NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|528501428|ref|XP_005157493|]
View 

transcriptional adapter 2-alpha isoform X1 [Danio rerio]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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];
28-442 1.26e-65

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: 216.86  E-value: 1.26e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501428  28 YIKCAECgpSPFLLCLQCFTRGYEYKKHQSDHKYEIM-TSDFPVLESGWTAQEEMALLEAVMDCGFGNWQDVAYQMRSKT 106
Cdd:COG5114   20 FIKCNEC--PAVDLCLPCFVNGIETGVHSPYHGYRIIeTNSYPIGEEGWGADEELLLIECLDTLGLGNWEDIADYIGSRA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501428 107 KEECEGHYMKNYINN---PLFSSTLLSLRHMDDHLSRTADTAIPFKPTDDPPRPSFDSQLSR-DMAGYMPARADFMEEFD 182
Cdd:COG5114   98 KEEIKSHYLKMYDESkyyPLPDITQNIHVPQDEFLEQRRHRIETFELPPINPRKPKASNPYChEIQGYMPGRLEFDVEYM 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501428 183 NYAEWDLKDIDFVDDDSDILHALKVAVVDIYHSRLKERQRRKKIIRDHGLINLRKFLILERRYPKEVQDLYDVMRRFARV 262
Cdd:COG5114  178 NEAEVPIKDMSFDGDKEELKKKLKNATLDIYNSRLTFRARRKHAIFGKNLMDYRNLQAKDKKRSKEECGLVNSIKWFARY 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501428 263 VGPIEHDKFIESHTLEFELRREIHRLQEYRSEGIQSFCGAKVYERVKRTREDERRKRNMLCDVLQYIHDTRACQQWLHKQ 342
Cdd:COG5114  258 LTKSDFNVFFRDILEGVYIEKRIHELQEWRNNGLTTLEAGLKYERDKFEKFGASTAASLSEGNSRYRSNSAHRSNAEYSQ 337

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501428 343 AAIDAGIApvvstistsgRRSAPPLNLTGLPGTEKLNEREKELCQVVRLVPGAYLEYKQALLNECRRQGG-LRLAQARSL 421
Cdd:COG5114  338 MDVKNILP----------SKNMTISDIQHAPDYALLSDDEQRLCETLNISPKPYLELKKEVISCFLRTRGeFTKEDFNRL 407

                        410       420
                 ....*....|....*....|.
gi 528501428 422 IKIDVNKTRKIYDFLIKEGYI 442
Cdd:COG5114  408 FGIDLGKADGLYDFFLERGWI 428
 
Name Accession Description Interval E-value
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
28-442 1.26e-65

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


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 216.86  E-value: 1.26e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501428  28 YIKCAECgpSPFLLCLQCFTRGYEYKKHQSDHKYEIM-TSDFPVLESGWTAQEEMALLEAVMDCGFGNWQDVAYQMRSKT 106
Cdd:COG5114   20 FIKCNEC--PAVDLCLPCFVNGIETGVHSPYHGYRIIeTNSYPIGEEGWGADEELLLIECLDTLGLGNWEDIADYIGSRA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501428 107 KEECEGHYMKNYINN---PLFSSTLLSLRHMDDHLSRTADTAIPFKPTDDPPRPSFDSQLSR-DMAGYMPARADFMEEFD 182
Cdd:COG5114   98 KEEIKSHYLKMYDESkyyPLPDITQNIHVPQDEFLEQRRHRIETFELPPINPRKPKASNPYChEIQGYMPGRLEFDVEYM 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501428 183 NYAEWDLKDIDFVDDDSDILHALKVAVVDIYHSRLKERQRRKKIIRDHGLINLRKFLILERRYPKEVQDLYDVMRRFARV 262
Cdd:COG5114  178 NEAEVPIKDMSFDGDKEELKKKLKNATLDIYNSRLTFRARRKHAIFGKNLMDYRNLQAKDKKRSKEECGLVNSIKWFARY 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501428 263 VGPIEHDKFIESHTLEFELRREIHRLQEYRSEGIQSFCGAKVYERVKRTREDERRKRNMLCDVLQYIHDTRACQQWLHKQ 342
Cdd:COG5114  258 LTKSDFNVFFRDILEGVYIEKRIHELQEWRNNGLTTLEAGLKYERDKFEKFGASTAASLSEGNSRYRSNSAHRSNAEYSQ 337

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501428 343 AAIDAGIApvvstistsgRRSAPPLNLTGLPGTEKLNEREKELCQVVRLVPGAYLEYKQALLNECRRQGG-LRLAQARSL 421
Cdd:COG5114  338 MDVKNILP----------SKNMTISDIQHAPDYALLSDDEQRLCETLNISPKPYLELKKEVISCFLRTRGeFTKEDFNRL 407

                        410       420
                 ....*....|....*....|.
gi 528501428 422 IKIDVNKTRKIYDFLIKEGYI 442
Cdd:COG5114  408 FGIDLGKADGLYDFFLERGWI 428
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 15-64 1.27e-16

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: 73.48  E-value: 1.27e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 528501428  15 PPCRGCSSYLVE-PYIKCAECGPspFLLCLQCFTRGYEYKKHQSDHKYEIM 64
Cdd:cd02335    1 YHCDYCSKDITGtIRIKCAECPD--FDLCLECFSAGAEIGKHRNDHNYRVV 49
SWIRM pfam04433
SWIRM domain; This SWIRM domain is a small alpha-helical domain of about 85 amino acid ...
 376-443 5.23e-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: 55.65  E-value: 5.23e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528501428  376 EKLNEREKELCQVVR----LVPGAYLEYKQALLNECRR--QGGLRLAQARSLIKIDVNKTRKIYDFLIKEGYIN 443
Cdd:pfam04433   4 DKLHPIEKRLLPEFFngksKTPEVYLEIRNFILNLWREnpKEYLTKTDARRALKGDVNLISRIHEFLERWGLIN 77
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
75-117 7.22e-08

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


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 48.76  E-value: 7.22e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 528501428    75 WTAQEEMALLEAVMDCGFGNWQDVAYQMRSKTKEECEGHYMKN 117
Cdd:smart00717   4 WTEEEDELLIELVKKYGKNNWEKIAKELPGRTAEQCRERWRNL 46
 
Name Accession Description Interval E-value
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
28-442 1.26e-65

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


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 216.86  E-value: 1.26e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501428  28 YIKCAECgpSPFLLCLQCFTRGYEYKKHQSDHKYEIM-TSDFPVLESGWTAQEEMALLEAVMDCGFGNWQDVAYQMRSKT 106
Cdd:COG5114   20 FIKCNEC--PAVDLCLPCFVNGIETGVHSPYHGYRIIeTNSYPIGEEGWGADEELLLIECLDTLGLGNWEDIADYIGSRA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501428 107 KEECEGHYMKNYINN---PLFSSTLLSLRHMDDHLSRTADTAIPFKPTDDPPRPSFDSQLSR-DMAGYMPARADFMEEFD 182
Cdd:COG5114   98 KEEIKSHYLKMYDESkyyPLPDITQNIHVPQDEFLEQRRHRIETFELPPINPRKPKASNPYChEIQGYMPGRLEFDVEYM 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501428 183 NYAEWDLKDIDFVDDDSDILHALKVAVVDIYHSRLKERQRRKKIIRDHGLINLRKFLILERRYPKEVQDLYDVMRRFARV 262
Cdd:COG5114  178 NEAEVPIKDMSFDGDKEELKKKLKNATLDIYNSRLTFRARRKHAIFGKNLMDYRNLQAKDKKRSKEECGLVNSIKWFARY 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501428 263 VGPIEHDKFIESHTLEFELRREIHRLQEYRSEGIQSFCGAKVYERVKRTREDERRKRNMLCDVLQYIHDTRACQQWLHKQ 342
Cdd:COG5114  258 LTKSDFNVFFRDILEGVYIEKRIHELQEWRNNGLTTLEAGLKYERDKFEKFGASTAASLSEGNSRYRSNSAHRSNAEYSQ 337

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501428 343 AAIDAGIApvvstistsgRRSAPPLNLTGLPGTEKLNEREKELCQVVRLVPGAYLEYKQALLNECRRQGG-LRLAQARSL 421
Cdd:COG5114  338 MDVKNILP----------SKNMTISDIQHAPDYALLSDDEQRLCETLNISPKPYLELKKEVISCFLRTRGeFTKEDFNRL 407

                        410       420
                 ....*....|....*....|.
gi 528501428 422 IKIDVNKTRKIYDFLIKEGYI 442
Cdd:COG5114  408 FGIDLGKADGLYDFFLERGWI 428
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 15-64 1.27e-16

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: 73.48  E-value: 1.27e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 528501428  15 PPCRGCSSYLVE-PYIKCAECGPspFLLCLQCFTRGYEYKKHQSDHKYEIM 64
Cdd:cd02335    1 YHCDYCSKDITGtIRIKCAECPD--FDLCLECFSAGAEIGKHRNDHNYRVV 49
SWIRM pfam04433
SWIRM domain; This SWIRM domain is a small alpha-helical domain of about 85 amino acid ...
 376-443 5.23e-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: 55.65  E-value: 5.23e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528501428  376 EKLNEREKELCQVVR----LVPGAYLEYKQALLNECRR--QGGLRLAQARSLIKIDVNKTRKIYDFLIKEGYIN 443
Cdd:pfam04433   4 DKLHPIEKRLLPEFFngksKTPEVYLEIRNFILNLWREnpKEYLTKTDARRALKGDVNLISRIHEFLERWGLIN 77
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 75-117 2.85e-08

'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: 49.50  E-value: 2.85e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 528501428  75 WTAQEEMALLEAVMDCGFGNWQDVAYQMRSKTKEECEGHYMKN 117
Cdd:cd00167    2 WTEEEDELLLEAVKKYGKNNWEKIAKELPGRTPKQCRERWRNL 44
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
75-117 7.22e-08

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


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 48.76  E-value: 7.22e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 528501428    75 WTAQEEMALLEAVMDCGFGNWQDVAYQMRSKTKEECEGHYMKN 117
Cdd:smart00717   4 WTEEEDELLIELVKKYGKNNWEKIAKELPGRTAEQCRERWRNL 46
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 17-64 2.02e-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: 47.43  E-value: 2.02e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 528501428  17 CRGCSSYLVEPYIKCAECgpSPFLLCLQCFTRGyeYKKHQSDHKYEIM 64
Cdd:cd02249    3 CDGCLKPIVGVRYHCLVC--EDFDLCSSCYAKG--KKGHPPDHSFTEI 46
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 75-117 3.34e-05

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: 40.95  E-value: 3.34e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 528501428   75 WTAQEEMALLEAVMDCGfGNWQDVAYQMRSKTKEECEGHYMKN 117
Cdd:pfam00249   4 WTPEEDELLLEAVEKLG-NRWKKIAKLLPGRTDNQCKNRWQNY 45
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 16-61 9.46e-04

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: 37.18  E-value: 9.46e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 528501428  16 PCRGCS-SYLVEPYIKCAECGPspFLLCLQCFTRGYEYKKHQSDHKY 61
Cdd:cd02345    2 SCSACRkQDISGIRFPCQVCRD--YSLCLGCYTKGRETKRHNSLHIM 46
RSC8 COG5259
RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / ...
 41-116 9.62e-04

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


Pssm-ID: 227584 [Multi-domain]  Cd Length: 531  Bit Score: 41.41  E-value: 9.62e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528501428  41 LCLQCFTRG-YEYKKHQSDHKyEIMTSDFPVlESGWTAQEEMALLEAVMDCGfGNWQDVAYQMRSKTKEECEGHYMK 116
Cdd:COG5259  249 SCSECYDQGrFPSEFTSSDFK-PVTISLLIR-DKNWSRQELLLLLEGIEMYG-DDWDKVARHVGTKTKEQCILHFLQ 322
SANT_TRF cd11660
Telomere repeat binding factor-like DNA-binding domains of the SANT/myb-like family; Human ...
 75-98 2.21e-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: 36.01  E-value: 2.21e-03
                         10        20
                 ....*....|....*....|....
gi 528501428  75 WTAQEEMALLEAVMDCGFGNWQDV 98
Cdd:cd11660    3 WTDEEDEALVEGVEKYGVGNWAKI 26
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH