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Conserved domains on  [gi|1907181246|ref|XP_036009000|]
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zinc finger protein 536 isoform X3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-C2H2_assoc super family cl24981
Unstructured conserved, between two C2H2-type zinc-fingers; This domain is found on a set of ...
 657-718 1.74e-26

Unstructured conserved, between two C2H2-type zinc-fingers; This domain is found on a set of eukaryotic Zinc finger protein 536 transcriptional regulator proteins sandwiched between zf-C2H2, pfam00096 and zf-H2C2_2 pfam13465. It is not conserved between other pairs of the zinc-fingers on these sequences. It is natively unstructured, and its function is not known. The proteins recognize and bind 2 copies of the core DNA sequence 5'-CCCCCA-3'.


The actual alignment was detected with superfamily member pfam16606:

Pssm-ID: 465193  Cd Length: 80  Bit Score: 103.90  E-value: 1.74e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907181246  657 RKSDEDALHVGvgLEERRGSGSDQESQSVSRSTTPGSSNVTEESGAGGGLSQTGSAQEDSPH 718
Cdd:pfam16606    1 RKALEEALHQG--LDERRGSASDPESQSISRSTTPGSSNITEESGAGGGLSQTGSAQEDSPH 60
zf-H2C2_2 pfam13465
Zinc-finger double domain;
145-169 5.05e-06

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.28  E-value: 5.05e-06
                           10        20
                   ....*....|....*....|....*
gi 1907181246  145 LSLHMRTHTGEKPFKCPYCDHRAAQ 169
Cdd:pfam13465    2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_5 pfam13909
C2H2-type zinc-finger domain;
730-753 1.45e-04

C2H2-type zinc-finger domain;


:

Pssm-ID: 404746 [Multi-domain]  Cd Length: 25  Bit Score: 39.84  E-value: 1.45e-04
                           10        20
                   ....*....|....*....|....
gi 1907181246  730 YKCPHCDYAGTQSASLKYHLERHH 753
Cdd:pfam13909    1 YKCSQCDYSTAWKSNLKRHLRKHT 24
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
103-180 1.27e-03

FOG: Zn-finger [General function prediction only];


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.76  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181246  103 QQFLNGQNLGIMSQMSDIEDDARKNRKYPCPLCGKRFRFNSILSLHMRTHTGEKPFKCPYCDHRAAQK--GNLKIHLRTH 180
Cdd:COG5048      7 QSSSSNNSVLSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTH 86
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 345-367 1.82e-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: 36.89  E-value: 1.82e-03
                           10        20
                   ....*....|....*....|...
gi 1907181246  345 FRCEVCGQVFSQAWFLKGHMRKH 367
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 373-395 8.11e-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: 8.11e-03
                           10        20
                   ....*....|....*....|...
gi 1907181246  373 HCCQICGRRFKEPWFLKNHMKVH 395
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
zf-C2H2_assoc pfam16606
Unstructured conserved, between two C2H2-type zinc-fingers; This domain is found on a set of ...
 657-718 1.74e-26

Unstructured conserved, between two C2H2-type zinc-fingers; This domain is found on a set of eukaryotic Zinc finger protein 536 transcriptional regulator proteins sandwiched between zf-C2H2, pfam00096 and zf-H2C2_2 pfam13465. It is not conserved between other pairs of the zinc-fingers on these sequences. It is natively unstructured, and its function is not known. The proteins recognize and bind 2 copies of the core DNA sequence 5'-CCCCCA-3'.


Pssm-ID: 465193  Cd Length: 80  Bit Score: 103.90  E-value: 1.74e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907181246  657 RKSDEDALHVGvgLEERRGSGSDQESQSVSRSTTPGSSNVTEESGAGGGLSQTGSAQEDSPH 718
Cdd:pfam16606    1 RKALEEALHQG--LDERRGSASDPESQSISRSTTPGSSNITEESGAGGGLSQTGSAQEDSPH 60
zf-H2C2_2 pfam13465
Zinc-finger double domain;
145-169 5.05e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.28  E-value: 5.05e-06
                           10        20
                   ....*....|....*....|....*
gi 1907181246  145 LSLHMRTHTGEKPFKCPYCDHRAAQ 169
Cdd:pfam13465    2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_5 pfam13909
C2H2-type zinc-finger domain;
730-753 1.45e-04

C2H2-type zinc-finger domain;


Pssm-ID: 404746 [Multi-domain]  Cd Length: 25  Bit Score: 39.84  E-value: 1.45e-04
                           10        20
                   ....*....|....*....|....
gi 1907181246  730 YKCPHCDYAGTQSASLKYHLERHH 753
Cdd:pfam13909    1 YKCSQCDYSTAWKSNLKRHLRKHT 24
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
103-180 1.27e-03

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.76  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181246  103 QQFLNGQNLGIMSQMSDIEDDARKNRKYPCPLCGKRFRFNSILSLHMRTHTGEKPFKCPYCDHRAAQK--GNLKIHLRTH 180
Cdd:COG5048      7 QSSSSNNSVLSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTH 86
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 345-367 1.82e-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: 36.89  E-value: 1.82e-03
                           10        20
                   ....*....|....*....|...
gi 1907181246  345 FRCEVCGQVFSQAWFLKGHMRKH 367
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 130-152 3.81e-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: 36.12  E-value: 3.81e-03
                           10        20
                   ....*....|....*....|...
gi 1907181246  130 YPCPLCGKRFRFNSILSLHMRTH 152
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 373-395 8.11e-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: 8.11e-03
                           10        20
                   ....*....|....*....|...
gi 1907181246  373 HCCQICGRRFKEPWFLKNHMKVH 395
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
RPC10 COG1996
DNA-directed RNA polymerase, subunit RPC12/RpoP, contains C4-type Zn-finger [Transcription]; ...
 128-166 8.39e-03

DNA-directed RNA polymerase, subunit RPC12/RpoP, contains C4-type Zn-finger [Transcription]; DNA-directed RNA polymerase, subunit RPC12/RpoP, contains C4-type Zn-finger is part of the Pathway/BioSystem: RNA polymerase


Pssm-ID: 441599  Cd Length: 48  Bit Score: 35.83  E-value: 8.39e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1907181246  128 RKYPCPLCGKRFRFNsilslhmrthTGEKPFKCPYCDHR 166
Cdd:COG1996      4 VEYKCPRCGAEVELD----------EGTPAIRCPYCGSR 32
 
Name Accession Description Interval E-value
zf-C2H2_assoc pfam16606
Unstructured conserved, between two C2H2-type zinc-fingers; This domain is found on a set of ...
 657-718 1.74e-26

Unstructured conserved, between two C2H2-type zinc-fingers; This domain is found on a set of eukaryotic Zinc finger protein 536 transcriptional regulator proteins sandwiched between zf-C2H2, pfam00096 and zf-H2C2_2 pfam13465. It is not conserved between other pairs of the zinc-fingers on these sequences. It is natively unstructured, and its function is not known. The proteins recognize and bind 2 copies of the core DNA sequence 5'-CCCCCA-3'.


Pssm-ID: 465193  Cd Length: 80  Bit Score: 103.90  E-value: 1.74e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907181246  657 RKSDEDALHVGvgLEERRGSGSDQESQSVSRSTTPGSSNVTEESGAGGGLSQTGSAQEDSPH 718
Cdd:pfam16606    1 RKALEEALHQG--LDERRGSASDPESQSISRSTTPGSSNITEESGAGGGLSQTGSAQEDSPH 60
zf-H2C2_2 pfam13465
Zinc-finger double domain;
145-169 5.05e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.28  E-value: 5.05e-06
                           10        20
                   ....*....|....*....|....*
gi 1907181246  145 LSLHMRTHTGEKPFKCPYCDHRAAQ 169
Cdd:pfam13465    2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_5 pfam13909
C2H2-type zinc-finger domain;
158-181 1.25e-05

C2H2-type zinc-finger domain;


Pssm-ID: 404746 [Multi-domain]  Cd Length: 25  Bit Score: 42.92  E-value: 1.25e-05
                           10        20
                   ....*....|....*....|....
gi 1907181246  158 FKCPYCDHRAAQKGNLKIHLRTHK 181
Cdd:pfam13909    1 YKCSQCDYSTAWKSNLKRHLRKHT 24
zf-H2C2_5 pfam13909
C2H2-type zinc-finger domain;
730-753 1.45e-04

C2H2-type zinc-finger domain;


Pssm-ID: 404746 [Multi-domain]  Cd Length: 25  Bit Score: 39.84  E-value: 1.45e-04
                           10        20
                   ....*....|....*....|....
gi 1907181246  730 YKCPHCDYAGTQSASLKYHLERHH 753
Cdd:pfam13909    1 YKCSQCDYSTAWKSNLKRHLRKHT 24
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
103-180 1.27e-03

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.76  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907181246  103 QQFLNGQNLGIMSQMSDIEDDARKNRKYPCPLCGKRFRFNSILSLHMRTHTGEKPFKCPYCDHRAAQK--GNLKIHLRTH 180
Cdd:COG5048      7 QSSSSNNSVLSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTH 86
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 345-367 1.82e-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: 36.89  E-value: 1.82e-03
                           10        20
                   ....*....|....*....|...
gi 1907181246  345 FRCEVCGQVFSQAWFLKGHMRKH 367
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 158-180 2.24e-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: 36.51  E-value: 2.24e-03
                           10        20
                   ....*....|....*....|...
gi 1907181246  158 FKCPYCDHRAAQKGNLKIHLRTH 180
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 130-152 3.81e-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: 36.12  E-value: 3.81e-03
                           10        20
                   ....*....|....*....|...
gi 1907181246  130 YPCPLCGKRFRFNSILSLHMRTH 152
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 373-395 8.11e-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: 8.11e-03
                           10        20
                   ....*....|....*....|...
gi 1907181246  373 HCCQICGRRFKEPWFLKNHMKVH 395
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
RPC10 COG1996
DNA-directed RNA polymerase, subunit RPC12/RpoP, contains C4-type Zn-finger [Transcription]; ...
 128-166 8.39e-03

DNA-directed RNA polymerase, subunit RPC12/RpoP, contains C4-type Zn-finger [Transcription]; DNA-directed RNA polymerase, subunit RPC12/RpoP, contains C4-type Zn-finger is part of the Pathway/BioSystem: RNA polymerase


Pssm-ID: 441599  Cd Length: 48  Bit Score: 35.83  E-value: 8.39e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1907181246  128 RKYPCPLCGKRFRFNsilslhmrthTGEKPFKCPYCDHR 166
Cdd:COG1996      4 VEYKCPRCGAEVELD----------EGTPAIRCPYCGSR 32
 
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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