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Conserved domains on  [gi|574957236|ref|NP_001276323|]
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zinc finger protein ZFAT isoform 2 [Homo sapiens]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 10443135)

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_5 pfam13909
C2H2-type zinc-finger domain;
287-311 1.28e-05

C2H2-type zinc-finger domain;


:

Pssm-ID: 404746 [Multi-domain]  Cd Length: 25  Bit Score: 42.92  E-value: 1.28e-05
                           10        20
                   ....*....|....*....|....*
gi 574957236   287 YKCPQCSYASAIKANLNVHLRKHTG 311
Cdd:pfam13909    1 YKCSQCDYSTAWKSNLKRHLRKHTG 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
273-297 1.90e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.90e-04
                           10        20
                   ....*....|....*....|....*
gi 574957236   273 SLQAHLRIHTNEKPYKCPQCSYASA 297
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
259-281 1.08e-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: 37.28  E-value: 1.08e-03
                           10        20
                   ....*....|....*....|...
gi 574957236   259 FTCEYCNKVFKFKHSLQAHLRIH 281
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_5 pfam13909
C2H2-type zinc-finger domain;
954-976 3.92e-03

C2H2-type zinc-finger domain;


:

Pssm-ID: 404746 [Multi-domain]  Cd Length: 25  Bit Score: 35.99  E-value: 3.92e-03
                           10        20
                   ....*....|....*....|...
gi 574957236   954 FKCTVCDYTAAQKPQLLRHMEQH 976
Cdd:pfam13909    1 YKCSQCDYSTAWKSNLKRHLRKH 23
rne super family cl35953
ribonuclease E; Reviewed
1096-1230 5.61e-03

ribonuclease E; Reviewed


The actual alignment was detected with superfamily member PRK10811:

Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 41.18  E-value: 5.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574957236 1096 VAALQDlrytSESGDRLDPTAVNILQQIIELGAEThDATALASVVAMAPGTVTVVKQVTEEEPSSNHTVMIQETVQQASV 1175
Cdd:PRK10811  847 VVRPQD----VQVEEQREAEEVQVQPVVAEVPVAA-AVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIA 921
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 574957236 1176 E-LAEQHHLVVSSDDVEGIETVTVYTQGGEASEFIVYVQEAMQPVEEQAVEQPAQE 1230
Cdd:PRK10811  922 ApVTEQPQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVA 977
 
Name Accession Description Interval E-value
zf-H2C2_5 pfam13909
C2H2-type zinc-finger domain;
287-311 1.28e-05

C2H2-type zinc-finger domain;


Pssm-ID: 404746 [Multi-domain]  Cd Length: 25  Bit Score: 42.92  E-value: 1.28e-05
                           10        20
                   ....*....|....*....|....*
gi 574957236   287 YKCPQCSYASAIKANLNVHLRKHTG 311
Cdd:pfam13909    1 YKCSQCDYSTAWKSNLKRHLRKHTG 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
273-297 1.90e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.90e-04
                           10        20
                   ....*....|....*....|....*
gi 574957236   273 SLQAHLRIHTNEKPYKCPQCSYASA 297
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
259-281 1.08e-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: 37.28  E-value: 1.08e-03
                           10        20
                   ....*....|....*....|...
gi 574957236   259 FTCEYCNKVFKFKHSLQAHLRIH 281
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_5 pfam13909
C2H2-type zinc-finger domain;
954-976 3.92e-03

C2H2-type zinc-finger domain;


Pssm-ID: 404746 [Multi-domain]  Cd Length: 25  Bit Score: 35.99  E-value: 3.92e-03
                           10        20
                   ....*....|....*....|...
gi 574957236   954 FKCTVCDYTAAQKPQLLRHMEQH 976
Cdd:pfam13909    1 YKCSQCDYSTAWKSNLKRHLRKH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
261-338 4.31e-03

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 37.54  E-value: 4.31e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 574957236  261 CEYCNKVFKFKHSLQAHLRIHTnekpYKCPQCSyasaikanlnvhlRKHTgekfacdycsftclSKGHLKVHIERVHK 338
Cdd:cd20908     4 CYYCDREFDDEKILIQHQKAKH----FKCHICH-------------KKLY--------------TAGGLAVHCLQVHK 50
rne PRK10811
ribonuclease E; Reviewed
1096-1230 5.61e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 41.18  E-value: 5.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574957236 1096 VAALQDlrytSESGDRLDPTAVNILQQIIELGAEThDATALASVVAMAPGTVTVVKQVTEEEPSSNHTVMIQETVQQASV 1175
Cdd:PRK10811  847 VVRPQD----VQVEEQREAEEVQVQPVVAEVPVAA-AVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIA 921
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 574957236 1176 E-LAEQHHLVVSSDDVEGIETVTVYTQGGEASEFIVYVQEAMQPVEEQAVEQPAQE 1230
Cdd:PRK10811  922 ApVTEQPQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVA 977
 
Name Accession Description Interval E-value
zf-H2C2_5 pfam13909
C2H2-type zinc-finger domain;
287-311 1.28e-05

C2H2-type zinc-finger domain;


Pssm-ID: 404746 [Multi-domain]  Cd Length: 25  Bit Score: 42.92  E-value: 1.28e-05
                           10        20
                   ....*....|....*....|....*
gi 574957236   287 YKCPQCSYASAIKANLNVHLRKHTG 311
Cdd:pfam13909    1 YKCSQCDYSTAWKSNLKRHLRKHTG 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
273-297 1.90e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.90e-04
                           10        20
                   ....*....|....*....|....*
gi 574957236   273 SLQAHLRIHTNEKPYKCPQCSYASA 297
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
259-281 1.08e-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: 37.28  E-value: 1.08e-03
                           10        20
                   ....*....|....*....|...
gi 574957236   259 FTCEYCNKVFKFKHSLQAHLRIH 281
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_5 pfam13909
C2H2-type zinc-finger domain;
954-976 3.92e-03

C2H2-type zinc-finger domain;


Pssm-ID: 404746 [Multi-domain]  Cd Length: 25  Bit Score: 35.99  E-value: 3.92e-03
                           10        20
                   ....*....|....*....|...
gi 574957236   954 FKCTVCDYTAAQKPQLLRHMEQH 976
Cdd:pfam13909    1 YKCSQCDYSTAWKSNLKRHLRKH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
261-338 4.31e-03

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 37.54  E-value: 4.31e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 574957236  261 CEYCNKVFKFKHSLQAHLRIHTnekpYKCPQCSyasaikanlnvhlRKHTgekfacdycsftclSKGHLKVHIERVHK 338
Cdd:cd20908     4 CYYCDREFDDEKILIQHQKAKH----FKCHICH-------------KKLY--------------TAGGLAVHCLQVHK 50
rne PRK10811
ribonuclease E; Reviewed
1096-1230 5.61e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 41.18  E-value: 5.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574957236 1096 VAALQDlrytSESGDRLDPTAVNILQQIIELGAEThDATALASVVAMAPGTVTVVKQVTEEEPSSNHTVMIQETVQQASV 1175
Cdd:PRK10811  847 VVRPQD----VQVEEQREAEEVQVQPVVAEVPVAA-AVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIA 921
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 574957236 1176 E-LAEQHHLVVSSDDVEGIETVTVYTQGGEASEFIVYVQEAMQPVEEQAVEQPAQE 1230
Cdd:PRK10811  922 ApVTEQPQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVA 977
 
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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