NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1620184992|ref|XP_028541431|]
View 

Plasmodium exported protein (PHISTb), unknown function [Plasmodium sp. gorilla clade G2]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
223-329 9.42e-12

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: 62.29  E-value: 9.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620184992 223 DTKLMYTIWCRVMKNEEDKYYLVKEELHNFYENLPKSKFVPLDISNRLFYSCNDIIFINGINNEPYIVDIFEIWFKNNET 302
Cdd:pfam09687  19 SKKDMYIIWNYVNKNEKKKYYNMIEKLWKYFEELAKKYNIPEEYKKKLWKECYKEITKELKKKEKFYNKDFYSFLNKGKL 98
                          90       100
                  ....*....|....*....|....*..
gi 1620184992 303 NIREYKILLDATKLSWRKLKEDVLNSC 329
Cdd:pfam09687  99 SRDEFKEFINSCRKSWKKLRKELEKKW 125
 
Name Accession Description Interval E-value
PRESAN pfam09687
Plasmodium RESA N-terminal; The short, four-helical domain first identified in the Plasmodium ...
223-329 9.42e-12

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: 62.29  E-value: 9.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620184992 223 DTKLMYTIWCRVMKNEEDKYYLVKEELHNFYENLPKSKFVPLDISNRLFYSCNDIIFINGINNEPYIVDIFEIWFKNNET 302
Cdd:pfam09687  19 SKKDMYIIWNYVNKNEKKKYYNMIEKLWKYFEELAKKYNIPEEYKKKLWKECYKEITKELKKKEKFYNKDFYSFLNKGKL 98
                          90       100
                  ....*....|....*....|....*..
gi 1620184992 303 NIREYKILLDATKLSWRKLKEDVLNSC 329
Cdd:pfam09687  99 SRDEFKEFINSCRKSWKKLRKELEKKW 125
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
211-340 2.53e-07

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 53.64  E-value: 2.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620184992  211 KELDAFIKHGCSDTKLMYTIWCRVMKNEEDKYYLVKEELHNFYENLPKSKFVPLDISNRLFYSCNDIIFINGINNEPYIV 290
Cdd:PTZ00341   176 EKVDNLGRSGGDIIKKMQTLWDEIMDINKRKYDFLKEKLQKTYSQYKVQYDMPKEAYESKWGQCIKLIDQGGDNLEERLN 255
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1620184992  291 DIFEIWFKNNETNIREYKILLDATKLSWRKLKEDVLNSCKEIMMNGVNNF 340
Cdd:PTZ00341   256 SQFKNWYRQKYLNLEEYRRLTVLNQIAWKALSNQIQYSCRKIMNSDISSF 305
 
Name Accession Description Interval E-value
PRESAN pfam09687
Plasmodium RESA N-terminal; The short, four-helical domain first identified in the Plasmodium ...
223-329 9.42e-12

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: 62.29  E-value: 9.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620184992 223 DTKLMYTIWCRVMKNEEDKYYLVKEELHNFYENLPKSKFVPLDISNRLFYSCNDIIFINGINNEPYIVDIFEIWFKNNET 302
Cdd:pfam09687  19 SKKDMYIIWNYVNKNEKKKYYNMIEKLWKYFEELAKKYNIPEEYKKKLWKECYKEITKELKKKEKFYNKDFYSFLNKGKL 98
                          90       100
                  ....*....|....*....|....*..
gi 1620184992 303 NIREYKILLDATKLSWRKLKEDVLNSC 329
Cdd:pfam09687  99 SRDEFKEFINSCRKSWKKLRKELEKKW 125
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
211-340 2.53e-07

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 53.64  E-value: 2.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620184992  211 KELDAFIKHGCSDTKLMYTIWCRVMKNEEDKYYLVKEELHNFYENLPKSKFVPLDISNRLFYSCNDIIFINGINNEPYIV 290
Cdd:PTZ00341   176 EKVDNLGRSGGDIIKKMQTLWDEIMDINKRKYDFLKEKLQKTYSQYKVQYDMPKEAYESKWGQCIKLIDQGGDNLEERLN 255
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1620184992  291 DIFEIWFKNNETNIREYKILLDATKLSWRKLKEDVLNSCKEIMMNGVNNF 340
Cdd:PTZ00341   256 SQFKNWYRQKYLNLEEYRRLTVLNQIAWKALSNQIQYSCRKIMNSDISSF 305
 
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