NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|595763471|ref|NP_001277749|]
View 

zinc finger and SCAN domain-containing protein 29 isoform b [Mus musculus]

Protein Classification

myb/SANT-like DNA-binding domain-containing protein( domain architecture ID 10619758)

nyb/SANT (SWI3, ADA2, N-CoR and TFIIIB)-like DNA-binding domain-containing protein may bind DNA and function as a transcription factor

CATH:  1.20.58.1880
Gene Ontology:  GO:0003700|GO:0003677
PubMed:  8882580
SCOP:  4000317

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
132-213 1.74e-18

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.


:

Pssm-ID: 463994  Cd Length: 84  Bit Score: 78.46  E-value: 1.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763471  132 GVHWGYKETRTLLAILSqtEFYEALR--NCHRNSQVYGAVAGRLREYGFLRTLEQCRTKFKGLQKSYRKVKSGH--PPDT 207
Cdd:pfam13837   1 RNKWTEEETLALIEIWG--ERLELRFqeSKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKYRKEKEGNngSGSS 78

                  ....*.
gi 595763471  208 CPFFEE 213
Cdd:pfam13837  79 WPFFEE 84
 
Name Accession Description Interval E-value
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
132-213 1.74e-18

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.


Pssm-ID: 463994  Cd Length: 84  Bit Score: 78.46  E-value: 1.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763471  132 GVHWGYKETRTLLAILSqtEFYEALR--NCHRNSQVYGAVAGRLREYGFLRTLEQCRTKFKGLQKSYRKVKSGH--PPDT 207
Cdd:pfam13837   1 RNKWTEEETLALIEIWG--ERLELRFqeSKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKYRKEKEGNngSGSS 78

                  ....*.
gi 595763471  208 CPFFEE 213
Cdd:pfam13837  79 WPFFEE 84
GT1 cd12203
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription ...
135-200 9.30e-07

GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription factors. GT-1 binds the GT cis-element of rbcS-3A, a light-induced gene, as a dimer. Arabidopsis GT-1 is a trans-activator and acts in the stabilization of components of the transcription pre-initiation complex comprised of TFIIA-TBP-TATA. The isolated GT-1 DNA-binding domain is sufficient to bind DNA. This region closely resembles the myb domain, but with longer helices. It has been proposed that GT-1 may respond to light signals via calcium-dependent phosphorylation to create a light-modulated molecular switch. These proteins are members of the SANT/myb group. SANT is named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. The SANT domain resembles the 3 alpha-helix bundle of the DNA-binding Myb domains and is found in a diverse set of proteins.


Pssm-ID: 213402  Cd Length: 66  Bit Score: 45.35  E-value: 9.30e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 595763471 135 WGYKETRTLLAIlsQTEFYEALRNCHRNSQVYGAVAGRLREYGFLRTLEQCRTKFKGLQKSYRKVK 200
Cdd:cd12203    3 WPREETLSLIRL--RREMESRFQETKSKKALWEEIAAKMRELGYNRSAKQCKEKWENLNKYYKKVK 66
 
Name Accession Description Interval E-value
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
132-213 1.74e-18

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.


Pssm-ID: 463994  Cd Length: 84  Bit Score: 78.46  E-value: 1.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595763471  132 GVHWGYKETRTLLAILSqtEFYEALR--NCHRNSQVYGAVAGRLREYGFLRTLEQCRTKFKGLQKSYRKVKSGH--PPDT 207
Cdd:pfam13837   1 RNKWTEEETLALIEIWG--ERLELRFqeSKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKYRKEKEGNngSGSS 78

                  ....*.
gi 595763471  208 CPFFEE 213
Cdd:pfam13837  79 WPFFEE 84
GT1 cd12203
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription ...
135-200 9.30e-07

GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription factors. GT-1 binds the GT cis-element of rbcS-3A, a light-induced gene, as a dimer. Arabidopsis GT-1 is a trans-activator and acts in the stabilization of components of the transcription pre-initiation complex comprised of TFIIA-TBP-TATA. The isolated GT-1 DNA-binding domain is sufficient to bind DNA. This region closely resembles the myb domain, but with longer helices. It has been proposed that GT-1 may respond to light signals via calcium-dependent phosphorylation to create a light-modulated molecular switch. These proteins are members of the SANT/myb group. SANT is named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. The SANT domain resembles the 3 alpha-helix bundle of the DNA-binding Myb domains and is found in a diverse set of proteins.


Pssm-ID: 213402  Cd Length: 66  Bit Score: 45.35  E-value: 9.30e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 595763471 135 WGYKETRTLLAIlsQTEFYEALRNCHRNSQVYGAVAGRLREYGFLRTLEQCRTKFKGLQKSYRKVK 200
Cdd:cd12203    3 WPREETLSLIRL--RREMESRFQETKSKKALWEEIAAKMRELGYNRSAKQCKEKWENLNKYYKKVK 66
MADF_DNA_bdg pfam10545
Alcohol dehydrogenase transcription factor Myb/SANT-like; The myb/SANT-like domain in Adf-1 ...
157-217 1.41e-03

Alcohol dehydrogenase transcription factor Myb/SANT-like; The myb/SANT-like domain in Adf-1 (MADF) is an approximately 80-amino-acid module that directs sequence specific DNA binding to a site consisting of multiple tri-nucleotide repeats. The MADF domain is found in one or more copies in eukaryotic and viral proteins and is often associated with the BESS domain. It is likely that the MADF domain is more closely related to the myb/SANT domain than it is to other HTH domains.


Pssm-ID: 463144  Cd Length: 84  Bit Score: 36.88  E-value: 1.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 595763471  157 RNCHRNSQVYGAVAgrlREYGFLRTLEQCRTKFKGLQKSYRKVK-------SGHPPDTCPFFEEMEAL 217
Cdd:pfam10545  20 RNRDARERAWEEIA---EELGSDVPVEDCKKRWKNLRDQYRRELrrkrtnsGELYKSRWYYYEELSFL 84
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH