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Conserved domains on  [gi|15242493|ref|NP_196536|]
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histone acetyltransferase of the MYST family 2 [Arabidopsis thaliana]

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

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List of domain hits

 Name Accession Description Interval E-value
PLN00104 PLN00104
MYST -like histone acetyltransferase; Provisional
 1-445 0e+00

MYST -like histone acetyltransferase; Provisional


:

Pssm-ID: 215056 [Multi-domain]  Cd Length: 450  Bit Score: 869.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493    1 MGSSANTETNGNAPPPSSNQKPPATNGVDGSHPppppltPDQAIIESDPSKKRKMGMLPLEVGTRVMCRWR-DGKHHPVK 79
Cdd:PLN00104   1 SMEAPATEDAGRPAAPAASDDAAATDGAGANAA------APAAPAESDPSKKRPGVMLPLEVGTRVMCRWRfDGKYHPVK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493   80 VIERRRIHNGGQNDYEYYVHYTEFNRRLDEWTQLDQLDLDSVECAVDEKVEDKVTSLKMTRHQKRKIDETHIE-GHEELD 158
Cdd:PLN00104  75 VIERRRGGSGGPNDYEYYVHYTEFNRRLDEWVKLEQLDLDTVETVGDEKVEDKVASLKMTRHQKRKIDETHVEeGHEELD 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493  159 AASLREHEEFTKVKNISTIELGKYEIETWYFSPFPPEYNDCVKLFFCEFCLNFMKRKEQLQRHMRKCDLKHPPGDEIYRS 238
Cdd:PLN00104 155 AASLREHEEFTKVKNIATIELGRYEIDTWYFSPFPPEYNDCSKLYFCEFCLKFMKRKEQLQRHMKKCDLKHPPGDEIYRH 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493  239 GT----LSMFEVDGKKNKVYAQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEKHSEEAYNLACILT 314
Cdd:PLN00104 235 PTrqegLSMFEVDGKKNKVYCQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEKHSEEDYNLACILT 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493  315 LPSYQRKGYGKFLIAFSYELSKKEGKVGTPERPLSDLGLLSYRGYWTRVLLEILKKHKGNISIKELSDVTAIKAEDILST 394
Cdd:PLN00104 315 LPPYQRKGYGKFLIAFSYELSKREGKVGTPERPLSDLGLVSYRGYWTRVLLEILKKHKGNISIKELSDMTAIKAEDIVST 394

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15242493  395 LQSLELIQYRKGQHVICADPKVLDRHLKAAGRGGLDVDASKLIWTPYKDQS 445
Cdd:PLN00104 395 LQSLNLIQYRKGQHVICADPKVLEEHLKAAGRGGLEVDPSKLIWTPYKEQP 445
 
Name Accession Description Interval E-value
PLN00104 PLN00104
MYST -like histone acetyltransferase; Provisional
 1-445 0e+00

MYST -like histone acetyltransferase; Provisional


Pssm-ID: 215056 [Multi-domain]  Cd Length: 450  Bit Score: 869.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493    1 MGSSANTETNGNAPPPSSNQKPPATNGVDGSHPppppltPDQAIIESDPSKKRKMGMLPLEVGTRVMCRWR-DGKHHPVK 79
Cdd:PLN00104   1 SMEAPATEDAGRPAAPAASDDAAATDGAGANAA------APAAPAESDPSKKRPGVMLPLEVGTRVMCRWRfDGKYHPVK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493   80 VIERRRIHNGGQNDYEYYVHYTEFNRRLDEWTQLDQLDLDSVECAVDEKVEDKVTSLKMTRHQKRKIDETHIE-GHEELD 158
Cdd:PLN00104  75 VIERRRGGSGGPNDYEYYVHYTEFNRRLDEWVKLEQLDLDTVETVGDEKVEDKVASLKMTRHQKRKIDETHVEeGHEELD 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493  159 AASLREHEEFTKVKNISTIELGKYEIETWYFSPFPPEYNDCVKLFFCEFCLNFMKRKEQLQRHMRKCDLKHPPGDEIYRS 238
Cdd:PLN00104 155 AASLREHEEFTKVKNIATIELGRYEIDTWYFSPFPPEYNDCSKLYFCEFCLKFMKRKEQLQRHMKKCDLKHPPGDEIYRH 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493  239 GT----LSMFEVDGKKNKVYAQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEKHSEEAYNLACILT 314
Cdd:PLN00104 235 PTrqegLSMFEVDGKKNKVYCQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEKHSEEDYNLACILT 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493  315 LPSYQRKGYGKFLIAFSYELSKKEGKVGTPERPLSDLGLLSYRGYWTRVLLEILKKHKGNISIKELSDVTAIKAEDILST 394
Cdd:PLN00104 315 LPPYQRKGYGKFLIAFSYELSKREGKVGTPERPLSDLGLVSYRGYWTRVLLEILKKHKGNISIKELSDMTAIKAEDIVST 394

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15242493  395 LQSLELIQYRKGQHVICADPKVLDRHLKAAGRGGLDVDASKLIWTPYKDQS 445
Cdd:PLN00104 395 LQSLNLIQYRKGQHVICADPKVLEEHLKAAGRGGLEVDPSKLIWTPYKEQP 445
SAS2 COG5027
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics];
88-438 6.01e-131

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


Pssm-ID: 227360 [Multi-domain]  Cd Length: 395  Bit Score: 383.35  E-value: 6.01e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493  88 NGGQNDYEYYVHYTEFNRRLDEWTQLDQLDLDS-VECAVDEKVEDKVTSLKMTRHQKR---KIDETHIEGHEELDAASLR 163
Cdd:COG5027  29 NTRKSRIKFYVHYVELNRRLDEWITADLINLGAaISIPKRKKQTEKGKKEKKPKVSDRmdlDNENVQLEMLYSISNEREI 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493 164 EHEEF-----------TKVKNISTIELGKYEIETWYFSPFPPEYNDCVKLFFCEFCLNFMKRKEQLQRHMRKCDLKHPPG 232
Cdd:COG5027 109 RQLRFggskvqnphegARVKNINEIKLGNYEIEPWYFSPYPEEFSDLDIVYICEFCLKYYGSQTSLVRHRKKCSLQHPPG 188

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493 233 DEIYRSGTLSMFEVDGKKNKVYAQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEKHSEEAYNLACI 312
Cdd:COG5027 189 NEIYRDKYISFFEIDGRKQRLYCRNLCLLSKLFLDHKTLYYDVDPFLFYVLTERGDTGCHLVGYFSKEKESEQDYNLACI 268

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493 313 LTLPSYQRKGYGKFLIAFSYELSKKEGKVGTPERPLSDLGLLSYRGYWTRVLLEILKKHKGNI-SIKELSDVTAIKAEDI 391
Cdd:COG5027 269 LTLPPYQRRGYGKLLIDFSYLLSQKEGKVGSPEKPLSDLGLLSYRAYWSEIVAKLLLKMDKEItDINEISKETGMSTDDV 348

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 15242493 392 LSTLQSLELIQYRKGQHVICADPKVLDRHLKAAGRGGLDVDASKLIW 438
Cdd:COG5027 349 IHTLEALNILREYKGQYIISLNSDKLHNYLRLWSKKRRRINPDLLLW 395
MOZ_SAS pfam01853
MOZ/SAS family; This region of these proteins has been suggested to be homologous to ...
 230-407 2.93e-130

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: 373.30  E-value: 2.93e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493   230 PPGDEIYRSGTLSMFEVDGKKNKVYAQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEKHSEEAYNL 309
Cdd:pfam01853   1 PPGNEIYRKGNISIFEVDGRKQKLYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTETDETGCHIVGYFSKEKESSDNYNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493   310 ACILTLPSYQRKGYGKFLIAFSYELSKKEGKVGTPERPLSDLGLLSYRGYWTRVLLEILKKH-KGNISIKELSDVTAIKA 388
Cdd:pfam01853  81 ACILTLPPYQRKGYGKLLIEFSYELSKREGKIGGPEKPLSDLGLLSYRSYWSEVILEYLLKHrKEGISIEDISKATGITP 160

                         170
                  ....*....|....*....
gi 15242493   389 EDILSTLQSLELIQYRKGQ 407
Cdd:pfam01853 161 EDIISTLQSLNMLKYYKGQ 179
CBD_MOF_like cd18642
chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar ...
 63-132 4.12e-25

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: 97.50  E-value: 4.12e-25
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493  63 GTRVMCRWRDGKHHPVKVIERRRIHNGgqnDYEYYVHYTEFNRRLDEWTQLDQLDLDSVECAVDEKVEDK 132
Cdd:cd18642   1 IKCRCWVQRNDEEHLAEVLSRRTRKHA---PPEFYVHYVELNRRLDEWITTDRIDLDLKECELPKKKATK 67
CHROMO smart00298
Chromatin organization modifier domain;
74-122 6.84e-04

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 37.58  E-value: 6.84e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 15242493     74 KHHPVKVIERRRIHNGGqndYEYYVHYTEFNRRLDEWTQLDQLDLDSVE 122
Cdd:smart00298   1 EYEVEKILDHRWKKKGE---LEYLVKWKGYSYSEDTWEPEENLLNCSKK 46
 
Name Accession Description Interval E-value
PLN00104 PLN00104
MYST -like histone acetyltransferase; Provisional
 1-445 0e+00

MYST -like histone acetyltransferase; Provisional


Pssm-ID: 215056 [Multi-domain]  Cd Length: 450  Bit Score: 869.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493    1 MGSSANTETNGNAPPPSSNQKPPATNGVDGSHPppppltPDQAIIESDPSKKRKMGMLPLEVGTRVMCRWR-DGKHHPVK 79
Cdd:PLN00104   1 SMEAPATEDAGRPAAPAASDDAAATDGAGANAA------APAAPAESDPSKKRPGVMLPLEVGTRVMCRWRfDGKYHPVK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493   80 VIERRRIHNGGQNDYEYYVHYTEFNRRLDEWTQLDQLDLDSVECAVDEKVEDKVTSLKMTRHQKRKIDETHIE-GHEELD 158
Cdd:PLN00104  75 VIERRRGGSGGPNDYEYYVHYTEFNRRLDEWVKLEQLDLDTVETVGDEKVEDKVASLKMTRHQKRKIDETHVEeGHEELD 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493  159 AASLREHEEFTKVKNISTIELGKYEIETWYFSPFPPEYNDCVKLFFCEFCLNFMKRKEQLQRHMRKCDLKHPPGDEIYRS 238
Cdd:PLN00104 155 AASLREHEEFTKVKNIATIELGRYEIDTWYFSPFPPEYNDCSKLYFCEFCLKFMKRKEQLQRHMKKCDLKHPPGDEIYRH 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493  239 GT----LSMFEVDGKKNKVYAQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEKHSEEAYNLACILT 314
Cdd:PLN00104 235 PTrqegLSMFEVDGKKNKVYCQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEKHSEEDYNLACILT 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493  315 LPSYQRKGYGKFLIAFSYELSKKEGKVGTPERPLSDLGLLSYRGYWTRVLLEILKKHKGNISIKELSDVTAIKAEDILST 394
Cdd:PLN00104 315 LPPYQRKGYGKFLIAFSYELSKREGKVGTPERPLSDLGLVSYRGYWTRVLLEILKKHKGNISIKELSDMTAIKAEDIVST 394

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15242493  395 LQSLELIQYRKGQHVICADPKVLDRHLKAAGRGGLDVDASKLIWTPYKDQS 445
Cdd:PLN00104 395 LQSLNLIQYRKGQHVICADPKVLEEHLKAAGRGGLEVDPSKLIWTPYKEQP 445
PLN03238 PLN03238
probable histone acetyltransferase MYST; Provisional
 157-422 2.55e-152

probable histone acetyltransferase MYST; Provisional


Pssm-ID: 215642 [Multi-domain]  Cd Length: 290  Bit Score: 433.90  E-value: 2.55e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493  157 LDAASLREHEEFTKVKNISTIELGKYEIETWYFSPFPPEYNDCVKLFFCEFCLNFMKRKEQLQRHMRKCDLKHPPGDEIY 236
Cdd:PLN03238   3 VLAELEREHEETTKVKNIEMIELGKYEMDTWYYSPYPEPYASCTKLYICEYCLKYMRKKKSLLRHLAKCDIRQPPGGGIY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493  237 RS---GTLSMFEVDGKKNKVYAQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEKHSEEAYNLACIL 313
Cdd:PLN03238  83 GAvteGPLSVFEVDGKKAKVYCQNLCLLAKLFLDHKTLYYDVDPFLFYVMTEVDDHGSHIVGYFSKEKVSAEDYNLACIL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493  314 TLPSYQRKGYGKFLIAFSYELSKKEGKVGTPERPLSDLGLLSYRGYWTRVLLEILKKHKGNISIKELSDVTAIKAEDILS 393
Cdd:PLN03238 163 TLPPYQRKGYGKFLISFAYELSKREGKVGTPERPLSDLGKVSFRSYWTRVLLEQLRDVKGDVSIKDLSLATGIRGEDIVS 242

                        250       260
                 ....*....|....*....|....*....
gi 15242493  394 TLQSLELIQYRKGQHVICADPKVLDRHLK 422
Cdd:PLN03238 243 TLQSLNLIKYWKGQHVIHVDQRVLDEHWA 271
PLN03239 PLN03239
histone acetyltransferase; Provisional
 96-441 5.96e-144

histone acetyltransferase; Provisional


Pssm-ID: 178777 [Multi-domain]  Cd Length: 351  Bit Score: 414.82  E-value: 5.96e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493   96 YYVHYTEFNRRLDEWTQLDQ-----LDLDSVECAVDEKVEDKVTSLKmtrhqKRKIDEthiegHEELDAASLREHEEFTK 170
Cdd:PLN03239   1 YYVHYKDFNRRMDEWISKDKsneeiLALPSDHLATHTVGEDVVATIA-----APELDE-----HEGLDDAALKEHEEVTK 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493  171 VKNISTIELGKYEIETWYFSPFPPE-YND---CVKLFFCEFCLNFMKRKEQLQRHMRKC---DLKHPPGDEIYRSGTLSM 243
Cdd:PLN03239  71 VKNVAFLELGPYQMDTWYFSPLPKElFKAggfIDVLYVCEFSFGFFARKSELLRFQAKElpkERRHPPGNEIYRCGDLAM 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493  244 FEVDGKKNKVYAQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEKHSEEAYNLACILTLPSYQRKGY 323
Cdd:PLN03239 151 FEVDGFEERIYCQNLCYIAKLFLDHKTLYFDVDPFLFYVLCEVDERGFHPVGYYSKEKYSDVGYNLACILTFPAHQRKGY 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493  324 GKFLIAFSYELSKKEGKVGTPERPLSDLGLLSYRGYWTRVLLEILKKHKGN---ISIKELSDVTAIKAEDILSTLQSLEL 400
Cdd:PLN03239 231 GRFLIAFSYELSKKEEKVGSPEKPMSDLGQQAYIPYWGSTIVDFLLNHSGNdssLSIMDIAKKTSIMAEDIVFALNQLGI 310

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 15242493  401 IQYRKGQHVICADPKVLDRHLKAAGRGGLDVDASKLIWTPY 441
Cdd:PLN03239 311 LKFINGIYFIAAEKGLLEELAEKHPVKEPRVDPSKLHWTPF 351
SAS2 COG5027
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics];
88-438 6.01e-131

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


Pssm-ID: 227360 [Multi-domain]  Cd Length: 395  Bit Score: 383.35  E-value: 6.01e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493  88 NGGQNDYEYYVHYTEFNRRLDEWTQLDQLDLDS-VECAVDEKVEDKVTSLKMTRHQKR---KIDETHIEGHEELDAASLR 163
Cdd:COG5027  29 NTRKSRIKFYVHYVELNRRLDEWITADLINLGAaISIPKRKKQTEKGKKEKKPKVSDRmdlDNENVQLEMLYSISNEREI 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493 164 EHEEF-----------TKVKNISTIELGKYEIETWYFSPFPPEYNDCVKLFFCEFCLNFMKRKEQLQRHMRKCDLKHPPG 232
Cdd:COG5027 109 RQLRFggskvqnphegARVKNINEIKLGNYEIEPWYFSPYPEEFSDLDIVYICEFCLKYYGSQTSLVRHRKKCSLQHPPG 188

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493 233 DEIYRSGTLSMFEVDGKKNKVYAQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEKHSEEAYNLACI 312
Cdd:COG5027 189 NEIYRDKYISFFEIDGRKQRLYCRNLCLLSKLFLDHKTLYYDVDPFLFYVLTERGDTGCHLVGYFSKEKESEQDYNLACI 268

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493 313 LTLPSYQRKGYGKFLIAFSYELSKKEGKVGTPERPLSDLGLLSYRGYWTRVLLEILKKHKGNI-SIKELSDVTAIKAEDI 391
Cdd:COG5027 269 LTLPPYQRRGYGKLLIDFSYLLSQKEGKVGSPEKPLSDLGLLSYRAYWSEIVAKLLLKMDKEItDINEISKETGMSTDDV 348

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 15242493 392 LSTLQSLELIQYRKGQHVICADPKVLDRHLKAAGRGGLDVDASKLIW 438
Cdd:COG5027 349 IHTLEALNILREYKGQYIISLNSDKLHNYLRLWSKKRRRINPDLLLW 395
MOZ_SAS pfam01853
MOZ/SAS family; This region of these proteins has been suggested to be homologous to ...
 230-407 2.93e-130

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: 373.30  E-value: 2.93e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493   230 PPGDEIYRSGTLSMFEVDGKKNKVYAQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEKHSEEAYNL 309
Cdd:pfam01853   1 PPGNEIYRKGNISIFEVDGRKQKLYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTETDETGCHIVGYFSKEKESSDNYNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493   310 ACILTLPSYQRKGYGKFLIAFSYELSKKEGKVGTPERPLSDLGLLSYRGYWTRVLLEILKKH-KGNISIKELSDVTAIKA 388
Cdd:pfam01853  81 ACILTLPPYQRKGYGKLLIEFSYELSKREGKIGGPEKPLSDLGLLSYRSYWSEVILEYLLKHrKEGISIEDISKATGITP 160

                         170
                  ....*....|....*....
gi 15242493   389 EDILSTLQSLELIQYRKGQ 407
Cdd:pfam01853 161 EDIISTLQSLNMLKYYKGQ 179
PTZ00064 PTZ00064
histone acetyltransferase; Provisional
 93-441 7.53e-122

histone acetyltransferase; Provisional


Pssm-ID: 173359 [Multi-domain]  Cd Length: 552  Bit Score: 365.88  E-value: 7.53e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493   93 DYEYYVHYTEFNRRLDEWTQLDQLDLD-SVECAVDEKVEDKVTSLKM----------------TRHQKRKIDETHI---- 151
Cdd:PTZ00064 148 DYEFYVHFRGLNRRLDRWVKGKDIKLSfDVEELNDPNLIERFQKQGIkfisslsvsnsanksgNKSKKRNVGVLDIsdge 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493  152 --EGHEELDAASLREHEEFTKVKNISTIELGKYEIETWYFSPFPPEYNDCVKLFFCEFCLNFMKRKEQLQRHMRKCDLKH 229
Cdd:PTZ00064 228 dpDEHEGMDHSAILDHEETTRLRTIGRVRIGKFILDTWYFSPLPDEYQNVDTLHFCEYCLDFFCFEDELIRHLSRCQLRH 307

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493  230 PPGDEIYRSGTLSMFEVDGKKNKVYAQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEKHSEEAYNL 309
Cdd:PTZ00064 308 PPGNEIYRKDNISVFEIDGALTRGYAENLCYLAKLFLDHKTLQYDVEPFLFYIVTEVDEEGCHIVGYFSKEKVSLLHYNL 387

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493  310 ACILTLPSYQRKGYGKFLIAFSYELSKKEGKVGTPERPLSDLGLLSYRGYW----TRVLLEILKKHK-----GN------ 374
Cdd:PTZ00064 388 ACILTLPCYQRKGYGKLLVDLSYKLSLKEGKWGHPERPLSDLGRAIYNNWWahriSEYLLEYFKQNKicergGSkqplqv 467

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15242493  375 ----ISIKELSDVTAIKAEDILSTLQSLELIQYRKGQHVICADPKVLDRHLKAAGRGGLDVDASKLIWTPY 441
Cdd:PTZ00064 468 snywKFIDNVVRSTGIRREDVIRILEENGIMRNIKDQHYIFCNQEFLKGIVKRSGRPGITLIDKYFNWVPF 538
zf-MYST pfam17772
MYST family zinc finger domain; This zinc finger domain is found in the MYST family of histone ...
 171-225 9.21e-26

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: 98.84  E-value: 9.21e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15242493   171 VKNISTIELGKYEIETWYFSPFPPEYNDCVKLFFCEFCLNFMKRKEQLQRHMRKC 225
Cdd:pfam17772   1 VKNIEKIQFGRYEIDTWYFSPYPEEYTNVDKLYVCEFCLKYMKSRKSYKRHRKKC 55
CBD_MOF_like cd18642
chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar ...
 63-132 4.12e-25

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: 97.50  E-value: 4.12e-25
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242493  63 GTRVMCRWRDGKHHPVKVIERRRIHNGgqnDYEYYVHYTEFNRRLDEWTQLDQLDLDSVECAVDEKVEDK 132
Cdd:cd18642   1 IKCRCWVQRNDEEHLAEVLSRRTRKHA---PPEFYVHYVELNRRLDEWITTDRIDLDLKECELPKKKATK 67
Tudor-knot pfam11717
RNA binding activity-knot of a chromodomain; This is a novel knotted tudor domain which is ...
 60-118 3.49e-21

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: 86.49  E-value: 3.49e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15242493    60 LEVGTRVMCRWRDGKHHPVKVIERRRIHNGgqndYEYYVHYTEFNRRLDEWTQLDQLDL 118
Cdd:pfam11717   1 IEIGCKVLVRKRDGEWRLAEILSIRPKKGK----YEYYVHYVGFNKRLDEWVPEDRIDL 55
CBD_MOF_like cd18984
chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar ...
 63-110 5.56e-08

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: 49.48  E-value: 5.56e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 15242493  63 GTRVMCRWRDGKHHPVKVIERRRIHNGGQNdyEYYVHYTEFNRRLDEW 110
Cdd:cd18984   1 GSTYYCRRSDDTVHRAEVIQSRTTKQAGRE--EYYVHYVGLNRRLDEW 46
CBD_ESA1_like cd18986
chromo barrel domain of yeast NuA4 histone acetyltransferase complex catalytic subunit ESA1, ...
 96-130 2.29e-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: 42.20  E-value: 2.29e-05
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 15242493  96 YYVHYTEFNRRLDEWTQLDQLDLD-SVECAVDEKVE 130
Cdd:cd18986  30 FYVHYEDFNKRLDEWITADRINLSkEVLYPKPKATE 65
MBT_PHF20L1-like cd20104
malignant brain tumor (MBT) repeat found in PHD finger protein 20-like protein 1 (PHF20L1) and ...
 60-110 4.47e-05

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: 41.07  E-value: 4.47e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 15242493  60 LEVGTRVMCRWRDGKHHPVKVIERRRIHNggqndyEYYVHYTEFNRRLDEW 110
Cdd:cd20104   1 FKVGDRVDALDGEGKWYEAKIVEVDEEEN------KVLVHYDGWSSRYDEW 45
CBD_TIP60_like cd18985
chromo barrel domain of human tat-interactive protein 60, and similar proteins; ...
 96-122 7.94e-05

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: 40.65  E-value: 7.94e-05
                        10        20
                ....*....|....*....|....*..
gi 15242493  96 YYVHYTEFNRRLDEWTQLDQLDLDSVE 122
Cdd:cd18985  30 FYVHYIDFNKRLDEWVTHERLDLKKIQ 56
CHROMO smart00298
Chromatin organization modifier domain;
74-122 6.84e-04

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 37.58  E-value: 6.84e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 15242493     74 KHHPVKVIERRRIHNGGqndYEYYVHYTEFNRRLDEWTQLDQLDLDSVE 122
Cdd:smart00298   1 EYEVEKILDHRWKKKGE---LEYLVKWKGYSYSEDTWEPEENLLNCSKK 46
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 281-339 1.48e-03

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: 36.87  E-value: 1.48e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15242493 281 YVLCECDDRgchMVGY--FSKEKHSEEAYNLACILTLPSYQRKGYGKFLIAFSYELSKKEG 339
Cdd:cd04301   1 FLVAEDDGE---IVGFasLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERG 58
CBD cd18643
chromo barrel domain of MOF acetyltransferase, and similar proteins; This group includes the ...
 69-116 1.60e-03

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: 36.77  E-value: 1.60e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 15242493  69 RWRDGKHHPVKVIERRRIHNGGQNDyEYYVHYTEFNRRLDEWTQLDQL 116
Cdd:cd18643   9 DPKARVLYDAKILSVITGKDGRAPP-EYLVHYVGWNRRLDEWVAEDRV 55
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 268-330 6.62e-03

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 36.89  E-value: 6.62e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15242493 268 HKTLYYDVDLFLFYVlCECDDRgchMVGYFSKEKHSEEAYNLACILTLPSYQRKGYGKFLIAF 330
Cdd:COG1246  18 IRPYALEEEIGEFWV-AEEDGE---IVGCAALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEA 76
 
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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