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Conserved domains on  [gi|1907075912|ref|XP_036011768|]
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zinc finger and BTB domain-containing protein 2 isoform X1 [Mus musculus]

Protein Classification

zinc finger and BTB domain-containing protein( domain architecture ID 13605653)

C2H2 zinc finger and BTB (BR-C, ttk and bab)/POZ (Pox virus and Zinc finger) domain-containing protein may be involved in transcriptional regulation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BTB_POZ super family cl38908
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
1-38 1.16e-17

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain superfamily; Proteins in this superfamily are characterized by the presence of a common protein-protein interaction motif of about 100 amino acids, known as the BTB/POZ domain. Members include transcription factors, oncogenic proteins, ion channel proteins, and potassium channel tetramerization domain (KCTD) proteins. They have been identified in poxviruses and many eukaryotes, and have diverse functions, such as transcriptional regulation, chromatin remodeling, protein degradation and cytoskeletal regulation. Many BTB/POZ proteins contain one or two additional domains, such as kelch repeats, zinc-finger domains, FYVE (Fab1, YOTB, Vac1, and EEA1) fingers, or ankyrin repeats, among others. These special additional domains or interaction partners provide unique characteristics and functions to BTB/POZ proteins. In ion channel proteins and KCTD proteins, the BTB/POZ domain is also called the tetramerization (T1) domain.


The actual alignment was detected with superfamily member cd18193:

Pssm-ID: 453885 [Multi-domain]  Cd Length: 115  Bit Score: 78.50  E-value: 1.16e-17
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1907075912   1 MYTGKMAPQLIDPVRLEQGIKFLHAYPLIQEASLASQG 38
Cdd:cd18193    78 MYTGKMAPQLIDPVRLEQGIKFLHAYPLIQEASLASHG 115
zf-H2C2_2 pfam13465
Zinc-finger double domain;
298-320 7.27e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 7.27e-05
                          10        20
                  ....*....|....*....|....
gi 1907075912 298 HWREHMYIHTG-KPFKCSTCDKSF 320
Cdd:pfam13465   1 NLKRHMRTHTGeKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
284-306 1.74e-04

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: 38.44  E-value: 1.74e-04
                          10        20
                  ....*....|....*....|...
gi 1907075912 284 YECTICGRKFIQKSHWREHMYIH 306
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
175-197 1.04e-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: 36.12  E-value: 1.04e-03
                          10        20
                  ....*....|....*....|...
gi 1907075912 175 YACHLCGRRFTLRSSLREHLQIH 197
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
BTB_POZ_ZBTB2 cd18193
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
1-38 1.16e-17

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 2 (ZBTB2); ZBTB2 is a POZ domain Kruppel-like zinc finger (POK) family transcription factor acting as a potent repressor of the ARF-HDM2-p53-p21 pathway, which is important in cell cycle regulation. It represses transcription of the ARF, p53, and p21 genes, but activates the HDM2 gene. ZBTB2 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349502 [Multi-domain]  Cd Length: 115  Bit Score: 78.50  E-value: 1.16e-17
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1907075912   1 MYTGKMAPQLIDPVRLEQGIKFLHAYPLIQEASLASQG 38
Cdd:cd18193    78 MYTGKMAPQLIDPVRLEQGIKFLHAYPLIQEASLASHG 115
zf-H2C2_2 pfam13465
Zinc-finger double domain;
298-320 7.27e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 7.27e-05
                          10        20
                  ....*....|....*....|....
gi 1907075912 298 HWREHMYIHTG-KPFKCSTCDKSF 320
Cdd:pfam13465   1 NLKRHMRTHTGeKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
284-306 1.74e-04

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: 38.44  E-value: 1.74e-04
                          10        20
                  ....*....|....*....|...
gi 1907075912 284 YECTICGRKFIQKSHWREHMYIH 306
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
175-197 1.04e-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: 36.12  E-value: 1.04e-03
                          10        20
                  ....*....|....*....|...
gi 1907075912 175 YACHLCGRRFTLRSSLREHLQIH 197
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
284-306 1.48e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.90  E-value: 1.48e-03
                           10        20
                   ....*....|....*....|...
gi 1907075912  284 YECTICGRKFIQKSHWREHMYIH 306
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
ZnF_C2H2 smart00355
zinc finger;
175-197 1.89e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.52  E-value: 1.89e-03
                           10        20
                   ....*....|....*....|...
gi 1907075912  175 YACHLCGRRFTLRSSLREHLQIH 197
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
 
Name Accession Description Interval E-value
BTB_POZ_ZBTB2 cd18193
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
1-38 1.16e-17

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 2 (ZBTB2); ZBTB2 is a POZ domain Kruppel-like zinc finger (POK) family transcription factor acting as a potent repressor of the ARF-HDM2-p53-p21 pathway, which is important in cell cycle regulation. It represses transcription of the ARF, p53, and p21 genes, but activates the HDM2 gene. ZBTB2 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349502 [Multi-domain]  Cd Length: 115  Bit Score: 78.50  E-value: 1.16e-17
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1907075912   1 MYTGKMAPQLIDPVRLEQGIKFLHAYPLIQEASLASQG 38
Cdd:cd18193    78 MYTGKMAPQLIDPVRLEQGIKFLHAYPLIQEASLASHG 115
BTB_POZ_ZBTB25_ZNF46_KUP cd18213
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
1-55 1.45e-06

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 25 (ZBTB25); ZBTB25, also called zinc finger protein 46 (ZNF46) or zinc finger protein KUP, is a transcription repressor that facilitates viral RNA transcription and replication. It interacts with viral RNA-dependent RNA polymerase (RdRp) proteins and modulates their transcription activity. It also functions as a viral RNA-binding protein, binding preferentially to the U-rich sequence within 5' UTR of vRNA. ZBTB25 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349522 [Multi-domain]  Cd Length: 128  Bit Score: 47.20  E-value: 1.45e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907075912   1 MYTGKMAPQLIDPVRLEQGIKFLHAYPLIQEASLASQGSFSHPEQvfplASSLYG 55
Cdd:cd18213    78 MYTGKGPKQSVDHSRLEEGIRFLHANYLSRIATEMNQDFSPETMQ----SSNLYG 128
zf-H2C2_2 pfam13465
Zinc-finger double domain;
298-320 7.27e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 7.27e-05
                          10        20
                  ....*....|....*....|....
gi 1907075912 298 HWREHMYIHTG-KPFKCSTCDKSF 320
Cdd:pfam13465   1 NLKRHMRTHTGeKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
284-306 1.74e-04

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: 38.44  E-value: 1.74e-04
                          10        20
                  ....*....|....*....|...
gi 1907075912 284 YECTICGRKFIQKSHWREHMYIH 306
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
175-197 1.04e-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: 36.12  E-value: 1.04e-03
                          10        20
                  ....*....|....*....|...
gi 1907075912 175 YACHLCGRRFTLRSSLREHLQIH 197
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
284-306 1.48e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.90  E-value: 1.48e-03
                           10        20
                   ....*....|....*....|...
gi 1907075912  284 YECTICGRKFIQKSHWREHMYIH 306
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
ZnF_C2H2 smart00355
zinc finger;
175-197 1.89e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.52  E-value: 1.89e-03
                           10        20
                   ....*....|....*....|...
gi 1907075912  175 YACHLCGRRFTLRSSLREHLQIH 197
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 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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