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Conserved domains on  [gi|2462491233|ref|XP_054185289|]
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transcriptional adapter 2-alpha isoform X3 [Homo sapiens]

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];
28-386 9.00e-53

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: 181.42  E-value: 9.00e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462491233  28 YIKCAECgpPPFFLCLQCFTRGFEYKKHQSDHTYEIM-TSDFPVLDPSWTAQEEMALLEAVMDCGFGNWQDVANQMCTKT 106
Cdd:COG5114    20 FIKCNEC--PAVDLCLPCFVNGIETGVHSPYHGYRIIeTNSYPIGEEGWGADEELLLIECLDTLGLGNWEDIADYIGSRA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462491233 107 KEECEKHYMKHFI------------NNPLFASTLLNLKQAEEAKTADTAI----PFHS---------------------- 148
Cdd:COG5114    98 KEEIKSHYLKMYDeskyyplpditqNIHVPQDEFLEQRRHRIETFELPPInprkPKASnpycheiqgympgrlefdveym 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462491233 149 ----------------------LKMAVVDIYHSRLKERQRRKKIIRDHGLINLRKFQLMERRYPKEVQDLYETMRRFARI 206
Cdd:COG5114   178 neaevpikdmsfdgdkeelkkkLKNATLDIYNSRLTFRARRKHAIFGKNLMDYRNLQAKDKKRSKEECGLVNSIKWFARY 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462491233 207 VGPVEHDKFIESHALEFELRREIKRLQEYRTAGITNFCSARTYDHLKKTREEERLKRTMLSEVLQYIQDSSACQQWLRRQ 286
Cdd:COG5114   258 LTKSDFNVFFRDILEGVYIEKRIHELQEWRNNGLTTLEAGLKYERDKFEKFGASTAASLSEGNSRYRSNSAHRSNAEYSQ 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462491233 287 ADIDSGLSpsipmasnsgRRSAPPLNLTGLPGTEKLNEKEKELCQMVRLVPGAYLEYKSALLNECNKQGG-LRLAQARAL 365
Cdd:COG5114   338 MDVKNILP----------SKNMTISDIQHAPDYALLSDDEQRLCETLNISPKPYLELKKEVISCFLRTRGeFTKEDFNRL 407
                         410       420
                  ....*....|....*....|.
gi 2462491233 366 IKIDVNKTRKIYDFLIREGYI 386
Cdd:COG5114   408 FGIDLGKADGLYDFFLERGWI 428
 
Name Accession Description Interval E-value
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
28-386 9.00e-53

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


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 181.42  E-value: 9.00e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462491233  28 YIKCAECgpPPFFLCLQCFTRGFEYKKHQSDHTYEIM-TSDFPVLDPSWTAQEEMALLEAVMDCGFGNWQDVANQMCTKT 106
Cdd:COG5114    20 FIKCNEC--PAVDLCLPCFVNGIETGVHSPYHGYRIIeTNSYPIGEEGWGADEELLLIECLDTLGLGNWEDIADYIGSRA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462491233 107 KEECEKHYMKHFI------------NNPLFASTLLNLKQAEEAKTADTAI----PFHS---------------------- 148
Cdd:COG5114    98 KEEIKSHYLKMYDeskyyplpditqNIHVPQDEFLEQRRHRIETFELPPInprkPKASnpycheiqgympgrlefdveym 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462491233 149 ----------------------LKMAVVDIYHSRLKERQRRKKIIRDHGLINLRKFQLMERRYPKEVQDLYETMRRFARI 206
Cdd:COG5114   178 neaevpikdmsfdgdkeelkkkLKNATLDIYNSRLTFRARRKHAIFGKNLMDYRNLQAKDKKRSKEECGLVNSIKWFARY 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462491233 207 VGPVEHDKFIESHALEFELRREIKRLQEYRTAGITNFCSARTYDHLKKTREEERLKRTMLSEVLQYIQDSSACQQWLRRQ 286
Cdd:COG5114   258 LTKSDFNVFFRDILEGVYIEKRIHELQEWRNNGLTTLEAGLKYERDKFEKFGASTAASLSEGNSRYRSNSAHRSNAEYSQ 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462491233 287 ADIDSGLSpsipmasnsgRRSAPPLNLTGLPGTEKLNEKEKELCQMVRLVPGAYLEYKSALLNECNKQGG-LRLAQARAL 365
Cdd:COG5114   338 MDVKNILP----------SKNMTISDIQHAPDYALLSDDEQRLCETLNISPKPYLELKKEVISCFLRTRGeFTKEDFNRL 407
                         410       420
                  ....*....|....*....|.
gi 2462491233 366 IKIDVNKTRKIYDFLIREGYI 386
Cdd:COG5114   408 FGIDLGKADGLYDFFLERGWI 428
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
15-64 1.79e-18

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: 78.10  E-value: 1.79e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462491233  15 PPCRGCSSYLME-PYIKCAECgpPPFFLCLQCFTRGFEYKKHQSDHTYEIM 64
Cdd:cd02335     1 YHCDYCSKDITGtIRIKCAEC--PDFDLCLECFSAGAEIGKHRNDHNYRVV 49
SWIRM pfam04433
SWIRM domain; This SWIRM domain is a small alpha-helical domain of about 85 amino acid ...
320-386 7.65e-10

SWIRM domain; This SWIRM domain is a small alpha-helical domain of about 85 amino acid residues found in chromosomal proteins. It contains a helix-turn helix motif and binds to DNA.


Pssm-ID: 461307 [Multi-domain]  Cd Length: 78  Bit Score: 54.87  E-value: 7.65e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462491233 320 EKLNEKEKELCQMVR----LVPGAYLEYKSALLNE--CNKQGGLRLAQARALIKIDVNKTRKIYDFLIREGYI 386
Cdd:pfam04433   4 DKLHPIEKRLLPEFFngksKTPEVYLEIRNFILNLwrENPKEYLTKTDARRALKGDVNLISRIHEFLERWGLI 76
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
74-118 1.80e-09

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


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 53.00  E-value: 1.80e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2462491233   74 SWTAQEEMALLEAVMDCGFGNWQDVANQMCTKTKEECEKHYMKHF 118
Cdd:smart00717   3 EWTEEEDELLIELVKKYGKNNWEKIAKELPGRTAEQCRERWRNLL 47
 
Name Accession Description Interval E-value
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
28-386 9.00e-53

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


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 181.42  E-value: 9.00e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462491233  28 YIKCAECgpPPFFLCLQCFTRGFEYKKHQSDHTYEIM-TSDFPVLDPSWTAQEEMALLEAVMDCGFGNWQDVANQMCTKT 106
Cdd:COG5114    20 FIKCNEC--PAVDLCLPCFVNGIETGVHSPYHGYRIIeTNSYPIGEEGWGADEELLLIECLDTLGLGNWEDIADYIGSRA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462491233 107 KEECEKHYMKHFI------------NNPLFASTLLNLKQAEEAKTADTAI----PFHS---------------------- 148
Cdd:COG5114    98 KEEIKSHYLKMYDeskyyplpditqNIHVPQDEFLEQRRHRIETFELPPInprkPKASnpycheiqgympgrlefdveym 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462491233 149 ----------------------LKMAVVDIYHSRLKERQRRKKIIRDHGLINLRKFQLMERRYPKEVQDLYETMRRFARI 206
Cdd:COG5114   178 neaevpikdmsfdgdkeelkkkLKNATLDIYNSRLTFRARRKHAIFGKNLMDYRNLQAKDKKRSKEECGLVNSIKWFARY 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462491233 207 VGPVEHDKFIESHALEFELRREIKRLQEYRTAGITNFCSARTYDHLKKTREEERLKRTMLSEVLQYIQDSSACQQWLRRQ 286
Cdd:COG5114   258 LTKSDFNVFFRDILEGVYIEKRIHELQEWRNNGLTTLEAGLKYERDKFEKFGASTAASLSEGNSRYRSNSAHRSNAEYSQ 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462491233 287 ADIDSGLSpsipmasnsgRRSAPPLNLTGLPGTEKLNEKEKELCQMVRLVPGAYLEYKSALLNECNKQGG-LRLAQARAL 365
Cdd:COG5114   338 MDVKNILP----------SKNMTISDIQHAPDYALLSDDEQRLCETLNISPKPYLELKKEVISCFLRTRGeFTKEDFNRL 407
                         410       420
                  ....*....|....*....|.
gi 2462491233 366 IKIDVNKTRKIYDFLIREGYI 386
Cdd:COG5114   408 FGIDLGKADGLYDFFLERGWI 428
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
15-64 1.79e-18

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: 78.10  E-value: 1.79e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462491233  15 PPCRGCSSYLME-PYIKCAECgpPPFFLCLQCFTRGFEYKKHQSDHTYEIM 64
Cdd:cd02335     1 YHCDYCSKDITGtIRIKCAEC--PDFDLCLECFSAGAEIGKHRNDHNYRVV 49
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
74-118 3.37e-10

'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: 54.89  E-value: 3.37e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2462491233  74 SWTAQEEMALLEAVMDCGFGNWQDVANQMCTKTKEECEKHYMKHF 118
Cdd:cd00167     1 PWTEEEDELLLEAVKKYGKNNWEKIAKELPGRTPKQCRERWRNLL 45
SWIRM pfam04433
SWIRM domain; This SWIRM domain is a small alpha-helical domain of about 85 amino acid ...
320-386 7.65e-10

SWIRM domain; This SWIRM domain is a small alpha-helical domain of about 85 amino acid residues found in chromosomal proteins. It contains a helix-turn helix motif and binds to DNA.


Pssm-ID: 461307 [Multi-domain]  Cd Length: 78  Bit Score: 54.87  E-value: 7.65e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462491233 320 EKLNEKEKELCQMVR----LVPGAYLEYKSALLNE--CNKQGGLRLAQARALIKIDVNKTRKIYDFLIREGYI 386
Cdd:pfam04433   4 DKLHPIEKRLLPEFFngksKTPEVYLEIRNFILNLwrENPKEYLTKTDARRALKGDVNLISRIHEFLERWGLI 76
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
74-118 1.80e-09

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


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 53.00  E-value: 1.80e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2462491233   74 SWTAQEEMALLEAVMDCGFGNWQDVANQMCTKTKEECEKHYMKHF 118
Cdd:smart00717   3 EWTEEEDELLIELVKKYGKNNWEKIAKELPGRTAEQCRERWRNLL 47
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
74-118 3.06e-08

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: 49.42  E-value: 3.06e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2462491233  74 SWTAQEEMALLEAVMDCGfGNWQDVANQMCTKTKEECEKHYMKHF 118
Cdd:pfam00249   3 PWTPEEDELLLEAVEKLG-NRWKKIAKLLPGRTDNQCKNRWQNYL 46
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
17-64 3.86e-08

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: 48.97  E-value: 3.86e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2462491233  17 CRGCSSYLMEPYIKCAECgpPPFFLCLQCFTRGFeyKKHQSDHTYEIM 64
Cdd:cd02249     3 CDGCLKPIVGVRYHCLVC--EDFDLCSSCYAKGK--KGHPPDHSFTEI 46
RSC8 COG5259
RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / ...
31-195 5.77e-05

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


Pssm-ID: 227584 [Multi-domain]  Cd Length: 531  Bit Score: 44.88  E-value: 5.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462491233  31 CAECGPPPFF------------LCLQCFTRGFEYKKHQSDHTYEIMTSDFPVlDPSWTAQEEMALLEAVMDCGfGNWQDV 98
Cdd:COG5259   227 CSCCGNKSFNtryhnlraekynSCSECYDQGRFPSEFTSSDFKPVTISLLIR-DKNWSRQELLLLLEGIEMYG-DDWDKV 304
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462491233  99 ANQMCTKTKEECekhyMKHFINNPLFASTL-------LNLKQAEEAKTADTaiPFHSLKMAVVDIYHSRLKERQRRKKII 171
Cdd:COG5259   305 ARHVGTKTKEQC----ILHFLQLPIEDNYLskgdgkgDNSKGRLPFDGSEN--PVLSTISFLAGIVNPRVQSEKQRAIIK 378
                         170       180
                  ....*....|....*....|....
gi 2462491233 172 RDHGLINLRKFQLMERRYPKEVQD 195
Cdd:COG5259   379 SGKISHINRESQEHIEEVIEYALD 402
SANT_TRF cd11660
Telomere repeat binding factor-like DNA-binding domains of the SANT/myb-like family; Human ...
75-101 1.26e-03

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: 36.39  E-value: 1.26e-03
                          10        20
                  ....*....|....*....|....*..
gi 2462491233  75 WTAQEEMALLEAVMDCGFGNWQDVANQ 101
Cdd:cd11660     3 WTDEEDEALVEGVEKYGVGNWAKILKD 29
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
16-59 4.58e-03

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: 34.87  E-value: 4.58e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2462491233  16 PCRGCS-SYLMEPYIKCAECgpPPFFLCLQCFTRGFEYKKHQSDH 59
Cdd:cd02345     2 SCSACRkQDISGIRFPCQVC--RDYSLCLGCYTKGRETKRHNSLH 44
 
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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