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Conserved domains on  [gi|6755576|ref|NP_035545|]
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zinc finger protein SNAI2 [Mus musculus]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 10604075)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation

CATH:  3.30.160.60
Gene Ontology:  GO:0008270|GO:0003677
PubMed:  11361095|22803940|30718982
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
201-224 1.03e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.03e-03
                          10        20
                  ....*....|....*....|....
gi 6755576    201 LQGHIRTHTGEKPFSCPHCNRAFA 224
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 214-236 1.64e-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: 34.97  E-value: 1.64e-03
                          10        20
                  ....*....|....*....|...
gi 6755576    214 FSCPHCNRAFADRSNLRAHLQTH 236
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 super family cl25788
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 102-183 2.67e-03

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: 38.93  E-value: 2.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755576  102 GSESPISDEEERLQPKLSDPHAIEAEKfqcnlCNKTYSTFSGLAKHK-QLHC--------DAQSRKSFS-------CKYC 165
Cdd:COG5189 330 GGERNIDTPSRMLKVKDGKPYKCPVEG-----CNKKYKNQNGLKYHMlHGHQnqklhenpSPEKMNIFSakdkpyrCEVC 404

                        90
                ....*....|....*...
gi 6755576  166 DKEYVSLGALKMHiRTHT 183
Cdd:COG5189 405 DKRYKNLNGLKYH-RKHS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
228-253 8.63e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.11  E-value: 8.63e-03
                          10        20
                  ....*....|....*....|....*.
gi 6755576    228 NLRAHLQTHSDVKKYQCKNCSKTFSR 253
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
201-224 1.03e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.03e-03
                          10        20
                  ....*....|....*....|....
gi 6755576    201 LQGHIRTHTGEKPFSCPHCNRAFA 224
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 214-236 1.64e-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: 34.97  E-value: 1.64e-03
                          10        20
                  ....*....|....*....|...
gi 6755576    214 FSCPHCNRAFADRSNLRAHLQTH 236
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 102-183 2.67e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 38.93  E-value: 2.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755576  102 GSESPISDEEERLQPKLSDPHAIEAEKfqcnlCNKTYSTFSGLAKHK-QLHC--------DAQSRKSFS-------CKYC 165
Cdd:COG5189 330 GGERNIDTPSRMLKVKDGKPYKCPVEG-----CNKKYKNQNGLKYHMlHGHQnqklhenpSPEKMNIFSakdkpyrCEVC 404

                        90
                ....*....|....*...
gi 6755576  166 DKEYVSLGALKMHiRTHT 183
Cdd:COG5189 405 DKRYKNLNGLKYH-RKHS 421
InsA COG3677
Transposase InsA [Mobilome: prophages, transposons];
204-252 5.83e-03

Transposase InsA [Mobilome: prophages, transposons];


Pssm-ID: 442893 [Multi-domain]  Cd Length: 241  Bit Score: 37.15  E-value: 5.83e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 6755576  204 HIRTHTGEKPFSCPHCNRafadrSNLRAHLQTHSDVKKYQCKNCSKTFS 252
Cdd:COG3677   7 LLEQIRWPNGPVCPHCGS-----TRIVKNGKTRNGRQRYRCKDCGRTFT 50
zf-H2C2_2 pfam13465
Zinc-finger double domain;
228-253 8.63e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.11  E-value: 8.63e-03
                          10        20
                  ....*....|....*....|....*.
gi 6755576    228 NLRAHLQTHSDVKKYQCKNCSKTFSR 253
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
201-224 1.03e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.03e-03
                          10        20
                  ....*....|....*....|....
gi 6755576    201 LQGHIRTHTGEKPFSCPHCNRAFA 224
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 214-236 1.64e-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: 34.97  E-value: 1.64e-03
                          10        20
                  ....*....|....*....|...
gi 6755576    214 FSCPHCNRAFADRSNLRAHLQTH 236
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 102-183 2.67e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 38.93  E-value: 2.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755576  102 GSESPISDEEERLQPKLSDPHAIEAEKfqcnlCNKTYSTFSGLAKHK-QLHC--------DAQSRKSFS-------CKYC 165
Cdd:COG5189 330 GGERNIDTPSRMLKVKDGKPYKCPVEG-----CNKKYKNQNGLKYHMlHGHQnqklhenpSPEKMNIFSakdkpyrCEVC 404

                        90
                ....*....|....*...
gi 6755576  166 DKEYVSLGALKMHiRTHT 183
Cdd:COG5189 405 DKRYKNLNGLKYH-RKHS 421
InsA COG3677
Transposase InsA [Mobilome: prophages, transposons];
204-252 5.83e-03

Transposase InsA [Mobilome: prophages, transposons];


Pssm-ID: 442893 [Multi-domain]  Cd Length: 241  Bit Score: 37.15  E-value: 5.83e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 6755576  204 HIRTHTGEKPFSCPHCNRafadrSNLRAHLQTHSDVKKYQCKNCSKTFS 252
Cdd:COG3677   7 LLEQIRWPNGPVCPHCGS-----TRIVKNGKTRNGRQRYRCKDCGRTFT 50
zf-H2C2_2 pfam13465
Zinc-finger double domain;
228-253 8.63e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.11  E-value: 8.63e-03
                          10        20
                  ....*....|....*....|....*.
gi 6755576    228 NLRAHLQTHSDVKKYQCKNCSKTFSR 253
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
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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