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Conserved domains on  [gi|1958746760|ref|XP_038953709|]
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zinc finger protein SNAI3 isoform X2 [Rattus norvegicus]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 11815261)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
222-245 1.77e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 1.77e-04
                          10        20
                  ....*....|....*....|....
gi 1958746760 222 LQGHIRTHTGEKPYTCSHCSRAFA 245
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
207-229 6.96e-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: 33.43  E-value: 6.96e-03
                          10        20
                  ....*....|....*....|...
gi 1958746760 207 CVCKVCGKAFSRPWLLQGHIRTH 229
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA00733 super family cl26169
hypothetical protein
181-226 9.96e-03

hypothetical protein


The actual alignment was detected with superfamily member PHA00733:

Pssm-ID: 177301  Cd Length: 128  Bit Score: 35.62  E-value: 9.96e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1958746760 181 FTCRYCDKEYASLGALKMHIRTHTLPCVCKVCGKAFSRPWLLQGHI 226
Cdd:PHA00733   74 YVCPLCLMPFSSSVSLKQHIRYTEHSKVCPVCGKEFRNTDSTLDHV 119
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
222-245 1.77e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 1.77e-04
                          10        20
                  ....*....|....*....|....
gi 1958746760 222 LQGHIRTHTGEKPYTCSHCSRAFA 245
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
212-257 1.48e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 39.68  E-value: 1.48e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958746760 212 CGKAFSRPWLLQGHIRTHTGEKPYTCSHCSRA--FADRSNLRAHLQTH 257
Cdd:COG5048    39 CTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTH 86
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
207-229 6.96e-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: 33.43  E-value: 6.96e-03
                          10        20
                  ....*....|....*....|...
gi 1958746760 207 CVCKVCGKAFSRPWLLQGHIRTH 229
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA00733 PHA00733
hypothetical protein
181-226 9.96e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 35.62  E-value: 9.96e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1958746760 181 FTCRYCDKEYASLGALKMHIRTHTLPCVCKVCGKAFSRPWLLQGHI 226
Cdd:PHA00733   74 YVCPLCLMPFSSSVSLKQHIRYTEHSKVCPVCGKEFRNTDSTLDHV 119
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
222-245 1.77e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 1.77e-04
                          10        20
                  ....*....|....*....|....
gi 1958746760 222 LQGHIRTHTGEKPYTCSHCSRAFA 245
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
212-257 1.48e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 39.68  E-value: 1.48e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958746760 212 CGKAFSRPWLLQGHIRTHTGEKPYTCSHCSRA--FADRSNLRAHLQTH 257
Cdd:COG5048    39 CTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTH 86
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
207-229 6.96e-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: 33.43  E-value: 6.96e-03
                          10        20
                  ....*....|....*....|...
gi 1958746760 207 CVCKVCGKAFSRPWLLQGHIRTH 229
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA00733 PHA00733
hypothetical protein
181-226 9.96e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 35.62  E-value: 9.96e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1958746760 181 FTCRYCDKEYASLGALKMHIRTHTLPCVCKVCGKAFSRPWLLQGHI 226
Cdd:PHA00733   74 YVCPLCLMPFSSSVSLKQHIRYTEHSKVCPVCGKEFRNTDSTLDHV 119
 
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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