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Conserved domains on  [gi|1834198873|ref|NP_001287254|]
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uncharacterized protein Dmel_CG16779, isoform G [Drosophila melanogaster]

Protein Classification

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 ...
 1738-1782 1.65e-10

'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: 58.01  E-value: 1.65e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1834198873 1738 KWTAYELEQFLRGLEKNGKDFGKIASE-LQTKSSGECVQMYYFWKK 1782
Cdd:cd11661      1 EWSESEAKLFEEGLRKYGKDFHDIRQDfLPWKSVGELVEFYYMWKK 46
ELM2 pfam01448
ELM2 domain; The ELM2 (Egl-27 and MTA1 homology 2) domain is a small domain of unknown ...
 1646-1696 3.65e-07

ELM2 domain; The ELM2 (Egl-27 and MTA1 homology 2) domain is a small domain of unknown function. It is found in the MTA1 protein that is part of the NuRD complex. The domain is usually found to the N terminus of a myb-like DNA binding domain pfam00249. ELM2 is also found associated with an ARID DNA binding domain pfam01388 in Swiss:O82364. This suggests that ELM2 may also be involved in DNA binding, or perhaps is a protein-protein interaction domain.


:

Pssm-ID: 460214  Cd Length: 53  Bit Score: 48.76  E-value: 3.65e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1834198873 1646 VNLGSTYQAQIPSCRPLEEALRDSPGAEMM--WNPEVQEDEKILMRYIDLSKS 1696
Cdd:pfam01448    1 IRVGPRYQAEIPELLPPSEEEDRYEEEDELlvWDPNHNLPDRKLDEYLVVARS 53
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 355-377 2.25e-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: 39.98  E-value: 2.25e-04
                           10        20
                   ....*....|....*....|...
gi 1834198873  355 YICALCSKAFKRQDHLNGHMMTH 377
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2_6 pfam13912
C2H2-type zinc finger;
1952-1975 1.91e-03

C2H2-type zinc finger;


:

Pssm-ID: 433576  Cd Length: 27  Bit Score: 37.22  E-value: 1.91e-03
                           10        20
                   ....*....|....*....|....
gi 1834198873 1952 FPCKVCGKVFNKVKSRSAHMKTHR 1975
Cdd:pfam13912    2 HECSECGKSFPSYQALGGHKKSHR 25
 
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 ...
 1738-1782 1.65e-10

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: 58.01  E-value: 1.65e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1834198873 1738 KWTAYELEQFLRGLEKNGKDFGKIASE-LQTKSSGECVQMYYFWKK 1782
Cdd:cd11661      1 EWSESEAKLFEEGLRKYGKDFHDIRQDfLPWKSVGELVEFYYMWKK 46
ELM2 pfam01448
ELM2 domain; The ELM2 (Egl-27 and MTA1 homology 2) domain is a small domain of unknown ...
 1646-1696 3.65e-07

ELM2 domain; The ELM2 (Egl-27 and MTA1 homology 2) domain is a small domain of unknown function. It is found in the MTA1 protein that is part of the NuRD complex. The domain is usually found to the N terminus of a myb-like DNA binding domain pfam00249. ELM2 is also found associated with an ARID DNA binding domain pfam01388 in Swiss:O82364. This suggests that ELM2 may also be involved in DNA binding, or perhaps is a protein-protein interaction domain.


Pssm-ID: 460214  Cd Length: 53  Bit Score: 48.76  E-value: 3.65e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1834198873 1646 VNLGSTYQAQIPSCRPLEEALRDSPGAEMM--WNPEVQEDEKILMRYIDLSKS 1696
Cdd:pfam01448    1 IRVGPRYQAEIPELLPPSEEEDRYEEEDELlvWDPNHNLPDRKLDEYLVVARS 53
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
1738-1782 3.66e-06

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


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 45.68  E-value: 3.66e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1834198873  1738 KWTAYELEQFLRGLEKNG-KDFGKIASELQTKSSGECVQMYYFWKK 1782
Cdd:smart00717    3 EWTEEEDELLIELVKKYGkNNWEKIAKELPGRTAEQCRERWRNLLK 48
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 1737-1781 7.13e-06

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: 44.80  E-value: 7.13e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1834198873 1737 MKWTAYELEQFLRGLEKNGKDFGKIASELQTKSSGECVQMYYFWK 1781
Cdd:pfam00249    2 GPWTPEEDELLLEAVEKLGNRWKKIAKLLPGRTDNQCKNRWQNYL 46
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 355-377 2.25e-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: 39.98  E-value: 2.25e-04
                           10        20
                   ....*....|....*....|...
gi 1834198873  355 YICALCSKAFKRQDHLNGHMMTH 377
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2_6 pfam13912
C2H2-type zinc finger;
1952-1975 1.91e-03

C2H2-type zinc finger;


Pssm-ID: 433576  Cd Length: 27  Bit Score: 37.22  E-value: 1.91e-03
                           10        20
                   ....*....|....*....|....
gi 1834198873 1952 FPCKVCGKVFNKVKSRSAHMKTHR 1975
Cdd:pfam13912    2 HECSECGKSFPSYQALGGHKKSHR 25
ZnF_C2H2 smart00355
zinc finger;
355-377 4.58e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 36.29  E-value: 4.58e-03
                            10        20
                    ....*....|....*....|...
gi 1834198873   355 YICALCSKAFKRQDHLNGHMMTH 377
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 ...
 1738-1782 1.65e-10

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: 58.01  E-value: 1.65e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1834198873 1738 KWTAYELEQFLRGLEKNGKDFGKIASE-LQTKSSGECVQMYYFWKK 1782
Cdd:cd11661      1 EWSESEAKLFEEGLRKYGKDFHDIRQDfLPWKSVGELVEFYYMWKK 46
ELM2 pfam01448
ELM2 domain; The ELM2 (Egl-27 and MTA1 homology 2) domain is a small domain of unknown ...
 1646-1696 3.65e-07

ELM2 domain; The ELM2 (Egl-27 and MTA1 homology 2) domain is a small domain of unknown function. It is found in the MTA1 protein that is part of the NuRD complex. The domain is usually found to the N terminus of a myb-like DNA binding domain pfam00249. ELM2 is also found associated with an ARID DNA binding domain pfam01388 in Swiss:O82364. This suggests that ELM2 may also be involved in DNA binding, or perhaps is a protein-protein interaction domain.


Pssm-ID: 460214  Cd Length: 53  Bit Score: 48.76  E-value: 3.65e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1834198873 1646 VNLGSTYQAQIPSCRPLEEALRDSPGAEMM--WNPEVQEDEKILMRYIDLSKS 1696
Cdd:pfam01448    1 IRVGPRYQAEIPELLPPSEEEDRYEEEDELlvWDPNHNLPDRKLDEYLVVARS 53
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 1738-1781 1.61e-06

'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: 46.41  E-value: 1.61e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1834198873 1738 KWTAYELEQFLRGLEKNG-KDFGKIASELQTKSSGECVQMYYFWK 1781
Cdd:cd00167      1 PWTEEEDELLLEAVKKYGkNNWEKIAKELPGRTPKQCRERWRNLL 45
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
1738-1782 3.66e-06

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


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 45.68  E-value: 3.66e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1834198873  1738 KWTAYELEQFLRGLEKNG-KDFGKIASELQTKSSGECVQMYYFWKK 1782
Cdd:smart00717    3 EWTEEEDELLIELVKKYGkNNWEKIAKELPGRTAEQCRERWRNLLK 48
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 1737-1781 7.13e-06

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: 44.80  E-value: 7.13e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1834198873 1737 MKWTAYELEQFLRGLEKNGKDFGKIASELQTKSSGECVQMYYFWK 1781
Cdd:pfam00249    2 GPWTPEEDELLLEAVEKLGNRWKKIAKLLPGRTDNQCKNRWQNYL 46
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 355-377 2.25e-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: 39.98  E-value: 2.25e-04
                           10        20
                   ....*....|....*....|...
gi 1834198873  355 YICALCSKAFKRQDHLNGHMMTH 377
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2_6 pfam13912
C2H2-type zinc finger;
355-378 1.58e-03

C2H2-type zinc finger;


Pssm-ID: 433576  Cd Length: 27  Bit Score: 37.61  E-value: 1.58e-03
                           10        20
                   ....*....|....*....|....
gi 1834198873  355 YICALCSKAFKRQDHLNGHMMTHR 378
Cdd:pfam13912    2 HECSECGKSFPSYQALGGHKKSHR 25
zf-C2H2_6 pfam13912
C2H2-type zinc finger;
1952-1975 1.91e-03

C2H2-type zinc finger;


Pssm-ID: 433576  Cd Length: 27  Bit Score: 37.22  E-value: 1.91e-03
                           10        20
                   ....*....|....*....|....
gi 1834198873 1952 FPCKVCGKVFNKVKSRSAHMKTHR 1975
Cdd:pfam13912    2 HECSECGKSFPSYQALGGHKKSHR 25
ZnF_C2H2 smart00355
zinc finger;
355-377 4.58e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 36.29  E-value: 4.58e-03
                            10        20
                    ....*....|....*....|...
gi 1834198873   355 YICALCSKAFKRQDHLNGHMMTH 377
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 1952-1974 6.13e-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: 35.74  E-value: 6.13e-03
                           10        20
                   ....*....|....*....|...
gi 1834198873 1952 FPCKVCGKVFNKVKSRSAHMKTH 1974
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 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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