NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1207184422|ref|XP_005167580|]
View 

zinc finger E-box-binding homeobox 2 isoform X1 [Danio rerio]

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;
299-322 7.78e-06

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.51  E-value: 7.78e-06
                           10        20
                   ....*....|....*....|....
gi 1207184422  299 HLKEHLRIHSGEKPYECSNCKKRF 322
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
1016-1041 1.41e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 1.41e-05
                           10        20
                   ....*....|....*....|....*.
gi 1207184422 1016 HLIEHSRLHSGEKPYQCDKCGKRFSH 1041
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 285-307 1.48e-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: 42.67  E-value: 1.48e-05
                           10        20
                   ....*....|....*....|...
gi 1207184422  285 FKCTECGKAFKYKHHLKEHLRIH 307
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-Di19 super family cl05267
Drought induced 19 protein (Di19), zinc-binding; This family consists of several drought ...
 212-266 5.62e-04

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: 38.82  E-value: 5.62e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207184422  212 QLLTCPYCDRGYKrLTSLKEHIKYRHEKNDESFPCPLCSDTFAyrTQLERHMATH 266
Cdd:pfam05605    1 DEFTCPFCGEDFD-VVSLCEHVEDEHPVESKNVVCPVCAAKVG--KDMIGHLTLQ 52
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 1002-1024 9.45e-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: 37.66  E-value: 9.45e-04
                           10        20
                   ....*....|....*....|...
gi 1207184422 1002 HQCQICKKAFKHKHHLIEHSRLH 1024
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
299-322 7.78e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.51  E-value: 7.78e-06
                           10        20
                   ....*....|....*....|....
gi 1207184422  299 HLKEHLRIHSGEKPYECSNCKKRF 322
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
1016-1041 1.41e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 1.41e-05
                           10        20
                   ....*....|....*....|....*.
gi 1207184422 1016 HLIEHSRLHSGEKPYQCDKCGKRFSH 1041
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 285-307 1.48e-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: 42.67  E-value: 1.48e-05
                           10        20
                   ....*....|....*....|...
gi 1207184422  285 FKCTECGKAFKYKHHLKEHLRIH 307
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-Di19 pfam05605
Drought induced 19 protein (Di19), zinc-binding; This family consists of several drought ...
 212-266 5.62e-04

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: 38.82  E-value: 5.62e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207184422  212 QLLTCPYCDRGYKrLTSLKEHIKYRHEKNDESFPCPLCSDTFAyrTQLERHMATH 266
Cdd:pfam05605    1 DEFTCPFCGEDFD-VVSLCEHVEDEHPVESKNVVCPVCAAKVG--KDMIGHLTLQ 52
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 1002-1024 9.45e-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: 37.66  E-value: 9.45e-04
                           10        20
                   ....*....|....*....|...
gi 1207184422 1002 HQCQICKKAFKHKHHLIEHSRLH 1024
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
285-307 1.09e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 37.45  E-value: 1.09e-03
                            10        20
                    ....*....|....*....|...
gi 1207184422   285 FKCTECGKAFKYKHHLKEHLRIH 307
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
999-1052 1.56e-03

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.38  E-value: 1.56e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207184422  999 KRPHQCQICKKAFKHKHHLIEHSRLHSGEKPYQC--DKCGKRFSHSGSYSQHMNHR 1052
Cdd:COG5048     31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTH 86
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
299-322 7.78e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.51  E-value: 7.78e-06
                           10        20
                   ....*....|....*....|....
gi 1207184422  299 HLKEHLRIHSGEKPYECSNCKKRF 322
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
1016-1041 1.41e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 1.41e-05
                           10        20
                   ....*....|....*....|....*.
gi 1207184422 1016 HLIEHSRLHSGEKPYQCDKCGKRFSH 1041
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 285-307 1.48e-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: 42.67  E-value: 1.48e-05
                           10        20
                   ....*....|....*....|...
gi 1207184422  285 FKCTECGKAFKYKHHLKEHLRIH 307
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-Di19 pfam05605
Drought induced 19 protein (Di19), zinc-binding; This family consists of several drought ...
 212-266 5.62e-04

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: 38.82  E-value: 5.62e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207184422  212 QLLTCPYCDRGYKrLTSLKEHIKYRHEKNDESFPCPLCSDTFAyrTQLERHMATH 266
Cdd:pfam05605    1 DEFTCPFCGEDFD-VVSLCEHVEDEHPVESKNVVCPVCAAKVG--KDMIGHLTLQ 52
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 1002-1024 9.45e-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: 37.66  E-value: 9.45e-04
                           10        20
                   ....*....|....*....|...
gi 1207184422 1002 HQCQICKKAFKHKHHLIEHSRLH 1024
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
285-307 1.09e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 37.45  E-value: 1.09e-03
                            10        20
                    ....*....|....*....|...
gi 1207184422   285 FKCTECGKAFKYKHHLKEHLRIH 307
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
999-1052 1.56e-03

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.38  E-value: 1.56e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207184422  999 KRPHQCQICKKAFKHKHHLIEHSRLHSGEKPYQC--DKCGKRFSHSGSYSQHMNHR 1052
Cdd:COG5048     31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTH 86
zf-H2C2_2 pfam13465
Zinc-finger double domain;
259-296 7.93e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 7.93e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1207184422  259 LERHMATHKpardqpqllnegaGNRKFKCTECGKAFKY 296
Cdd:pfam13465    2 LKRHMRTHT-------------GEKPYKCPECGKSFKS 26
 
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