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Conserved domains on  [gi|9968471|emb|CAC06698|]
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Kruppel like factor, partial [Mus musculus]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 11472214)

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
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SP6-9_N super family cl41771
N-terminal domains of transcription factor Specificity Proteins (SP) 6-9, and similar proteins; ...
 1-31 8.10e-14

N-terminal domains of transcription factor Specificity Proteins (SP) 6-9, and similar proteins; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in the chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. SPs belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. This model represents the related N-terminal domains of SP6-SP9, and similar proteins.


The actual alignment was detected with superfamily member cd22544:

Pssm-ID: 425402 [Multi-domain]  Cd Length: 245  Bit Score: 66.10  E-value: 8.10e-14
                        10        20        30
                ....*....|....*....|....*....|.
gi 9968471    1 QTVCRCPNCLEAERLGAPcgPDGGKKKHLHN 31
Cdd:cd22544 217 QAACRCPNCQEAERLGPP--PDGGKKKHLHN 245
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
37-112 1.70e-05

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.53  E-value: 1.70e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9968471   37 CGKAYAKTSHLKAHLRW--HSG--DRPFVCNWLFCGKRFTRSDELQRHLQTHTGTKKFPCavCSRVFMRSDHLAKHMKTH 112
Cdd:COG5048 295 CNISFSRSSPLTRHLRSvnHSGesLKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKE--KLLNSSSKFSPLLNNEPP 372
 
Name Accession Description Interval E-value
SP6_N cd22544
N-terminal domain of transcription factor Specificity Protein (SP) 6; Specificity Proteins ...
 1-31 8.10e-14

N-terminal domain of transcription factor Specificity Protein (SP) 6; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP6, also known as epiprofin, shows specific expression pattern in hair follicles and the apical ectodermal ridge (AER) of the developing limbs. SP6 null mice are nude and show defects in skin, teeth, limbs (syndactyly and oligodactyly), and lung alveoli. SP6 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. This model represents the N-terminal domain of SP6.


Pssm-ID: 411693 [Multi-domain]  Cd Length: 245  Bit Score: 66.10  E-value: 8.10e-14
                        10        20        30
                ....*....|....*....|....*....|.
gi 9968471    1 QTVCRCPNCLEAERLGAPcgPDGGKKKHLHN 31
Cdd:cd22544 217 QAACRCPNCQEAERLGPP--PDGGKKKHLHN 245
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
37-112 1.70e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.53  E-value: 1.70e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9968471   37 CGKAYAKTSHLKAHLRW--HSG--DRPFVCNWLFCGKRFTRSDELQRHLQTHTGTKKFPCavCSRVFMRSDHLAKHMKTH 112
Cdd:COG5048 295 CNISFSRSSPLTRHLRSvnHSGesLKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKE--KLLNSSSKFSPLLNNEPP 372
zf-H2C2_2 pfam13465
Zinc-finger double domain;
76-99 7.80e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 32.34  E-value: 7.80e-03
                          10        20
                  ....*....|....*....|....
gi 9968471     76 ELQRHLQTHTGTKKFPCAVCSRVF 99
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
 
Name Accession Description Interval E-value
SP6_N cd22544
N-terminal domain of transcription factor Specificity Protein (SP) 6; Specificity Proteins ...
 1-31 8.10e-14

N-terminal domain of transcription factor Specificity Protein (SP) 6; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP6, also known as epiprofin, shows specific expression pattern in hair follicles and the apical ectodermal ridge (AER) of the developing limbs. SP6 null mice are nude and show defects in skin, teeth, limbs (syndactyly and oligodactyly), and lung alveoli. SP6 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. This model represents the N-terminal domain of SP6.


Pssm-ID: 411693 [Multi-domain]  Cd Length: 245  Bit Score: 66.10  E-value: 8.10e-14
                        10        20        30
                ....*....|....*....|....*....|.
gi 9968471    1 QTVCRCPNCLEAERLGAPcgPDGGKKKHLHN 31
Cdd:cd22544 217 QAACRCPNCQEAERLGPP--PDGGKKKHLHN 245
SP6-9_N cd22543
N-terminal domains of transcription factor Specificity Proteins (SP) 6-9, and similar proteins; ...
 1-31 5.53e-10

N-terminal domains of transcription factor Specificity Proteins (SP) 6-9, and similar proteins; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in the chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. SPs belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. This model represents the related N-terminal domains of SP6-SP9, and similar proteins.


Pssm-ID: 411692  Cd Length: 162  Bit Score: 54.56  E-value: 5.53e-10
                        10        20        30
                ....*....|....*....|....*....|.
gi 9968471    1 QTVCRCPNCLEAERLGAPcgPDGGKKKHLHN 31
Cdd:cd22543 134 RATCDCPNCQEAERLGPA--GAGLRKKGLHS 162
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
37-112 1.70e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.53  E-value: 1.70e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9968471   37 CGKAYAKTSHLKAHLRW--HSG--DRPFVCNWLFCGKRFTRSDELQRHLQTHTGTKKFPCavCSRVFMRSDHLAKHMKTH 112
Cdd:COG5048 295 CNISFSRSSPLTRHLRSvnHSGesLKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKE--KLLNSSSKFSPLLNNEPP 372
SP9_N cd22549
N-terminal domain of transcription factor Specificity Protein (SP) 9 and similar proteins; ...
 4-31 5.80e-03

N-terminal domain of transcription factor Specificity Protein (SP) 9 and similar proteins; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP9 plays a role in limb outgrowth. It is expressed during embryogenesis in the forming apical ectodermal ridge, restricted regions of the central nervous system, and tail bud. SP8 and SP9 are two closely related transcription factors that mediate FGF10 signaling, which in turn regulates FGF8 expression which is essential for normal limb development. Both SP8 and SP9 have been found in vertebrates, but only SP8 is present in invertebrates. SP9 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. This model represents the N-terminal domain of SP9.


Pssm-ID: 411695 [Multi-domain]  Cd Length: 299  Bit Score: 35.73  E-value: 5.80e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 9968471    4 CRCPNCLEAERLgapcGPDGG--KKKHLHN 31
Cdd:cd22549 274 CDCPNCQEAERL----GPAGAslRRKGLHS 299
zf-H2C2_2 pfam13465
Zinc-finger double domain;
76-99 7.80e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 32.34  E-value: 7.80e-03
                          10        20
                  ....*....|....*....|....
gi 9968471     76 ELQRHLQTHTGTKKFPCAVCSRVF 99
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
 
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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