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Conserved domains on  [gi|1720431207|ref|XP_030100134|]
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zinc finger protein ZIC 4 isoform X11 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SFP1 super family cl25788
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 20-80 3.10e-06

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


The actual alignment was detected with superfamily member COG5189:

Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 44.71  E-value: 3.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431207  20 LKESSEKPFRCEFEGCERRFANSSDRKKHS-HVHTS------------------DKPYMCKVrgCDKCYTHPSSLRKHMK 80
Cdd:COG5189   342 LKVKDGKPYKCPVEGCNKKYKNQNGLKYHMlHGHQNqklhenpspekmnifsakDKPYRCEV--CDKRYKNLNGLKYHRK 419
 
Name Accession Description Interval E-value
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 20-80 3.10e-06

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 44.71  E-value: 3.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431207  20 LKESSEKPFRCEFEGCERRFANSSDRKKHS-HVHTS------------------DKPYMCKVrgCDKCYTHPSSLRKHMK 80
Cdd:COG5189   342 LKVKDGKPYKCPVEGCNKKYKNQNGLKYHMlHGHQNqklhenpspekmnifsakDKPYRCEV--CDKRYKNLNGLKYHRK 419
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 58-82 5.88e-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: 32.27  E-value: 5.88e-03
                          10        20
                  ....*....|....*....|....*
gi 1720431207  58 YMCKvrGCDKCYTHPSSLRKHMKVH 82
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 20-80 3.10e-06

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 44.71  E-value: 3.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431207  20 LKESSEKPFRCEFEGCERRFANSSDRKKHS-HVHTS------------------DKPYMCKVrgCDKCYTHPSSLRKHMK 80
Cdd:COG5189   342 LKVKDGKPYKCPVEGCNKKYKNQNGLKYHMlHGHQNqklhenpspekmnifsakDKPYRCEV--CDKRYKNLNGLKYHRK 419
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 56-87 2.28e-03

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 36.62  E-value: 2.28e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1720431207  56 KPYMCKVRGCDKCYTHPSSLRKHMKvHGRSPP 87
Cdd:COG5189   348 KPYKCPVEGCNKKYKNQNGLKYHML-HGHQNQ 378
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 58-82 5.88e-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: 32.27  E-value: 5.88e-03
                          10        20
                  ....*....|....*....|....*
gi 1720431207  58 YMCKvrGCDKCYTHPSSLRKHMKVH 82
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 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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