NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1958699133|ref|XP_038951330|]
View 

zinc finger E-box-binding homeobox 1 isoform X2 [Rattus norvegicus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
906-931 3.89e-07

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 46.98  E-value: 3.89e-07
                           10        20
                   ....*....|....*....|....*.
gi 1958699133  906 HLIEHMRLHSGEKPYQCDKCGKRFSH 931
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
217-240 4.92e-07

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 46.98  E-value: 4.92e-07
                           10        20
                   ....*....|....*....|....
gi 1958699133  217 HLKEHLRIHSGEKPYECPNCKKRF 240
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
203-225 4.37e-06

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: 44.21  E-value: 4.37e-06
                           10        20
                   ....*....|....*....|...
gi 1958699133  203 FKCTECGKAFKYKHHLKEHLRIH 225
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
878-903 4.96e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.20  E-value: 4.96e-05
                           10        20
                   ....*....|....*....|....*.
gi 1958699133  878 SLLRHKYEHTGKRPHECGICRKAFKH 903
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
Homeodomain super family cl47488
Homeodomain;
543-590 2.04e-03

Homeodomain;


The actual alignment was detected with superfamily member pfam00046:

Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 37.48  E-value: 2.04e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958699133  543 LSPSQpplknlLSLLKAYYALNAQPSTEELTKIADSVNLPLDVVKKWF 590
Cdd:pfam00046    7 FTPEQ------LEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWF 48
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
163-185 5.07e-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: 35.35  E-value: 5.07e-03
                           10        20
                   ....*....|....*....|...
gi 1958699133  163 FSCSLCSYTFAYRTQLERHMTSH 185
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
906-931 3.89e-07

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 46.98  E-value: 3.89e-07
                           10        20
                   ....*....|....*....|....*.
gi 1958699133  906 HLIEHMRLHSGEKPYQCDKCGKRFSH 931
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
217-240 4.92e-07

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 46.98  E-value: 4.92e-07
                           10        20
                   ....*....|....*....|....
gi 1958699133  217 HLKEHLRIHSGEKPYECPNCKKRF 240
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
203-225 4.37e-06

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: 44.21  E-value: 4.37e-06
                           10        20
                   ....*....|....*....|...
gi 1958699133  203 FKCTECGKAFKYKHHLKEHLRIH 225
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
878-903 4.96e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.20  E-value: 4.96e-05
                           10        20
                   ....*....|....*....|....*.
gi 1958699133  878 SLLRHKYEHTGKRPHECGICRKAFKH 903
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
ZnF_C2H2 smart00355
zinc finger;
203-225 4.97e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 38.22  E-value: 4.97e-04
                            10        20
                    ....*....|....*....|...
gi 1958699133   203 FKCTECGKAFKYKHHLKEHLRIH 225
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
Homeodomain pfam00046
Homeodomain;
543-590 2.04e-03

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 37.48  E-value: 2.04e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958699133  543 LSPSQpplknlLSLLKAYYALNAQPSTEELTKIADSVNLPLDVVKKWF 590
Cdd:pfam00046    7 FTPEQ------LEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWF 48
ZnF_C2H2 smart00355
zinc finger;
892-914 4.52e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.52  E-value: 4.52e-03
                            10        20
                    ....*....|....*....|...
gi 1958699133   892 HECGICRKAFKHKHHLIEHMRLH 914
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
163-185 5.07e-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: 35.35  E-value: 5.07e-03
                           10        20
                   ....*....|....*....|...
gi 1958699133  163 FSCSLCSYTFAYRTQLERHMTSH 185
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
163-185 6.44e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.13  E-value: 6.44e-03
                            10        20
                    ....*....|....*....|...
gi 1958699133   163 FSCSLCSYTFAYRTQLERHMTSH 185
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
906-931 3.89e-07

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 46.98  E-value: 3.89e-07
                           10        20
                   ....*....|....*....|....*.
gi 1958699133  906 HLIEHMRLHSGEKPYQCDKCGKRFSH 931
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
217-240 4.92e-07

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 46.98  E-value: 4.92e-07
                           10        20
                   ....*....|....*....|....
gi 1958699133  217 HLKEHLRIHSGEKPYECPNCKKRF 240
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
203-225 4.37e-06

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: 44.21  E-value: 4.37e-06
                           10        20
                   ....*....|....*....|...
gi 1958699133  203 FKCTECGKAFKYKHHLKEHLRIH 225
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
878-903 4.96e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.20  E-value: 4.96e-05
                           10        20
                   ....*....|....*....|....*.
gi 1958699133  878 SLLRHKYEHTGKRPHECGICRKAFKH 903
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
892-914 8.01e-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: 40.36  E-value: 8.01e-05
                           10        20
                   ....*....|....*....|...
gi 1958699133  892 HECGICRKAFKHKHHLIEHMRLH 914
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
203-225 4.97e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 38.22  E-value: 4.97e-04
                            10        20
                    ....*....|....*....|...
gi 1958699133   203 FKCTECGKAFKYKHHLKEHLRIH 225
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
Homeodomain pfam00046
Homeodomain;
543-590 2.04e-03

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 37.48  E-value: 2.04e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958699133  543 LSPSQpplknlLSLLKAYYALNAQPSTEELTKIADSVNLPLDVVKKWF 590
Cdd:pfam00046    7 FTPEQ------LEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWF 48
ZnF_C2H2 smart00355
zinc finger;
892-914 4.52e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.52  E-value: 4.52e-03
                            10        20
                    ....*....|....*....|...
gi 1958699133   892 HECGICRKAFKHKHHLIEHMRLH 914
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
920-940 4.88e-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: 35.35  E-value: 4.88e-03
                           10        20
                   ....*....|....*....|.
gi 1958699133  920 YQCDKCGKRFSHSGSYSQHMN 940
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLR 21
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
163-185 5.07e-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: 35.35  E-value: 5.07e-03
                           10        20
                   ....*....|....*....|...
gi 1958699133  163 FSCSLCSYTFAYRTQLERHMTSH 185
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
203-225 5.75e-03

C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.


Pssm-ID: 464025  Cd Length: 24  Bit Score: 35.31  E-value: 5.75e-03
                           10        20
                   ....*....|....*....|...
gi 1958699133  203 FKCTECGKAFKYKHHLKEHLRIH 225
Cdd:pfam13894    1 FKCPICGKSFSSKKSLKRHLKTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
178-214 5.86e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 5.86e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1958699133  178 LERHMTSHKsgreqrhvtqsgGNRKFKCTECGKAFKY 214
Cdd:pfam13465    2 LKRHMRTHT------------GEKPYKCPECGKSFKS 26
ZnF_C2H2 smart00355
zinc finger;
163-185 6.44e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.13  E-value: 6.44e-03
                            10        20
                    ....*....|....*....|...
gi 1958699133   163 FSCSLCSYTFAYRTQLERHMTSH 185
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH