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Conserved domains on  [gi|87080817|ref|NP_001034566|]
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protein THEMIS2 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CABIT super family cl28785
Cell-cycle sustaining, positive selection,; The 'CABIT' domain (for 'cysteine-containing, all- ...
18-61 2.27e-07

Cell-cycle sustaining, positive selection,; The 'CABIT' domain (for 'cysteine-containing, all- in Themis') is found in a newly identified gene family that has three mammalian homologs (Themis, Icb1 and 9130404H23Rik) that encode proteins with two CABIT domains and a highly conserved proline-rich region. In contrast, Fam59A, Fam59B and related proteins from mammals to cnidarians, including the insect Serrano proteins, have a single copy of the CABIT domain, a proline-rich region and often a C-terminal SAM (sterile-motif) domain. Multiple-sequence alignment has predicted that the CABIT domain adopts an all-strand structure with at least 12 strands, ie a dyad of six-stranded beta-barrel units. The CABIT domain contains a nearly absolutely conserved cysteine residue which is likely to be central to its function. CABIT domain proteins function downstream of tyrosine kinase signalling and interact with GRB2.


The actual alignment was detected with superfamily member pfam12736:

Pssm-ID: 463686  Cd Length: 261  Bit Score: 47.44  E-value: 2.27e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 87080817    18 LPRVLRVCSGVYFEGSIYeisgnecCLSTGDLIKVTQVRLQKVV 61
Cdd:pfam12736   1 LPQVVKVTSGIYGEGSVY-------CLSKGDVLLIHGLKQAKKV 37
 
Name Accession Description Interval E-value
CABIT pfam12736
Cell-cycle sustaining, positive selection,; The 'CABIT' domain (for 'cysteine-containing, all- ...
18-61 2.27e-07

Cell-cycle sustaining, positive selection,; The 'CABIT' domain (for 'cysteine-containing, all- in Themis') is found in a newly identified gene family that has three mammalian homologs (Themis, Icb1 and 9130404H23Rik) that encode proteins with two CABIT domains and a highly conserved proline-rich region. In contrast, Fam59A, Fam59B and related proteins from mammals to cnidarians, including the insect Serrano proteins, have a single copy of the CABIT domain, a proline-rich region and often a C-terminal SAM (sterile-motif) domain. Multiple-sequence alignment has predicted that the CABIT domain adopts an all-strand structure with at least 12 strands, ie a dyad of six-stranded beta-barrel units. The CABIT domain contains a nearly absolutely conserved cysteine residue which is likely to be central to its function. CABIT domain proteins function downstream of tyrosine kinase signalling and interact with GRB2.


Pssm-ID: 463686  Cd Length: 261  Bit Score: 47.44  E-value: 2.27e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 87080817    18 LPRVLRVCSGVYFEGSIYeisgnecCLSTGDLIKVTQVRLQKVV 61
Cdd:pfam12736   1 LPQVVKVTSGIYGEGSVY-------CLSKGDVLLIHGLKQAKKV 37
 
Name Accession Description Interval E-value
CABIT pfam12736
Cell-cycle sustaining, positive selection,; The 'CABIT' domain (for 'cysteine-containing, all- ...
18-61 2.27e-07

Cell-cycle sustaining, positive selection,; The 'CABIT' domain (for 'cysteine-containing, all- in Themis') is found in a newly identified gene family that has three mammalian homologs (Themis, Icb1 and 9130404H23Rik) that encode proteins with two CABIT domains and a highly conserved proline-rich region. In contrast, Fam59A, Fam59B and related proteins from mammals to cnidarians, including the insect Serrano proteins, have a single copy of the CABIT domain, a proline-rich region and often a C-terminal SAM (sterile-motif) domain. Multiple-sequence alignment has predicted that the CABIT domain adopts an all-strand structure with at least 12 strands, ie a dyad of six-stranded beta-barrel units. The CABIT domain contains a nearly absolutely conserved cysteine residue which is likely to be central to its function. CABIT domain proteins function downstream of tyrosine kinase signalling and interact with GRB2.


Pssm-ID: 463686  Cd Length: 261  Bit Score: 47.44  E-value: 2.27e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 87080817    18 LPRVLRVCSGVYFEGSIYeisgnecCLSTGDLIKVTQVRLQKVV 61
Cdd:pfam12736   1 LPQVVKVTSGIYGEGSVY-------CLSKGDVLLIHGLKQAKKV 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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