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Conserved domains on  [gi|298676444|ref|NP_001163925|]
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transcriptional adapter 2-beta [Mus musculus]

Protein Classification

transcriptional adapter( domain architecture ID 709052)

transcriptional adapter facilitates the assembly and activation of the transcriptional machinery at specific gene promoters or enhancer regions; similar to Homo sapiens transcriptional adapter 2-alpha, a component of the ATAC (Ada-Two-A-containing) complex, which is a protein complex involved in regulating chromatin accessibility and gene expression

Gene Ontology:  GO:0003677|GO:0008270

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5114 super family cl27155
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
6-415 5.43e-64

Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];


The actual alignment was detected with superfamily member COG5114:

Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 211.85  E-value: 5.43e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676444   6 KKYCVYCLAEVSPL-RFRCTECQDIELCPECFSAGAEIGHHRRYHGYQLVDggrfTLWGPEAEGGWTSREEQLLLDAIEQ 84
Cdd:COG5114    5 KIHCDVCFLDMTDLtFIKCNECPAVDLCLPCFVNGIETGVHSPYHGYRIIE----TNSYPIGEEGWGADEELLLIECLDT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676444  85 FGFGNWEDMAAHVGaSRTPQEVMEHYVSMYIHGNLGKacIPDTIPNRVTDHTCPSGGPLSPSLTTPLPPLD-----ISVA 159
Cdd:COG5114   81 LGLGNWEDIADYIG-SRAKEEIKSHYLKMYDESKYYP--LPDITQNIHVPQDEFLEQRRHRIETFELPPINprkpkASNP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676444 160 EQQQL-GYMPLRDDYEIEYDQDAETLISGLSVNYDDDDVEIELKRAHVDMYVRKLKERQRRKNIARDYNLVpaflgkdKK 238
Cdd:COG5114  158 YCHEIqGYMPGRLEFDVEYMNEAEVPIKDMSFDGDKEELKKKLKNATLDIYNSRLTFRARRKHAIFGKNLM-------DY 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676444 239 EKEKTLKRKITKEEKELRLKLRPLYQFMSCKEFDDLFENMHKEKMLRAKIRELQRYRRNGITKMEesaeyeaARHKRERR 318
Cdd:COG5114  231 RNLQAKDKKRSKEECGLVNSIKWFARYLTKSDFNVFFRDILEGVYIEKRIHELQEWRNNGLTTLE-------AGLKYERD 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676444 319 KENKNLASSKRGKEDG---------------------------KDSEFAAIENLPGFELLSDREKVLCSSLNLSPARYVT 371
Cdd:COG5114  304 KFEKFGASTAASLSEGnsryrsnsahrsnaeysqmdvknilpsKNMTISDIQHAPDYALLSDDEQRLCETLNISPKPYLE 383

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 298676444 372 VKTIIIKDHLQKRqGIPSKSRLPSYLDKVLKK--RILNFLTESGWI 415
Cdd:COG5114  384 LKKEVISCFLRTR-GEFTKEDFNRLFGIDLGKadGLYDFFLERGWI 428
 
Name Accession Description Interval E-value
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
6-415 5.43e-64

Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 211.85  E-value: 5.43e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676444   6 KKYCVYCLAEVSPL-RFRCTECQDIELCPECFSAGAEIGHHRRYHGYQLVDggrfTLWGPEAEGGWTSREEQLLLDAIEQ 84
Cdd:COG5114    5 KIHCDVCFLDMTDLtFIKCNECPAVDLCLPCFVNGIETGVHSPYHGYRIIE----TNSYPIGEEGWGADEELLLIECLDT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676444  85 FGFGNWEDMAAHVGaSRTPQEVMEHYVSMYIHGNLGKacIPDTIPNRVTDHTCPSGGPLSPSLTTPLPPLD-----ISVA 159
Cdd:COG5114   81 LGLGNWEDIADYIG-SRAKEEIKSHYLKMYDESKYYP--LPDITQNIHVPQDEFLEQRRHRIETFELPPINprkpkASNP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676444 160 EQQQL-GYMPLRDDYEIEYDQDAETLISGLSVNYDDDDVEIELKRAHVDMYVRKLKERQRRKNIARDYNLVpaflgkdKK 238
Cdd:COG5114  158 YCHEIqGYMPGRLEFDVEYMNEAEVPIKDMSFDGDKEELKKKLKNATLDIYNSRLTFRARRKHAIFGKNLM-------DY 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676444 239 EKEKTLKRKITKEEKELRLKLRPLYQFMSCKEFDDLFENMHKEKMLRAKIRELQRYRRNGITKMEesaeyeaARHKRERR 318
Cdd:COG5114  231 RNLQAKDKKRSKEECGLVNSIKWFARYLTKSDFNVFFRDILEGVYIEKRIHELQEWRNNGLTTLE-------AGLKYERD 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676444 319 KENKNLASSKRGKEDG---------------------------KDSEFAAIENLPGFELLSDREKVLCSSLNLSPARYVT 371
Cdd:COG5114  304 KFEKFGASTAASLSEGnsryrsnsahrsnaeysqmdvknilpsKNMTISDIQHAPDYALLSDDEQRLCETLNISPKPYLE 383

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 298676444 372 VKTIIIKDHLQKRqGIPSKSRLPSYLDKVLKK--RILNFLTESGWI 415
Cdd:COG5114  384 LKKEVISCFLRTR-GEFTKEDFNRLFGIDLGKadGLYDFFLERGWI 428
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 7-54 5.98e-20

Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239075 [Multi-domain]  Cd Length: 49  Bit Score: 82.73  E-value: 5.98e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 298676444   7 KYCVYCLAEVSPL-RFRCTECQDIELCPECFSAGAEIGHHRRYHGYQLV 54
Cdd:cd02335    1 YHCDYCSKDITGTiRIKCAECPDFDLCLECFSAGAEIGKHRNDHNYRVV 49
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
70-110 3.53e-08

SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 49.53  E-value: 3.53e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 298676444    70 WTSREEQLLLDAIEQFGFGNWEDMAAHVGaSRTPQEVMEHY 110
Cdd:smart00717   4 WTEEEDELLIELVKKYGKNNWEKIAKELP-GRTAEQCRERW 43
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 67-110 2.03e-06

Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.


Pssm-ID: 459731 [Multi-domain]  Cd Length: 46  Bit Score: 44.42  E-value: 2.03e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 298676444   67 EGGWTSREEQLLLDAIEQFGfGNWEDMAAHVGaSRTPQEVMEHY 110
Cdd:pfam00249   1 RGPWTPEEDELLLEAVEKLG-NRWKKIAKLLP-GRTDNQCKNRW 42
 
Name Accession Description Interval E-value
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
6-415 5.43e-64

Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 211.85  E-value: 5.43e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676444   6 KKYCVYCLAEVSPL-RFRCTECQDIELCPECFSAGAEIGHHRRYHGYQLVDggrfTLWGPEAEGGWTSREEQLLLDAIEQ 84
Cdd:COG5114    5 KIHCDVCFLDMTDLtFIKCNECPAVDLCLPCFVNGIETGVHSPYHGYRIIE----TNSYPIGEEGWGADEELLLIECLDT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676444  85 FGFGNWEDMAAHVGaSRTPQEVMEHYVSMYIHGNLGKacIPDTIPNRVTDHTCPSGGPLSPSLTTPLPPLD-----ISVA 159
Cdd:COG5114   81 LGLGNWEDIADYIG-SRAKEEIKSHYLKMYDESKYYP--LPDITQNIHVPQDEFLEQRRHRIETFELPPINprkpkASNP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676444 160 EQQQL-GYMPLRDDYEIEYDQDAETLISGLSVNYDDDDVEIELKRAHVDMYVRKLKERQRRKNIARDYNLVpaflgkdKK 238
Cdd:COG5114  158 YCHEIqGYMPGRLEFDVEYMNEAEVPIKDMSFDGDKEELKKKLKNATLDIYNSRLTFRARRKHAIFGKNLM-------DY 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676444 239 EKEKTLKRKITKEEKELRLKLRPLYQFMSCKEFDDLFENMHKEKMLRAKIRELQRYRRNGITKMEesaeyeaARHKRERR 318
Cdd:COG5114  231 RNLQAKDKKRSKEECGLVNSIKWFARYLTKSDFNVFFRDILEGVYIEKRIHELQEWRNNGLTTLE-------AGLKYERD 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676444 319 KENKNLASSKRGKEDG---------------------------KDSEFAAIENLPGFELLSDREKVLCSSLNLSPARYVT 371
Cdd:COG5114  304 KFEKFGASTAASLSEGnsryrsnsahrsnaeysqmdvknilpsKNMTISDIQHAPDYALLSDDEQRLCETLNISPKPYLE 383

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 298676444 372 VKTIIIKDHLQKRqGIPSKSRLPSYLDKVLKK--RILNFLTESGWI 415
Cdd:COG5114  384 LKKEVISCFLRTR-GEFTKEDFNRLFGIDLGKadGLYDFFLERGWI 428
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 7-54 5.98e-20

Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239075 [Multi-domain]  Cd Length: 49  Bit Score: 82.73  E-value: 5.98e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 298676444   7 KYCVYCLAEVSPL-RFRCTECQDIELCPECFSAGAEIGHHRRYHGYQLV 54
Cdd:cd02335    1 YHCDYCSKDITGTiRIKCAECPDFDLCLECFSAGAEIGKHRNDHNYRVV 49
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 70-113 7.52e-09

'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.


Pssm-ID: 238096 [Multi-domain]  Cd Length: 45  Bit Score: 51.04  E-value: 7.52e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 298676444  70 WTSREEQLLLDAIEQFGFGNWEDMAAHVGaSRTPQEVMEHYVSM 113
Cdd:cd00167    2 WTEEEDELLLEAVKKYGKNNWEKIAKELP-GRTPKQCRERWRNL 44
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
70-110 3.53e-08

SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 49.53  E-value: 3.53e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 298676444    70 WTSREEQLLLDAIEQFGFGNWEDMAAHVGaSRTPQEVMEHY 110
Cdd:smart00717   4 WTEEEDELLIELVKKYGKNNWEKIAKELP-GRTAEQCRERW 43
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 9-45 2.25e-07

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 47.05  E-value: 2.25e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 298676444     9 CVYCLAEVSPLRFRCTECQDIELCPECFSAG-AEIGHH 45
Cdd:smart00291   7 CDTCGKPIVGVRYHCLVCPDYDLCQSCFAKGsAGGEHS 44
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 20-54 2.72e-07

Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination.


Pssm-ID: 239078  Cd Length: 49  Bit Score: 46.96  E-value: 2.72e-07
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 298676444  20 RFRCTECQDIELCPECFSAGAEIGHHRRYHGYQLV 54
Cdd:cd02338   15 RYKCLICYDYDLCADCYDSGVTTERHLFDHPMQCI 49
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 9-51 7.75e-07

Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins.


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 45.50  E-value: 7.75e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 298676444   9 CVYCLAEVSPLRFRCTECQDIELCPECFSAGAEIghHRRYHGY 51
Cdd:cd02249    3 CDGCLKPIVGVRYHCLVCEDFDLCSSCYAKGKKG--HPPDHSF 43
RSC8 COG5259
RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / ...
 3-118 1.99e-06

RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / Transcription];


Pssm-ID: 227584 [Multi-domain]  Cd Length: 531  Bit Score: 49.88  E-value: 1.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676444   3 ELGKKYCVYCLAEVSPLRFRCTECQDIELCPECFSAGaeighhRRYHGYQLVDGGRFTLWGPEAEGGWTSREEQLLLDAI 82
Cdd:COG5259  221 EKHPSSCSCCGNKSFNTRYHNLRAEKYNSCSECYDQG------RFPSEFTSSDFKPVTISLLIRDKNWSRQELLLLLEGI 294

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 298676444  83 EQFGfGNWEDMAAHVGaSRTPQEVMEHYVSMYIHGN 118
Cdd:COG5259  295 EMYG-DDWDKVARHVG-TKTKEQCILHFLQLPIEDN 328
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 67-110 2.03e-06

Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.


Pssm-ID: 459731 [Multi-domain]  Cd Length: 46  Bit Score: 44.42  E-value: 2.03e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 298676444   67 EGGWTSREEQLLLDAIEQFGfGNWEDMAAHVGaSRTPQEVMEHY 110
Cdd:pfam00249   1 RGPWTPEEDELLLEAVEKLG-NRWKKIAKLLP-GRTDNQCKNRW 42
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 9-49 2.82e-05

Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dah (discontinuous actin hexagon) is a membrane associated protein essential for cortical furrow formation in Drosophila.


Pssm-ID: 239085  Cd Length: 49  Bit Score: 41.42  E-value: 2.82e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 298676444   9 CVYCLAE-VSPLRFRCTECQDIELCPECFSAGAEIGHHRRYH 49
Cdd:cd02345    3 CSACRKQdISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLH 44
SANT_TRF cd11660
Telomere repeat binding factor-like DNA-binding domains of the SANT/myb-like family; Human ...
 70-103 2.91e-04

Telomere repeat binding factor-like DNA-binding domains of the SANT/myb-like family; Human telomere repeat binding factors, TRF1 and TRF2, function as part of the 6 component shelterin complex. TRF2 binds DNA and recruits RAP1 (via binding to the RAP1 protein c-terminal (RCT)) and TIN2 in the protection of telomeres from DNA repair machinery. Metazoan shelterin consists of 3 DNA binding proteins (TRF2, TRF1, and POT1) and 3 recruited proteins that bind to one or more of these DNA-binding proteins (RAP1, TIN2, TPP1). Schizosaccharomyces pombe TAZ1 is an orthlog and binds RAP1. Human TRF1 and TRF2 bind double-stranded DNA. hTRF2 consists of a basic N-terminus, a TRF homology domain, the RAP1 binding motif (RBM), the TIN2 binding motif (TBM) and a myb-like DNA binding domain, SANT, named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. Tandem copies of the domain bind telomeric DNA tandem repeats as part of the capping complex. The single myb-like domain of TRF-type proteins is similar to the tandem myb_like domains found in yeast RAP1.


Pssm-ID: 212558 [Multi-domain]  Cd Length: 50  Bit Score: 38.32  E-value: 2.91e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 298676444  70 WTSREEQLLLDAIEQFGFGNWEDMAAH--VGASRTP 103
Cdd:cd11660    3 WTDEEDEALVEGVEKYGVGNWAKILKDyfFVNNRTS 38
 
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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