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Conserved domains on  [gi|1831514709|ref|NP_001367237|]
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CXXC-type zinc finger protein 1 [Caenorhabditis elegans]

Protein Classification

CpG_bind_C domain-containing protein( domain architecture ID 10573920)

CpG_bind_C domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CpG_bind_C pfam12269
CpG binding protein C-terminal domain; CpG-binding protein is a transcriptional activator that ...
1-248 7.59e-98

CpG binding protein C-terminal domain; CpG-binding protein is a transcriptional activator that exhibits a DNA binding specificity for unmethylated CpG motifs. CpG is made of a PHD1, an acidic, a basic, a coiled-coil, and a PHD2 domains. This protein contains three cysteine-rich domains identified at the N-terminal, central region and C-terminal of the protein, where the central cysteine-rich domain is located within the DNA-binding domain, found between PHD1 and the acidic domains. This domain is found in eukaryotes, and is approximately 240 amino acids in length. It is found at the C-terminal of the CpG-binding protein containing the coiled-coil and PHD2 domains.


:

Pssm-ID: 463514  Cd Length: 235  Bit Score: 288.43  E-value: 7.59e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831514709   1 MRLTEILPNRCKQYFFEgpsggPRSLEDEIKPKRAKINREVQKLTESEKNMMAFLNKLVEFIKTQLKLqPLGTEE----- 75
Cdd:pfam12269   3 NRIYEILPQRIQEWQLS-----PCVAEEENKKKLEKIRKEQQEAREALKELDARHQELDAIIERAKKL-PVDTEEeendd 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831514709  76 RYDDNLYEGCIVCGLpDIPLLKYTKHIELCWARSEKAISFGAPEKNNDM---FYCEKYDSRTNSFCKRLKSLCPEHRKLG 152
Cdd:pfam12269  77 EDDDELSIYCVTCGH-EIHSRTAIKHMEKCFNKYESQTSFGSIYKTRIEgnsMFCDFYNPQQKTYCKRLKVLCPEHTKEP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831514709 153 DEQHLKVCGYPKkwedgmietaktvseLIEMEDPFGEEgCRTKKDACHKHHKWIPSLRGTIELEQACLFQKMYELCHEMH 232
Cdd:pfam12269 156 KIPDTEVCGCPL---------------VRNVFDPTGEF-CRAPKKKCVKHYCWEKLRRAEIDLERVRQWLKLDELFEQER 219
                         250
                  ....*....|....*.
gi 1831514709 233 KLNAHAEWTTNALSIM 248
Cdd:pfam12269 220 QIRTAMANRAGVLGLM 235
 
Name Accession Description Interval E-value
CpG_bind_C pfam12269
CpG binding protein C-terminal domain; CpG-binding protein is a transcriptional activator that ...
1-248 7.59e-98

CpG binding protein C-terminal domain; CpG-binding protein is a transcriptional activator that exhibits a DNA binding specificity for unmethylated CpG motifs. CpG is made of a PHD1, an acidic, a basic, a coiled-coil, and a PHD2 domains. This protein contains three cysteine-rich domains identified at the N-terminal, central region and C-terminal of the protein, where the central cysteine-rich domain is located within the DNA-binding domain, found between PHD1 and the acidic domains. This domain is found in eukaryotes, and is approximately 240 amino acids in length. It is found at the C-terminal of the CpG-binding protein containing the coiled-coil and PHD2 domains.


Pssm-ID: 463514  Cd Length: 235  Bit Score: 288.43  E-value: 7.59e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831514709   1 MRLTEILPNRCKQYFFEgpsggPRSLEDEIKPKRAKINREVQKLTESEKNMMAFLNKLVEFIKTQLKLqPLGTEE----- 75
Cdd:pfam12269   3 NRIYEILPQRIQEWQLS-----PCVAEEENKKKLEKIRKEQQEAREALKELDARHQELDAIIERAKKL-PVDTEEeendd 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831514709  76 RYDDNLYEGCIVCGLpDIPLLKYTKHIELCWARSEKAISFGAPEKNNDM---FYCEKYDSRTNSFCKRLKSLCPEHRKLG 152
Cdd:pfam12269  77 EDDDELSIYCVTCGH-EIHSRTAIKHMEKCFNKYESQTSFGSIYKTRIEgnsMFCDFYNPQQKTYCKRLKVLCPEHTKEP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831514709 153 DEQHLKVCGYPKkwedgmietaktvseLIEMEDPFGEEgCRTKKDACHKHHKWIPSLRGTIELEQACLFQKMYELCHEMH 232
Cdd:pfam12269 156 KIPDTEVCGCPL---------------VRNVFDPTGEF-CRAPKKKCVKHYCWEKLRRAEIDLERVRQWLKLDELFEQER 219
                         250
                  ....*....|....*.
gi 1831514709 233 KLNAHAEWTTNALSIM 248
Cdd:pfam12269 220 QIRTAMANRAGVLGLM 235
 
Name Accession Description Interval E-value
CpG_bind_C pfam12269
CpG binding protein C-terminal domain; CpG-binding protein is a transcriptional activator that ...
1-248 7.59e-98

CpG binding protein C-terminal domain; CpG-binding protein is a transcriptional activator that exhibits a DNA binding specificity for unmethylated CpG motifs. CpG is made of a PHD1, an acidic, a basic, a coiled-coil, and a PHD2 domains. This protein contains three cysteine-rich domains identified at the N-terminal, central region and C-terminal of the protein, where the central cysteine-rich domain is located within the DNA-binding domain, found between PHD1 and the acidic domains. This domain is found in eukaryotes, and is approximately 240 amino acids in length. It is found at the C-terminal of the CpG-binding protein containing the coiled-coil and PHD2 domains.


Pssm-ID: 463514  Cd Length: 235  Bit Score: 288.43  E-value: 7.59e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831514709   1 MRLTEILPNRCKQYFFEgpsggPRSLEDEIKPKRAKINREVQKLTESEKNMMAFLNKLVEFIKTQLKLqPLGTEE----- 75
Cdd:pfam12269   3 NRIYEILPQRIQEWQLS-----PCVAEEENKKKLEKIRKEQQEAREALKELDARHQELDAIIERAKKL-PVDTEEeendd 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831514709  76 RYDDNLYEGCIVCGLpDIPLLKYTKHIELCWARSEKAISFGAPEKNNDM---FYCEKYDSRTNSFCKRLKSLCPEHRKLG 152
Cdd:pfam12269  77 EDDDELSIYCVTCGH-EIHSRTAIKHMEKCFNKYESQTSFGSIYKTRIEgnsMFCDFYNPQQKTYCKRLKVLCPEHTKEP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831514709 153 DEQHLKVCGYPKkwedgmietaktvseLIEMEDPFGEEgCRTKKDACHKHHKWIPSLRGTIELEQACLFQKMYELCHEMH 232
Cdd:pfam12269 156 KIPDTEVCGCPL---------------VRNVFDPTGEF-CRAPKKKCVKHYCWEKLRRAEIDLERVRQWLKLDELFEQER 219
                         250
                  ....*....|....*.
gi 1831514709 233 KLNAHAEWTTNALSIM 248
Cdd:pfam12269 220 QIRTAMANRAGVLGLM 235
 
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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