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Conserved domains on  [gi|406686226|gb|AFS51422|]
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seven in absentia 1A, partial [Corydoras serratus]

Protein Classification

Sina domain-containing protein( domain architecture ID 10504344)

Sina domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Sina pfam03145
Seven in absentia protein family; The seven in absentia (sina) gene was first identified in ...
 8-117 8.42e-72

Seven in absentia protein family; The seven in absentia (sina) gene was first identified in Drosophila. The Drosophila Sina protein is essential for the determination of the R7 pathway in photoreceptor cell development: the loss of functional Sina results in the transformation of the R7 precursor cell to a non- neuronal cell type. The Sina protein contains an N-terminal RING finger domain pfam00097. Through this domain, Sina binds E2 ubiquitin-conjugating enzymes (UbcD1) Sina also interacts with Tramtrack (TTK88) via PHYL. Tramtrack is a transcriptional repressor that blocks photoreceptor determination, while PHYL down-regulates the activity of TTK88. In turn, the activity of PHYL requires the activation of the Sevenless receptor tyrosine kinase, a process essential for R7 determination. It is thought that thus Sina targets TTK88 for degradation, therefore promoting the R7 pathway. Murine and human homologs of Sina have also been identified. The human homolog Siah-1 also binds E2 enzymes (UbcH5) and through a series of physical interactions, targets beta-catenin for ubiquitin degradation. Siah-1 expression is enhanced by p53, itself promoted by DNA damage. Thus this pathway links DNA damage to beta-catenin degradation. Sina proteins, therefore, physically interact with a variety of proteins. The N-terminal RING finger domain that binds ubiquitin conjugating enzymes is described in pfam00097, and does not form part of the alignment for this family. The remainder C-terminal part is involved in interactions with other proteins, and is included in this alignment. In addition to the Drosophila protein and mammalian homologs, whose similarity was noted previously, this family also includes putative homologs from Caenorhabditis elegans, Arabidopsis thaliana.


:

Pssm-ID: 460824 [Multi-domain]  Cd Length: 198  Bit Score: 212.46  E-value: 8.42e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406686226    8 IRNLAMEKVANSVLFPCKYASSGCEVTLPHTDKADHEDLCEFRPYSCPCPGASCKWQGSLDAVMPHLLHQHKSITTLQGE 87
Cdd:pfam03145   1 IRNLALEKVAESLLFPCKYASSGCSETLPYTEKADHEERCEFRPYSCPCPGSSCTWQGSLDAVMPHLMDDHKKVTTLQGE 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 406686226   88 DIVFLATDIN-LPGAVDWVMMQTCFGFHFLY 117
Cdd:pfam03145  81 DFVFLATDINkLDGAVDWVMVQSCFGEHFML 111
 
Name Accession Description Interval E-value
Sina pfam03145
Seven in absentia protein family; The seven in absentia (sina) gene was first identified in ...
 8-117 8.42e-72

Seven in absentia protein family; The seven in absentia (sina) gene was first identified in Drosophila. The Drosophila Sina protein is essential for the determination of the R7 pathway in photoreceptor cell development: the loss of functional Sina results in the transformation of the R7 precursor cell to a non- neuronal cell type. The Sina protein contains an N-terminal RING finger domain pfam00097. Through this domain, Sina binds E2 ubiquitin-conjugating enzymes (UbcD1) Sina also interacts with Tramtrack (TTK88) via PHYL. Tramtrack is a transcriptional repressor that blocks photoreceptor determination, while PHYL down-regulates the activity of TTK88. In turn, the activity of PHYL requires the activation of the Sevenless receptor tyrosine kinase, a process essential for R7 determination. It is thought that thus Sina targets TTK88 for degradation, therefore promoting the R7 pathway. Murine and human homologs of Sina have also been identified. The human homolog Siah-1 also binds E2 enzymes (UbcH5) and through a series of physical interactions, targets beta-catenin for ubiquitin degradation. Siah-1 expression is enhanced by p53, itself promoted by DNA damage. Thus this pathway links DNA damage to beta-catenin degradation. Sina proteins, therefore, physically interact with a variety of proteins. The N-terminal RING finger domain that binds ubiquitin conjugating enzymes is described in pfam00097, and does not form part of the alignment for this family. The remainder C-terminal part is involved in interactions with other proteins, and is included in this alignment. In addition to the Drosophila protein and mammalian homologs, whose similarity was noted previously, this family also includes putative homologs from Caenorhabditis elegans, Arabidopsis thaliana.


Pssm-ID: 460824 [Multi-domain]  Cd Length: 198  Bit Score: 212.46  E-value: 8.42e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406686226    8 IRNLAMEKVANSVLFPCKYASSGCEVTLPHTDKADHEDLCEFRPYSCPCPGASCKWQGSLDAVMPHLLHQHKSITTLQGE 87
Cdd:pfam03145   1 IRNLALEKVAESLLFPCKYASSGCSETLPYTEKADHEERCEFRPYSCPCPGSSCTWQGSLDAVMPHLMDDHKKVTTLQGE 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 406686226   88 DIVFLATDIN-LPGAVDWVMMQTCFGFHFLY 117
Cdd:pfam03145  81 DFVFLATDINkLDGAVDWVMVQSCFGEHFML 111
Sina cd03829
Seven in absentia (Sina) protein family, C-terminal substrate binding domain; composed of the ...
 81-116 1.71e-19

Seven in absentia (Sina) protein family, C-terminal substrate binding domain; composed of the Drosophila Sina protein, the mammalian Sina homolog (Siah), the plant protein SINAT5, and similar proteins. Sina, Siah and SINAT5 are RING-containing proteins that function as E3 ubiquitin ligases, acting either as single proteins or as a part of multiprotein complexes. Sina is expressed in many cells in the developing eye but is essential specifically for R7 photoreceptor cell development. Sina cooperates with Phyllopod (Phyl), Ebi and the E2 ubiquitin-conjugating enzyme Ubcd1 to catalyze the ubiquitination and subsequent degradation of Tramtrack (Ttk88); Ttk88 is a transcriptional repressor that blocks photoreceptor differentiation. Similarly, the mammalian homologue Siah1 cooperates with SIP (Siah-interacting protein), Ebi and the adaptor protein Skp1, to target beta-catenin for ubiquitination and degradation via a p53-dependent mechanism. SINAT5 targets NAC1 for ubiquitin-mediated degradation resulting in the downregulation of auxin, a hormone that controls many aspects of plant development. Other targets of Sina family proteins include c-Myb, synaptophysin, group 1 glutamate receptors, promyelocytic leukemia protein, alpha-synuclein, synphilin-1 and alpha-ketoglutarate dehydrogenase, among others. Sina proteins also bind proteins that are not targets for ubiquitination such as Phyl, adenomatous polyposis coli, VAV, BAG-1 and Dab-1. Siah binds to a consensus motif, PXAXVXP, which is present in Siah-binding proteins. Siah is a dimeric protein consisting of an N-terminal RING domain, two zinc finger motifs and a C-terminal substrate-binding domain (SBD); this SBD contains an eight-stranded antiparallel beta-sandwich fold similar to the MATH (meprin and TRAF-C homology) domain.


Pssm-ID: 239753  Cd Length: 127  Bit Score: 77.43  E-value: 1.71e-19
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 406686226  81 ITTLQGEDIVFLATDINLPGAVDWVMMQTCFGFHFL 116
Cdd:cd03829    1 VTTLQGEDIVFLATDINLPGATDWVMMQSCFGHHFM 36
 
Name Accession Description Interval E-value
Sina pfam03145
Seven in absentia protein family; The seven in absentia (sina) gene was first identified in ...
 8-117 8.42e-72

Seven in absentia protein family; The seven in absentia (sina) gene was first identified in Drosophila. The Drosophila Sina protein is essential for the determination of the R7 pathway in photoreceptor cell development: the loss of functional Sina results in the transformation of the R7 precursor cell to a non- neuronal cell type. The Sina protein contains an N-terminal RING finger domain pfam00097. Through this domain, Sina binds E2 ubiquitin-conjugating enzymes (UbcD1) Sina also interacts with Tramtrack (TTK88) via PHYL. Tramtrack is a transcriptional repressor that blocks photoreceptor determination, while PHYL down-regulates the activity of TTK88. In turn, the activity of PHYL requires the activation of the Sevenless receptor tyrosine kinase, a process essential for R7 determination. It is thought that thus Sina targets TTK88 for degradation, therefore promoting the R7 pathway. Murine and human homologs of Sina have also been identified. The human homolog Siah-1 also binds E2 enzymes (UbcH5) and through a series of physical interactions, targets beta-catenin for ubiquitin degradation. Siah-1 expression is enhanced by p53, itself promoted by DNA damage. Thus this pathway links DNA damage to beta-catenin degradation. Sina proteins, therefore, physically interact with a variety of proteins. The N-terminal RING finger domain that binds ubiquitin conjugating enzymes is described in pfam00097, and does not form part of the alignment for this family. The remainder C-terminal part is involved in interactions with other proteins, and is included in this alignment. In addition to the Drosophila protein and mammalian homologs, whose similarity was noted previously, this family also includes putative homologs from Caenorhabditis elegans, Arabidopsis thaliana.


Pssm-ID: 460824 [Multi-domain]  Cd Length: 198  Bit Score: 212.46  E-value: 8.42e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406686226    8 IRNLAMEKVANSVLFPCKYASSGCEVTLPHTDKADHEDLCEFRPYSCPCPGASCKWQGSLDAVMPHLLHQHKSITTLQGE 87
Cdd:pfam03145   1 IRNLALEKVAESLLFPCKYASSGCSETLPYTEKADHEERCEFRPYSCPCPGSSCTWQGSLDAVMPHLMDDHKKVTTLQGE 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 406686226   88 DIVFLATDIN-LPGAVDWVMMQTCFGFHFLY 117
Cdd:pfam03145  81 DFVFLATDINkLDGAVDWVMVQSCFGEHFML 111
Sina cd03829
Seven in absentia (Sina) protein family, C-terminal substrate binding domain; composed of the ...
 81-116 1.71e-19

Seven in absentia (Sina) protein family, C-terminal substrate binding domain; composed of the Drosophila Sina protein, the mammalian Sina homolog (Siah), the plant protein SINAT5, and similar proteins. Sina, Siah and SINAT5 are RING-containing proteins that function as E3 ubiquitin ligases, acting either as single proteins or as a part of multiprotein complexes. Sina is expressed in many cells in the developing eye but is essential specifically for R7 photoreceptor cell development. Sina cooperates with Phyllopod (Phyl), Ebi and the E2 ubiquitin-conjugating enzyme Ubcd1 to catalyze the ubiquitination and subsequent degradation of Tramtrack (Ttk88); Ttk88 is a transcriptional repressor that blocks photoreceptor differentiation. Similarly, the mammalian homologue Siah1 cooperates with SIP (Siah-interacting protein), Ebi and the adaptor protein Skp1, to target beta-catenin for ubiquitination and degradation via a p53-dependent mechanism. SINAT5 targets NAC1 for ubiquitin-mediated degradation resulting in the downregulation of auxin, a hormone that controls many aspects of plant development. Other targets of Sina family proteins include c-Myb, synaptophysin, group 1 glutamate receptors, promyelocytic leukemia protein, alpha-synuclein, synphilin-1 and alpha-ketoglutarate dehydrogenase, among others. Sina proteins also bind proteins that are not targets for ubiquitination such as Phyl, adenomatous polyposis coli, VAV, BAG-1 and Dab-1. Siah binds to a consensus motif, PXAXVXP, which is present in Siah-binding proteins. Siah is a dimeric protein consisting of an N-terminal RING domain, two zinc finger motifs and a C-terminal substrate-binding domain (SBD); this SBD contains an eight-stranded antiparallel beta-sandwich fold similar to the MATH (meprin and TRAF-C homology) domain.


Pssm-ID: 239753  Cd Length: 127  Bit Score: 77.43  E-value: 1.71e-19
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 406686226  81 ITTLQGEDIVFLATDINLPGAVDWVMMQTCFGFHFL 116
Cdd:cd03829    1 VTTLQGEDIVFLATDINLPGATDWVMMQSCFGHHFM 36
 
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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