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Conserved domains on  [gi|78706696|ref|NP_001027151|]
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transcriptional adaptor 2b, isoform B [Drosophila melanogaster]

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];
10-341 3.67e-40

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: 150.99  E-value: 3.67e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706696  10 KYNCTNCQDDI-QGIRVHCAECENFDLCLQCFAAGAEIGAHQNNHSYQFMDTGTSILsvfrGKGAWTAREEIRLLDAIEQ 88
Cdd:COG5114   5 KIHCDVCFLDMtDLTFIKCNECPAVDLCLPCFVNGIETGVHSPYHGYRIIETNSYPI----GEEGWGADEELLLIECLDT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706696  89 YGFGNWEDISKHIETKSAEDAKEEYVNKFVngtigRATWTPAQSqrPRLIDHTGDDDAGPLGTNALSTLPPLEINSDEAM 168
Cdd:COG5114  81 LGLGNWEDIADYIGSRAKEEIKSHYLKMYD-----ESKYYPLPD--ITQNIHVPQDEFLEQRRHRIETFELPPINPRKPK 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706696 169 Q--------LGYMPNRDSFEREYDPTAEQLISNISLSSEDTEVDVMLKLAHVDIYTRRLRERARRKRMVRDYQLVSnfFR 240
Cdd:COG5114 154 AsnpycheiQGYMPGRLEFDVEYMNEAEVPIKDMSFDGDKEELKKKLKNATLDIYNSRLTFRARRKHAIFGKNLMD--YR 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706696 241 NRNyAQQQGLTKEQREFRDRFRVYAQFYTCNEYERLLGSLEREKELRIRQSELYRYRYNGLTKIAECTHFEQHAATATHR 320
Cdd:COG5114 232 NLQ-AKDKKRSKEECGLVNSIKWFARYLTKSDFNVFFRDILEGVYIEKRIHELQEWRNNGLTTLEAGLKYERDKFEKFGA 310

                       330       340
                ....*....|....*....|.
gi 78706696 321 STGPYGHGKtDHTHTSNGSHR 341
Cdd:COG5114 311 STAASLSEG-NSRYRSNSAHR 330
 
Name Accession Description Interval E-value
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
10-341 3.67e-40

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


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 150.99  E-value: 3.67e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706696  10 KYNCTNCQDDI-QGIRVHCAECENFDLCLQCFAAGAEIGAHQNNHSYQFMDTGTSILsvfrGKGAWTAREEIRLLDAIEQ 88
Cdd:COG5114   5 KIHCDVCFLDMtDLTFIKCNECPAVDLCLPCFVNGIETGVHSPYHGYRIIETNSYPI----GEEGWGADEELLLIECLDT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706696  89 YGFGNWEDISKHIETKSAEDAKEEYVNKFVngtigRATWTPAQSqrPRLIDHTGDDDAGPLGTNALSTLPPLEINSDEAM 168
Cdd:COG5114  81 LGLGNWEDIADYIGSRAKEEIKSHYLKMYD-----ESKYYPLPD--ITQNIHVPQDEFLEQRRHRIETFELPPINPRKPK 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706696 169 Q--------LGYMPNRDSFEREYDPTAEQLISNISLSSEDTEVDVMLKLAHVDIYTRRLRERARRKRMVRDYQLVSnfFR 240
Cdd:COG5114 154 AsnpycheiQGYMPGRLEFDVEYMNEAEVPIKDMSFDGDKEELKKKLKNATLDIYNSRLTFRARRKHAIFGKNLMD--YR 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706696 241 NRNyAQQQGLTKEQREFRDRFRVYAQFYTCNEYERLLGSLEREKELRIRQSELYRYRYNGLTKIAECTHFEQHAATATHR 320
Cdd:COG5114 232 NLQ-AKDKKRSKEECGLVNSIKWFARYLTKSDFNVFFRDILEGVYIEKRIHELQEWRNNGLTTLEAGLKYERDKFEKFGA 310

                       330       340
                ....*....|....*....|.
gi 78706696 321 STGPYGHGKtDHTHTSNGSHR 341
Cdd:COG5114 311 STAASLSEG-NSRYRSNSAHR 330
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 11-58 6.68e-22

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: 88.89  E-value: 6.68e-22
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 78706696  11 YNCTNCQDDI-QGIRVHCAECENFDLCLQCFAAGAEIGAHQNNHSYQFM 58
Cdd:cd02335   1 YHCDYCSKDItGTIRIKCAECPDFDLCLECFSAGAEIGKHRNDHNYRVV 49
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 10-54 4.65e-10

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: 55.14  E-value: 4.65e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 78706696     10 KYNCTNCQDDIQGIRVHCAECENFDLCLQCFAAgaeiGAHQNNHS 54
Cdd:smart00291   4 SYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAK----GSAGGEHS 44
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 71-115 2.68e-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: 49.81  E-value: 2.68e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 78706696    71 KGAWTAREEIRLLDAIEQYGfGNWEDISKHIETKSAEDAKEEYVN 115
Cdd:pfam00249   1 RGPWTPEEDELLLEAVEKLG-NRWKKIAKLLPGRTDNQCKNRWQN 44
 
Name Accession Description Interval E-value
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
10-341 3.67e-40

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


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 150.99  E-value: 3.67e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706696  10 KYNCTNCQDDI-QGIRVHCAECENFDLCLQCFAAGAEIGAHQNNHSYQFMDTGTSILsvfrGKGAWTAREEIRLLDAIEQ 88
Cdd:COG5114   5 KIHCDVCFLDMtDLTFIKCNECPAVDLCLPCFVNGIETGVHSPYHGYRIIETNSYPI----GEEGWGADEELLLIECLDT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706696  89 YGFGNWEDISKHIETKSAEDAKEEYVNKFVngtigRATWTPAQSqrPRLIDHTGDDDAGPLGTNALSTLPPLEINSDEAM 168
Cdd:COG5114  81 LGLGNWEDIADYIGSRAKEEIKSHYLKMYD-----ESKYYPLPD--ITQNIHVPQDEFLEQRRHRIETFELPPINPRKPK 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706696 169 Q--------LGYMPNRDSFEREYDPTAEQLISNISLSSEDTEVDVMLKLAHVDIYTRRLRERARRKRMVRDYQLVSnfFR 240
Cdd:COG5114 154 AsnpycheiQGYMPGRLEFDVEYMNEAEVPIKDMSFDGDKEELKKKLKNATLDIYNSRLTFRARRKHAIFGKNLMD--YR 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706696 241 NRNyAQQQGLTKEQREFRDRFRVYAQFYTCNEYERLLGSLEREKELRIRQSELYRYRYNGLTKIAECTHFEQHAATATHR 320
Cdd:COG5114 232 NLQ-AKDKKRSKEECGLVNSIKWFARYLTKSDFNVFFRDILEGVYIEKRIHELQEWRNNGLTTLEAGLKYERDKFEKFGA 310

                       330       340
                ....*....|....*....|.
gi 78706696 321 STGPYGHGKtDHTHTSNGSHR 341
Cdd:COG5114 311 STAASLSEG-NSRYRSNSAHR 330
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 11-58 6.68e-22

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: 88.89  E-value: 6.68e-22
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 78706696  11 YNCTNCQDDI-QGIRVHCAECENFDLCLQCFAAGAEIGAHQNNHSYQFM 58
Cdd:cd02335   1 YHCDYCSKDItGTIRIKCAECPDFDLCLECFSAGAEIGKHRNDHNYRVV 49
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 11-58 1.52e-13

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: 64.76  E-value: 1.52e-13
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 78706696  11 YNCTNCQDDIQGIRVHCAECENFDLCLQCFAAGAEIgaHQNNHSYQFM 58
Cdd:cd02249   1 YSCDGCLKPIVGVRYHCLVCEDFDLCSSCYAKGKKG--HPPDHSFTEI 46
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 10-54 4.65e-10

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: 55.14  E-value: 4.65e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 78706696     10 KYNCTNCQDDIQGIRVHCAECENFDLCLQCFAAgaeiGAHQNNHS 54
Cdd:smart00291   4 SYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAK----GSAGGEHS 44
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
71-115 6.30e-10

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


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 54.54  E-value: 6.30e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 78706696     71 KGAWTAREEIRLLDAIEQYGFGNWEDISKHIETKSAEDAKEEYVN 115
Cdd:smart00717   1 KGEWTEEEDELLIELVKKYGKNNWEKIAKELPGRTAEQCRERWRN 45
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 73-115 1.50e-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: 53.35  E-value: 1.50e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 78706696  73 AWTAREEIRLLDAIEQYGFGNWEDISKHIETKSAEDAKEEYVN 115
Cdd:cd00167   1 PWTEEEDELLLEAVKKYGKNNWEKIAKELPGRTPKQCRERWRN 43
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 71-115 2.68e-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: 49.81  E-value: 2.68e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 78706696    71 KGAWTAREEIRLLDAIEQYGfGNWEDISKHIETKSAEDAKEEYVN 115
Cdd:pfam00249   1 RGPWTPEEDELLLEAVEKLG-NRWKKIAKLLPGRTDNQCKNRWQN 44
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 13-43 4.09e-08

Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.


Pssm-ID: 239080  Cd Length: 43  Bit Score: 49.57  E-value: 4.09e-08
                        10        20        30
                ....*....|....*....|....*....|.
gi 78706696  13 CTNCQDDIQGIRVHCAECENFDLCLQCFAAG 43
Cdd:cd02340   3 CDGCQGPIVGVRYKCLVCPDYDLCESCEAKG 33
Myb_DNA-bind_6 pfam13921
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 74-134 7.77e-07

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


Pssm-ID: 372817 [Multi-domain]  Cd Length: 60  Bit Score: 46.15  E-value: 7.77e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78706696    74 WTAREEIRLLDAIEQYGFgNWEDISKHIETKSAEDAKEEYVNKFvNGTIGRATWTPAQSQR 134
Cdd:pfam13921   1 WTEEEDEKLLKLVEKYGN-DWKQIAKELGRRTPKQCFDRWRRKL-NPKISRGPWSKEEDQR 59
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 13-53 1.10e-06

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: 45.66  E-value: 1.10e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 78706696  13 CTNCQ-DDIQGIRVHCAECENFDLCLQCFAAGAEIGAHQNNH 53
Cdd:cd02345   3 CSACRkQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLH 44
RSC8 COG5259
RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / ...
 11-115 5.87e-06

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


Pssm-ID: 227584 [Multi-domain]  Cd Length: 531  Bit Score: 49.11  E-value: 5.87e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706696  11 YNCTNCQDDIQGIRVHCAECENFDLCLQCFAAGAeigAHQNNHSYQFMDTGTSILSVfrgKGAWTAREEIRLLDAIEQYG 90
Cdd:COG5259 225 SSCSCCGNKSFNTRYHNLRAEKYNSCSECYDQGR---FPSEFTSSDFKPVTISLLIR---DKNWSRQELLLLLEGIEMYG 298

                        90       100
                ....*....|....*....|....*
gi 78706696  91 fGNWEDISKHIETKSAEDAKEEYVN 115
Cdd:COG5259 299 -DDWDKVARHVGTKTKEQCILHFLQ 322
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 13-53 5.93e-06

Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.


Pssm-ID: 239074  Cd Length: 49  Bit Score: 43.50  E-value: 5.93e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 78706696  13 CTNCQDD-IQGIRVHCAECENFDLCLQCFAAGAEIGAHQNNH 53
Cdd:cd02334   3 CNICKEFpITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSH 44
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 13-57 1.33e-05

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: 42.33  E-value: 1.33e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 78706696  13 CTNCQD-DIQGIRVHCAECENFDLCLQCFAAGAEIGAHQNNHSYQF 57
Cdd:cd02338   3 CDGCGKsNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDHPMQC 48
SANT_TRF cd11660
Telomere repeat binding factor-like DNA-binding domains of the SANT/myb-like family; Human ...
 74-115 4.34e-05

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: 41.01  E-value: 4.34e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 78706696  74 WTAREEIRLLDAIEQYGFGNWEDISKH---IETKSAEDAKEEYVN 115
Cdd:cd11660   3 WTDEEDEALVEGVEKYGVGNWAKILKDyffVNNRTSVDLKDKWRN 47
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
 11-53 6.09e-05

Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239081  Cd Length: 48  Bit Score: 40.49  E-value: 6.09e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 78706696  11 YNCTNC-QDDIQGIRVHCAECEN--FDLCLQCFAAGaeiGAHQNNH 53
Cdd:cd02341   1 FKCDSCgIEPIPGTRYHCSECDDgdFDLCQDCVVKG---ESHQEDH 43
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 13-41 1.14e-04

Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster.


Pssm-ID: 239079  Cd Length: 45  Bit Score: 39.75  E-value: 1.14e-04
                        10        20        30
                ....*....|....*....|....*....|
gi 78706696  13 CTNCQDD-IQGIRVHCAECENFDLCLQCFA 41
Cdd:cd02339   3 CDTCRKQgIIGIRWKCAECPNYDLCTTCYH 32
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 10-40 1.95e-04

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 39.00  E-value: 1.95e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 78706696    10 KYNCTNCQ-DDIQGIRVHCAECENFDLCLQCF 40
Cdd:pfam00569   4 VYTCNGCSnDPSIGVRYHCLRCSDYDLCQSCF 35
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 11-40 4.56e-03

Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear.


Pssm-ID: 239077  Cd Length: 41  Bit Score: 35.23  E-value: 4.56e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 78706696  11 YNCTNCQDDIQgIRVHCAECENFDLCLQCF 40
Cdd:cd02337   1 YTCNECKHHVE-TRWHCTVCEDYDLCITCY 29
ZZ_EF cd02343
Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif ...
 12-53 5.50e-03

Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239083  Cd Length: 48  Bit Score: 34.98  E-value: 5.50e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 78706696  12 NCTNCQDDIQGIRVHCAECENFDLCLQCFAAGAEIGAHQNNH 53
Cdd:cd02343   2 SCDGCDEIAPWHRYRCLQCTDMDLCKTCFLGGVKPEGHEDDH 43
 
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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