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Conserved domains on  [gi|2361033427|emb|CAI4781526|]
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CAS_1a_G0051280.mRNA.1.CDS.1 [Saccharomyces cerevisiae]

Protein Classification

MOZ/SAS family histone acetyltransferase( domain architecture ID 11472106)

MOZ/SAS family histone acetyltransferase similar to Saccharomyces cerevisiae histone acetyltransferases ESA1, SAS2 and SAS3

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAS2 COG5027
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics];
16-431 0e+00

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


:

Pssm-ID: 227360 [Multi-domain]  Cd Length: 395  Bit Score: 614.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427  16 NSVDDIIIKCQCWVQKNDEERLAEILSINTRKAPPKFYVHYVNYNKRLDEWITTDRINLDKEVLYPKLKATDEDNkkqkk 95
Cdd:COG5027     1 NKIKDIIIKSKVASEKDGEARKAEILEINTRKSRIKFYVHYVELNRRLDEWITADLINLGAAISIPKRKKQTEKG----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427  96 kkATNTSETpqdslqdgvdgfsreNTDVMDLDNLNVQGIKDENISHEDEIKKLRTSGSMTQNPHEVARVRNLNRIIMGKY 175
Cdd:COG5027    76 --KKEKKPK---------------VSDRMDLDNENVQLEMLYSISNEREIRQLRFGGSKVQNPHEGARVKNINEIKLGNY 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 176 EIEPWYFSPYPIELTDEDFIYIDDFTLQYFGSKKQYERYRKKCTLRHPPGNEIYRDDYVSFFEIDGRKQRTWCRNLCLLS 255
Cdd:COG5027   139 EIEPWYFSPYPEEFSDLDIVYICEFCLKYYGSQTSLVRHRKKCSLQHPPGNEIYRDKYISFFEIDGRKQRLYCRNLCLLS 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 256 KLFLDHKTLYYDVDPFLFYCMTRRDELGHHLVGYFSKEKESADGYNVACILTLPQYQRMGYGKLLIEFSYELSKKENKVG 335
Cdd:COG5027   219 KLFLDHKTLYYDVDPFLFYVLTERGDTGCHLVGYFSKEKESEQDYNLACILTLPPYQRRGYGKLLIDFSYLLSQKEGKVG 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 336 SPEKPLSDLGLLSYRAYWSDTLITLLVEHQKEIT-IDEISSMTSMTTTDILHTAKTLNILRYYKGQHIIFLNEDILDRYN 414
Cdd:COG5027   299 SPEKPLSDLGLLSYRAYWSEIVAKLLLKMDKEITdINEISKETGMSTDDVIHTLEALNILREYKGQYIISLNSDKLHNYL 378

                         410
                  ....*....|....*..
gi 2361033427 415 RLKAKKRRTIDPNRLIW 431
Cdd:COG5027   379 RLWSKKRRRINPDLLLW 395
 
Name Accession Description Interval E-value
SAS2 COG5027
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics];
16-431 0e+00

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


Pssm-ID: 227360 [Multi-domain]  Cd Length: 395  Bit Score: 614.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427  16 NSVDDIIIKCQCWVQKNDEERLAEILSINTRKAPPKFYVHYVNYNKRLDEWITTDRINLDKEVLYPKLKATDEDNkkqkk 95
Cdd:COG5027     1 NKIKDIIIKSKVASEKDGEARKAEILEINTRKSRIKFYVHYVELNRRLDEWITADLINLGAAISIPKRKKQTEKG----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427  96 kkATNTSETpqdslqdgvdgfsreNTDVMDLDNLNVQGIKDENISHEDEIKKLRTSGSMTQNPHEVARVRNLNRIIMGKY 175
Cdd:COG5027    76 --KKEKKPK---------------VSDRMDLDNENVQLEMLYSISNEREIRQLRFGGSKVQNPHEGARVKNINEIKLGNY 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 176 EIEPWYFSPYPIELTDEDFIYIDDFTLQYFGSKKQYERYRKKCTLRHPPGNEIYRDDYVSFFEIDGRKQRTWCRNLCLLS 255
Cdd:COG5027   139 EIEPWYFSPYPEEFSDLDIVYICEFCLKYYGSQTSLVRHRKKCSLQHPPGNEIYRDKYISFFEIDGRKQRLYCRNLCLLS 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 256 KLFLDHKTLYYDVDPFLFYCMTRRDELGHHLVGYFSKEKESADGYNVACILTLPQYQRMGYGKLLIEFSYELSKKENKVG 335
Cdd:COG5027   219 KLFLDHKTLYYDVDPFLFYVLTERGDTGCHLVGYFSKEKESEQDYNLACILTLPPYQRRGYGKLLIDFSYLLSQKEGKVG 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 336 SPEKPLSDLGLLSYRAYWSDTLITLLVEHQKEIT-IDEISSMTSMTTTDILHTAKTLNILRYYKGQHIIFLNEDILDRYN 414
Cdd:COG5027   299 SPEKPLSDLGLLSYRAYWSEIVAKLLLKMDKEITdINEISKETGMSTDDVIHTLEALNILREYKGQYIISLNSDKLHNYL 378

                         410
                  ....*....|....*..
gi 2361033427 415 RLKAKKRRTIDPNRLIW 431
Cdd:COG5027   379 RLWSKKRRRINPDLLLW 395
PLN00104 PLN00104
MYST -like histone acetyltransferase; Provisional
 51-443 6.88e-149

MYST -like histone acetyltransferase; Provisional


Pssm-ID: 215056 [Multi-domain]  Cd Length: 450  Bit Score: 431.10  E-value: 6.88e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427  51 KFYVHYVNYNKRLDEWITTDRINLDkevlypklkatdednkkqkkkkatnTSETPQDSLQDGvDGFSRENTDVmdldnln 130
Cdd:PLN00104   90 EYYVHYTEFNRRLDEWVKLEQLDLD-------------------------TVETVGDEKVED-KVASLKMTRH------- 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 131 vQGIKDENISHEDEIKKLRTSgsMTQNPHEVARVRNLNRIIMGKYEIEPWYFSPYPIELTDEDFIYIDDFTLQYFGSKKQ 210
Cdd:PLN00104  137 -QKRKIDETHVEEGHEELDAA--SLREHEEFTKVKNIATIELGRYEIDTWYFSPFPPEYNDCSKLYFCEFCLKFMKRKEQ 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 211 YERYRKKCTLRHPPGNEIYR----DDYVSFFEIDGRKQRTWCRNLCLLSKLFLDHKTLYYDVDPFLFYCMTRRDELGHHL 286
Cdd:PLN00104  214 LQRHMKKCDLKHPPGDEIYRhptrQEGLSMFEVDGKKNKVYCQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHM 293

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 287 VGYFSKEKESADGYNVACILTLPQYQRMGYGKLLIEFSYELSKKENKVGSPEKPLSDLGLLSYRAYWSDTLITLLVEHQK 366
Cdd:PLN00104  294 VGYFSKEKHSEEDYNLACILTLPPYQRKGYGKFLIAFSYELSKREGKVGTPERPLSDLGLVSYRGYWTRVLLEILKKHKG 373

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2361033427 367 EITIDEISSMTSMTTTDILHTAKTLNILRYYKGQHIIFLNEDILDRYNRLKAKKRRTIDPNRLIWKPPVFTASQLRF 443
Cdd:PLN00104  374 NISIKELSDMTAIKAEDIVSTLQSLNLIQYRKGQHVICADPKVLEEHLKAAGRGGLEVDPSKLIWTPYKEQPPRKPF 450
MOZ_SAS pfam01853
MOZ/SAS family; This region of these proteins has been suggested to be homologous to ...
 223-400 9.75e-128

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: 366.75  E-value: 9.75e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 223 PPGNEIYRDDYVSFFEIDGRKQRTWCRNLCLLSKLFLDHKTLYYDVDPFLFYCMTRRDELGHHLVGYFSKEKESADGYNV 302
Cdd:pfam01853   1 PPGNEIYRKGNISIFEVDGRKQKLYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTETDETGCHIVGYFSKEKESSDNYNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 303 ACILTLPQYQRMGYGKLLIEFSYELSKKENKVGSPEKPLSDLGLLSYRAYWSDTLITLLVEHQKE-ITIDEISSMTSMTT 381
Cdd:pfam01853  81 ACILTLPPYQRKGYGKLLIEFSYELSKREGKIGGPEKPLSDLGLLSYRSYWSEVILEYLLKHRKEgISIEDISKATGITP 160

                         170
                  ....*....|....*....
gi 2361033427 382 TDILHTAKTLNILRYYKGQ 400
Cdd:pfam01853 161 EDIISTLQSLNMLKYYKGQ 179
CBD_ESA1_like cd18986
chromo barrel domain of yeast NuA4 histone acetyltransferase complex catalytic subunit ESA1, ...
 23-87 3.97e-38

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: 132.72  E-value: 3.97e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2361033427  23 IKCQCWVQKNDEERLAEILSINTRKAPPKFYVHYVNYNKRLDEWITTDRINLDKEVLYPKLKATD 87
Cdd:cd18986     1 IGCKCWVQKDGEERLAEILSINTRKAPPKFYVHYEDFNKRLDEWITADRINLSKEVLYPKPKATE 65
CHROMO smart00298
Chromatin organization modifier domain;
34-79 9.75e-05

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 39.89  E-value: 9.75e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2361033427   34 EERLAEILSI-NTRKAPPKFYVHYVNYNKRLDEWITTDRINLDKEVL 79
Cdd:smart00298   1 EYEVEKILDHrWKKKGELEYLVKWKGYSYSEDTWEPEENLLNCSKKL 47
 
Name Accession Description Interval E-value
SAS2 COG5027
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics];
16-431 0e+00

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


Pssm-ID: 227360 [Multi-domain]  Cd Length: 395  Bit Score: 614.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427  16 NSVDDIIIKCQCWVQKNDEERLAEILSINTRKAPPKFYVHYVNYNKRLDEWITTDRINLDKEVLYPKLKATDEDNkkqkk 95
Cdd:COG5027     1 NKIKDIIIKSKVASEKDGEARKAEILEINTRKSRIKFYVHYVELNRRLDEWITADLINLGAAISIPKRKKQTEKG----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427  96 kkATNTSETpqdslqdgvdgfsreNTDVMDLDNLNVQGIKDENISHEDEIKKLRTSGSMTQNPHEVARVRNLNRIIMGKY 175
Cdd:COG5027    76 --KKEKKPK---------------VSDRMDLDNENVQLEMLYSISNEREIRQLRFGGSKVQNPHEGARVKNINEIKLGNY 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 176 EIEPWYFSPYPIELTDEDFIYIDDFTLQYFGSKKQYERYRKKCTLRHPPGNEIYRDDYVSFFEIDGRKQRTWCRNLCLLS 255
Cdd:COG5027   139 EIEPWYFSPYPEEFSDLDIVYICEFCLKYYGSQTSLVRHRKKCSLQHPPGNEIYRDKYISFFEIDGRKQRLYCRNLCLLS 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 256 KLFLDHKTLYYDVDPFLFYCMTRRDELGHHLVGYFSKEKESADGYNVACILTLPQYQRMGYGKLLIEFSYELSKKENKVG 335
Cdd:COG5027   219 KLFLDHKTLYYDVDPFLFYVLTERGDTGCHLVGYFSKEKESEQDYNLACILTLPPYQRRGYGKLLIDFSYLLSQKEGKVG 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 336 SPEKPLSDLGLLSYRAYWSDTLITLLVEHQKEIT-IDEISSMTSMTTTDILHTAKTLNILRYYKGQHIIFLNEDILDRYN 414
Cdd:COG5027   299 SPEKPLSDLGLLSYRAYWSEIVAKLLLKMDKEITdINEISKETGMSTDDVIHTLEALNILREYKGQYIISLNSDKLHNYL 378

                         410
                  ....*....|....*..
gi 2361033427 415 RLKAKKRRTIDPNRLIW 431
Cdd:COG5027   379 RLWSKKRRRINPDLLLW 395
PLN00104 PLN00104
MYST -like histone acetyltransferase; Provisional
 51-443 6.88e-149

MYST -like histone acetyltransferase; Provisional


Pssm-ID: 215056 [Multi-domain]  Cd Length: 450  Bit Score: 431.10  E-value: 6.88e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427  51 KFYVHYVNYNKRLDEWITTDRINLDkevlypklkatdednkkqkkkkatnTSETPQDSLQDGvDGFSRENTDVmdldnln 130
Cdd:PLN00104   90 EYYVHYTEFNRRLDEWVKLEQLDLD-------------------------TVETVGDEKVED-KVASLKMTRH------- 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 131 vQGIKDENISHEDEIKKLRTSgsMTQNPHEVARVRNLNRIIMGKYEIEPWYFSPYPIELTDEDFIYIDDFTLQYFGSKKQ 210
Cdd:PLN00104  137 -QKRKIDETHVEEGHEELDAA--SLREHEEFTKVKNIATIELGRYEIDTWYFSPFPPEYNDCSKLYFCEFCLKFMKRKEQ 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 211 YERYRKKCTLRHPPGNEIYR----DDYVSFFEIDGRKQRTWCRNLCLLSKLFLDHKTLYYDVDPFLFYCMTRRDELGHHL 286
Cdd:PLN00104  214 LQRHMKKCDLKHPPGDEIYRhptrQEGLSMFEVDGKKNKVYCQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHM 293

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 287 VGYFSKEKESADGYNVACILTLPQYQRMGYGKLLIEFSYELSKKENKVGSPEKPLSDLGLLSYRAYWSDTLITLLVEHQK 366
Cdd:PLN00104  294 VGYFSKEKHSEEDYNLACILTLPPYQRKGYGKFLIAFSYELSKREGKVGTPERPLSDLGLVSYRGYWTRVLLEILKKHKG 373

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2361033427 367 EITIDEISSMTSMTTTDILHTAKTLNILRYYKGQHIIFLNEDILDRYNRLKAKKRRTIDPNRLIWKPPVFTASQLRF 443
Cdd:PLN00104  374 NISIKELSDMTAIKAEDIVSTLQSLNLIQYRKGQHVICADPKVLEEHLKAAGRGGLEVDPSKLIWTPYKEQPPRKPF 450
MOZ_SAS pfam01853
MOZ/SAS family; This region of these proteins has been suggested to be homologous to ...
 223-400 9.75e-128

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: 366.75  E-value: 9.75e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 223 PPGNEIYRDDYVSFFEIDGRKQRTWCRNLCLLSKLFLDHKTLYYDVDPFLFYCMTRRDELGHHLVGYFSKEKESADGYNV 302
Cdd:pfam01853   1 PPGNEIYRKGNISIFEVDGRKQKLYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTETDETGCHIVGYFSKEKESSDNYNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 303 ACILTLPQYQRMGYGKLLIEFSYELSKKENKVGSPEKPLSDLGLLSYRAYWSDTLITLLVEHQKE-ITIDEISSMTSMTT 381
Cdd:pfam01853  81 ACILTLPPYQRKGYGKLLIEFSYELSKREGKIGGPEKPLSDLGLLSYRSYWSEVILEYLLKHRKEgISIEDISKATGITP 160

                         170
                  ....*....|....*....
gi 2361033427 382 TDILHTAKTLNILRYYKGQ 400
Cdd:pfam01853 161 EDIISTLQSLNMLKYYKGQ 179
PLN03238 PLN03238
probable histone acetyltransferase MYST; Provisional
 159-433 5.02e-122

probable histone acetyltransferase MYST; Provisional


Pssm-ID: 215642 [Multi-domain]  Cd Length: 290  Bit Score: 356.86  E-value: 5.02e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 159 HEVARVRNLNRIIMGKYEIEPWYFSPYPIELTDEDFIYIDDFTLQYFGSKKQYERYRKKCTLRHPPGNEIYR---DDYVS 235
Cdd:PLN03238   12 EETTKVKNIEMIELGKYEMDTWYYSPYPEPYASCTKLYICEYCLKYMRKKKSLLRHLAKCDIRQPPGGGIYGavtEGPLS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 236 FFEIDGRKQRTWCRNLCLLSKLFLDHKTLYYDVDPFLFYCMTRRDELGHHLVGYFSKEKESADGYNVACILTLPQYQRMG 315
Cdd:PLN03238   92 VFEVDGKKAKVYCQNLCLLAKLFLDHKTLYYDVDPFLFYVMTEVDDHGSHIVGYFSKEKVSAEDYNLACILTLPPYQRKG 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 316 YGKLLIEFSYELSKKENKVGSPEKPLSDLGLLSYRAYWSDTLITLLVEHQKEITIDEISSMTSMTTTDILHTAKTLNILR 395
Cdd:PLN03238  172 YGKFLISFAYELSKREGKVGTPERPLSDLGKVSFRSYWTRVLLEQLRDVKGDVSIKDLSLATGIRGEDIVSTLQSLNLIK 251

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2361033427 396 YYKGQHIIFLNEDILDRYNRLKAKKrRTIDPNRLIWKP 433
Cdd:PLN03238  252 YWKGQHVIHVDQRVLDEHWAKFAHQ-RVIEVDCLHWQP 288
PLN03239 PLN03239
histone acetyltransferase; Provisional
 52-433 2.71e-111

histone acetyltransferase; Provisional


Pssm-ID: 178777 [Multi-domain]  Cd Length: 351  Bit Score: 331.62  E-value: 2.71e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427  52 FYVHYVNYNKRLDEWITTDRINldKEVLYPklkATDEDNKKQKKKKATNTSETPQDSLQDGVDGFS-REntdvmdldnln 130
Cdd:PLN03239    1 YYVHYKDFNRRMDEWISKDKSN--EEILAL---PSDHLATHTVGEDVVATIAAPELDEHEGLDDAAlKE----------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 131 vqgikdenisHEdeikklrtsgsmtqnphEVARVRNLNRIIMGKYEIEPWYFSPYPIELTDE----DFIYIDDFTLQYFG 206
Cdd:PLN03239   65 ----------HE-----------------EVTKVKNVAFLELGPYQMDTWYFSPLPKELFKAggfiDVLYVCEFSFGFFA 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 207 SKKQYERYRKKC---TLRHPPGNEIYRDDYVSFFEIDGRKQRTWCRNLCLLSKLFLDHKTLYYDVDPFLFYCMTRRDELG 283
Cdd:PLN03239  118 RKSELLRFQAKElpkERRHPPGNEIYRCGDLAMFEVDGFEERIYCQNLCYIAKLFLDHKTLYFDVDPFLFYVLCEVDERG 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 284 HHLVGYFSKEKESADGYNVACILTLPQYQRMGYGKLLIEFSYELSKKENKVGSPEKPLSDLGLLSYRAYWSDTLITLLVE 363
Cdd:PLN03239  198 FHPVGYYSKEKYSDVGYNLACILTFPAHQRKGYGRFLIAFSYELSKKEEKVGSPEKPMSDLGQQAYIPYWGSTIVDFLLN 277

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2361033427 364 H---QKEITIDEISSMTSMTTTDILHTAKTLNILRYYKGQHIIFLNEDILDRYNRLKAKKRRTIDPNRLIWKP 433
Cdd:PLN03239  278 HsgnDSSLSIMDIAKKTSIMAEDIVFALNQLGILKFINGIYFIAAEKGLLEELAEKHPVKEPRVDPSKLHWTP 350
PTZ00064 PTZ00064
histone acetyltransferase; Provisional
 51-411 2.20e-94

histone acetyltransferase; Provisional


Pssm-ID: 173359 [Multi-domain]  Cd Length: 552  Bit Score: 295.00  E-value: 2.20e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427  51 KFYVHYVNYNKRLDEWITTDRINLDKEVlyPKLKATDEDNKKQKKKKATNTSETPQDSLQDGVDGFSRENTDVMDLDNln 130
Cdd:PTZ00064  150 EFYVHFRGLNRRLDRWVKGKDIKLSFDV--EELNDPNLIERFQKQGIKFISSLSVSNSANKSGNKSKKRNVGVLDISD-- 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 131 vqgikdenisHEDEIKKLRTSGSMTQNPHEVARVRNLNRIIMGKYEIEPWYFSPYPIELTDEDFIYIDDFTLQYFGSKKQ 210
Cdd:PTZ00064  226 ----------GEDPDEHEGMDHSAILDHEETTRLRTIGRVRIGKFILDTWYFSPLPDEYQNVDTLHFCEYCLDFFCFEDE 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 211 YERYRKKCTLRHPPGNEIYRDDYVSFFEIDGRKQRTWCRNLCLLSKLFLDHKTLYYDVDPFLFYCMTRRDELGHHLVGYF 290
Cdd:PTZ00064  296 LIRHLSRCQLRHPPGNEIYRKDNISVFEIDGALTRGYAENLCYLAKLFLDHKTLQYDVEPFLFYIVTEVDEEGCHIVGYF 375

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 291 SKEKESADGYNVACILTLPQYQRMGYGKLLIEFSYELSKKENKVGSPEKPLSDLGLLSYRAYWSDTLITLLVEHQKE--- 367
Cdd:PTZ00064  376 SKEKVSLLHYNLACILTLPCYQRKGYGKLLVDLSYKLSLKEGKWGHPERPLSDLGRAIYNNWWAHRISEYLLEYFKQnki 455

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361033427 368 ----------------ITIDEISSMTSMTTTDILHTAKTLNILRYYKGQHIIFLNEDILD 411
Cdd:PTZ00064  456 cerggskqplqvsnywKFIDNVVRSTGIRREDVIRILEENGIMRNIKDQHYIFCNQEFLK 515
CBD_ESA1_like cd18986
chromo barrel domain of yeast NuA4 histone acetyltransferase complex catalytic subunit ESA1, ...
 23-87 3.97e-38

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: 132.72  E-value: 3.97e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2361033427  23 IKCQCWVQKNDEERLAEILSINTRKAPPKFYVHYVNYNKRLDEWITTDRINLDKEVLYPKLKATD 87
Cdd:cd18986     1 IGCKCWVQKDGEERLAEILSINTRKAPPKFYVHYEDFNKRLDEWITADRINLSKEVLYPKPKATE 65
CBD_MOF_like cd18642
chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar ...
 23-87 4.58e-27

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: 102.89  E-value: 4.58e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2361033427  23 IKCQCWVQKNDEERLAEILSINTRK-APPKFYVHYVNYNKRLDEWITTDRINLD-KEVLYPKLKATD 87
Cdd:cd18642     1 IKCRCWVQRNDEEHLAEVLSRRTRKhAPPEFYVHYVELNRRLDEWITTDRIDLDlKECELPKKKATK 67
zf-MYST pfam17772
MYST family zinc finger domain; This zinc finger domain is found in the MYST family of histone ...
 164-218 2.19e-24

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: 95.38  E-value: 2.19e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2361033427 164 VRNLNRIIMGKYEIEPWYFSPYPIELTDEDFIYIDDFTLQYFGSKKQYERYRKKC 218
Cdd:pfam17772   1 VKNIEKIQFGRYEIDTWYFSPYPEEYTNVDKLYVCEFCLKYMKSRKSYKRHRKKC 55
Tudor-knot pfam11717
RNA binding activity-knot of a chromodomain; This is a novel knotted tudor domain which is ...
 21-74 1.05e-20

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: 84.95  E-value: 1.05e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2361033427  21 IIIKCQCWVQKNDEE-RLAEILSINTRKAPPKFYVHYVNYNKRLDEWITTDRINL 74
Cdd:pfam11717   1 IEIGCKVLVRKRDGEwRLAEILSIRPKKGKYEYYVHYVGFNKRLDEWVPEDRIDL 55
CBD cd18643
chromo barrel domain of MOF acetyltransferase, and similar proteins; This group includes the ...
 25-85 3.18e-15

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: 69.90  E-value: 3.18e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2361033427  25 CQCWVQKND----EERLAEILSINTRK---APPKFYVHYVNYNKRLDEWITTDRInldkevlYPKLKA 85
Cdd:cd18643     1 EKVLVFEPDpkarVLYDAKILSVITGKdgrAPPEYLVHYVGWNRRLDEWVAEDRV-------LPDLDE 61
CBD_TIP60_like cd18985
chromo barrel domain of human tat-interactive protein 60, and similar proteins; ...
 25-85 3.23e-11

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: 58.75  E-value: 3.23e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2361033427  25 CQCWVQKNDEERLAEILSINTRKAPPKFYVHYVNYNKRLDEWITTDRINLdKEVLYPKLKA 85
Cdd:cd18985     3 LRVRMHKTDEWPLAEILSVKDISGRKLFYVHYIDFNKRLDEWVTHERLDL-KKIQFPKKEA 62
CBD_MOF_like cd18984
chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar ...
 38-87 4.85e-06

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: 44.08  E-value: 4.85e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2361033427  38 AEILSINTRK--APPKFYVHYVNYNKRLDEWITTDRINLDKEVLYPKLKATD 87
Cdd:cd18984    16 AEVIQSRTTKqaGREEYYVHYVGLNRRLDEWVDKSRLSLNDLGKIVKTPAPP 67
CHROMO smart00298
Chromatin organization modifier domain;
34-79 9.75e-05

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 39.89  E-value: 9.75e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2361033427   34 EERLAEILSI-NTRKAPPKFYVHYVNYNKRLDEWITTDRINLDKEVL 79
Cdd:smart00298   1 EYEVEKILDHrWKKKGELEYLVKWKGYSYSEDTWEPEENLLNCSKKL 47
CBD_RBP1_like cd18641
chromo barrel domain of retinoblastoma binding protein 1, and similar proteins; ...
 38-76 2.30e-04

chromo barrel domain of retinoblastoma binding protein 1, and similar proteins; Retinoblastoma-binding protein 1 (RBP1), also termed AT-rich interaction domain 4A, is a ubiquitously expressed nuclear protein. RBP1 is a tumor and leukemia suppressor that binds both methylated histone tails and DNA, and is involved in epigenetic regulation in leukemia and Prader-Willi/Angelman syndromes. The chromo barrel domain of RBP1 has been reported to recognize histone H4K20me3 weakly, and this binding is enhanced by the simultaneous binding of DNA. RBP1 binds directly, with several other proteins, to retinoblastoma protein (pRB) which regulates cell proliferation; pRB represses transcription by recruiting RBP1. 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.


Pssm-ID: 350843 [Multi-domain]  Cd Length: 59  Bit Score: 39.18  E-value: 2.30e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2361033427  38 AEILSINTRKAPPKFYVHYVNYNKRLDEWITTDRI--NLDK 76
Cdd:cd18641    18 ASIKSTEIDDGEVLYLVHYYGWNVRYDEWVKADRIiwPLDK 58
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 281-332 5.06e-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: 38.41  E-value: 5.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2361033427 281 ELGHHLVGY--FSKEKESADGYNVACILTLPQYQRMGYGKLLIEFSYELSKKEN 332
Cdd:cd04301     5 EDDGEIVGFasLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERG 58
CBD_MSL3_like cd18983
chromo barrel domain of human male-specific lethal complex subunit 3, and similar proteins; ...
 38-89 5.92e-04

chromo barrel domain of human male-specific lethal complex subunit 3, and similar proteins; This subgroup includes human male-specific lethal (MSL) complex subunit 3 (MSL3, also known as MSL3L1). The MSL3 chromodomain specifically recognizes the H4K20 monomethyl mark, in a DNA-dependent manner, and may be involved in chromosomal targeting of the MSL complex. Also included is MORF-related gene on chromosome 15 (MRG15, also known as MORF4L1) which specifically binds to Lys36-methylated histone H3 and plays a role in transcriptional regulation and in DNA repair. This subgroup also includes Arabidopsis thaliana Morf Related Gene 2 (MRG2) which acts as a H3K4me3/H3K36me3 reader involved in the regulation of Arabidopsis flowering. 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.


Pssm-ID: 350846  Cd Length: 57  Bit Score: 37.81  E-value: 5.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2361033427  38 AEILSINTRKAPPKFYVHYVNYNKRLDEWITTDRInldkevlypkLKATDED 89
Cdd:cd18983    14 AKILDVIPDKKEWKYFIHYNGWNKSWDEWVPEDRV----------LKYTDEN 55
 
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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