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Conserved domains on  [gi|119602839|gb|EAW82433|]
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hCG2039195, isoform CRA_a [Homo sapiens]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 10603440)

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

CATH:  3.30.160.60
Gene Ontology:  GO:0008270|GO:0003677
PubMed:  11361095|22803940|30718982
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
32-57 7.98e-07

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.28  E-value: 7.98e-07
                          10        20
                  ....*....|....*....|....*.
gi 119602839   32 DLRRHVRTHTGEKPYTCEICNKCFTR 57
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
5-27 7.67e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 7.67e-04
                          10        20
                  ....*....|....*....|...
gi 119602839    5 LVKHRIRHTGERPYSCSACGKCF 27
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
32-57 7.98e-07

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.28  E-value: 7.98e-07
                          10        20
                  ....*....|....*....|....*.
gi 119602839   32 DLRRHVRTHTGEKPYTCEICNKCFTR 57
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
5-27 7.67e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 7.67e-04
                          10        20
                  ....*....|....*....|...
gi 119602839    5 LVKHRIRHTGERPYSCSACGKCF 27
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
ZnF_C2H2 smart00355
zinc finger;
46-68 3.08e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 34.36  E-value: 3.08e-03
                           10        20
                   ....*....|....*....|...
gi 119602839    46 YTCEICNKCFTRSAVLRRHKKMH 68
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
32-57 7.98e-07

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.28  E-value: 7.98e-07
                          10        20
                  ....*....|....*....|....*.
gi 119602839   32 DLRRHVRTHTGEKPYTCEICNKCFTR 57
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 46-68 2.06e-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: 2.06e-04
                          10        20
                  ....*....|....*....|...
gi 119602839   46 YTCEICNKCFTRSAVLRRHKKMH 68
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
5-27 7.67e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 7.67e-04
                          10        20
                  ....*....|....*....|...
gi 119602839    5 LVKHRIRHTGERPYSCSACGKCF 27
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 18-40 2.03e-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: 34.58  E-value: 2.03e-03
                          10        20
                  ....*....|....*....|...
gi 119602839   18 YSCSACGKCFGGSGDLRRHVRTH 40
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
46-68 3.08e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 34.36  E-value: 3.08e-03
                           10        20
                   ....*....|....*....|...
gi 119602839    46 YTCEICNKCFTRSAVLRRHKKMH 68
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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