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Conserved domains on  [gi|10436729|dbj|BAB14897|]
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unnamed protein product [Homo sapiens]

Protein Classification

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List of domain hits

 Name Accession Description Interval E-value
nlz1 super family cl13791
NocA-like zinc-finger protein 1; This domain family is found in eukaryotes, and is typically ...
 311-338 5.22e-04

NocA-like zinc-finger protein 1; This domain family is found in eukaryotes, and is typically between 42 and 57 amino acids in length. There is a conserved GAY sequence motif. There is a single completely conserved residue G that may be functionally important. Nlz1 self-associated via its C terminus, interacted with Nlz2, and bound to histone deacetylases.


The actual alignment was detected with superfamily member pfam12402:

Pssm-ID: 403564  Cd Length: 58  Bit Score: 38.44  E-value: 5.22e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 10436729   311 SSIGYHGSIVGAYAGYPSQFVP---GLDPSK 338
Cdd:pfam12402   1 AGISYPGSLAGAYAGYPPQFLPhgvGLDPTK 31
SP1-4_N super family cl41773
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 67-102 6.70e-04

N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; 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 chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. SPs belong 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. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP1-4.


The actual alignment was detected with superfamily member cd22540:

Pssm-ID: 425404 [Multi-domain]  Cd Length: 511  Bit Score: 42.61  E-value: 6.70e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 10436729  67 EYLQPLSSTpvspiELDAKKSPLALLAQTCSQIGKP 102
Cdd:cd22540  10 EYLQPAAST-----TQDSQPSPLALLAATCSKIGPP 40
 
Name Accession Description Interval E-value
nlz1 pfam12402
NocA-like zinc-finger protein 1; This domain family is found in eukaryotes, and is typically ...
 311-338 5.22e-04

NocA-like zinc-finger protein 1; This domain family is found in eukaryotes, and is typically between 42 and 57 amino acids in length. There is a conserved GAY sequence motif. There is a single completely conserved residue G that may be functionally important. Nlz1 self-associated via its C terminus, interacted with Nlz2, and bound to histone deacetylases.


Pssm-ID: 403564  Cd Length: 58  Bit Score: 38.44  E-value: 5.22e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 10436729   311 SSIGYHGSIVGAYAGYPSQFVP---GLDPSK 338
Cdd:pfam12402   1 AGISYPGSLAGAYAGYPPQFLPhgvGLDPTK 31
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 67-102 6.70e-04

N-terminal domain of transcription factor Specificity Protein (SP) 2; 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. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 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. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.


Pssm-ID: 411776 [Multi-domain]  Cd Length: 511  Bit Score: 42.61  E-value: 6.70e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 10436729  67 EYLQPLSSTpvspiELDAKKSPLALLAQTCSQIGKP 102
Cdd:cd22540  10 EYLQPAAST-----TQDSQPSPLALLAATCSKIGPP 40
 
Name Accession Description Interval E-value
nlz1 pfam12402
NocA-like zinc-finger protein 1; This domain family is found in eukaryotes, and is typically ...
 311-338 5.22e-04

NocA-like zinc-finger protein 1; This domain family is found in eukaryotes, and is typically between 42 and 57 amino acids in length. There is a conserved GAY sequence motif. There is a single completely conserved residue G that may be functionally important. Nlz1 self-associated via its C terminus, interacted with Nlz2, and bound to histone deacetylases.


Pssm-ID: 403564  Cd Length: 58  Bit Score: 38.44  E-value: 5.22e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 10436729   311 SSIGYHGSIVGAYAGYPSQFVP---GLDPSK 338
Cdd:pfam12402   1 AGISYPGSLAGAYAGYPPQFLPhgvGLDPTK 31
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 67-102 6.70e-04

N-terminal domain of transcription factor Specificity Protein (SP) 2; 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. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 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. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.


Pssm-ID: 411776 [Multi-domain]  Cd Length: 511  Bit Score: 42.61  E-value: 6.70e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 10436729  67 EYLQPLSSTpvspiELDAKKSPLALLAQTCSQIGKP 102
Cdd:cd22540  10 EYLQPAAST-----TQDSQPSPLALLAATCSKIGPP 40
SP3_N cd22537
N-terminal domain of transcription factor Specificity Protein (SP) 3; Specificity Proteins ...
 78-125 8.50e-04

N-terminal domain of transcription factor Specificity Protein (SP) 3; 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. SP1 and SP3 can interact with and recruit a large number of proteins including the transcription initiation complex, histone modifying enzymes, and chromatin remodeling complexes, which strongly suggest that SP1 and SP3 are important transcription factors in remodeling chromatin and the regulation of gene expression. SP3 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. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP3.


Pssm-ID: 411774 [Multi-domain]  Cd Length: 574  Bit Score: 42.24  E-value: 8.50e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 10436729  78 SPIELDAKKSPLALLAQTCSQIGkpdPPPSSKLNSVAAAANGLGAEKD 125
Cdd:cd22537   1 GAAEQDTQPSPLALLAATCSKIG---SPSPGDDAAAAGNAASAGQTGD 45
SP1-4_N cd22545
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 83-114 3.30e-03

N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; 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 chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. SPs belong 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. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP1-4.


Pssm-ID: 411777 [Multi-domain]  Cd Length: 82  Bit Score: 36.65  E-value: 3.30e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 10436729  83 DAKKSPLALLAQTCSQIGKPDPPPSSKLNSVA 114
Cdd:cd22545   6 DSQPSPLALLAATCSKIGSPAENSTGPGGNIQ 37
 
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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