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Conserved domains on  [gi|442615135|ref|NP_001259233|]
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Tat interactive protein 60kDa, isoform B [Drosophila melanogaster]

Protein Classification

chromo domain-containing protein( domain architecture ID 13040247)

chromo (chromatin organization modifier) domain-containing protein may bind methylated histone tails

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN00104 super family cl33410
MYST -like histone acetyltransferase; Provisional
255-453 4.84e-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: 386.80  E-value: 4.84e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615135 255 TRMKNVEMIELGRHRIKPWYFSPYPQELCQMPCIYICEFCLKYRKSRKCLERHLSKCNLRHPPGNEIYRK----HTISFF 330
Cdd:PLN00104 165 TKVKNIATIELGRYEIDTWYFSPFPPEYNDCSKLYFCEFCLKFMKRKEQLQRHMKKCDLKHPPGDEIYRHptrqEGLSMF 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615135 331 EIDGRKNKVYAQNLCLLAKLFLDHKTLYYDTDPFLFYVMTEFDSRGFHIVGYFSKEKESTEDYNVACILTMPPYQRKGYG 410
Cdd:PLN00104 245 EVDGKKNKVYCQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEKHSEEDYNLACILTLPPYQRKGYG 324
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 442615135 411 KLLIEFSYELSKFEGKTGSPEKPLSDLGLLSYRSYWAQTILEI 453
Cdd:PLN00104 325 KFLIAFSYELSKREGKVGTPERPLSDLGLVSYRGYWTRVLLEI 367
CBD_TIP60_like cd18985
chromo barrel domain of human tat-interactive protein 60, and similar proteins; ...
27-90 1.13e-40

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: 140.03  E-value: 1.13e-40
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442615135  27 CRLPVRMHKTDDWPLAEIVSIKELDGRRQFYVHYVDFNKRLDEWVNEEDLYTRKVQFPRRDGSQ 90
Cdd:cd18985    1 CRLRVRMHKTDEWPLAEILSVKDISGRKLFYVHYIDFNKRLDEWVTHERLDLKKIQFPKKEAKT 64
 
Name Accession Description Interval E-value
PLN00104 PLN00104
MYST -like histone acetyltransferase; Provisional
255-453 4.84e-131

MYST -like histone acetyltransferase; Provisional


Pssm-ID: 215056 [Multi-domain]  Cd Length: 450  Bit Score: 386.80  E-value: 4.84e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615135 255 TRMKNVEMIELGRHRIKPWYFSPYPQELCQMPCIYICEFCLKYRKSRKCLERHLSKCNLRHPPGNEIYRK----HTISFF 330
Cdd:PLN00104 165 TKVKNIATIELGRYEIDTWYFSPFPPEYNDCSKLYFCEFCLKFMKRKEQLQRHMKKCDLKHPPGDEIYRHptrqEGLSMF 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615135 331 EIDGRKNKVYAQNLCLLAKLFLDHKTLYYDTDPFLFYVMTEFDSRGFHIVGYFSKEKESTEDYNVACILTMPPYQRKGYG 410
Cdd:PLN00104 245 EVDGKKNKVYCQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEKHSEEDYNLACILTLPPYQRKGYG 324
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 442615135 411 KLLIEFSYELSKFEGKTGSPEKPLSDLGLLSYRSYWAQTILEI 453
Cdd:PLN00104 325 KFLIAFSYELSKREGKVGTPERPLSDLGLVSYRGYWTRVLLEI 367
MOZ_SAS pfam01853
MOZ/SAS family; This region of these proteins has been suggested to be homologous to ...
316-471 1.42e-117

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: 342.10  E-value: 1.42e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615135  316 PPGNEIYRKHTISFFEIDGRKNKVYAQNLCLLAKLFLDHKTLYYDTDPFLFYVMTEFDSRGFHIVGYFSKEKESTEDYNV 395
Cdd:pfam01853   1 PPGNEIYRKGNISIFEVDGRKQKLYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTETDETGCHIVGYFSKEKESSDNYNL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442615135  396 ACILTMPPYQRKGYGKLLIEFSYELSKFEGKTGSPEKPLSDLGLLSYRSYWAQTILEIFISQNPStdgekpTITIK 471
Cdd:pfam01853  81 ACILTLPPYQRKGYGKLLIEFSYELSKREGKIGGPEKPLSDLGLLSYRSYWSEVILEYLLKHRKE------GISIE 150
SAS2 COG5027
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics];
241-455 1.20e-116

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


Pssm-ID: 227360 [Multi-domain]  Cd Length: 395  Bit Score: 347.91  E-value: 1.20e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615135 241 RQSGSMV--THQddvVTRMKNVEMIELGRHRIKPWYFSPYPQELCQMPCIYICEFCLKYRKSRKCLERHLSKCNLRHPPG 318
Cdd:COG5027  112 RFGGSKVqnPHE---GARVKNINEIKLGNYEIEPWYFSPYPEEFSDLDIVYICEFCLKYYGSQTSLVRHRKKCSLQHPPG 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615135 319 NEIYRKHTISFFEIDGRKNKVYAQNLCLLAKLFLDHKTLYYDTDPFLFYVMTEFDSRGFHIVGYFSKEKESTEDYNVACI 398
Cdd:COG5027  189 NEIYRDKYISFFEIDGRKQRLYCRNLCLLSKLFLDHKTLYYDVDPFLFYVLTERGDTGCHLVGYFSKEKESEQDYNLACI 268
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442615135 399 LTMPPYQRKGYGKLLIEFSYELSKFEGKTGSPEKPLSDLGLLSYRSYWAQTILEIFI 455
Cdd:COG5027  269 LTLPPYQRRGYGKLLIDFSYLLSQKEGKVGSPEKPLSDLGLLSYRAYWSEIVAKLLL 325
CBD_TIP60_like cd18985
chromo barrel domain of human tat-interactive protein 60, and similar proteins; ...
27-90 1.13e-40

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: 140.03  E-value: 1.13e-40
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442615135  27 CRLPVRMHKTDDWPLAEIVSIKELDGRRQFYVHYVDFNKRLDEWVNEEDLYTRKVQFPRRDGSQ 90
Cdd:cd18985    1 CRLRVRMHKTDEWPLAEILSVKDISGRKLFYVHYIDFNKRLDEWVTHERLDLKKIQFPKKEAKT 64
Tudor-knot pfam11717
RNA binding activity-knot of a chromodomain; This is a novel knotted tudor domain which is ...
23-78 1.89e-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: 87.26  E-value: 1.89e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 442615135   23 LTEGCRLPVRMHkTDDWPLAEIVSIKELDGRRQFYVHYVDFNKRLDEWVNEEDLYT 78
Cdd:pfam11717   1 IEIGCKVLVRKR-DGEWRLAEILSIRPKKGKYEYYVHYVGFNKRLDEWVPEDRIDL 55
CHROMO smart00298
Chromatin organization modifier domain;
38-76 6.16e-07

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 46.05  E-value: 6.16e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 442615135    38 DWPLAEIVSIK-ELDGRRQFYVHYVDFNKRLDEWVNEEDL 76
Cdd:smart00298   1 EYEVEKILDHRwKKKGELEYLVKWKGYSYSEDTWEPEENL 40
 
Name Accession Description Interval E-value
PLN00104 PLN00104
MYST -like histone acetyltransferase; Provisional
255-453 4.84e-131

MYST -like histone acetyltransferase; Provisional


Pssm-ID: 215056 [Multi-domain]  Cd Length: 450  Bit Score: 386.80  E-value: 4.84e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615135 255 TRMKNVEMIELGRHRIKPWYFSPYPQELCQMPCIYICEFCLKYRKSRKCLERHLSKCNLRHPPGNEIYRK----HTISFF 330
Cdd:PLN00104 165 TKVKNIATIELGRYEIDTWYFSPFPPEYNDCSKLYFCEFCLKFMKRKEQLQRHMKKCDLKHPPGDEIYRHptrqEGLSMF 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615135 331 EIDGRKNKVYAQNLCLLAKLFLDHKTLYYDTDPFLFYVMTEFDSRGFHIVGYFSKEKESTEDYNVACILTMPPYQRKGYG 410
Cdd:PLN00104 245 EVDGKKNKVYCQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEKHSEEDYNLACILTLPPYQRKGYG 324
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 442615135 411 KLLIEFSYELSKFEGKTGSPEKPLSDLGLLSYRSYWAQTILEI 453
Cdd:PLN00104 325 KFLIAFSYELSKREGKVGTPERPLSDLGLVSYRGYWTRVLLEI 367
MOZ_SAS pfam01853
MOZ/SAS family; This region of these proteins has been suggested to be homologous to ...
316-471 1.42e-117

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: 342.10  E-value: 1.42e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615135  316 PPGNEIYRKHTISFFEIDGRKNKVYAQNLCLLAKLFLDHKTLYYDTDPFLFYVMTEFDSRGFHIVGYFSKEKESTEDYNV 395
Cdd:pfam01853   1 PPGNEIYRKGNISIFEVDGRKQKLYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTETDETGCHIVGYFSKEKESSDNYNL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442615135  396 ACILTMPPYQRKGYGKLLIEFSYELSKFEGKTGSPEKPLSDLGLLSYRSYWAQTILEIFISQNPStdgekpTITIK 471
Cdd:pfam01853  81 ACILTLPPYQRKGYGKLLIEFSYELSKREGKIGGPEKPLSDLGLLSYRSYWSEVILEYLLKHRKE------GISIE 150
SAS2 COG5027
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics];
241-455 1.20e-116

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


Pssm-ID: 227360 [Multi-domain]  Cd Length: 395  Bit Score: 347.91  E-value: 1.20e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615135 241 RQSGSMV--THQddvVTRMKNVEMIELGRHRIKPWYFSPYPQELCQMPCIYICEFCLKYRKSRKCLERHLSKCNLRHPPG 318
Cdd:COG5027  112 RFGGSKVqnPHE---GARVKNINEIKLGNYEIEPWYFSPYPEEFSDLDIVYICEFCLKYYGSQTSLVRHRKKCSLQHPPG 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615135 319 NEIYRKHTISFFEIDGRKNKVYAQNLCLLAKLFLDHKTLYYDTDPFLFYVMTEFDSRGFHIVGYFSKEKESTEDYNVACI 398
Cdd:COG5027  189 NEIYRDKYISFFEIDGRKQRLYCRNLCLLSKLFLDHKTLYYDVDPFLFYVLTERGDTGCHLVGYFSKEKESEQDYNLACI 268
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442615135 399 LTMPPYQRKGYGKLLIEFSYELSKFEGKTGSPEKPLSDLGLLSYRSYWAQTILEIFI 455
Cdd:COG5027  269 LTLPPYQRRGYGKLLIDFSYLLSQKEGKVGSPEKPLSDLGLLSYRAYWSEIVAKLLL 325
PLN03238 PLN03238
probable histone acetyltransferase MYST; Provisional
254-462 2.26e-111

probable histone acetyltransferase MYST; Provisional


Pssm-ID: 215642 [Multi-domain]  Cd Length: 290  Bit Score: 330.66  E-value: 2.26e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615135 254 VTRMKNVEMIELGRHRIKPWYFSPYPQELCQMPCIYICEFCLKYRKSRKCLERHLSKCNLRHPPGNEIYR---KHTISFF 330
Cdd:PLN03238  14 TTKVKNIEMIELGKYEMDTWYYSPYPEPYASCTKLYICEYCLKYMRKKKSLLRHLAKCDIRQPPGGGIYGavtEGPLSVF 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615135 331 EIDGRKNKVYAQNLCLLAKLFLDHKTLYYDTDPFLFYVMTEFDSRGFHIVGYFSKEKESTEDYNVACILTMPPYQRKGYG 410
Cdd:PLN03238  94 EVDGKKAKVYCQNLCLLAKLFLDHKTLYYDVDPFLFYVMTEVDDHGSHIVGYFSKEKVSAEDYNLACILTLPPYQRKGYG 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 442615135 411 KLLIEFSYELSKFEGKTGSPEKPLSDLGLLSYRSYWAQTILEIFisQNPSTD 462
Cdd:PLN03238 174 KFLISFAYELSKREGKVGTPERPLSDLGKVSFRSYWTRVLLEQL--RDVKGD 223
PLN03239 PLN03239
histone acetyltransferase; Provisional
244-458 2.34e-91

histone acetyltransferase; Provisional


Pssm-ID: 178777 [Multi-domain]  Cd Length: 351  Bit Score: 281.54  E-value: 2.34e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615135 244 GSMVTHQDdvVTRMKNVEMIELGRHRIKPWYFSPYPQELCQ----MPCIYICEFCLKYRKSRKCLERHLSKC---NLRHP 316
Cdd:PLN03239  60 AALKEHEE--VTKVKNVAFLELGPYQMDTWYFSPLPKELFKaggfIDVLYVCEFSFGFFARKSELLRFQAKElpkERRHP 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615135 317 PGNEIYRKHTISFFEIDGRKNKVYAQNLCLLAKLFLDHKTLYYDTDPFLFYVMTEFDSRGFHIVGYFSKEKESTEDYNVA 396
Cdd:PLN03239 138 PGNEIYRCGDLAMFEVDGFEERIYCQNLCYIAKLFLDHKTLYFDVDPFLFYVLCEVDERGFHPVGYYSKEKYSDVGYNLA 217
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442615135 397 CILTMPPYQRKGYGKLLIEFSYELSKFEGKTGSPEKPLSDLGLLSYRSYWAQTILEIFISQN 458
Cdd:PLN03239 218 CILTFPAHQRKGYGRFLIAFSYELSKKEEKVGSPEKPMSDLGQQAYIPYWGSTIVDFLLNHS 279
PTZ00064 PTZ00064
histone acetyltransferase; Provisional
234-455 3.68e-91

histone acetyltransferase; Provisional


Pssm-ID: 173359 [Multi-domain]  Cd Length: 552  Bit Score: 287.68  E-value: 3.68e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615135 234 DGKTPTPRQS---GSMVTHQDdvVTRMKNVEMIELGRHRIKPWYFSPYPQELCQMPCIYICEFCLKYRKSRKCLERHLSK 310
Cdd:PTZ00064 225 DGEDPDEHEGmdhSAILDHEE--TTRLRTIGRVRIGKFILDTWYFSPLPDEYQNVDTLHFCEYCLDFFCFEDELIRHLSR 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615135 311 CNLRHPPGNEIYRKHTISFFEIDGRKNKVYAQNLCLLAKLFLDHKTLYYDTDPFLFYVMTEFDSRGFHIVGYFSKEKEST 390
Cdd:PTZ00064 303 CQLRHPPGNEIYRKDNISVFEIDGALTRGYAENLCYLAKLFLDHKTLQYDVEPFLFYIVTEVDEEGCHIVGYFSKEKVSL 382
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442615135 391 EDYNVACILTMPPYQRKGYGKLLIEFSYELSKFEGKTGSPEKPLSDLGLLSYRSYWAQTILEIFI 455
Cdd:PTZ00064 383 LHYNLACILTLPCYQRKGYGKLLVDLSYKLSLKEGKWGHPERPLSDLGRAIYNNWWAHRISEYLL 447
CBD_TIP60_like cd18985
chromo barrel domain of human tat-interactive protein 60, and similar proteins; ...
27-90 1.13e-40

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: 140.03  E-value: 1.13e-40
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442615135  27 CRLPVRMHKTDDWPLAEIVSIKELDGRRQFYVHYVDFNKRLDEWVNEEDLYTRKVQFPRRDGSQ 90
Cdd:cd18985    1 CRLRVRMHKTDEWPLAEILSVKDISGRKLFYVHYIDFNKRLDEWVTHERLDLKKIQFPKKEAKT 64
zf-MYST pfam17772
MYST family zinc finger domain; This zinc finger domain is found in the MYST family of histone ...
257-311 2.91e-27

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: 103.47  E-value: 2.91e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442615135  257 MKNVEMIELGRHRIKPWYFSPYPQELCQMPCIYICEFCLKYRKSRKCLERHLSKC 311
Cdd:pfam17772   1 VKNIEKIQFGRYEIDTWYFSPYPEEYTNVDKLYVCEFCLKYMKSRKSYKRHRKKC 55
Tudor-knot pfam11717
RNA binding activity-knot of a chromodomain; This is a novel knotted tudor domain which is ...
23-78 1.89e-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: 87.26  E-value: 1.89e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 442615135   23 LTEGCRLPVRMHkTDDWPLAEIVSIKELDGRRQFYVHYVDFNKRLDEWVNEEDLYT 78
Cdd:pfam11717   1 IEIGCKVLVRKR-DGEWRLAEILSIRPKKGKYEYYVHYVGFNKRLDEWVPEDRIDL 55
CBD_MOF_like cd18642
chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar ...
25-86 8.76e-15

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: 69.00  E-value: 8.76e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442615135  25 EGCRLPVRmhKTDDWPLAEIVSIKEL-DGRRQFYVHYVDFNKRLDEWVNEE--DLYTRKVQFPRR 86
Cdd:cd18642    1 IKCRCWVQ--RNDEEHLAEVLSRRTRkHAPPEFYVHYVELNRRLDEWITTDriDLDLKECELPKK 63
CBD_ESA1_like cd18986
chromo barrel domain of yeast NuA4 histone acetyltransferase complex catalytic subunit ESA1, ...
26-85 2.63e-12

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: 61.85  E-value: 2.63e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442615135  26 GCRLPVRmhKTDDWPLAEIVSIKELDGRRQFYVHYVDFNKRLDEWVNEEDL-YTRKVQFPR 85
Cdd:cd18986    2 GCKCWVQ--KDGEERLAEILSINTRKAPPKFYVHYEDFNKRLDEWITADRInLSKEVLYPK 60
CHROMO smart00298
Chromatin organization modifier domain;
38-76 6.16e-07

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 46.05  E-value: 6.16e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 442615135    38 DWPLAEIVSIK-ELDGRRQFYVHYVDFNKRLDEWVNEEDL 76
Cdd:smart00298   1 EYEVEKILDHRwKKKGELEYLVKWKGYSYSEDTWEPEENL 40
CBD_MOF_like cd18984
chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar ...
37-72 2.20e-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: 45.24  E-value: 2.20e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 442615135  37 DDWPLAEIVSIK--ELDGRRQFYVHYVDFNKRLDEWVN 72
Cdd:cd18984   11 DTVHRAEVIQSRttKQAGREEYYVHYVGLNRRLDEWVD 48
CBD cd18643
chromo barrel domain of MOF acetyltransferase, and similar proteins; This group includes the ...
35-77 1.73e-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: 42.55  E-value: 1.73e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 442615135  35 KTDDWPLAEIVSI---KELDGRRQFYVHYVDFNKRLDEWVNEEDLY 77
Cdd:cd18643   11 KARVLYDAKILSVitgKDGRAPPEYLVHYVGWNRRLDEWVAEDRVL 56
MBT_PHF20L1-like cd20104
malignant brain tumor (MBT) repeat found in PHD finger protein 20-like protein 1 (PHF20L1) and ...
35-84 5.10e-03

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: 35.29  E-value: 5.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 442615135  35 KTDDWPLAEIVSIKELDGRrqFYVHYVDFNKRLDEWVNEEDLYTRKVQFP 84
Cdd:cd20104   12 GEGKWYEAKIVEVDEEENK--VLVHYDGWSSRYDEWIDRDSERLRPLHTP 59
 
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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