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Conserved domains on  [gi|42572929|ref|NP_974561|]
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ADA2 2B [Arabidopsis thaliana]

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];
41-482 1.56e-80

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: 256.92  E-value: 1.56e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572929  41 GGGKYNCDYCQKDITGKIRIKCAVCPDFDLCIECMSVGAEITPHKCDHPYRVMGNLTFPLICPDWSADDEMLLLEGLEIY 120
Cdd:COG5114   2 GGVKIHCDVCFLDMTDLTFIKCNECPAVDLCLPCFVNGIETGVHSPYHGYRIIETNSYPIGEEGWGADEELLLIECLDTL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572929 121 GLGNWAEVAEHVGTKSKEQCLEHYRNIYLNSPFFPLPDMSHVAGKNRKELQAMAKGRIddkkeqnmkeeypfsppkvkve 200
Cdd:COG5114  82 GLGNWEDIADYIGSRAKEEIKSHYLKMYDESKYYPLPDITQNIHVPQDEFLEQRRHRI---------------------- 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572929 201 dtqkESFVDRSFGGKKPVSTsvNNSLVELSNYNQKREEFDPEYDNDAEQLLAEMEFKENDTPEEHELKLRVLRIYSKRLD 280
Cdd:COG5114 140 ----ETFELPPINPRKPKAS--NPYCHEIQGYMPGRLEFDVEYMNEAEVPIKDMSFDGDKEELKKKLKNATLDIYNSRLT 213

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572929 281 ERKRRKEFIIERNLL-YPN--PFEKDLSQEEKVQCRRLDVFMRFHSKEEHDELLRNVVSEYRMVKRLKDLKEAqvagcRS 357
Cdd:COG5114 214 FRARRKHAIFGKNLMdYRNlqAKDKKRSKEECGLVNSIKWFARYLTKSDFNVFFRDILEGVYIEKRIHELQEW-----RN 288

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572929 358 TAEAERYLGRKRKRENEEGMNRGKESGQFGQIAGEMGSRPPVQASSSYVNDLDLIG------------FTESQLLSESEK 425
Cdd:COG5114 289 NGLTTLEAGLKYERDKFEKFGASTAASLSEGNSRYRSNSAHRSNAEYSQMDVKNILpsknmtisdiqhAPDYALLSDDEQ 368

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42572929 426 RLCSEVKLVPPVYLQMQQVMSHEIFK--GNVTkKSDAYSLFKIDPTKVDRVYDMLVKKG 482
Cdd:COG5114 369 RLCETLNISPKPYLELKKEVISCFLRtrGEFT-KEDFNRLFGIDLGKADGLYDFFLERG 426
 
Name Accession Description Interval E-value
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
41-482 1.56e-80

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


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 256.92  E-value: 1.56e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572929  41 GGGKYNCDYCQKDITGKIRIKCAVCPDFDLCIECMSVGAEITPHKCDHPYRVMGNLTFPLICPDWSADDEMLLLEGLEIY 120
Cdd:COG5114   2 GGVKIHCDVCFLDMTDLTFIKCNECPAVDLCLPCFVNGIETGVHSPYHGYRIIETNSYPIGEEGWGADEELLLIECLDTL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572929 121 GLGNWAEVAEHVGTKSKEQCLEHYRNIYLNSPFFPLPDMSHVAGKNRKELQAMAKGRIddkkeqnmkeeypfsppkvkve 200
Cdd:COG5114  82 GLGNWEDIADYIGSRAKEEIKSHYLKMYDESKYYPLPDITQNIHVPQDEFLEQRRHRI---------------------- 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572929 201 dtqkESFVDRSFGGKKPVSTsvNNSLVELSNYNQKREEFDPEYDNDAEQLLAEMEFKENDTPEEHELKLRVLRIYSKRLD 280
Cdd:COG5114 140 ----ETFELPPINPRKPKAS--NPYCHEIQGYMPGRLEFDVEYMNEAEVPIKDMSFDGDKEELKKKLKNATLDIYNSRLT 213

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572929 281 ERKRRKEFIIERNLL-YPN--PFEKDLSQEEKVQCRRLDVFMRFHSKEEHDELLRNVVSEYRMVKRLKDLKEAqvagcRS 357
Cdd:COG5114 214 FRARRKHAIFGKNLMdYRNlqAKDKKRSKEECGLVNSIKWFARYLTKSDFNVFFRDILEGVYIEKRIHELQEW-----RN 288

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572929 358 TAEAERYLGRKRKRENEEGMNRGKESGQFGQIAGEMGSRPPVQASSSYVNDLDLIG------------FTESQLLSESEK 425
Cdd:COG5114 289 NGLTTLEAGLKYERDKFEKFGASTAASLSEGNSRYRSNSAHRSNAEYSQMDVKNILpsknmtisdiqhAPDYALLSDDEQ 368

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42572929 426 RLCSEVKLVPPVYLQMQQVMSHEIFK--GNVTkKSDAYSLFKIDPTKVDRVYDMLVKKG 482
Cdd:COG5114 369 RLCETLNISPKPYLELKKEVISCFLRtrGEFT-KEDFNRLFGIDLGKADGLYDFFLERG 426
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 45-93 2.46e-26

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: 100.83  E-value: 2.46e-26
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 42572929  45 YNCDYCQKDITGKIRIKCAVCPDFDLCIECMSVGAEITPHKCDHPYRVM 93
Cdd:cd02335   1 YHCDYCSKDITGTIRIKCAECPDFDLCLECFSAGAEIGKHRNDHNYRVV 49
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 44-85 6.03e-12

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: 60.15  E-value: 6.03e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 42572929     44 KYNCDYCQKDITGkIRIKCAVCPDFDLCIECMSVGAEITPHK 85
Cdd:smart00291   4 SYSCDTCGKPIVG-VRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 105-146 4.81e-09

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: 52.12  E-value: 4.81e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 42572929   105 WSADDEMLLLEGLEIYGlGNWAEVAEHVGTKSKEQCLEHYRN 146
Cdd:pfam00249   4 WTPEEDELLLEAVEKLG-NRWKKIAKLLPGRTDNQCKNRWQN 44
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 165-292 1.69e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 44.15  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572929  165 KNRKELQAMAKgriddKKEQNMKEEYPFSPPKVKVEDTQKESFVDRSFGGKKpvSTSVNNSLVELSNYNQKREEFDPEYD 244
Cdd:PRK05771 107 EEISELENEIK-----ELEQEIERLEPWGNFDLDLSLLLGFKYVSVFVGTVP--EDKLEELKLESDVENVEYISTDKGYV 179

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 42572929  245 -----------NDAEQLLAEMEFKENDTPEEHELKlRVLRIYSKRLDERKRRKEFIIER 292
Cdd:PRK05771 180 yvvvvvlkelsDEVEEELKKLGFERLELEEEGTPS-ELIREIKEELEEIEKERESLLEE 237
 
Name Accession Description Interval E-value
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
41-482 1.56e-80

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


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 256.92  E-value: 1.56e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572929  41 GGGKYNCDYCQKDITGKIRIKCAVCPDFDLCIECMSVGAEITPHKCDHPYRVMGNLTFPLICPDWSADDEMLLLEGLEIY 120
Cdd:COG5114   2 GGVKIHCDVCFLDMTDLTFIKCNECPAVDLCLPCFVNGIETGVHSPYHGYRIIETNSYPIGEEGWGADEELLLIECLDTL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572929 121 GLGNWAEVAEHVGTKSKEQCLEHYRNIYLNSPFFPLPDMSHVAGKNRKELQAMAKGRIddkkeqnmkeeypfsppkvkve 200
Cdd:COG5114  82 GLGNWEDIADYIGSRAKEEIKSHYLKMYDESKYYPLPDITQNIHVPQDEFLEQRRHRI---------------------- 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572929 201 dtqkESFVDRSFGGKKPVSTsvNNSLVELSNYNQKREEFDPEYDNDAEQLLAEMEFKENDTPEEHELKLRVLRIYSKRLD 280
Cdd:COG5114 140 ----ETFELPPINPRKPKAS--NPYCHEIQGYMPGRLEFDVEYMNEAEVPIKDMSFDGDKEELKKKLKNATLDIYNSRLT 213

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572929 281 ERKRRKEFIIERNLL-YPN--PFEKDLSQEEKVQCRRLDVFMRFHSKEEHDELLRNVVSEYRMVKRLKDLKEAqvagcRS 357
Cdd:COG5114 214 FRARRKHAIFGKNLMdYRNlqAKDKKRSKEECGLVNSIKWFARYLTKSDFNVFFRDILEGVYIEKRIHELQEW-----RN 288

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572929 358 TAEAERYLGRKRKRENEEGMNRGKESGQFGQIAGEMGSRPPVQASSSYVNDLDLIG------------FTESQLLSESEK 425
Cdd:COG5114 289 NGLTTLEAGLKYERDKFEKFGASTAASLSEGNSRYRSNSAHRSNAEYSQMDVKNILpsknmtisdiqhAPDYALLSDDEQ 368

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42572929 426 RLCSEVKLVPPVYLQMQQVMSHEIFK--GNVTkKSDAYSLFKIDPTKVDRVYDMLVKKG 482
Cdd:COG5114 369 RLCETLNISPKPYLELKKEVISCFLRtrGEFT-KEDFNRLFGIDLGKADGLYDFFLERG 426
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 45-93 2.46e-26

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: 100.83  E-value: 2.46e-26
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 42572929  45 YNCDYCQKDITGKIRIKCAVCPDFDLCIECMSVGAEITPHKCDHPYRVM 93
Cdd:cd02335   1 YHCDYCSKDITGTIRIKCAECPDFDLCLECFSAGAEIGKHRNDHNYRVV 49
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 45-90 3.18e-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: 63.99  E-value: 3.18e-13
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 42572929  45 YNCDYCQKDITGKiRIKCAVCPDFDLCIECMSVGAEItpHKCDHPY 90
Cdd:cd02249   1 YSCDGCLKPIVGV-RYHCLVCEDFDLCSSCYAKGKKG--HPPDHSF 43
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 44-85 6.03e-12

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: 60.15  E-value: 6.03e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 42572929     44 KYNCDYCQKDITGkIRIKCAVCPDFDLCIECMSVGAEITPHK 85
Cdd:smart00291   4 SYSCDTCGKPIVG-VRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 105-147 8.73e-12

'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: 59.51  E-value: 8.73e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 42572929 105 WSADDEMLLLEGLEIYGLGNWAEVAEHVGTKSKEQCLEHYRNI 147
Cdd:cd00167   2 WTEEEDELLLEAVKKYGKNNWEKIAKELPGRTPKQCRERWRNL 44
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
105-147 1.03e-10

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


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 56.85  E-value: 1.03e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 42572929    105 WSADDEMLLLEGLEIYGLGNWAEVAEHVGTKSKEQCLEHYRNI 147
Cdd:smart00717   4 WTEEEDELLIELVKKYGKNNWEKIAKELPGRTAEQCRERWRNL 46
RSC8 COG5259
RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / ...
 105-147 5.19e-10

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


Pssm-ID: 227584 [Multi-domain]  Cd Length: 531  Bit Score: 61.44  E-value: 5.19e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 42572929 105 WSADDEMLLLEGLEIYGlGNWAEVAEHVGTKSKEQCLEHYRNI 147
Cdd:COG5259 282 WSRQELLLLLEGIEMYG-DDWDKVARHVGTKTKEQCILHFLQL 323
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 47-74 1.20e-09

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: 53.42  E-value: 1.20e-09
                        10        20
                ....*....|....*....|....*...
gi 42572929  47 CDYCQKDITGkIRIKCAVCPDFDLCIEC 74
Cdd:cd02340   3 CDGCQGPIVG-VRYKCLVCPDYDLCESC 29
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 105-146 4.81e-09

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: 52.12  E-value: 4.81e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 42572929   105 WSADDEMLLLEGLEIYGlGNWAEVAEHVGTKSKEQCLEHYRN 146
Cdd:pfam00249   4 WTPEEDELLLEAVEKLG-NRWKKIAKLLPGRTDNQCKNRWQN 44
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 47-89 3.31e-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: 3.31e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 42572929  47 CDYCQK-DITGKiRIKCAVCPDFDLCIECMSVGAEITPHKCDHP 89
Cdd:cd02338   3 CDGCGKsNFTGR-RYKCLICYDYDLCADCYDSGVTTERHLFDHP 45
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 47-74 3.00e-06

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: 43.99  E-value: 3.00e-06
                        10        20
                ....*....|....*....|....*...
gi 42572929  47 CDYCQKDITGKIRIKCAVCPDFDLCIEC 74
Cdd:cd02339   3 CDTCRKQGIIGIRWKCAECPNYDLCTTC 30
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 47-88 1.39e-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: 42.19  E-value: 1.39e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 42572929  47 CDYCQKDITGKIRIKCAVCPDFDLCIECMSVGAEITPHKCDH 88
Cdd:cd02345   3 CSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLH 44
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 44-74 1.85e-05

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: 41.70  E-value: 1.85e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 42572929    44 KYNCDYCQKDITGKIRIKCAVCPDFDLCIEC 74
Cdd:pfam00569   4 VYTCNGCSNDPSIGVRYHCLRCSDYDLCQSC 34
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 165-292 1.69e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 44.15  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572929  165 KNRKELQAMAKgriddKKEQNMKEEYPFSPPKVKVEDTQKESFVDRSFGGKKpvSTSVNNSLVELSNYNQKREEFDPEYD 244
Cdd:PRK05771 107 EEISELENEIK-----ELEQEIERLEPWGNFDLDLSLLLGFKYVSVFVGTVP--EDKLEELKLESDVENVEYISTDKGYV 179

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 42572929  245 -----------NDAEQLLAEMEFKENDTPEEHELKlRVLRIYSKRLDERKRRKEFIIER 292
Cdd:PRK05771 180 yvvvvvlkelsDEVEEELKKLGFERLELEEEGTPS-ELIREIKEELEEIEKERESLLEE 237
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 45-85 1.90e-04

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: 38.70  E-value: 1.90e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 42572929  45 YNCDYCQKDITgkIRIKCAVCPDFDLCIECMSvgAEITPHK 85
Cdd:cd02337   1 YTCNECKHHVE--TRWHCTVCEDYDLCITCYN--TKNHPHK 37
SANT_TRF cd11660
Telomere repeat binding factor-like DNA-binding domains of the SANT/myb-like family; Human ...
 105-131 2.51e-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: 38.70  E-value: 2.51e-04
                        10        20
                ....*....|....*....|....*..
gi 42572929 105 WSADDEMLLLEGLEIYGLGNWAEVAEH 131
Cdd:cd11660   3 WTDEEDEALVEGVEKYGVGNWAKILKD 29
Myb_DNA-bind_6 pfam13921
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 105-146 8.23e-04

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: 37.67  E-value: 8.23e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 42572929   105 WSADDEMLLLEGLEIYGlGNWAEVAEHVGTKSKEQCLEHYRN 146
Cdd:pfam13921   1 WTEEEDEKLLKLVEKYG-NDWKQIAKELGRRTPKQCFDRWRR 41
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 47-89 1.01e-03

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: 36.95  E-value: 1.01e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 42572929  47 CDYCQKD-ITGkIRIKCAVCPDFDLCIECMSVGAEITPHKCDHP 89
Cdd:cd02334   3 CNICKEFpITG-FRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHP 45
 
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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