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Conserved domains on  [gi|19075511|ref|NP_588011|]
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SAGA complex subunit Ada2 [Schizosaccharomyces pombe]

Protein Classification

transcriptional adapter( domain architecture ID 11473817)

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

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];
1-437 0e+00

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


:

Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 739.19  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075511   1 MPPQKYHCNVCAQDITRSIHIRCVECVDFDLCIPCFTSGASLGTHHPSHPYRIIETNSYPIFDENWGADEELLLIDACET 80
Cdd:COG5114   1 MGGVKIHCDVCFLDMTDLTFIKCNECPAVDLCLPCFVNGIETGVHSPYHGYRIIETNSYPIGEEGWGADEELLLIECLDT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075511  81 LGLGNWADIADYVGnARTKEECRDHYLKTYIESDCYPLASVELPGPVDRIAFAARKRARIEAFQPPPIIPQKPLASTPQC 160
Cdd:COG5114  81 LGLGNWEDIADYIG-SRAKEEIKSHYLKMYDESKYYPLPDITQNIHVPQDEFLEQRRHRIETFELPPINPRKPKASNPYC 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075511 161 HEIQGYMPGRLEFDQEYMNEAELPIKDMNFDDDLHEsakHEMQLKLTMLNIYNSRLTRRAVRKQTIFNHNLLDYRRLQAN 240
Cdd:COG5114 160 HEIQGYMPGRLEFDVEYMNEAEVPIKDMSFDGDKEE---LKKKLKNATLDIYNSRLTFRARRKHAIFGKNLMDYRNLQAK 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075511 241 EKRMSKEERNLLNKTKAFARLLTGPDYQKFVNSYHEQITLKKQISDLQEWRQMGLTTLEQGHKYERDKTQKFLLSKASAS 320
Cdd:COG5114 237 DKKRSKEECGLVNSIKWFARYLTKSDFNVFFRDILEGVYIEKRIHELQEWRNNGLTTLEAGLKYERDKFEKFGASTAASL 316

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075511 321 YDKQLRHVKSFNQTTSAPFQVRDIQKIVPRKPATPTMFSASADRQLLSEDEQALCSKLQIFPKPFLALKFALISASLTSK 400
Cdd:COG5114 317 SEGNSRYRSNSAHRSNAEYSQMDVKNILPSKNMTISDIQHAPDYALLSDDEQRLCETLNISPKPYLELKKEVISCFLRTR 396

                       410       420       430
                ....*....|....*....|....*....|....*..
gi 19075511 401 KPFQKTDAVNLFKhLDANKVEQVYDFFHNARWIGAPT 437
Cdd:COG5114 397 GEFTKEDFNRLFG-IDLGKADGLYDFFLERGWIHEEK 432
 
Name Accession Description Interval E-value
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
1-437 0e+00

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


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 739.19  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075511   1 MPPQKYHCNVCAQDITRSIHIRCVECVDFDLCIPCFTSGASLGTHHPSHPYRIIETNSYPIFDENWGADEELLLIDACET 80
Cdd:COG5114   1 MGGVKIHCDVCFLDMTDLTFIKCNECPAVDLCLPCFVNGIETGVHSPYHGYRIIETNSYPIGEEGWGADEELLLIECLDT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075511  81 LGLGNWADIADYVGnARTKEECRDHYLKTYIESDCYPLASVELPGPVDRIAFAARKRARIEAFQPPPIIPQKPLASTPQC 160
Cdd:COG5114  81 LGLGNWEDIADYIG-SRAKEEIKSHYLKMYDESKYYPLPDITQNIHVPQDEFLEQRRHRIETFELPPINPRKPKASNPYC 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075511 161 HEIQGYMPGRLEFDQEYMNEAELPIKDMNFDDDLHEsakHEMQLKLTMLNIYNSRLTRRAVRKQTIFNHNLLDYRRLQAN 240
Cdd:COG5114 160 HEIQGYMPGRLEFDVEYMNEAEVPIKDMSFDGDKEE---LKKKLKNATLDIYNSRLTFRARRKHAIFGKNLMDYRNLQAK 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075511 241 EKRMSKEERNLLNKTKAFARLLTGPDYQKFVNSYHEQITLKKQISDLQEWRQMGLTTLEQGHKYERDKTQKFLLSKASAS 320
Cdd:COG5114 237 DKKRSKEECGLVNSIKWFARYLTKSDFNVFFRDILEGVYIEKRIHELQEWRNNGLTTLEAGLKYERDKFEKFGASTAASL 316

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075511 321 YDKQLRHVKSFNQTTSAPFQVRDIQKIVPRKPATPTMFSASADRQLLSEDEQALCSKLQIFPKPFLALKFALISASLTSK 400
Cdd:COG5114 317 SEGNSRYRSNSAHRSNAEYSQMDVKNILPSKNMTISDIQHAPDYALLSDDEQRLCETLNISPKPYLELKKEVISCFLRTR 396

                       410       420       430
                ....*....|....*....|....*....|....*..
gi 19075511 401 KPFQKTDAVNLFKhLDANKVEQVYDFFHNARWIGAPT 437
Cdd:COG5114 397 GEFTKEDFNRLFG-IDLGKADGLYDFFLERGWIHEEK 432
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 6-54 2.95e-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: 89.27  E-value: 2.95e-22
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 19075511   6 YHCNVCAQDITRSIHIRCVECVDFDLCIPCFTSGASLGTHHPSHPYRII 54
Cdd:cd02335   1 YHCDYCSKDITGTIRIKCAECPDFDLCLECFSAGAEIGKHRNDHNYRVV 49
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
64-108 6.64e-10

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


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 54.15  E-value: 6.64e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 19075511     64 ENWGADEELLLIDACETLGLGNWADIADYVGNaRTKEECRDHYLK 108
Cdd:smart00717   2 GEWTEEEDELLIELVKKYGKNNWEKIAKELPG-RTAEQCRERWRN 45
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 65-108 2.18e-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: 2.18e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 19075511    65 NWGADEELLLIDACETLGlGNWADIADYVGNaRTKEECRDHYLK 108
Cdd:pfam00249   3 PWTPEEDELLLEAVEKLG-NRWKKIAKLLPG-RTDNQCKNRWQN 44
 
Name Accession Description Interval E-value
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
1-437 0e+00

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


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 739.19  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075511   1 MPPQKYHCNVCAQDITRSIHIRCVECVDFDLCIPCFTSGASLGTHHPSHPYRIIETNSYPIFDENWGADEELLLIDACET 80
Cdd:COG5114   1 MGGVKIHCDVCFLDMTDLTFIKCNECPAVDLCLPCFVNGIETGVHSPYHGYRIIETNSYPIGEEGWGADEELLLIECLDT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075511  81 LGLGNWADIADYVGnARTKEECRDHYLKTYIESDCYPLASVELPGPVDRIAFAARKRARIEAFQPPPIIPQKPLASTPQC 160
Cdd:COG5114  81 LGLGNWEDIADYIG-SRAKEEIKSHYLKMYDESKYYPLPDITQNIHVPQDEFLEQRRHRIETFELPPINPRKPKASNPYC 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075511 161 HEIQGYMPGRLEFDQEYMNEAELPIKDMNFDDDLHEsakHEMQLKLTMLNIYNSRLTRRAVRKQTIFNHNLLDYRRLQAN 240
Cdd:COG5114 160 HEIQGYMPGRLEFDVEYMNEAEVPIKDMSFDGDKEE---LKKKLKNATLDIYNSRLTFRARRKHAIFGKNLMDYRNLQAK 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075511 241 EKRMSKEERNLLNKTKAFARLLTGPDYQKFVNSYHEQITLKKQISDLQEWRQMGLTTLEQGHKYERDKTQKFLLSKASAS 320
Cdd:COG5114 237 DKKRSKEECGLVNSIKWFARYLTKSDFNVFFRDILEGVYIEKRIHELQEWRNNGLTTLEAGLKYERDKFEKFGASTAASL 316

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075511 321 YDKQLRHVKSFNQTTSAPFQVRDIQKIVPRKPATPTMFSASADRQLLSEDEQALCSKLQIFPKPFLALKFALISASLTSK 400
Cdd:COG5114 317 SEGNSRYRSNSAHRSNAEYSQMDVKNILPSKNMTISDIQHAPDYALLSDDEQRLCETLNISPKPYLELKKEVISCFLRTR 396

                       410       420       430
                ....*....|....*....|....*....|....*..
gi 19075511 401 KPFQKTDAVNLFKhLDANKVEQVYDFFHNARWIGAPT 437
Cdd:COG5114 397 GEFTKEDFNRLFG-IDLGKADGLYDFFLERGWIHEEK 432
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 6-54 2.95e-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: 89.27  E-value: 2.95e-22
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 19075511   6 YHCNVCAQDITRSIHIRCVECVDFDLCIPCFTSGASLGTHHPSHPYRII 54
Cdd:cd02335   1 YHCDYCSKDITGTIRIKCAECPDFDLCLECFSAGAEIGKHRNDHNYRVV 49
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 65-108 3.45e-10

'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: 54.89  E-value: 3.45e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 19075511  65 NWGADEELLLIDACETLGLGNWADIADYVGNaRTKEECRDHYLK 108
Cdd:cd00167   1 PWTEEEDELLLEAVKKYGKNNWEKIAKELPG-RTPKQCRERWRN 43
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
64-108 6.64e-10

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


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 54.15  E-value: 6.64e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 19075511     64 ENWGADEELLLIDACETLGLGNWADIADYVGNaRTKEECRDHYLK 108
Cdd:smart00717   2 GEWTEEEDELLIELVKKYGKNNWEKIAKELPG-RTAEQCRERWRN 45
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 65-108 2.18e-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: 2.18e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 19075511    65 NWGADEELLLIDACETLGlGNWADIADYVGNaRTKEECRDHYLK 108
Cdd:pfam00249   3 PWTPEEDELLLEAVEKLG-NRWKKIAKLLPG-RTDNQCKNRWQN 44
RSC8 COG5259
RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / ...
 6-112 2.18e-08

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


Pssm-ID: 227584 [Multi-domain]  Cd Length: 531  Bit Score: 56.05  E-value: 2.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075511   6 YHCNVC--AQDITRSIHIRCVecvDFDLCIPCFTSGAsLGTHHPSHPYRIIETNSYPIfDENWGADEELLLIDACETLGl 83
Cdd:COG5259 225 SSCSCCgnKSFNTRYHNLRAE---KYNSCSECYDQGR-FPSEFTSSDFKPVTISLLIR-DKNWSRQELLLLLEGIEMYG- 298

                        90       100
                ....*....|....*....|....*....
gi 19075511  84 GNWADIADYVGNaRTKEECRDHYLKTYIE 112
Cdd:COG5259 299 DDWDKVARHVGT-KTKEQCILHFLQLPIE 326
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 6-51 4.65e-08

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: 48.97  E-value: 4.65e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 19075511   6 YHCNVCAQDITRsIHIRCVECVDFDLCIPCFTSGAslGTHHPSHPY 51
Cdd:cd02249   1 YSCDGCLKPIVG-VRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSF 43
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 8-49 6.02e-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: 46.04  E-value: 6.02e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 19075511   8 CNVCAQDITRSIHIRCVECVDFDLCIPCFTSGASLGTHHPSH 49
Cdd:cd02345   3 CSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLH 44
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 4-46 9.35e-07

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: 45.51  E-value: 9.35e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 19075511      4 QKYHCNVCAQDI--TRsihIRCVECVDFDLCIPCFTSGASLGTHH 46
Cdd:smart00291   3 HSYSCDTCGKPIvgVR---YHCLVCPDYDLCQSCFAKGSAGGEHS 44
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 5-38 1.67e-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: 44.78  E-value: 1.67e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 19075511     5 KYHCNVCAQDITRSIHIRCVECVDFDLCIPCFTS 38
Cdd:pfam00569   4 VYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQT 37
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 8-50 1.34e-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: 1.34e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 19075511   8 CNVCAQDITRSIHIRCVECVDFDLCIPCFTSGASLGTHHPSHP 50
Cdd:cd02334   3 CNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHP 45
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 8-50 1.58e-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: 41.95  E-value: 1.58e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 19075511   8 CNVCAQDITRSIHIRCVECVDFDLCIPCFTSGASLGTHHPSHP 50
Cdd:cd02338   3 CDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDHP 45
SWIRM pfam04433
SWIRM domain; This SWIRM domain is a small alpha-helical domain of about 85 amino acid ...
 362-433 4.19e-05

SWIRM domain; This SWIRM domain is a small alpha-helical domain of about 85 amino acid residues found in chromosomal proteins. It contains a helix-turn helix motif and binds to DNA.


Pssm-ID: 461307 [Multi-domain]  Cd Length: 78  Bit Score: 41.78  E-value: 4.19e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19075511   362 ADRQLLSEDEQALCSKL----QIFPKPFLALKFALISASLTS-KKPFQKTDAVNLFKHlDANKVEQVYDFFHNARWI 433
Cdd:pfam04433   1 SDPDKLHPIEKRLLPEFfngkSKTPEVYLEIRNFILNLWRENpKEYLTKTDARRALKG-DVNLISRIHEFLERWGLI 76
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 8-51 2.23e-04

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: 38.39  E-value: 2.23e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 19075511   8 CNVCAQDItRSIHIRCVECVDFDLCIPCFTSGAslgthHPSHPY 51
Cdd:cd02340   3 CDGCQGPI-VGVRYKCLVCPDYDLCESCEAKGV-----HPEHAM 40
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 6-36 1.58e-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: 36.00  E-value: 1.58e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 19075511   6 YHCNVCAQDITRSIHirCVECVDFDLCIPCF 36
Cdd:cd02337   1 YTCNECKHHVETRWH--CTVCEDYDLCITCY 29
SANT_TRF cd11660
Telomere repeat binding factor-like DNA-binding domains of the SANT/myb-like family; Human ...
 66-98 3.31e-03

Telomere repeat binding factor-like DNA-binding domains of the SANT/myb-like family; Human telomere repeat binding factors, TRF1 and TRF2, function as part of the 6 component shelterin complex. TRF2 binds DNA and recruits RAP1 (via binding to the RAP1 protein c-terminal (RCT)) and TIN2 in the protection of telomeres from DNA repair machinery. Metazoan shelterin consists of 3 DNA binding proteins (TRF2, TRF1, and POT1) and 3 recruited proteins that bind to one or more of these DNA-binding proteins (RAP1, TIN2, TPP1). Schizosaccharomyces pombe TAZ1 is an orthlog and binds RAP1. Human TRF1 and TRF2 bind double-stranded DNA. hTRF2 consists of a basic N-terminus, a TRF homology domain, the RAP1 binding motif (RBM), the TIN2 binding motif (TBM) and a myb-like DNA binding domain, SANT, named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. Tandem copies of the domain bind telomeric DNA tandem repeats as part of the capping complex. The single myb-like domain of TRF-type proteins is similar to the tandem myb_like domains found in yeast RAP1.


Pssm-ID: 212558 [Multi-domain]  Cd Length: 50  Bit Score: 35.62  E-value: 3.31e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 19075511  66 WGADEELLLIDACETLGLGNWADIADY--VGNART 98
Cdd:cd11660   3 WTDEEDEALVEGVEKYGVGNWAKILKDyfFVNNRT 37
ZZ_RSC8 cd02336
Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of ...
 6-39 4.35e-03

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: 34.99  E-value: 4.35e-03
                        10        20        30
                ....*....|....*....|....*....|....
gi 19075511   6 YHCNVCAQDITRsIHIRCVECVDFDLCIPCFTSG 39
Cdd:cd02336   1 YHCFTCGNDCTR-VRYHNLKAKKYDLCPSCYQEG 33
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
 6-46 9.76e-03

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: 33.95  E-value: 9.76e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 19075511   6 YHCNVCAQDITRSIHIRCVECV--DFDLCIPCFTSGASLGTHH 46
Cdd:cd02341   1 FKCDSCGIEPIPGTRYHCSECDdgDFDLCQDCVVKGESHQEDH 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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