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Conserved domains on  [gi|193208134|ref|NP_001122953|]
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Suppressor of activated egl-4 protein 1 [Caenorhabditis elegans]

Protein Classification

SANT/Myb-like DNA-binding domain-containing C2H2 zinc finger protein( domain architecture ID 11025975)

SANT (SWI3, ADA2, N-CoR and TFIIIB)/Myb-like DNA-binding domain-containing C2H2 (Cys2His2) zinc finger protein binds DNA and may function as a transcription factor, and may also bind zinc ions; similar to Caenorhabditis elegans suppressor of activated egl-4 protein 1

CATH:  1.20.58.1880
Gene Ontology:  GO:0046872|GO:0003714|GO:0045892|GO:0003677|GO:0006355|GO:0003700
PubMed:  8882580|22803940
SCOP:  4000317

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SANT super family cl21498
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 245-288 7.20e-09

'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.


The actual alignment was detected with superfamily member cd11661:

Pssm-ID: 473887 [Multi-domain]  Cd Length: 46  Bit Score: 51.85  E-value: 7.20e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 193208134 245 WTPDEIYQFQDAIYQSEKDFDKVAVE-LPGKSVKECVQFYYTWKK 288
Cdd:cd11661    2 WSESEAKLFEEGLRKYGKDFHDIRQDfLPWKSVGELVEFYYMWKK 46
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 416-438 1.32e-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: 36.12  E-value: 1.32e-03
                          10        20
                  ....*....|....*....|...
gi 193208134  416 FHCRLCDKCFEKVKSLNAHMKSH 438
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SANT_MTA3_like cd11661
Myb-Like Dna-Binding Domain of MTA3 and related proteins; Members in this SANT/myb family ...
 245-288 7.20e-09

Myb-Like Dna-Binding Domain of MTA3 and related proteins; Members in this SANT/myb family include domains found in mouse metastasis-associated protein 3 (MTA3) proteins and arginine-glutamic dipeptide (RERE) repeats proteins. SANT (SWI3, ADA2, N-CoR and TFIIIB) DNA-binding domains are a diverse set of proteins that share a common 3 alpha-helix bundle. MTA3 has been shown to interact with nucleosome remodeling and deacetylase (NuRD) proteins CHD4 and HDAC1, and the core cohesin complex protein RAD21 in the ovary, and regulate G2/M progression in proliferating granulosa cells. RERE belongs to the atrophin family and has been identified as a nuclear receptor corepressor; altered expression levels of RERE are associated with cancer in humans while mutations of Rere in mice cause failure in closing the anterior neural tube and fusion of the telencephalic and optic vesicles during embryogenesis.


Pssm-ID: 212559 [Multi-domain]  Cd Length: 46  Bit Score: 51.85  E-value: 7.20e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 193208134 245 WTPDEIYQFQDAIYQSEKDFDKVAVE-LPGKSVKECVQFYYTWKK 288
Cdd:cd11661    2 WSESEAKLFEEGLRKYGKDFHDIRQDfLPWKSVGELVEFYYMWKK 46
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 245-287 1.88e-07

Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.


Pssm-ID: 459731 [Multi-domain]  Cd Length: 46  Bit Score: 47.50  E-value: 1.88e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 193208134  245 WTPDEIYQFQDAIYQSEKDFDKVAVELPGKSVKECVQFYYTWK 287
Cdd:pfam00249   4 WTPEEDELLLEAVEKLGNRWKKIAKLLPGRTDNQCKNRWQNYL 46
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
245-288 2.56e-07

SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 47.22  E-value: 2.56e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 193208134   245 WTPDEIYQFQDAIYQS-EKDFDKVAVELPGKSVKECVQFYYTWKK 288
Cdd:smart00717   4 WTEEEDELLIELVKKYgKNNWEKIAKELPGRTAEQCRERWRNLLK 48
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 416-438 1.32e-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: 36.12  E-value: 1.32e-03
                          10        20
                  ....*....|....*....|...
gi 193208134  416 FHCRLCDKCFEKVKSLNAHMKSH 438
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
416-438 4.04e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.13  E-value: 4.04e-03
                           10        20
                   ....*....|....*....|...
gi 193208134   416 FHCRLCDKCFEKVKSLNAHMKSH 438
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
 
Name Accession Description Interval E-value
SANT_MTA3_like cd11661
Myb-Like Dna-Binding Domain of MTA3 and related proteins; Members in this SANT/myb family ...
 245-288 7.20e-09

Myb-Like Dna-Binding Domain of MTA3 and related proteins; Members in this SANT/myb family include domains found in mouse metastasis-associated protein 3 (MTA3) proteins and arginine-glutamic dipeptide (RERE) repeats proteins. SANT (SWI3, ADA2, N-CoR and TFIIIB) DNA-binding domains are a diverse set of proteins that share a common 3 alpha-helix bundle. MTA3 has been shown to interact with nucleosome remodeling and deacetylase (NuRD) proteins CHD4 and HDAC1, and the core cohesin complex protein RAD21 in the ovary, and regulate G2/M progression in proliferating granulosa cells. RERE belongs to the atrophin family and has been identified as a nuclear receptor corepressor; altered expression levels of RERE are associated with cancer in humans while mutations of Rere in mice cause failure in closing the anterior neural tube and fusion of the telencephalic and optic vesicles during embryogenesis.


Pssm-ID: 212559 [Multi-domain]  Cd Length: 46  Bit Score: 51.85  E-value: 7.20e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 193208134 245 WTPDEIYQFQDAIYQSEKDFDKVAVE-LPGKSVKECVQFYYTWKK 288
Cdd:cd11661    2 WSESEAKLFEEGLRKYGKDFHDIRQDfLPWKSVGELVEFYYMWKK 46
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 245-287 7.59e-08

'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.


Pssm-ID: 238096 [Multi-domain]  Cd Length: 45  Bit Score: 48.73  E-value: 7.59e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 193208134 245 WTPDEIYQFQDAIYQS-EKDFDKVAVELPGKSVKECVQFYYTWK 287
Cdd:cd00167    2 WTEEEDELLLEAVKKYgKNNWEKIAKELPGRTPKQCRERWRNLL 45
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 245-287 1.88e-07

Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.


Pssm-ID: 459731 [Multi-domain]  Cd Length: 46  Bit Score: 47.50  E-value: 1.88e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 193208134  245 WTPDEIYQFQDAIYQSEKDFDKVAVELPGKSVKECVQFYYTWK 287
Cdd:pfam00249   4 WTPEEDELLLEAVEKLGNRWKKIAKLLPGRTDNQCKNRWQNYL 46
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
245-288 2.56e-07

SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 47.22  E-value: 2.56e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 193208134   245 WTPDEIYQFQDAIYQS-EKDFDKVAVELPGKSVKECVQFYYTWKK 288
Cdd:smart00717   4 WTEEEDELLIELVKKYgKNNWEKIAKELPGRTAEQCRERWRNLLK 48
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 416-438 1.32e-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: 36.12  E-value: 1.32e-03
                          10        20
                  ....*....|....*....|...
gi 193208134  416 FHCRLCDKCFEKVKSLNAHMKSH 438
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 416-438 1.68e-03

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


Pssm-ID: 464025  Cd Length: 24  Bit Score: 36.08  E-value: 1.68e-03
                          10        20
                  ....*....|....*....|...
gi 193208134  416 FHCRLCDKCFEKVKSLNAHMKSH 438
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTH 23
ZnF_C2H2 smart00355
zinc finger;
416-438 4.04e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.13  E-value: 4.04e-03
                           10        20
                   ....*....|....*....|...
gi 193208134   416 FHCRLCDKCFEKVKSLNAHMKSH 438
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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