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Conserved domains on  [gi|221056711|ref|XP_002259493|]
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Plasmodium exported protein (PHIST), unknown function [Plasmodium knowlesi strain H]

Protein Classification

PRESAN domain-containing protein( domain architecture ID 10560507)

PRESAN (Plasmodium RESA N-terminal) domain-containing protein, similar to Plasmodium falciparum PHIST protein that binds the virulence factor PfEMP1 and comigrates to knobs on the host cell surface

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRESAN pfam09687
Plasmodium RESA N-terminal; The short, four-helical domain first identified in the Plasmodium ...
 754-874 2.01e-30

Plasmodium RESA N-terminal; The short, four-helical domain first identified in the Plasmodium export proteins PHISTa and PHISTc has been extended to become this six-helical PRESAN domain identified in the P. falciparum-specific RESA-type (Ring-infected erythrocyte surface antigen) proteins in association with the DnaJ domain. Overall, at least 67 proteins have been detected in P. falciparum with complete copies of the PRESAN domain. No versions of this domain were detected in other apicomplexan genera, suggesting that the domain was 'invented' after the divergence of the lineage leading to the genus Plasmodium undergoing a dramatic proliferation only in P. falciparum. A secondary structure-prediction derived from the multiple alignment of the PRESAN family reveals that it is composed of an all-helical fold with six conserved helical segments. There is some evidence it might localize to membranes.


:

Pssm-ID: 430754  Cd Length: 125  Bit Score: 116.22  E-value: 2.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056711  754 KHIRGMIDKLGSTVNTRDMFYLFNCLINHERRKYIDMEEITMLFWDRTAKSYGLPDYYKNRQWMKAFDGMTKELFYTEKK 833
Cdd:pfam09687   5 EEINKKINSLNEVVSKKDMYIIWNYVNKNEKKKYYNMIEKLWKYFEELAKKYNIPEEYKKKLWKECYKEITKELKKKEKF 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 221056711  834 LFDRLYHLLQHGSCSRSGFIQFLKEVKFTCHRMRKEMENQW 874
Cdd:pfam09687  85 YNKDFYSFLNKGKLSRDEFKEFINSCRKSWKKLRKELEKKW 125
 
Name Accession Description Interval E-value
PRESAN pfam09687
Plasmodium RESA N-terminal; The short, four-helical domain first identified in the Plasmodium ...
 754-874 2.01e-30

Plasmodium RESA N-terminal; The short, four-helical domain first identified in the Plasmodium export proteins PHISTa and PHISTc has been extended to become this six-helical PRESAN domain identified in the P. falciparum-specific RESA-type (Ring-infected erythrocyte surface antigen) proteins in association with the DnaJ domain. Overall, at least 67 proteins have been detected in P. falciparum with complete copies of the PRESAN domain. No versions of this domain were detected in other apicomplexan genera, suggesting that the domain was 'invented' after the divergence of the lineage leading to the genus Plasmodium undergoing a dramatic proliferation only in P. falciparum. A secondary structure-prediction derived from the multiple alignment of the PRESAN family reveals that it is composed of an all-helical fold with six conserved helical segments. There is some evidence it might localize to membranes.


Pssm-ID: 430754  Cd Length: 125  Bit Score: 116.22  E-value: 2.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056711  754 KHIRGMIDKLGSTVNTRDMFYLFNCLINHERRKYIDMEEITMLFWDRTAKSYGLPDYYKNRQWMKAFDGMTKELFYTEKK 833
Cdd:pfam09687   5 EEINKKINSLNEVVSKKDMYIIWNYVNKNEKKKYYNMIEKLWKYFEELAKKYNIPEEYKKKLWKECYKEITKELKKKEKF 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 221056711  834 LFDRLYHLLQHGSCSRSGFIQFLKEVKFTCHRMRKEMENQW 874
Cdd:pfam09687  85 YNKDFYSFLNKGKLSRDEFKEFINSCRKSWKKLRKELEKKW 125
 
Name Accession Description Interval E-value
PRESAN pfam09687
Plasmodium RESA N-terminal; The short, four-helical domain first identified in the Plasmodium ...
 754-874 2.01e-30

Plasmodium RESA N-terminal; The short, four-helical domain first identified in the Plasmodium export proteins PHISTa and PHISTc has been extended to become this six-helical PRESAN domain identified in the P. falciparum-specific RESA-type (Ring-infected erythrocyte surface antigen) proteins in association with the DnaJ domain. Overall, at least 67 proteins have been detected in P. falciparum with complete copies of the PRESAN domain. No versions of this domain were detected in other apicomplexan genera, suggesting that the domain was 'invented' after the divergence of the lineage leading to the genus Plasmodium undergoing a dramatic proliferation only in P. falciparum. A secondary structure-prediction derived from the multiple alignment of the PRESAN family reveals that it is composed of an all-helical fold with six conserved helical segments. There is some evidence it might localize to membranes.


Pssm-ID: 430754  Cd Length: 125  Bit Score: 116.22  E-value: 2.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056711  754 KHIRGMIDKLGSTVNTRDMFYLFNCLINHERRKYIDMEEITMLFWDRTAKSYGLPDYYKNRQWMKAFDGMTKELFYTEKK 833
Cdd:pfam09687   5 EEINKKINSLNEVVSKKDMYIIWNYVNKNEKKKYYNMIEKLWKYFEELAKKYNIPEEYKKKLWKECYKEITKELKKKEKF 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 221056711  834 LFDRLYHLLQHGSCSRSGFIQFLKEVKFTCHRMRKEMENQW 874
Cdd:pfam09687  85 YNKDFYSFLNKGKLSRDEFKEFINSCRKSWKKLRKELEKKW 125
 
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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