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Conserved domains on  [gi|398366605|ref|NP_010736.3|]
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TPA: chromatin-binding transcription regulator ADA2 [Saccharomyces cerevisiae S288C]

Protein Classification

COG5114 family protein (domain architecture ID 11473817)

COG5114 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
3-434 0e+00

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


:

Pssm-ID: 227445  Cd Length: 432  Bit Score: 738.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366605   3 NKFHCDVCSADCTNRVRVSCAICPEYDLCVPCFSQGSYTGKHRPYHDYRIIETNSYPILCPDWGADEELQLIKGAQTLGL 82
Cdd:COG5114    4 VKIHCDVCFLDMTDLTFIKCNECPAVDLCLPCFVNGIETGVHSPYHGYRIIETNSYPIGEEGWGADEELLLIECLDTLGL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366605  83 GNWQDIADHIGSRGKEEVKEHYLKYYLESKYYPIPDITQNIHVPQDEFLEQRRHRIESFRERPLEPpRKPMASVPSCHEV 162
Cdd:COG5114   84 GNWEDIADYIGSRAKEEIKSHYLKMYDESKYYPLPDITQNIHVPQDEFLEQRRHRIETFELPPINP-RKPKASNPYCHEI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366605 163 QGFMPGRLEFETEFENEAEGPVKDMVFEPDDQPLDIELKFAILDIYNSRLTTRAEKKRLLFENHLMDYRKLQAIDKKRSK 242
Cdd:COG5114  163 QGYMPGRLEFDVEYMNEAEVPIKDMSFDGDKEELKKKLKNATLDIYNSRLTFRARRKHAIFGKNLMDYRNLQAKDKKRSK 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366605 243 EAKELYNRIKPFARVMTAQDFEEFSKDILEELHCRARIQQLQEWRSNGLTTLEAGLKYERDKqarissFEKFGASTAASL 322
Cdd:COG5114  243 EECGLVNSIKWFARYLTKSDFNVFFRDILEGVYIEKRIHELQEWRNNGLTTLEAGLKYERDK------FEKFGASTAASL 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366605 323 SEGNSRYRSNSAHRSNAEYSQNYSENGGRKKNMTISDIQHAPDYALLSNDEQQLCIQLKILPKPYLVLKEVMFRELLKTG 402
Cdd:COG5114  317 SEGNSRYRSNSAHRSNAEYSQMDVKNILPSKNMTISDIQHAPDYALLSDDEQRLCETLNISPKPYLELKKEVISCFLRTR 396
                        410       420       430
                 ....*....|....*....|....*....|..
gi 398366605 403 GNLSKSACRELLNIDPIKANRIYDFFQSQNWM 434
Cdd:COG5114  397 GEFTKEDFNRLFGIDLGKADGLYDFFLERGWI 428
 
Name Accession Description Interval E-value
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
3-434 0e+00

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


Pssm-ID: 227445  Cd Length: 432  Bit Score: 738.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366605   3 NKFHCDVCSADCTNRVRVSCAICPEYDLCVPCFSQGSYTGKHRPYHDYRIIETNSYPILCPDWGADEELQLIKGAQTLGL 82
Cdd:COG5114    4 VKIHCDVCFLDMTDLTFIKCNECPAVDLCLPCFVNGIETGVHSPYHGYRIIETNSYPIGEEGWGADEELLLIECLDTLGL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366605  83 GNWQDIADHIGSRGKEEVKEHYLKYYLESKYYPIPDITQNIHVPQDEFLEQRRHRIESFRERPLEPpRKPMASVPSCHEV 162
Cdd:COG5114   84 GNWEDIADYIGSRAKEEIKSHYLKMYDESKYYPLPDITQNIHVPQDEFLEQRRHRIETFELPPINP-RKPKASNPYCHEI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366605 163 QGFMPGRLEFETEFENEAEGPVKDMVFEPDDQPLDIELKFAILDIYNSRLTTRAEKKRLLFENHLMDYRKLQAIDKKRSK 242
Cdd:COG5114  163 QGYMPGRLEFDVEYMNEAEVPIKDMSFDGDKEELKKKLKNATLDIYNSRLTFRARRKHAIFGKNLMDYRNLQAKDKKRSK 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366605 243 EAKELYNRIKPFARVMTAQDFEEFSKDILEELHCRARIQQLQEWRSNGLTTLEAGLKYERDKqarissFEKFGASTAASL 322
Cdd:COG5114  243 EECGLVNSIKWFARYLTKSDFNVFFRDILEGVYIEKRIHELQEWRNNGLTTLEAGLKYERDK------FEKFGASTAASL 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366605 323 SEGNSRYRSNSAHRSNAEYSQNYSENGGRKKNMTISDIQHAPDYALLSNDEQQLCIQLKILPKPYLVLKEVMFRELLKTG 402
Cdd:COG5114  317 SEGNSRYRSNSAHRSNAEYSQMDVKNILPSKNMTISDIQHAPDYALLSDDEQRLCETLNISPKPYLELKKEVISCFLRTR 396
                        410       420       430
                 ....*....|....*....|....*....|..
gi 398366605 403 GNLSKSACRELLNIDPIKANRIYDFFQSQNWM 434
Cdd:COG5114  397 GEFTKEDFNRLFGIDLGKADGLYDFFLERGWI 428
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
5-53 1.18e-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  Cd Length: 49  Bit Score: 91.20  E-value: 1.18e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 398366605   5 FHCDVCSADCTNRVRVSCAICPEYDLCVPCFSQGSYTGKHRPYHDYRII 53
Cdd:cd02335    1 YHCDYCSKDITGTIRIKCAECPDFDLCLECFSAGAEIGKHRNDHNYRVV 49
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
1-46 1.74e-15

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: 278966  Cd Length: 45  Bit Score: 71.73  E-value: 1.74e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 398366605    1 MSNKFHCDVCSADCTNRVRVSCAICPEYDLCVPCFSQGsYTGKHRP 46
Cdd:pfam00569   1 IHKVYTCNGCSNEPSIGVRYHCLRCSDYDLCQSCFQTG-KGGNHQM 45
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
1-45 2.40e-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  Cd Length: 44  Bit Score: 62.84  E-value: 2.40e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 398366605     1 MSNKFHCDVCSAdCTNRVRVSCAICPEYDLCVPCFSQGSYTGKHR 45
Cdd:smart00291   1 VHHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
 
Name Accession Description Interval E-value
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
3-434 0e+00

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


Pssm-ID: 227445  Cd Length: 432  Bit Score: 738.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366605   3 NKFHCDVCSADCTNRVRVSCAICPEYDLCVPCFSQGSYTGKHRPYHDYRIIETNSYPILCPDWGADEELQLIKGAQTLGL 82
Cdd:COG5114    4 VKIHCDVCFLDMTDLTFIKCNECPAVDLCLPCFVNGIETGVHSPYHGYRIIETNSYPIGEEGWGADEELLLIECLDTLGL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366605  83 GNWQDIADHIGSRGKEEVKEHYLKYYLESKYYPIPDITQNIHVPQDEFLEQRRHRIESFRERPLEPpRKPMASVPSCHEV 162
Cdd:COG5114   84 GNWEDIADYIGSRAKEEIKSHYLKMYDESKYYPLPDITQNIHVPQDEFLEQRRHRIETFELPPINP-RKPKASNPYCHEI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366605 163 QGFMPGRLEFETEFENEAEGPVKDMVFEPDDQPLDIELKFAILDIYNSRLTTRAEKKRLLFENHLMDYRKLQAIDKKRSK 242
Cdd:COG5114  163 QGYMPGRLEFDVEYMNEAEVPIKDMSFDGDKEELKKKLKNATLDIYNSRLTFRARRKHAIFGKNLMDYRNLQAKDKKRSK 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366605 243 EAKELYNRIKPFARVMTAQDFEEFSKDILEELHCRARIQQLQEWRSNGLTTLEAGLKYERDKqarissFEKFGASTAASL 322
Cdd:COG5114  243 EECGLVNSIKWFARYLTKSDFNVFFRDILEGVYIEKRIHELQEWRNNGLTTLEAGLKYERDK------FEKFGASTAASL 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366605 323 SEGNSRYRSNSAHRSNAEYSQNYSENGGRKKNMTISDIQHAPDYALLSNDEQQLCIQLKILPKPYLVLKEVMFRELLKTG 402
Cdd:COG5114  317 SEGNSRYRSNSAHRSNAEYSQMDVKNILPSKNMTISDIQHAPDYALLSDDEQRLCETLNISPKPYLELKKEVISCFLRTR 396
                        410       420       430
                 ....*....|....*....|....*....|..
gi 398366605 403 GNLSKSACRELLNIDPIKANRIYDFFQSQNWM 434
Cdd:COG5114  397 GEFTKEDFNRLFGIDLGKADGLYDFFLERGWI 428
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
5-53 1.18e-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  Cd Length: 49  Bit Score: 91.20  E-value: 1.18e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 398366605   5 FHCDVCSADCTNRVRVSCAICPEYDLCVPCFSQGSYTGKHRPYHDYRII 53
Cdd:cd02335    1 YHCDYCSKDITGTIRIKCAECPDFDLCLECFSAGAEIGKHRNDHNYRVV 49
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
1-46 1.74e-15

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: 278966  Cd Length: 45  Bit Score: 71.73  E-value: 1.74e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 398366605    1 MSNKFHCDVCSADCTNRVRVSCAICPEYDLCVPCFSQGsYTGKHRP 46
Cdd:pfam00569   1 IHKVYTCNGCSNEPSIGVRYHCLRCSDYDLCQSCFQTG-KGGNHQM 45
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
1-45 2.40e-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  Cd Length: 44  Bit Score: 62.84  E-value: 2.40e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 398366605     1 MSNKFHCDVCSAdCTNRVRVSCAICPEYDLCVPCFSQGSYTGKHR 45
Cdd:smart00291   1 VHHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
65-107 3.23e-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: 306708  Cd Length: 47  Bit Score: 51.02  E-value: 3.23e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 398366605   65 WGADEELQLIKGAQTLGLGNWQDIADHIGSRGKEEVKEHYLKY 107
Cdd:pfam00249   4 WTPEEDELLIEAVEKHGNGNWKKIAKHLPGRTDKQCKNRWQNY 46
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
65-107 1.37e-07

'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  Cd Length: 45  Bit Score: 49.11  E-value: 1.37e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 398366605  65 WGADEELQLIKGAQTLGLGNWQDIADHIGSRGKEEVKEHYLKY 107
Cdd:cd00167    2 WTEEEDELLLEAVKKYGKNNWEKIAKELPGRTPKQCRERWRNL 44
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
65-107 2.90e-07

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


Pssm-ID: 197842  Cd Length: 49  Bit Score: 48.37  E-value: 2.90e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 398366605    65 WGADEELQLIKGAQTLGLGNWQDIADHIGSRGKEEVKEHYLKY 107
Cdd:smart00717   4 WTEEEDELLIELVKKYGKNNWEKIAKELPGRTAEQCRERWRNL 46
SWIRM pfam04433
SWIRM domain; This SWIRM domain is a small alpha-helical domain of about 85 amino acid ...
368-433 4.95e-07

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: 309539  Cd Length: 75  Bit Score: 48.31  E-value: 4.95e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366605  368 LLSNDEQQLCIQLK----ILPKPYLVLKEVMFRELLKT-GGNLSKSACRELLNIDPIKANRIYDFFQSQNW 433
Cdd:pfam04433   2 KLHEIEKQLLPEFFsgkgKTPEVYLEIRNFILALWRENpKEYLTKTDARRALVGDVNLISRIHEFLERWGL 72
RSC8 COG5259
RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / ...
6-113 9.37e-07

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


Pssm-ID: 227584  Cd Length: 531  Bit Score: 50.65  E-value: 9.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366605   6 HCDVCSADCTNrVRVSCAICPEYDLCVPCFSQGSYTGkhrpyhdyriiETNSYPILCPD---------WGADEELQLIKG 76
Cdd:COG5259  226 SCSCCGNKSFN-TRYHNLRAEKYNSCSECYDQGRFPS-----------EFTSSDFKPVTisllirdknWSRQELLLLLEG 293
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 398366605  77 AQTLGlGNWQDIADHIGSRGKEEVKEHYLKYYLESKY 113
Cdd:COG5259  294 IEMYG-DDWDKVARHVGTKTKEQCILHFLQLPIEDNY 329
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
7-50 4.70e-06

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  Cd Length: 46  Bit Score: 44.73  E-value: 4.70e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 398366605   7 CDVCSADCTNrVRVSCAICPEYDLCVPCFSQGSytGKHRPYHDY 50
Cdd:cd02249    3 CDGCLKPIVG-VRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSF 43
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
7-48 1.69e-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: 43.49  E-value: 1.69e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 398366605   7 CDVCSADCTNRVRVSCAICPEYDLCVPCFSQGSYTGKHRPYH 48
Cdd:cd02338    3 CDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDH 44
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
7-48 1.80e-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: 40.27  E-value: 1.80e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 398366605   7 CDVCSADCTNRVRVSCAICPEYDLCVPCFSQGSYTGKHRPYH 48
Cdd:cd02345    3 CSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLH 44
ZZ_RSC8 cd02336
Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of ...
5-38 7.10e-04

Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of the RSC complex, which is closely related to the SWI/SNF complex and is involved in remodeling chromatin structure. The ZZ motif coordinates a zinc ion and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239076  Cd Length: 45  Bit Score: 38.45  E-value: 7.10e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 398366605   5 FHCDVCSADCTnRVRVSCAICPEYDLCVPCFSQG 38
Cdd:cd02336    1 YHCFTCGNDCT-RVRYHNLKAKKYDLCPSCYQEG 33
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
7-50 1.48e-03

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: 37.44  E-value: 1.48e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 398366605   7 CDVCSADCTNRVRVSCAICPEYDLCVPCFSqgsyTGKHRPYHDY 50
Cdd:cd02339    3 CDTCRKQGIIGIRWKCAECPNYDLCTTCYH----GDKHDLEHRF 42
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
7-43 2.18e-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: 37.16  E-value: 2.18e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 398366605   7 CDVCSADCTNRVRvsCAICPEYDLCVPCFSQGSYTGK 43
Cdd:cd02337    3 CNECKHHVETRWH--CTVCEDYDLCITCYNTKNHPHK 37
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
7-42 5.35e-03

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: 36.08  E-value: 5.35e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 398366605   7 CDVCSADCTNrVRVSCAICPEYDLCVPCFSQGSYTG 42
Cdd:cd02340    3 CDGCQGPIVG-VRYKCLVCPDYDLCESCEAKGVHPE 37
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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