NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2085999400|ref|WP_221875912|]
View 

hypothetical protein [Mesobacillus maritimus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Stevor super family cl38690
Subtelomeric Variable Open Reading frame; The parasite protein STEVOR (Subtelomeric Variable ...
10-38 8.04e-03

Subtelomeric Variable Open Reading frame; The parasite protein STEVOR (Subtelomeric Variable Open Reading frame) is an erythrocyte-binding protein recognizing Glycophorin C on the red blood cell (RBC) surface. The cytoplasmic domain of STEVOR is shown to interact with ankyrin complex at the erythrocyte skeleton. It is phosphorylated by protein kinase A (PKA) at a specific serine residue (S324). The N-terminal semi-conserved region of Stevor that is present in this domain is shown to specifically bind to to a chymotrypsin-resistant RBC receptor. The expression of STEVOR in multiple parasite stages including merozoites suggests that STEVOR mediates multiple distinct functions in parasitic infectious cycle.


The actual alignment was detected with superfamily member pfam17410:

Pssm-ID: 407484  Cd Length: 275  Bit Score: 31.98  E-value: 8.04e-03
                          10        20
                  ....*....|....*....|....*....
gi 2085999400  10 ISLLFTIAVPVSFVLLLIWIYQLKKNSEK 38
Cdd:pfam17410 238 IAALVLLILAVVLIILYIWLYRRRKNSWK 266
 
Name Accession Description Interval E-value
Stevor pfam17410
Subtelomeric Variable Open Reading frame; The parasite protein STEVOR (Subtelomeric Variable ...
10-38 8.04e-03

Subtelomeric Variable Open Reading frame; The parasite protein STEVOR (Subtelomeric Variable Open Reading frame) is an erythrocyte-binding protein recognizing Glycophorin C on the red blood cell (RBC) surface. The cytoplasmic domain of STEVOR is shown to interact with ankyrin complex at the erythrocyte skeleton. It is phosphorylated by protein kinase A (PKA) at a specific serine residue (S324). The N-terminal semi-conserved region of Stevor that is present in this domain is shown to specifically bind to to a chymotrypsin-resistant RBC receptor. The expression of STEVOR in multiple parasite stages including merozoites suggests that STEVOR mediates multiple distinct functions in parasitic infectious cycle.


Pssm-ID: 407484  Cd Length: 275  Bit Score: 31.98  E-value: 8.04e-03
                          10        20
                  ....*....|....*....|....*....
gi 2085999400  10 ISLLFTIAVPVSFVLLLIWIYQLKKNSEK 38
Cdd:pfam17410 238 IAALVLLILAVVLIILYIWLYRRRKNSWK 266
 
Name Accession Description Interval E-value
Stevor pfam17410
Subtelomeric Variable Open Reading frame; The parasite protein STEVOR (Subtelomeric Variable ...
10-38 8.04e-03

Subtelomeric Variable Open Reading frame; The parasite protein STEVOR (Subtelomeric Variable Open Reading frame) is an erythrocyte-binding protein recognizing Glycophorin C on the red blood cell (RBC) surface. The cytoplasmic domain of STEVOR is shown to interact with ankyrin complex at the erythrocyte skeleton. It is phosphorylated by protein kinase A (PKA) at a specific serine residue (S324). The N-terminal semi-conserved region of Stevor that is present in this domain is shown to specifically bind to to a chymotrypsin-resistant RBC receptor. The expression of STEVOR in multiple parasite stages including merozoites suggests that STEVOR mediates multiple distinct functions in parasitic infectious cycle.


Pssm-ID: 407484  Cd Length: 275  Bit Score: 31.98  E-value: 8.04e-03
                          10        20
                  ....*....|....*....|....*....
gi 2085999400  10 ISLLFTIAVPVSFVLLLIWIYQLKKNSEK 38
Cdd:pfam17410 238 IAALVLLILAVVLIILYIWLYRRRKNSWK 266
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH