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Conserved domains on  [gi|386765600|ref|NP_001247055|]
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ZAD and architectural function 1, isoform B [Drosophila melanogaster]

Protein Classification

zinc finger and BTB domain-containing protein( domain architecture ID 12222293)

H2C2 zinc finger and BTB (BR-C, ttk and bab)/POZ (Pox virus and Zinc finger) domain-containing protein similar to Homo sapiens zinc finger and BTB domain-containing protein 14 (ZBTB14/ZFP161/ZF5), a transcriptional activator of the dopamine transporter (DAT)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-AD smart00868
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 9-79 4.02e-07

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.


:

Pssm-ID: 214871  Cd Length: 73  Bit Score: 47.12  E-value: 4.02e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386765600     9 MCRTCRKKGtqSTLQSLFESNAHKLLI----SYAGTSVKPDDGLPDQICTVCLMQLEEVDRFLSACKQSDAHLRS 79
Cdd:smart00868   1 VCRLCLSES--ENLVSIFDESSEASLAekieECTGIEIEPDDGLPKVICGDCLEKLESFHKFRERCRESDELLRE 73
zf-H2C2_2 pfam13465
Zinc-finger double domain;
269-293 9.05e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 9.05e-05
                          10        20
                  ....*....|....*....|....*
gi 386765600  269 NLKTHMRTHTGEKPYQCCYCSRRFA 293
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
SFP1 super family cl25788
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 161-320 8.73e-04

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


The actual alignment was detected with superfamily member COG5189:

Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 41.24  E-value: 8.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765600 161 DIHQEDYT----ISDMDL--DREISDQNYSETYS--QESSAATDSIQETS--EDYHNLEPSADY-VIDLGVAC-EPDKYR 228
Cdd:COG5189  235 DIGHMMDThqfyLEDVDLmdDDILGPSNEEMLYKyiSPSQGSAELFEESSlgFDYEFIHKSVGNkEIRGGISTgEMIDVR 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765600 229 CKICSNTYRCL-----SQLNAHS----QVHRKEKDHQCEV--CQKTFRAACNLKTHMRTHtgekpyqccYCSRRFADNST 297
Cdd:COG5189  315 KLPCTNSSSNGklahgGERNIDTpsrmLKVKDGKPYKCPVegCNKKYKNQNGLKYHMLHG---------HQNQKLHENPS 385

                        170       180
                 ....*....|....*....|...
gi 386765600 298 HRKHERLHTNERPYACNICGKTF 320
Cdd:COG5189  386 PEKMNIFSAKDKPYRCEVCDKRY 408
 
Name Accession Description Interval E-value
zf-AD smart00868
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 9-79 4.02e-07

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.


Pssm-ID: 214871  Cd Length: 73  Bit Score: 47.12  E-value: 4.02e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386765600     9 MCRTCRKKGtqSTLQSLFESNAHKLLI----SYAGTSVKPDDGLPDQICTVCLMQLEEVDRFLSACKQSDAHLRS 79
Cdd:smart00868   1 VCRLCLSES--ENLVSIFDESSEASLAekieECTGIEIEPDDGLPKVICGDCLEKLESFHKFRERCRESDELLRE 73
zf-H2C2_2 pfam13465
Zinc-finger double domain;
269-293 9.05e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 9.05e-05
                          10        20
                  ....*....|....*....|....*
gi 386765600  269 NLKTHMRTHTGEKPYQCCYCSRRFA 293
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 161-320 8.73e-04

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 41.24  E-value: 8.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765600 161 DIHQEDYT----ISDMDL--DREISDQNYSETYS--QESSAATDSIQETS--EDYHNLEPSADY-VIDLGVAC-EPDKYR 228
Cdd:COG5189  235 DIGHMMDThqfyLEDVDLmdDDILGPSNEEMLYKyiSPSQGSAELFEESSlgFDYEFIHKSVGNkEIRGGISTgEMIDVR 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765600 229 CKICSNTYRCL-----SQLNAHS----QVHRKEKDHQCEV--CQKTFRAACNLKTHMRTHtgekpyqccYCSRRFADNST 297
Cdd:COG5189  315 KLPCTNSSSNGklahgGERNIDTpsrmLKVKDGKPYKCPVegCNKKYKNQNGLKYHMLHG---------HQNQKLHENPS 385

                        170       180
                 ....*....|....*....|...
gi 386765600 298 HRKHERLHTNERPYACNICGKTF 320
Cdd:COG5189  386 PEKMNIFSAKDKPYRCEVCDKRY 408
zf-H2C2_2 pfam13465
Zinc-finger double domain;
299-321 5.32e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 5.32e-03
                          10        20
                  ....*....|....*....|...
gi 386765600  299 RKHERLHTNERPYACNICGKTFS 321
Cdd:pfam13465   3 KRHMRTHTGEKPYKCPECGKSFK 25
 
Name Accession Description Interval E-value
zf-AD smart00868
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 9-79 4.02e-07

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.


Pssm-ID: 214871  Cd Length: 73  Bit Score: 47.12  E-value: 4.02e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386765600     9 MCRTCRKKGtqSTLQSLFESNAHKLLI----SYAGTSVKPDDGLPDQICTVCLMQLEEVDRFLSACKQSDAHLRS 79
Cdd:smart00868   1 VCRLCLSES--ENLVSIFDESSEASLAekieECTGIEIEPDDGLPKVICGDCLEKLESFHKFRERCRESDELLRE 73
zf-H2C2_2 pfam13465
Zinc-finger double domain;
269-293 9.05e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 9.05e-05
                          10        20
                  ....*....|....*....|....*
gi 386765600  269 NLKTHMRTHTGEKPYQCCYCSRRFA 293
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 161-320 8.73e-04

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 41.24  E-value: 8.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765600 161 DIHQEDYT----ISDMDL--DREISDQNYSETYS--QESSAATDSIQETS--EDYHNLEPSADY-VIDLGVAC-EPDKYR 228
Cdd:COG5189  235 DIGHMMDThqfyLEDVDLmdDDILGPSNEEMLYKyiSPSQGSAELFEESSlgFDYEFIHKSVGNkEIRGGISTgEMIDVR 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765600 229 CKICSNTYRCL-----SQLNAHS----QVHRKEKDHQCEV--CQKTFRAACNLKTHMRTHtgekpyqccYCSRRFADNST 297
Cdd:COG5189  315 KLPCTNSSSNGklahgGERNIDTpsrmLKVKDGKPYKCPVegCNKKYKNQNGLKYHMLHG---------HQNQKLHENPS 385

                        170       180
                 ....*....|....*....|...
gi 386765600 298 HRKHERLHTNERPYACNICGKTF 320
Cdd:COG5189  386 PEKMNIFSAKDKPYRCEVCDKRY 408
zf-H2C2_2 pfam13465
Zinc-finger double domain;
299-321 5.32e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 5.32e-03
                          10        20
                  ....*....|....*....|...
gi 386765600  299 RKHERLHTNERPYACNICGKTFS 321
Cdd:pfam13465   3 KRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 255-277 6.20e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 33.81  E-value: 6.20e-03
                          10        20
                  ....*....|....*....|...
gi 386765600  255 HQCEVCQKTFRAACNLKTHMRTH 277
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
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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