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Conserved domains on  [gi|1017353484|ref|NP_001309531|]
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histone acetyltransferase [Caenorhabditis elegans]

Protein Classification

MYST family histone acetyltransferase( domain architecture ID 1002286)

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

EC:  2.3.1.48
Gene Ontology:  GO:0004402
PubMed:  17374998

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PLN00104 super family cl33410
MYST -like histone acetyltransferase; Provisional
 83-467 4.05e-131

MYST -like histone acetyltransferase; Provisional


The actual alignment was detected with superfamily member PLN00104:

Pssm-ID: 215056 [Multi-domain]  Cd Length: 450  Bit Score: 389.11  E-value: 4.05e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484  83 GAKELMYYVHYEELDRRNDEWITLDKilVNEVVVEPVIKVPTKAPVEDLhkeivvgppvikpsgALTRSQRRTLEEYSHL 162
Cdd:PLN00104   85 GPNDYEYYVHYTEFNRRLDEWVKLEQ--LDLDTVETVGDEKVEDKVASL---------------KMTRHQKRKIDETHVE 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 163 KTDLNDLDAttarLEREHEERTKVKNIPQITIGAHEILAWYYSPFPP---DCENLdiYMCEYCLLYTPHHERFKQHIDTC 239
Cdd:PLN00104  148 EGHEELDAA----SLREHEEFTKVKNIATIELGRYEIDTWYFSPFPPeynDCSKL--YFCEFCLKFMKRKEQLQRHMKKC 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 240 KVRQPPGNEIYRK----DHLSVYEVDGSGQKLYCQCLCLLSKLFMDHKTLYFDVDDFMFYVLCETDEHGAHIVGYFSRE- 314
Cdd:PLN00104  222 DLKHPPGDEIYRHptrqEGLSMFEVDGKKNKVYCQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEk 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 315 -VESANNLACIMVFPPFQKKGYGKLLIQFSYELSRREGYIGMPEKPLSDLGKVSYRSYWWWRLMKLFHIHQGhTVTATFL 393
Cdd:PLN00104  302 hSEEDYNLACILTLPPYQRKGYGKFLIAFSYELSKREGKVGTPERPLSDLGLVSYRGYWTRVLLEILKKHKG-NISIKEL 380

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1017353484 394 SNESGIAVDDIVSTLITMRMCRQYKepefipGEWYVRIHRKIVDHcVMCGYGKpPRLLLDRTKVRWAPAQTRPE 467
Cdd:PLN00104  381 SDMTAIKAEDIVSTLQSLNLIQYRK------GQHVICADPKVLEE-HLKAAGR-GGLEVDPSKLIWTPYKEQPP 446
 
Name Accession Description Interval E-value
PLN00104 PLN00104
MYST -like histone acetyltransferase; Provisional
 83-467 4.05e-131

MYST -like histone acetyltransferase; Provisional


Pssm-ID: 215056 [Multi-domain]  Cd Length: 450  Bit Score: 389.11  E-value: 4.05e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484  83 GAKELMYYVHYEELDRRNDEWITLDKilVNEVVVEPVIKVPTKAPVEDLhkeivvgppvikpsgALTRSQRRTLEEYSHL 162
Cdd:PLN00104   85 GPNDYEYYVHYTEFNRRLDEWVKLEQ--LDLDTVETVGDEKVEDKVASL---------------KMTRHQKRKIDETHVE 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 163 KTDLNDLDAttarLEREHEERTKVKNIPQITIGAHEILAWYYSPFPP---DCENLdiYMCEYCLLYTPHHERFKQHIDTC 239
Cdd:PLN00104  148 EGHEELDAA----SLREHEEFTKVKNIATIELGRYEIDTWYFSPFPPeynDCSKL--YFCEFCLKFMKRKEQLQRHMKKC 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 240 KVRQPPGNEIYRK----DHLSVYEVDGSGQKLYCQCLCLLSKLFMDHKTLYFDVDDFMFYVLCETDEHGAHIVGYFSRE- 314
Cdd:PLN00104  222 DLKHPPGDEIYRHptrqEGLSMFEVDGKKNKVYCQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEk 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 315 -VESANNLACIMVFPPFQKKGYGKLLIQFSYELSRREGYIGMPEKPLSDLGKVSYRSYWWWRLMKLFHIHQGhTVTATFL 393
Cdd:PLN00104  302 hSEEDYNLACILTLPPYQRKGYGKFLIAFSYELSKREGKVGTPERPLSDLGLVSYRGYWTRVLLEILKKHKG-NISIKEL 380

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1017353484 394 SNESGIAVDDIVSTLITMRMCRQYKepefipGEWYVRIHRKIVDHcVMCGYGKpPRLLLDRTKVRWAPAQTRPE 467
Cdd:PLN00104  381 SDMTAIKAEDIVSTLQSLNLIQYRK------GQHVICADPKVLEE-HLKAAGR-GGLEVDPSKLIWTPYKEQPP 446
MOZ_SAS pfam01853
MOZ/SAS family; This region of these proteins has been suggested to be homologous to ...
 244-418 5.70e-115

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: 337.48  E-value: 5.70e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 244 PPGNEIYRKDHLSVYEVDGSGQKLYCQCLCLLSKLFMDHKTLYFDVDDFMFYVLCETDEHGAHIVGYFSREVESA--NNL 321
Cdd:pfam01853   1 PPGNEIYRKGNISIFEVDGRKQKLYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTETDETGCHIVGYFSKEKESSdnYNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 322 ACIMVFPPFQKKGYGKLLIQFSYELSRREGYIGMPEKPLSDLGKVSYRSYWWWRLMKLFHIHQGHTVTATFLSNESGIAV 401
Cdd:pfam01853  81 ACILTLPPYQRKGYGKLLIEFSYELSKREGKIGGPEKPLSDLGLLSYRSYWSEVILEYLLKHRKEGISIEDISKATGITP 160

                         170
                  ....*....|....*..
gi 1017353484 402 DDIVSTLITMRMCRQYK 418
Cdd:pfam01853 161 EDIISTLQSLNMLKYYK 177
SAS2 COG5027
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics];
89-418 9.50e-108

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


Pssm-ID: 227360 [Multi-domain]  Cd Length: 395  Bit Score: 327.11  E-value: 9.50e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484  89 YYVHYEELDRRNDEWITLDKIlvnevVVEPVIKVPT-KAPVEDLHKEivvGPPVIKPSGALTRSQRRTLEEYSHLKTDLN 167
Cdd:COG5027    37 FYVHYVELNRRLDEWITADLI-----NLGAAISIPKrKKQTEKGKKE---KKPKVSDRMDLDNENVQLEMLYSISNEREI 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 168 DLDATTARLEREHEERTKVKNIPQITIGAHEILAWYYSPFPPDCENLDI-YMCEYCLLYTPHHERFKQHIDTCKVRQPPG 246
Cdd:COG5027   109 RQLRFGGSKVQNPHEGARVKNINEIKLGNYEIEPWYFSPYPEEFSDLDIvYICEFCLKYYGSQTSLVRHRKKCSLQHPPG 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 247 NEIYRKDHLSVYEVDGSGQKLYCQCLCLLSKLFMDHKTLYFDVDDFMFYVLCETDEHGAHIVGYFSREVESA--NNLACI 324
Cdd:COG5027   189 NEIYRDKYISFFEIDGRKQRLYCRNLCLLSKLFLDHKTLYYDVDPFLFYVLTERGDTGCHLVGYFSKEKESEqdYNLACI 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 325 MVFPPFQKKGYGKLLIQFSYELSRREGYIGMPEKPLSDLGKVSYRSYWWWRLMKLFHIHQGHTVTATFLSNESGIAVDDI 404
Cdd:COG5027   269 LTLPPYQRRGYGKLLIDFSYLLSQKEGKVGSPEKPLSDLGLLSYRAYWSEIVAKLLLKMDKEITDINEISKETGMSTDDV 348

                         330
                  ....*....|....
gi 1017353484 405 VSTLITMRMCRQYK 418
Cdd:COG5027   349 IHTLEALNILREYK 362
CBD cd18643
chromo barrel domain of MOF acetyltransferase, and similar proteins; This group includes the ...
 63-110 4.50e-05

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: 41.39  E-value: 4.50e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1017353484  63 RKPPQEVRTNNYKSIENHEQGAKELMYYVHYEELDRRNDEWITLDKIL 110
Cdd:cd18643     9 DPKARVLYDAKILSVITGKDGRAPPEYLVHYVGWNRRLDEWVAEDRVL 56
CHROMO smart00298
Chromatin organization modifier domain;
77-117 9.63e-04

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 37.19  E-value: 9.63e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1017353484   77 IENHE-QGAKELMYYVHYEELDRRNDEWITLDKILVNEVVVE 117
Cdd:smart00298   7 ILDHRwKKKGELEYLVKWKGYSYSEDTWEPEENLLNCSKKLD 48
 
Name Accession Description Interval E-value
PLN00104 PLN00104
MYST -like histone acetyltransferase; Provisional
 83-467 4.05e-131

MYST -like histone acetyltransferase; Provisional


Pssm-ID: 215056 [Multi-domain]  Cd Length: 450  Bit Score: 389.11  E-value: 4.05e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484  83 GAKELMYYVHYEELDRRNDEWITLDKilVNEVVVEPVIKVPTKAPVEDLhkeivvgppvikpsgALTRSQRRTLEEYSHL 162
Cdd:PLN00104   85 GPNDYEYYVHYTEFNRRLDEWVKLEQ--LDLDTVETVGDEKVEDKVASL---------------KMTRHQKRKIDETHVE 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 163 KTDLNDLDAttarLEREHEERTKVKNIPQITIGAHEILAWYYSPFPP---DCENLdiYMCEYCLLYTPHHERFKQHIDTC 239
Cdd:PLN00104  148 EGHEELDAA----SLREHEEFTKVKNIATIELGRYEIDTWYFSPFPPeynDCSKL--YFCEFCLKFMKRKEQLQRHMKKC 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 240 KVRQPPGNEIYRK----DHLSVYEVDGSGQKLYCQCLCLLSKLFMDHKTLYFDVDDFMFYVLCETDEHGAHIVGYFSRE- 314
Cdd:PLN00104  222 DLKHPPGDEIYRHptrqEGLSMFEVDGKKNKVYCQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEk 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 315 -VESANNLACIMVFPPFQKKGYGKLLIQFSYELSRREGYIGMPEKPLSDLGKVSYRSYWWWRLMKLFHIHQGhTVTATFL 393
Cdd:PLN00104  302 hSEEDYNLACILTLPPYQRKGYGKFLIAFSYELSKREGKVGTPERPLSDLGLVSYRGYWTRVLLEILKKHKG-NISIKEL 380

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1017353484 394 SNESGIAVDDIVSTLITMRMCRQYKepefipGEWYVRIHRKIVDHcVMCGYGKpPRLLLDRTKVRWAPAQTRPE 467
Cdd:PLN00104  381 SDMTAIKAEDIVSTLQSLNLIQYRK------GQHVICADPKVLEE-HLKAAGR-GGLEVDPSKLIWTPYKEQPP 446
MOZ_SAS pfam01853
MOZ/SAS family; This region of these proteins has been suggested to be homologous to ...
 244-418 5.70e-115

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: 337.48  E-value: 5.70e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 244 PPGNEIYRKDHLSVYEVDGSGQKLYCQCLCLLSKLFMDHKTLYFDVDDFMFYVLCETDEHGAHIVGYFSREVESA--NNL 321
Cdd:pfam01853   1 PPGNEIYRKGNISIFEVDGRKQKLYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTETDETGCHIVGYFSKEKESSdnYNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 322 ACIMVFPPFQKKGYGKLLIQFSYELSRREGYIGMPEKPLSDLGKVSYRSYWWWRLMKLFHIHQGHTVTATFLSNESGIAV 401
Cdd:pfam01853  81 ACILTLPPYQRKGYGKLLIEFSYELSKREGKIGGPEKPLSDLGLLSYRSYWSEVILEYLLKHRKEGISIEDISKATGITP 160

                         170
                  ....*....|....*..
gi 1017353484 402 DDIVSTLITMRMCRQYK 418
Cdd:pfam01853 161 EDIISTLQSLNMLKYYK 177
SAS2 COG5027
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics];
89-418 9.50e-108

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


Pssm-ID: 227360 [Multi-domain]  Cd Length: 395  Bit Score: 327.11  E-value: 9.50e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484  89 YYVHYEELDRRNDEWITLDKIlvnevVVEPVIKVPT-KAPVEDLHKEivvGPPVIKPSGALTRSQRRTLEEYSHLKTDLN 167
Cdd:COG5027    37 FYVHYVELNRRLDEWITADLI-----NLGAAISIPKrKKQTEKGKKE---KKPKVSDRMDLDNENVQLEMLYSISNEREI 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 168 DLDATTARLEREHEERTKVKNIPQITIGAHEILAWYYSPFPPDCENLDI-YMCEYCLLYTPHHERFKQHIDTCKVRQPPG 246
Cdd:COG5027   109 RQLRFGGSKVQNPHEGARVKNINEIKLGNYEIEPWYFSPYPEEFSDLDIvYICEFCLKYYGSQTSLVRHRKKCSLQHPPG 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 247 NEIYRKDHLSVYEVDGSGQKLYCQCLCLLSKLFMDHKTLYFDVDDFMFYVLCETDEHGAHIVGYFSREVESA--NNLACI 324
Cdd:COG5027   189 NEIYRDKYISFFEIDGRKQRLYCRNLCLLSKLFLDHKTLYYDVDPFLFYVLTERGDTGCHLVGYFSKEKESEqdYNLACI 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 325 MVFPPFQKKGYGKLLIQFSYELSRREGYIGMPEKPLSDLGKVSYRSYWWWRLMKLFHIHQGHTVTATFLSNESGIAVDDI 404
Cdd:COG5027   269 LTLPPYQRRGYGKLLIDFSYLLSQKEGKVGSPEKPLSDLGLLSYRAYWSEIVAKLLLKMDKEITDINEISKETGMSTDDV 348

                         330
                  ....*....|....
gi 1017353484 405 VSTLITMRMCRQYK 418
Cdd:COG5027   349 IHTLEALNILREYK 362
PLN03238 PLN03238
probable histone acetyltransferase MYST; Provisional
 170-418 6.84e-107

probable histone acetyltransferase MYST; Provisional


Pssm-ID: 215642 [Multi-domain]  Cd Length: 290  Bit Score: 321.42  E-value: 6.84e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 170 DATTARLEREHEERTKVKNIPQITIGAHEILAWYYSPFPPDCENLD-IYMCEYCLLYTPHHERFKQHIDTCKVRQPPGNE 248
Cdd:PLN03238    1 DPVLAELEREHEETTKVKNIEMIELGKYEMDTWYYSPYPEPYASCTkLYICEYCLKYMRKKKSLLRHLAKCDIRQPPGGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 249 IYR---KDHLSVYEVDGSGQKLYCQCLCLLSKLFMDHKTLYFDVDDFMFYVLCETDEHGAHIVGYFSREVESAN--NLAC 323
Cdd:PLN03238   81 IYGavtEGPLSVFEVDGKKAKVYCQNLCLLAKLFLDHKTLYYDVDPFLFYVMTEVDDHGSHIVGYFSKEKVSAEdyNLAC 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 324 IMVFPPFQKKGYGKLLIQFSYELSRREGYIGMPEKPLSDLGKVSYRSYWWWRLMKLFHIHQgHTVTATFLSNESGIAVDD 403
Cdd:PLN03238  161 ILTLPPYQRKGYGKFLISFAYELSKREGKVGTPERPLSDLGKVSFRSYWTRVLLEQLRDVK-GDVSIKDLSLATGIRGED 239

                         250
                  ....*....|....*
gi 1017353484 404 IVSTLITMRMCRQYK 418
Cdd:PLN03238  240 IVSTLQSLNLIKYWK 254
PLN03239 PLN03239
histone acetyltransferase; Provisional
 89-461 9.97e-93

histone acetyltransferase; Provisional


Pssm-ID: 178777 [Multi-domain]  Cd Length: 351  Bit Score: 287.32  E-value: 9.97e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484  89 YYVHYEELDRRNDEWITLDKIlVNEVVVEPVIKVPTKAPVEDLhkeivvgppvikpsgaLTRSQRRTLEEYSHLKtdlnd 168
Cdd:PLN03239    1 YYVHYKDFNRRMDEWISKDKS-NEEILALPSDHLATHTVGEDV----------------VATIAAPELDEHEGLD----- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 169 lDATTarleREHEERTKVKNIPQITIGAHEILAWYYSPFPPDCEN----LDI-YMCEYCL-LYTPHHE--RFKQHIDTCK 240
Cdd:PLN03239   59 -DAAL----KEHEEVTKVKNVAFLELGPYQMDTWYFSPLPKELFKaggfIDVlYVCEFSFgFFARKSEllRFQAKELPKE 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 241 VRQPPGNEIYRKDHLSVYEVDGSGQKLYCQCLCLLSKLFMDHKTLYFDVDDFMFYVLCETDEHGAHIVGYFSREVES--A 318
Cdd:PLN03239  134 RRHPPGNEIYRCGDLAMFEVDGFEERIYCQNLCYIAKLFLDHKTLYFDVDPFLFYVLCEVDERGFHPVGYYSKEKYSdvG 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 319 NNLACIMVFPPFQKKGYGKLLIQFSYELSRREGYIGMPEKPLSDLGKVSYRSYWWWRLMKLFHIHQGHTVTATFL--SNE 396
Cdd:PLN03239  214 YNLACILTFPAHQRKGYGRFLIAFSYELSKKEEKVGSPEKPMSDLGQQAYIPYWGSTIVDFLLNHSGNDSSLSIMdiAKK 293

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1017353484 397 SGIAVDDIVSTLITMRMCRqykepeFIPGEWYVRIHRKIVDHCVMCGYGKPPRllLDRTKVRWAP 461
Cdd:PLN03239  294 TSIMAEDIVFALNQLGILK------FINGIYFIAAEKGLLEELAEKHPVKEPR--VDPSKLHWTP 350
PTZ00064 PTZ00064
histone acetyltransferase; Provisional
 57-466 1.55e-83

histone acetyltransferase; Provisional


Pssm-ID: 173359 [Multi-domain]  Cd Length: 552  Bit Score: 269.58  E-value: 1.55e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484  57 IIHIDFRKPPQEVRTNNYK--SIENHEQGAKELMYYVHYEELDRRNDEWITLDKILVN---EVVVEPVIKVPTKAPVEDL 131
Cdd:PTZ00064  117 LSHLVNKKTSGNKQNSLIKvsSSSNESQIKEDYEFYVHFRGLNRRLDRWVKGKDIKLSfdvEELNDPNLIERFQKQGIKF 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 132 HKEIVVGPPVIKpsgALTRSQRRTLEEYShlKTDLNDLDattarlERE---------HEERTKVKNIPQITIGAHEILAW 202
Cdd:PTZ00064  197 ISSLSVSNSANK---SGNKSKKRNVGVLD--ISDGEDPD------EHEgmdhsaildHEETTRLRTIGRVRIGKFILDTW 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 203 YYSPFPPDCENLDI-YMCEYCLLYTPHHERFKQHIDTCKVRQPPGNEIYRKDHLSVYEVDGSGQKLYCQCLCLLSKLFMD 281
Cdd:PTZ00064  266 YFSPLPDEYQNVDTlHFCEYCLDFFCFEDELIRHLSRCQLRHPPGNEIYRKDNISVFEIDGALTRGYAENLCYLAKLFLD 345

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 282 HKTLYFDVDDFMFYVLCETDEHGAHIVGYFSREVESA--NNLACIMVFPPFQKKGYGKLLIQFSYELSRREGYIGMPEKP 359
Cdd:PTZ00064  346 HKTLQYDVEPFLFYIVTEVDEEGCHIVGYFSKEKVSLlhYNLACILTLPCYQRKGYGKLLVDLSYKLSLKEGKWGHPERP 425

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017353484 360 LSDLGKVSYRSYWWWR----LMKLFHIHQ--------------GHTVTATFLSNESGIAVDDIVSTLITMRMCRQYKEPE 421
Cdd:PTZ00064  426 LSDLGRAIYNNWWAHRiseyLLEYFKQNKicerggskqplqvsNYWKFIDNVVRSTGIRREDVIRILEENGIMRNIKDQH 505

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1017353484 422 FIPGEWyvRIHRKIVDHCvmcgyGKPPRLLLDRTkVRWAPAQTRP 466
Cdd:PTZ00064  506 YIFCNQ--EFLKGIVKRS-----GRPGITLIDKY-FNWVPFSRAP 542
zf-MYST pfam17772
MYST family zinc finger domain; This zinc finger domain is found in the MYST family of histone ...
 186-239 1.57e-19

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: 81.90  E-value: 1.57e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1017353484 186 VKNIPQITIGAHEILAWYYSPFPPDCENLD-IYMCEYCLLYTPHHERFKQHIDTC 239
Cdd:pfam17772   1 VKNIEKIQFGRYEIDTWYFSPYPEEYTNVDkLYVCEFCLKYMKSRKSYKRHRKKC 55
Tudor-knot pfam11717
RNA binding activity-knot of a chromodomain; This is a novel knotted tudor domain which is ...
 89-110 1.31e-05

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: 42.58  E-value: 1.31e-05
                          10        20
                  ....*....|....*....|..
gi 1017353484  89 YYVHYEELDRRNDEWITLDKIL 110
Cdd:pfam11717  33 YYVHYVGFNKRLDEWVPEDRID 54
CBD cd18643
chromo barrel domain of MOF acetyltransferase, and similar proteins; This group includes the ...
 63-110 4.50e-05

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: 41.39  E-value: 4.50e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1017353484  63 RKPPQEVRTNNYKSIENHEQGAKELMYYVHYEELDRRNDEWITLDKIL 110
Cdd:cd18643     9 DPKARVLYDAKILSVITGKDGRAPPEYLVHYVGWNRRLDEWVAEDRVL 56
CBD_ESA1_like cd18986
chromo barrel domain of yeast NuA4 histone acetyltransferase complex catalytic subunit ESA1, ...
 89-123 5.67e-05

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: 41.05  E-value: 5.67e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1017353484  89 YYVHYEELDRRNDEWITLDKILVNEVVVEPVIKVP 123
Cdd:cd18986    30 FYVHYEDFNKRLDEWITADRINLSKEVLYPKPKAT 64
CBD_MOF_like cd18642
chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar ...
 89-109 6.76e-05

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: 40.88  E-value: 6.76e-05
                          10        20
                  ....*....|....*....|.
gi 1017353484  89 YYVHYEELDRRNDEWITLDKI 109
Cdd:cd18642    31 FYVHYVELNRRLDEWITTDRI 51
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 294-352 3.29e-04

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 38.80  E-value: 3.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1017353484 294 FYVLCETDEHGAHIVGYFSREVESANNLACIMVFPPFQKKGYGKLLIQFSYELSRREGY 352
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGA 59
CBD_MOF_like cd18984
chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar ...
 75-127 7.34e-04

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: 38.31  E-value: 7.34e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1017353484  75 KSIENHEQGAKElmYYVHYEELDRRNDEWITLDKILVNEVVVEPVIKVPTKAP 127
Cdd:cd18984    20 QSRTTKQAGREE--YYVHYVGLNRRLDEWVDKSRLSLNDLGKIVKTPAPPNAE 70
CHROMO smart00298
Chromatin organization modifier domain;
77-117 9.63e-04

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 37.19  E-value: 9.63e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1017353484   77 IENHE-QGAKELMYYVHYEELDRRNDEWITLDKILVNEVVVE 117
Cdd:smart00298   7 ILDHRwKKKGELEYLVKWKGYSYSEDTWEPEENLLNCSKKLD 48
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 276-352 9.89e-03

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 36.34  E-value: 9.89e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1017353484 276 SKLFMDHKTLYFDVDDFMFYVLCETDEHGAHIVGYFSREVESANNLACIMVFPPFQKKGYGKLLIQFSYELSRREGY 352
Cdd:pfam00583  17 PDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGC 93
 
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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