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Conserved domains on  [gi|334185172|ref|NP_001189840|]
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ADA2 2A [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];
51-555 9.47e-68

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: 225.33  E-value: 9.47e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185172  51 YCCNYCDKDLSGLVRFKCAVCMDFDLCVECFSVGVELNRHKNSHPYRVMvsfqrraDNLSFSLVTSDWNADEEILLLEAI 130
Cdd:COG5114    6 IHCDVCFLDMTDLTFIKCNECPAVDLCLPCFVNGIETGVHSPYHGYRII-------ETNSYPIGEEGWGADEELLLIECL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185172 131 ATYGFGNWKEVADHVGSKTTTECIKHFNSAYMQSPCFPLPDLSHTIGKSKDELLAMSKDSAVKTEIPAFVRLSPKEELPV 210
Cdd:COG5114   79 DTLGLGNWEDIADYIGSRAKEEIKSHYLKMYDESKYYPLPDITQNIHVPQDEFLEQRRHRIETFELPPINPRKPKASNPY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185172 211 SAEIKheasgkvneidpplsalagvkkkgnvpqakdiikleaakqqsdrsvgekklrlpgekvplvtelyGYNLKREEFE 290
Cdd:COG5114  159 CHEIQ-----------------------------------------------------------------GYMPGRLEFD 173

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185172 291 IEHDNDAEQLLADMEFKDSDTDAEREQKLQVLRIYSKRLDERKRRKEFVLERNLL---YPDQYEMSLSAEERKIYKSCKV 367
Cdd:COG5114  174 VEYMNEAEVPIKDMSFDGDKEELKKKLKNATLDIYNSRLTFRARRKHAIFGKNLMdyrNLQAKDKKRSKEECGLVNSIKW 253

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185172 368 FARFQSKEEHKELIKKVIEEHQILRRIEDLQEARTAGCRTTSDANR--------FIEEKRKKEAEESMLLRLNHGAPGSI 439
Cdd:COG5114  254 FARYLTKSDFNVFFRDILEGVYIEKRIHELQEWRNNGLTTLEAGLKyerdkfekFGASTAASLSEGNSRYRSNSAHRSNA 333

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185172 440 AGKTLKSPRGLPRNlhpfgsdslpKVTPPRIYSGLDTwdvdgllgaDLLSETEKKMCNETRILPVHYLKMLDILTRE-IK 518
Cdd:COG5114  334 EYSQMDVKNILPSK----------NMTISDIQHAPDY---------ALLSDDEQRLCETLNISPKPYLELKKEVISCfLR 394

                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 334185172 519 KGQIKKKSDAYSFFKVEPSKVDRVYDMLVHKG-IGDST 555
Cdd:COG5114  395 TRGEFTKEDFNRLFGIDLGKADGLYDFFLERGwIHEEK 432
rpoC2 super family cl35188
DNA-directed RNA polymerase subunit beta'; Provisional
 240-320 8.87e-03

DNA-directed RNA polymerase subunit beta'; Provisional


The actual alignment was detected with superfamily member PRK02597:

Pssm-ID: 235052 [Multi-domain]  Cd Length: 1331  Bit Score: 39.21  E-value: 8.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185172  240 NVPQAKDIIKLEAAKQQSDRSVGEKKL-RLP---GEKVPLVTelyGYNLKREEFEIEHDNDAEQLLADMEFKDsDTDAER 315
Cdd:PRK02597  739 TIPDEPQVPSQGSVKQEKGRSIGLRAVqRLPykdGERVKSVE---GVELLRTQLVLEIFDTTPQLTADIELIP-DEKDKE 814


                  ....*
gi 334185172  316 EQKLQ 320
Cdd:PRK02597  815 IQRLQ 819
 
Name Accession Description Interval E-value
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
51-555 9.47e-68

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


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 225.33  E-value: 9.47e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185172  51 YCCNYCDKDLSGLVRFKCAVCMDFDLCVECFSVGVELNRHKNSHPYRVMvsfqrraDNLSFSLVTSDWNADEEILLLEAI 130
Cdd:COG5114    6 IHCDVCFLDMTDLTFIKCNECPAVDLCLPCFVNGIETGVHSPYHGYRII-------ETNSYPIGEEGWGADEELLLIECL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185172 131 ATYGFGNWKEVADHVGSKTTTECIKHFNSAYMQSPCFPLPDLSHTIGKSKDELLAMSKDSAVKTEIPAFVRLSPKEELPV 210
Cdd:COG5114   79 DTLGLGNWEDIADYIGSRAKEEIKSHYLKMYDESKYYPLPDITQNIHVPQDEFLEQRRHRIETFELPPINPRKPKASNPY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185172 211 SAEIKheasgkvneidpplsalagvkkkgnvpqakdiikleaakqqsdrsvgekklrlpgekvplvtelyGYNLKREEFE 290
Cdd:COG5114  159 CHEIQ-----------------------------------------------------------------GYMPGRLEFD 173

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185172 291 IEHDNDAEQLLADMEFKDSDTDAEREQKLQVLRIYSKRLDERKRRKEFVLERNLL---YPDQYEMSLSAEERKIYKSCKV 367
Cdd:COG5114  174 VEYMNEAEVPIKDMSFDGDKEELKKKLKNATLDIYNSRLTFRARRKHAIFGKNLMdyrNLQAKDKKRSKEECGLVNSIKW 253

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185172 368 FARFQSKEEHKELIKKVIEEHQILRRIEDLQEARTAGCRTTSDANR--------FIEEKRKKEAEESMLLRLNHGAPGSI 439
Cdd:COG5114  254 FARYLTKSDFNVFFRDILEGVYIEKRIHELQEWRNNGLTTLEAGLKyerdkfekFGASTAASLSEGNSRYRSNSAHRSNA 333

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185172 440 AGKTLKSPRGLPRNlhpfgsdslpKVTPPRIYSGLDTwdvdgllgaDLLSETEKKMCNETRILPVHYLKMLDILTRE-IK 518
Cdd:COG5114  334 EYSQMDVKNILPSK----------NMTISDIQHAPDY---------ALLSDDEQRLCETLNISPKPYLELKKEVISCfLR 394

                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 334185172 519 KGQIKKKSDAYSFFKVEPSKVDRVYDMLVHKG-IGDST 555
Cdd:COG5114  395 TRGEFTKEDFNRLFGIDLGKADGLYDFFLERGwIHEEK 432
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 51-99 3.60e-24

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: 95.05  E-value: 3.60e-24
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 334185172  51 YCCNYCDKDLSGLVRFKCAVCMDFDLCVECFSVGVELNRHKNSHPYRVM 99
Cdd:cd02335    1 YHCDYCSKDITGTIRIKCAECPDFDLCLECFSAGAEIGKHRNDHNYRVV 49
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 51-91 1.27e-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: 56.68  E-value: 1.27e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 334185172    51 YCCNYCDKDLSGlVRFKCAVCMDFDLCVECFSVGVELNRHK 91
Cdd:smart00291   5 YSCDTCGKPIVG-VRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 118-159 2.91e-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: 52.89  E-value: 2.91e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 334185172  118 WNADEEILLLEAIATYGfGNWKEVADHVGSKTTTECIKHFNS 159
Cdd:pfam00249   4 WTPEEDELLLEAVEKLG-NRWKKIAKLLPGRTDNQCKNRWQN 44
rpoC2 PRK02597
DNA-directed RNA polymerase subunit beta'; Provisional
 240-320 8.87e-03

DNA-directed RNA polymerase subunit beta'; Provisional


Pssm-ID: 235052 [Multi-domain]  Cd Length: 1331  Bit Score: 39.21  E-value: 8.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185172  240 NVPQAKDIIKLEAAKQQSDRSVGEKKL-RLP---GEKVPLVTelyGYNLKREEFEIEHDNDAEQLLADMEFKDsDTDAER 315
Cdd:PRK02597  739 TIPDEPQVPSQGSVKQEKGRSIGLRAVqRLPykdGERVKSVE---GVELLRTQLVLEIFDTTPQLTADIELIP-DEKDKE 814


                  ....*
gi 334185172  316 EQKLQ 320
Cdd:PRK02597  815 IQRLQ 819
 
Name Accession Description Interval E-value
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
51-555 9.47e-68

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


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 225.33  E-value: 9.47e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185172  51 YCCNYCDKDLSGLVRFKCAVCMDFDLCVECFSVGVELNRHKNSHPYRVMvsfqrraDNLSFSLVTSDWNADEEILLLEAI 130
Cdd:COG5114    6 IHCDVCFLDMTDLTFIKCNECPAVDLCLPCFVNGIETGVHSPYHGYRII-------ETNSYPIGEEGWGADEELLLIECL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185172 131 ATYGFGNWKEVADHVGSKTTTECIKHFNSAYMQSPCFPLPDLSHTIGKSKDELLAMSKDSAVKTEIPAFVRLSPKEELPV 210
Cdd:COG5114   79 DTLGLGNWEDIADYIGSRAKEEIKSHYLKMYDESKYYPLPDITQNIHVPQDEFLEQRRHRIETFELPPINPRKPKASNPY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185172 211 SAEIKheasgkvneidpplsalagvkkkgnvpqakdiikleaakqqsdrsvgekklrlpgekvplvtelyGYNLKREEFE 290
Cdd:COG5114  159 CHEIQ-----------------------------------------------------------------GYMPGRLEFD 173

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185172 291 IEHDNDAEQLLADMEFKDSDTDAEREQKLQVLRIYSKRLDERKRRKEFVLERNLL---YPDQYEMSLSAEERKIYKSCKV 367
Cdd:COG5114  174 VEYMNEAEVPIKDMSFDGDKEELKKKLKNATLDIYNSRLTFRARRKHAIFGKNLMdyrNLQAKDKKRSKEECGLVNSIKW 253

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185172 368 FARFQSKEEHKELIKKVIEEHQILRRIEDLQEARTAGCRTTSDANR--------FIEEKRKKEAEESMLLRLNHGAPGSI 439
Cdd:COG5114  254 FARYLTKSDFNVFFRDILEGVYIEKRIHELQEWRNNGLTTLEAGLKyerdkfekFGASTAASLSEGNSRYRSNSAHRSNA 333

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185172 440 AGKTLKSPRGLPRNlhpfgsdslpKVTPPRIYSGLDTwdvdgllgaDLLSETEKKMCNETRILPVHYLKMLDILTRE-IK 518
Cdd:COG5114  334 EYSQMDVKNILPSK----------NMTISDIQHAPDY---------ALLSDDEQRLCETLNISPKPYLELKKEVISCfLR 394

                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 334185172 519 KGQIKKKSDAYSFFKVEPSKVDRVYDMLVHKG-IGDST 555
Cdd:COG5114  395 TRGEFTKEDFNRLFGIDLGKADGLYDFFLERGwIHEEK 432
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 51-99 3.60e-24

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: 95.05  E-value: 3.60e-24
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 334185172  51 YCCNYCDKDLSGLVRFKCAVCMDFDLCVECFSVGVELNRHKNSHPYRVM 99
Cdd:cd02335    1 YHCDYCSKDITGTIRIKCAECPDFDLCLECFSAGAEIGKHRNDHNYRVV 49
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 51-96 3.21e-12

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: 61.30  E-value: 3.21e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 334185172  51 YCCNYCDKDLSGlVRFKCAVCMDFDLCVECFSVGVElnRHKNSHPY 96
Cdd:cd02249    1 YSCDGCLKPIVG-VRYHCLVCEDFDLCSSCYAKGKK--GHPPDHSF 43
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 118-158 8.99e-11

'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: 56.81  E-value: 8.99e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 334185172 118 WNADEEILLLEAIATYGFGNWKEVADHVGSKTTTECIKHFN 158
Cdd:cd00167    2 WTEEEDELLLEAVKKYGKNNWEKIAKELPGRTPKQCRERWR 42
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 51-91 1.27e-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: 56.68  E-value: 1.27e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 334185172    51 YCCNYCDKDLSGlVRFKCAVCMDFDLCVECFSVGVELNRHK 91
Cdd:smart00291   5 YSCDTCGKPIVG-VRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
118-158 3.98e-10

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


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 55.31  E-value: 3.98e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 334185172   118 WNADEEILLLEAIATYGFGNWKEVADHVGSKTTTECIKHFN 158
Cdd:smart00717   4 WTEEEDELLIELVKKYGKNNWEKIAKELPGRTAEQCRERWR 44
RSC8 COG5259
RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / ...
 73-157 1.53e-09

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


Pssm-ID: 227584 [Multi-domain]  Cd Length: 531  Bit Score: 60.28  E-value: 1.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185172  73 DFDLCVECFSVGVeLNRHKNSHPYRvmvsfqrRADNLSFSlVTSDWNADEEILLLEAIATYGfGNWKEVADHVGSKTTTE 152
Cdd:COG5259  246 KYNSCSECYDQGR-FPSEFTSSDFK-------PVTISLLI-RDKNWSRQELLLLLEGIEMYG-DDWDKVARHVGTKTKEQ 315


                 ....*
gi 334185172 153 CIKHF 157
Cdd:COG5259  316 CILHF 320
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 118-159 2.91e-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: 52.89  E-value: 2.91e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 334185172  118 WNADEEILLLEAIATYGfGNWKEVADHVGSKTTTECIKHFNS 159
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 ...
 52-95 3.23e-08

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: 50.04  E-value: 3.23e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 334185172  52 CCNYCDK-DLSGlVRFKCAVCMDFDLCVECFSVGVELNRHKNSHP 95
Cdd:cd02338    2 SCDGCGKsNFTG-RRYKCLICYDYDLCADCYDSGVTTERHLFDHP 45
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 53-94 1.03e-07

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: 48.35  E-value: 1.03e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 334185172  53 CNYCDKDLSGLVRFKCAVCMDFDLCVECFSVGVELNRHKNSH 94
Cdd:cd02345    3 CSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLH 44
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 52-100 1.73e-07

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: 47.64  E-value: 1.73e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 334185172  52 CCNYCDKDLSGlVRFKCAVCMDFDLCVECFSvgvelnrhKNSHPYRVMV 100
Cdd:cd02340    2 ICDGCQGPIVG-VRYKCLVCPDYDLCESCEA--------KGVHPEHAML 41
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 51-82 7.61e-06

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: 43.24  E-value: 7.61e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 334185172   51 YCCNYCDKDLSGLVRFKCAVCMDFDLCVECFS 82
Cdd:pfam00569   5 YTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQ 36
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 53-95 1.61e-05

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: 42.34  E-value: 1.61e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 334185172  53 CNYCDKD-LSGLvRFKCAVCMDFDLCVECFSVGVELNRHKNSHP 95
Cdd:cd02334    3 CNICKEFpITGF-RYRCLKCFNYDLCQSCFFSGRTSKSHKNSHP 45
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 53-96 1.68e-05

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: 42.06  E-value: 1.68e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 334185172  53 CNYCDKDLSGLVRFKCAVCMDFDLCVECFSVgvelNRHKNSHPY 96
Cdd:cd02339    3 CDTCRKQGIIGIRWKCAECPNYDLCTTCYHG----DKHDLEHRF 42
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 51-97 5.88e-05

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: 40.62  E-value: 5.88e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 334185172  51 YCCNYCDkdLSGLVRFKCAVCMDFDLCVECFSvgvelnrhKNSHPYR 97
Cdd:cd02337    1 YTCNECK--HHVETRWHCTVCEDYDLCITCYN--------TKNHPHK 37
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
 51-94 3.72e-04

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: 38.57  E-value: 3.72e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 334185172  51 YCCNYCDKDLSGLVRFKCAVC--MDFDLCVECFSVGVelnRHKNSH 94
Cdd:cd02341    1 FKCDSCGIEPIPGTRYHCSECddGDFDLCQDCVVKGE---SHQEDH 43
ZZ_EF cd02343
Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif ...
 53-94 1.95e-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: 36.52  E-value: 1.95e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 334185172  53 CNYCDKdLSGLVRFKCAVCMDFDLCVECFSVGVELNRHKNSH 94
Cdd:cd02343    3 CDGCDE-IAPWHRYRCLQCTDMDLCKTCFLGGVKPEGHEDDH 43
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 53-90 5.77e-03

Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential E3 ubiquitin protein ligase and/or guanine nucleotide exchange factor. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239084  Cd Length: 45  Bit Score: 34.87  E-value: 5.77e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 334185172  53 CNYCDKDLSGLVRFKCAVCMDFDLCVECFSVGVELNRH 90
Cdd:cd02344    3 CDGCQMFPINGPRFKCRNCDDFDFCENCFKTRKHNTRH 40
rpoC2 PRK02597
DNA-directed RNA polymerase subunit beta'; Provisional
 240-320 8.87e-03

DNA-directed RNA polymerase subunit beta'; Provisional


Pssm-ID: 235052 [Multi-domain]  Cd Length: 1331  Bit Score: 39.21  E-value: 8.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185172  240 NVPQAKDIIKLEAAKQQSDRSVGEKKL-RLP---GEKVPLVTelyGYNLKREEFEIEHDNDAEQLLADMEFKDsDTDAER 315
Cdd:PRK02597  739 TIPDEPQVPSQGSVKQEKGRSIGLRAVqRLPykdGERVKSVE---GVELLRTQLVLEIFDTTPQLTADIELIP-DEKDKE 814


                  ....*
gi 334185172  316 EQKLQ 320
Cdd:PRK02597  815 IQRLQ 819
 
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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