLWLCEYCLK-YMKFEKSYRFHLGQC--QWRQPPGKEIY 241
Cdd:PLN03239  64 EHEEVTKVKNVAFLELGPYQMDTWYFSPLPKelfkAGGFIDVLYVCEFSFGfFARKSELLRFQAKELpkERRHPPGNEIY 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790  242 RKSNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNVACILTLP 321
Cdd:PLN03239 144 RCGDLAMFEVDGFEERIYCQNLCYIAKLFLDHKTLYFDVDPFLFYVLCEVDERGFHPVGYYSKEKYSDVGYNLACILTFP 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790  322 PYQRRGYGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDFRG---TLSIKDLSQMTSITQNDIIS 398
Cdd:PLN03239 224 AHQRKGYGRFLIAFSYELSKKEEKVGSPEKPMSDLGQQAYIPYWGSTIVDFLLNHSGndsSLSIMDIAKKTSIMAEDIVF 303

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 21312790  399 TLQSLNMVKYWKGQHVICVTPKLVEEHLKSAQYKKPpiTVDSVCLKWAP 447
Cdd:PLN03239 304 ALNQLGILKFINGIYFIAAEKGLLEELAEKHPVKEP--RVDPSKLHWTP 350
PTZ00064 PTZ00064
histone acetyltransferase; Provisional
 76-447 6.36e-103

histone acetyltransferase; Provisional


Pssm-ID: 173359 [Multi-domain]  Cd Length: 552  Bit Score: 317.73  E-value: 6.36e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790   76 IQSRVNDQEGRE--EFYVHYVGFNRRLDEWVDKNRLALTKTVKD--------AVQKNSEKYLSEL--AEQPERKITRNQK 143
Cdd:PTZ00064 136 VSSSSNESQIKEdyEFYVHFRGLNRRLDRWVKGKDIKLSFDVEElndpnlieRFQKQGIKFISSLsvSNSANKSGNKSKK 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790  144 RKhdeINHVQKTYAEmDPTT------AALEkEHEAITKVKYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKYM 217
Cdd:PTZ00064 216 RN---VGVLDISDGE-DPDEhegmdhSAIL-DHEETTRLRTIGRVRIGKFILDTWYFSPLPDEYQNVDTLHFCEYCLDFF 290

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790  218 KFEKSYRFHLGQCQWRQPPGKEIYRKSNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAH 297
Cdd:PTZ00064 291 CFEDELIRHLSRCQLRHPPGNEIYRKDNISVFEIDGALTRGYAENLCYLAKLFLDHKTLQYDVEPFLFYIVTEVDEEGCH 370

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790  298 IVGYFSKEKESPDGNNVACILTLPPYQRRGYGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYW----SWVLLEIL 373
Cdd:PTZ00064 371 IVGYFSKEKVSLLHYNLACILTLPCYQRKGYGKLLVDLSYKLSLKEGKWGHPERPLSDLGRAIYNNWWahriSEYLLEYF 450

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790  374 RD----FRG-----------TLSIKDLSQMTSITQNDIISTLQSLNMVKYWKGQHVICVTPKLVEEHLKSAqyKKPPITV 438
Cdd:PTZ00064 451 KQnkicERGgskqplqvsnyWKFIDNVVRSTGIRREDVIRILEENGIMRNIKDQHYIFCNQEFLKGIVKRS--GRPGITL 528


                 ....*....
gi 21312790  439 DSVCLKWAP 447
Cdd:PTZ00064 529 IDKYFNWVP 537
CBD_MOF_like cd18984
chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar ...
 58-124 2.02e-31

chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar proteins; This subgroup includes the chromo barrel domain of Drosophila melanogaster males-absent on the first (MOF) protein. The histone H4 lysine 16 (H4K16)-specific acetyltransferase MOF is part of two distinct complexes involved in X chromosome dosage compensation and autosomal transcription regulation. Its chromobarrel domain is essential for H4K16 acetylation throughout the Drosophila genome and controls spreading of the male-specific lethal (MSL) complex on the X chromosome. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains, and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromodomain. The MOF-like chromo barrels may be may be auto-inhibited, i.e. they seem to have occluded peptide binding sites.


Pssm-ID: 350847 [Multi-domain]  Cd Length: 70  Bit Score: 114.96  E-value: 2.02e-31
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312790  58 GETYLCRRPDSTWHSAEVIQSRVNDQEGREEFYVHYVGFNRRLDEWVDKNRLALT---KTVKDAVQKNSE 124
Cdd:cd18984   1 GSTYYCRRSDDTVHRAEVIQSRTTKQAGREEYYVHYVGLNRRLDEWVDKSRLSLNdlgKIVKTPAPPNAE 70
zf-MYST pfam17772
MYST family zinc finger domain; This zinc finger domain is found in the MYST family of histone ...
 176-230 4.12e-25

MYST family zinc finger domain; This zinc finger domain is found in the MYST family of histone acetyltransferases.


Pssm-ID: 407644 [Multi-domain]  Cd Length: 55  Bit Score: 97.30  E-value: 4.12e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 21312790   176 VKYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKYMKFEKSYRFHLGQC 230
Cdd:pfam17772   1 VKNIEKIQFGRYEIDTWYFSPYPEEYTNVDKLYVCEFCLKYMKSRKSYKRHRKKC 55
Tudor-knot pfam11717
RNA binding activity-knot of a chromodomain; This is a novel knotted tudor domain which is ...
 55-111 1.11e-19

RNA binding activity-knot of a chromodomain; This is a novel knotted tudor domain which is required for binding to RNA. The know influences the loop conformation of the helical turn Ht2 - residues 61-6 3- that is located at the side opposite the knot in the tudor domain-chromodomain; stabilization of Ht2 is essential for RNA binding.


Pssm-ID: 432022 [Multi-domain]  Cd Length: 55  Bit Score: 82.25  E-value: 1.11e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 21312790    55 VEIGETYLCRRPDSTWHSAEVIQSRvnDQEGREEFYVHYVGFNRRLDEWVDKNRLAL 111
Cdd:pfam11717   1 IEIGCKVLVRKRDGEWRLAEILSIR--PKKGKYEYYVHYVGFNKRLDEWVPEDRIDL 55
CBD_MOF_like cd18642
chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar ...
 62-111 4.19e-14

chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar proteins; This subgroup includes the chromo barrel domains found in human Tat-interactive protein 60 (TIP60, (also known as KAT5 or HTATIP), Drosophila melanogaster males-absent on the first (MOF) protein, and Saccharomyces ESA1. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains, and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain. The MOF-like chromo barrels may be may be auto-inhibited, i.e. they seem to have occluded peptide binding sites.


Pssm-ID: 350844 [Multi-domain]  Cd Length: 67  Bit Score: 67.07  E-value: 4.19e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 21312790  62 LCRRPDSTWHSAEVIQSRVNdQEGREEFYVHYVGFNRRLDEWVDKNRLAL 111
Cdd:cd18642   5 CWVQRNDEEHLAEVLSRRTR-KHAPPEFYVHYVELNRRLDEWITTDRIDL 53
CBD_TIP60_like cd18985
chromo barrel domain of human tat-interactive protein 60, and similar proteins; ...
 63-113 6.57e-10

chromo barrel domain of human tat-interactive protein 60, and similar proteins; Tat-interactive protein 60 (also known as KAT5 or HTATIP) catalyzes the acetylation of lysine side chains in various histone and nonhistone proteins, and in itself. It plays roles in multiple cellular processes including remodeling, transcription, DNA double-strand break repair, apoptosis, embryonic stem cell identity, and embryonic development. The TIP60 chromo barrel domain recognizes trimethylated lysine at site 9 of histone H3 (H3K9me3) which triggers TIP60 to acetylate and activate ataxia telangiectasia-mutated kinase, thereby promoting the DSB repair pathway. In a different study, the TIP60 chromo barrel domain was shown to bind H3K4me1, which stabilizes TIP60 recruitment to a subset of estrogen receptor alpha target genes, facilitating regulation of the associated gene transcription. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains, and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromodomain. This subgroup belongs to the MOF-like chromo barrels may be may be auto-inhibited, i.e. they seem to have occluded peptide binding sites.


Pssm-ID: 350848 [Multi-domain]  Cd Length: 64  Bit Score: 54.90  E-value: 6.57e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 21312790  63 CRRP---DSTWHSAEVIQsrVNDQEGREEFYVHYVGFNRRLDEWVDKNRLALTK 113
Cdd:cd18985   3 LRVRmhkTDEWPLAEILS--VKDISGRKLFYVHYIDFNKRLDEWVTHERLDLKK 54
CBD cd18643
chromo barrel domain of MOF acetyltransferase, and similar proteins; This group includes the ...
 59-109 1.51e-08

chromo barrel domain of MOF acetyltransferase, and similar proteins; This group includes the chromo barrel domains found in human Tat-interactive protein 60 (TIP60, (also known as KAT5 or HTATIP), Drosophila melanogaster males-absent on the first (MOF) protein, human male-specific lethal (MSL) complex subunit 3 (MSL3), and retinoblastoma binding protein 1. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains, and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain. The chromobarrel domains include a MOF-like subgroup which may be may be auto-inhibited, i.e. they seem to have occluded peptide binding sites.


Pssm-ID: 350845 [Multi-domain]  Cd Length: 61  Bit Score: 51.02  E-value: 1.51e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21312790  59 ETYLCRRPDS---TWHSAEVIQSRVNDQEGRE-EFYVHYVGFNRRLDEWVDKNRL 109
Cdd:cd18643   1 EKVLVFEPDPkarVLYDAKILSVITGKDGRAPpEYLVHYVGWNRRLDEWVAEDRV 55
CBD_ESA1_like cd18986
chromo barrel domain of yeast NuA4 histone acetyltransferase complex catalytic subunit ESA1, ...
 73-115 1.67e-07

chromo barrel domain of yeast NuA4 histone acetyltransferase complex catalytic subunit ESA1, and similar proteins; The subgroup includes the chromo barrel domain of NuA4 histone acetyltransferase (HAT) complex catalytic subunit Esa1 (also known as Tas1 and Kat5). Yeast Esa1p acetylates specific histones nonrandomly in H4, H3, and H2A. Esa1 also plays roles in cell cycle progression. In addition, its chromo barrel domain plays a role in the yeast Piccolo NuA4 complex's ability to distinguish between histones and nucleosomes; however, the chromodomain is not required for the Piccolo to bind to nucleosomes. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains, and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromodomain. This subgroup belongs to the MOF-like chromo barrels may be may be auto-inhibited, i.e. they seem to have occluded peptide binding sites.


Pssm-ID: 350849 [Multi-domain]  Cd Length: 65  Bit Score: 47.98  E-value: 1.67e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 21312790  73 AEVIQsrVNDQEGREEFYVHYVGFNRRLDEWVDKNRLALTKTV 115
Cdd:cd18986  16 AEILS--INTRKAPPKFYVHYEDFNKRLDEWITADRINLSKEV 56
MBT_PHF20L1-like cd20104
malignant brain tumor (MBT) repeat found in PHD finger protein 20-like protein 1 (PHF20L1) and ...
 55-114 6.33e-06

malignant brain tumor (MBT) repeat found in PHD finger protein 20-like protein 1 (PHF20L1) and similar domains; PHF20L1 associates with SOX2, antagonizes SOX2 ubiquitination and the sequential degradation induced by MLL1/WDR5 complexes. It binds both monomethylated Lys-42 and Lys-117 in SOX2 and thereby prevents SOX2 proteolysis. PHF20L1 also reads and controls enzyme levels of methylated DNMT1 in cells, thus representing a novel antagonist of DNMT1 degradation. PHF20L1 contains one MBT (malignant brain tumor) repeat. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the MBT repeat of PHF20L1 and similar domains that contains the semi-aromatic cage that may bind methylated lysine residues.


Pssm-ID: 439094 [Multi-domain]  Cd Length: 60  Bit Score: 43.38  E-value: 6.33e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21312790  55 VEIGETYLCRRPDSTWHSAEVIQSRVNDQEgreeFYVHYVGFNRRLDEWVDKN--RLALTKT 114
Cdd:cd20104   1 FKVGDRVDALDGEGKWYEAKIVEVDEEENK----VLVHYDGWSSRYDEWIDRDseRLRPLHT 58
CHROMO smart00298
Chromatin organization modifier domain;
71-111 6.32e-05

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 40.66  E-value: 6.32e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 21312790     71 HSAEVIQSRVNDQEGREEFYVHYVGFNRRLDEWVDKNRLAL 111
Cdd:smart00298   2 YEVEKILDHRWKKKGELEYLVKWKGYSYSEDTWEPEENLLN 42
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH