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Conserved domains on  [gi|27532961|ref|NP_082008|]
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doublesex- and mab-3-related transcription factor C2 [Mus musculus]

Protein Classification

DM domain-containing protein; doublesex- and mab-3-related transcription factor family protein( domain architecture ID 11107823)

DM (doublesex- and mab-3) domain-containing protein may dimerize and bind palindromic DNA; similar to Caenorhabditis elegans protein male abnormal 3 and doublesex- and mab-3-related transcription factor dmd-10; doublesex- and mab-3-related transcription factor (DMRT) family protein similar to human DMRT2, also called doublesex-like 2 protein, a transcriptional activator that directly regulates early activation of the myogenic determination gene MYF5 by binding in a sequence-specific manner to its early epaxial enhancer element

Gene Ontology:  GO:0043565|GO:0006355
PubMed:  22310892

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DMRT-like pfam15791
Doublesex-and mab-3-related transcription factor C1 and C2; DMRT-like is a C-terminal domain ...
 242-369 7.35e-41

Doublesex-and mab-3-related transcription factor C1 and C2; DMRT-like is a C-terminal domain found on eukaryotic proteins for doublesex-and mab-3-related transcription factors C1 and C2. This is not the DM DNA-binding region. The family is all disorder and low-complexity.


:

Pssm-ID: 464871  Cd Length: 119  Bit Score: 139.94  E-value: 7.35e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27532961   242 LSGEPQGPPNLPHTCSTLILQSCGTPDSLLLQPQAPGASCLAWTSGPSERQLQREAAEALVGLKDSSQAPrltpsvppnP 321
Cdd:pfam15791   1 LSGEPQGPPALPSTCSSLILQPCATPDPLLLQPQVPEASSLAWVSAASEWQRKLEAAEALLALKDSPQAP---------P 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 27532961   322 AWISLLHPCGPPAPPGGRGFQPVGPPLRPSPGSSVSLHIGRLGSISLL 369
Cdd:pfam15791  72 DSISLLHPCGPPAPAGGRGFQPPGPSLRPRPAPSVSLHIGHLGCISLL 119
DM pfam00751
DM DNA binding domain; The DM domain is named after dsx and mab-3. dsx contains a single ...
 38-84 5.00e-24

DM DNA binding domain; The DM domain is named after dsx and mab-3. dsx contains a single amino-terminal DM domain, whereas mab-3 contains two amino-terminal domains. The DM domain has a pattern of conserved zinc chelating residues C2H2C4. The dsx DM domain has been shown to dimerize and bind palindromic DNA.


:

Pssm-ID: 459924  Cd Length: 47  Bit Score: 93.11  E-value: 5.00e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 27532961    38 RSPTCARCRNHGVTAHLKGHKRLCLFQACECHKCVLILERRRVMAAQ 84
Cdd:pfam00751   1 RSPKCARCRNHGVRVPLKGHKRYCPYRDCSCPKCLLVAERQRVMAAQ 47
 
Name Accession Description Interval E-value
DMRT-like pfam15791
Doublesex-and mab-3-related transcription factor C1 and C2; DMRT-like is a C-terminal domain ...
 242-369 7.35e-41

Doublesex-and mab-3-related transcription factor C1 and C2; DMRT-like is a C-terminal domain found on eukaryotic proteins for doublesex-and mab-3-related transcription factors C1 and C2. This is not the DM DNA-binding region. The family is all disorder and low-complexity.


Pssm-ID: 464871  Cd Length: 119  Bit Score: 139.94  E-value: 7.35e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27532961   242 LSGEPQGPPNLPHTCSTLILQSCGTPDSLLLQPQAPGASCLAWTSGPSERQLQREAAEALVGLKDSSQAPrltpsvppnP 321
Cdd:pfam15791   1 LSGEPQGPPALPSTCSSLILQPCATPDPLLLQPQVPEASSLAWVSAASEWQRKLEAAEALLALKDSPQAP---------P 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 27532961   322 AWISLLHPCGPPAPPGGRGFQPVGPPLRPSPGSSVSLHIGRLGSISLL 369
Cdd:pfam15791  72 DSISLLHPCGPPAPAGGRGFQPPGPSLRPRPAPSVSLHIGHLGCISLL 119
DM pfam00751
DM DNA binding domain; The DM domain is named after dsx and mab-3. dsx contains a single ...
 38-84 5.00e-24

DM DNA binding domain; The DM domain is named after dsx and mab-3. dsx contains a single amino-terminal DM domain, whereas mab-3 contains two amino-terminal domains. The DM domain has a pattern of conserved zinc chelating residues C2H2C4. The dsx DM domain has been shown to dimerize and bind palindromic DNA.


Pssm-ID: 459924  Cd Length: 47  Bit Score: 93.11  E-value: 5.00e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 27532961    38 RSPTCARCRNHGVTAHLKGHKRLCLFQACECHKCVLILERRRVMAAQ 84
Cdd:pfam00751   1 RSPKCARCRNHGVRVPLKGHKRYCPYRDCSCPKCLLVAERQRVMAAQ 47
DM smart00301
Doublesex DNA-binding motif;
38-91 5.92e-19

Doublesex DNA-binding motif;


Pssm-ID: 214606  Cd Length: 54  Bit Score: 79.71  E-value: 5.92e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 27532961     38 RSPTCARCRNHGVTAHLKGHKRLCLFQACECHKCVLILERRRVMAAQVALRRQQ 91
Cdd:smart00301   1 RIPYCQKCENHGVKVPLKGHKPECPFRDCECEKCTLVEKRRALMALQIKLKREQ 54
 
Name Accession Description Interval E-value
DMRT-like pfam15791
Doublesex-and mab-3-related transcription factor C1 and C2; DMRT-like is a C-terminal domain ...
 242-369 7.35e-41

Doublesex-and mab-3-related transcription factor C1 and C2; DMRT-like is a C-terminal domain found on eukaryotic proteins for doublesex-and mab-3-related transcription factors C1 and C2. This is not the DM DNA-binding region. The family is all disorder and low-complexity.


Pssm-ID: 464871  Cd Length: 119  Bit Score: 139.94  E-value: 7.35e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27532961   242 LSGEPQGPPNLPHTCSTLILQSCGTPDSLLLQPQAPGASCLAWTSGPSERQLQREAAEALVGLKDSSQAPrltpsvppnP 321
Cdd:pfam15791   1 LSGEPQGPPALPSTCSSLILQPCATPDPLLLQPQVPEASSLAWVSAASEWQRKLEAAEALLALKDSPQAP---------P 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 27532961   322 AWISLLHPCGPPAPPGGRGFQPVGPPLRPSPGSSVSLHIGRLGSISLL 369
Cdd:pfam15791  72 DSISLLHPCGPPAPAGGRGFQPPGPSLRPRPAPSVSLHIGHLGCISLL 119
DM pfam00751
DM DNA binding domain; The DM domain is named after dsx and mab-3. dsx contains a single ...
 38-84 5.00e-24

DM DNA binding domain; The DM domain is named after dsx and mab-3. dsx contains a single amino-terminal DM domain, whereas mab-3 contains two amino-terminal domains. The DM domain has a pattern of conserved zinc chelating residues C2H2C4. The dsx DM domain has been shown to dimerize and bind palindromic DNA.


Pssm-ID: 459924  Cd Length: 47  Bit Score: 93.11  E-value: 5.00e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 27532961    38 RSPTCARCRNHGVTAHLKGHKRLCLFQACECHKCVLILERRRVMAAQ 84
Cdd:pfam00751   1 RSPKCARCRNHGVRVPLKGHKRYCPYRDCSCPKCLLVAERQRVMAAQ 47
DM smart00301
Doublesex DNA-binding motif;
38-91 5.92e-19

Doublesex DNA-binding motif;


Pssm-ID: 214606  Cd Length: 54  Bit Score: 79.71  E-value: 5.92e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 27532961     38 RSPTCARCRNHGVTAHLKGHKRLCLFQACECHKCVLILERRRVMAAQVALRRQQ 91
Cdd:smart00301   1 RIPYCQKCENHGVKVPLKGHKPECPFRDCECEKCTLVEKRRALMALQIKLKREQ 54
 
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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