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Conserved domains on  [gi|40254564|ref|NP_056568|]
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zinc finger E-box-binding homeobox 2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
296-319 3.99e-06

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.28  E-value: 3.99e-06
                           10        20
                   ....*....|....*....|....
gi 40254564    296 HLKEHLRIHSGEKPYECPNCKKRF 319
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
1041-1066 2.81e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 2.81e-05
                           10        20
                   ....*....|....*....|....*.
gi 40254564   1041 HLIEHSRLHSGEKPYQCDKCGKRFSH 1066
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 282-304 3.00e-05

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: 41.90  E-value: 3.00e-05
                           10        20
                   ....*....|....*....|...
gi 40254564    282 FKCTECGKAFKYKHHLKEHLRIH 304
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
1013-1038 1.75e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.75e-04
                           10        20
                   ....*....|....*....|....*.
gi 40254564   1013 SLLRHKYEHTGKRPHQCQICKKAFKH 1038
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 241-263 8.35e-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: 34.97  E-value: 8.35e-03
                           10        20
                   ....*....|....*....|...
gi 40254564    241 FSCPLCSYTFAYRTQLERHMVTH 263
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-Di19 super family cl05267
Drought induced 19 protein (Di19), zinc-binding; This family consists of several drought ...
 209-263 8.52e-03

Drought induced 19 protein (Di19), zinc-binding; This family consists of several drought induced 19 (Di19) like proteins. Di19 has been found to be strongly expressed in both the roots and leaves of Arabidopsis thaliana during progressive drought. This domain is a zinc-binding domain.


The actual alignment was detected with superfamily member pfam05605:

Pssm-ID: 428539  Cd Length: 54  Bit Score: 35.74  E-value: 8.52e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 40254564    209 QLLTCPYCDRGYKrLTSLKEHIKYRHEKNEENFSCPLCSytfayrTQLERHMVTH 263
Cdd:pfam05605    1 DEFTCPFCGEDFD-VVSLCEHVEDEHPVESKNVVCPVCA------AKVGKDMIGH 48
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
296-319 3.99e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.28  E-value: 3.99e-06
                           10        20
                   ....*....|....*....|....
gi 40254564    296 HLKEHLRIHSGEKPYECPNCKKRF 319
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
1041-1066 2.81e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 2.81e-05
                           10        20
                   ....*....|....*....|....*.
gi 40254564   1041 HLIEHSRLHSGEKPYQCDKCGKRFSH 1066
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 282-304 3.00e-05

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: 41.90  E-value: 3.00e-05
                           10        20
                   ....*....|....*....|...
gi 40254564    282 FKCTECGKAFKYKHHLKEHLRIH 304
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
1013-1038 1.75e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.75e-04
                           10        20
                   ....*....|....*....|....*.
gi 40254564   1013 SLLRHKYEHTGKRPHQCQICKKAFKH 1038
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
ZnF_C2H2 smart00355
zinc finger;
282-304 2.25e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 36.67  E-value: 2.25e-03
                            10        20
                    ....*....|....*....|...
gi 40254564     282 FKCTECGKAFKYKHHLKEHLRIH 304
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 241-263 8.35e-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: 34.97  E-value: 8.35e-03
                           10        20
                   ....*....|....*....|...
gi 40254564    241 FSCPLCSYTFAYRTQLERHMVTH 263
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-Di19 pfam05605
Drought induced 19 protein (Di19), zinc-binding; This family consists of several drought ...
 209-263 8.52e-03

Drought induced 19 protein (Di19), zinc-binding; This family consists of several drought induced 19 (Di19) like proteins. Di19 has been found to be strongly expressed in both the roots and leaves of Arabidopsis thaliana during progressive drought. This domain is a zinc-binding domain.


Pssm-ID: 428539  Cd Length: 54  Bit Score: 35.74  E-value: 8.52e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 40254564    209 QLLTCPYCDRGYKrLTSLKEHIKYRHEKNEENFSCPLCSytfayrTQLERHMVTH 263
Cdd:pfam05605    1 DEFTCPFCGEDFD-VVSLCEHVEDEHPVESKNVVCPVCA------AKVGKDMIGH 48
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
296-319 3.99e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.28  E-value: 3.99e-06
                           10        20
                   ....*....|....*....|....
gi 40254564    296 HLKEHLRIHSGEKPYECPNCKKRF 319
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
1041-1066 2.81e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 2.81e-05
                           10        20
                   ....*....|....*....|....*.
gi 40254564   1041 HLIEHSRLHSGEKPYQCDKCGKRFSH 1066
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 282-304 3.00e-05

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: 41.90  E-value: 3.00e-05
                           10        20
                   ....*....|....*....|...
gi 40254564    282 FKCTECGKAFKYKHHLKEHLRIH 304
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
1013-1038 1.75e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.75e-04
                           10        20
                   ....*....|....*....|....*.
gi 40254564   1013 SLLRHKYEHTGKRPHQCQICKKAFKH 1038
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 1027-1049 1.79e-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: 36.89  E-value: 1.79e-03
                           10        20
                   ....*....|....*....|...
gi 40254564   1027 HQCQICKKAFKHKHHLIEHSRLH 1049
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
282-304 2.25e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 36.67  E-value: 2.25e-03
                            10        20
                    ....*....|....*....|...
gi 40254564     282 FKCTECGKAFKYKHHLKEHLRIH 304
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 241-263 8.35e-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: 34.97  E-value: 8.35e-03
                           10        20
                   ....*....|....*....|...
gi 40254564    241 FSCPLCSYTFAYRTQLERHMVTH 263
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-Di19 pfam05605
Drought induced 19 protein (Di19), zinc-binding; This family consists of several drought ...
 209-263 8.52e-03

Drought induced 19 protein (Di19), zinc-binding; This family consists of several drought induced 19 (Di19) like proteins. Di19 has been found to be strongly expressed in both the roots and leaves of Arabidopsis thaliana during progressive drought. This domain is a zinc-binding domain.


Pssm-ID: 428539  Cd Length: 54  Bit Score: 35.74  E-value: 8.52e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 40254564    209 QLLTCPYCDRGYKrLTSLKEHIKYRHEKNEENFSCPLCSytfayrTQLERHMVTH 263
Cdd:pfam05605    1 DEFTCPFCGEDFD-VVSLCEHVEDEHPVESKNVVCPVCA------AKVGKDMIGH 48
 
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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