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Conserved domains on  [gi|258597015|ref|XP_001347392|]
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uncharacterized protein PF3D7_1011000 [Plasmodium falciparum 3D7]

Protein Classification

ISP3_C superfamily-containing protein( domain architecture ID 1563436)

ISP3_C superfamily-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ISP3_C super family cl39033
ISP3 C-terminal; This is the C-terminal domain of ISP3 protein, which plays a role in asexual ...
 34-138 8.33e-32

ISP3 C-terminal; This is the C-terminal domain of ISP3 protein, which plays a role in asexual daughter cell formation, for example in T.gondii. The domain consists of a seven-stranded antiparallel beta-sandwich bordered on one end by a interstrand loop (open end) and capped at the other end by an amphipathic C-terminal helix (closed end). The loop between beta 5 and beta 6 is extended and variable. The domain adopts a pleckstrin homology (PH) fold, despite having neglible sequence similarity. PH domains are often found in proteins that support protein-lipid and play a role in mediating membrane localization through IP binding. However, the Phospholipid Binding Properties of PH domains is not conserved in the ISP3. Unlike PH domains, ISP3 is cysteine rich. The cysteine-rich nature of the ISP3s and the number of surface-exposed cysteines may result in redox instability and may also facilitate higher order multimerization. There are no disulfide bonds in ISP3 unlike in ISP1. It is worth noting that ISP1 and ISP3 share low sequence identity but contain the same secondary core elements.


The actual alignment was detected with superfamily member pfam18161:

Pssm-ID: 453938  Cd Length: 107  Bit Score: 109.07  E-value: 8.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597015   34 FKKRLKNNIQIVVLLQDGTKLPCNLQANFQEKTLCISCHQKVRMINFSDIRSLLYGEEQLKRVETQANLINDNCCLALHL 113
Cdd:pfam18161   2 WIRRLKSGNSIKVLLPDGSELQCTLHYNFKDNYLELSCDDKVRVIKFSDIKCILHTKSELTRVETEANLLKDPKVIAIHL 81

                          90       100
                  ....*....|....*....|....*
gi 258597015  114 DDSGNCIPIKFGSVKEKNLFIFIMK 138
Cdd:pfam18161  82 IESGNCIPLSFDNPGEKRIFLDFLQ 106
 
Name Accession Description Interval E-value
ISP1_C pfam18161
ISP1 C-terminal; This is the C-terminal domain of ISP1 protein, which plays a role in asexual ...
 34-138 8.33e-32

ISP1 C-terminal; This is the C-terminal domain of ISP1 protein, which plays a role in asexual daughter cell formation, such as in Toxi. gondii. The domain consists of a seven-stranded antiparallel beta-sandwich bordered on one end by an inter-strand loop (open end) and capped at the other end by an amphipathic C-terminal helix (closed end). The domain adopts a pleckstrin homology (PH) fold, despite having negligible sequence similarity. PH domains are often found in proteins that support protein-lipid and play a role in mediating membrane localization through IP binding. However, the Phospholipid Binding Properties of PH domains is not conserved in the TgISP1. Unlike PH domains, ISP1 is cysteine rich. The cysteine-rich nature of the ISPs and the number of surface-exposed cysteines may result in redox instability and may also facilitate higher order multimerization. A disulfide bond between beta 2 and beta 3 is likely a structural feature of the ISP1, as both cysteines appear broadly conserved.


Pssm-ID: 436320  Cd Length: 107  Bit Score: 109.07  E-value: 8.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597015   34 FKKRLKNNIQIVVLLQDGTKLPCNLQANFQEKTLCISCHQKVRMINFSDIRSLLYGEEQLKRVETQANLINDNCCLALHL 113
Cdd:pfam18161   2 WIRRLKSGNSIKVLLPDGSELQCTLHYNFKDNYLELSCDDKVRVIKFSDIKCILHTKSELTRVETEANLLKDPKVIAIHL 81

                          90       100
                  ....*....|....*....|....*
gi 258597015  114 DDSGNCIPIKFGSVKEKNLFIFIMK 138
Cdd:pfam18161  82 IESGNCIPLSFDNPGEKRIFLDFLQ 106
 
Name Accession Description Interval E-value
ISP1_C pfam18161
ISP1 C-terminal; This is the C-terminal domain of ISP1 protein, which plays a role in asexual ...
 34-138 8.33e-32

ISP1 C-terminal; This is the C-terminal domain of ISP1 protein, which plays a role in asexual daughter cell formation, such as in Toxi. gondii. The domain consists of a seven-stranded antiparallel beta-sandwich bordered on one end by an inter-strand loop (open end) and capped at the other end by an amphipathic C-terminal helix (closed end). The domain adopts a pleckstrin homology (PH) fold, despite having negligible sequence similarity. PH domains are often found in proteins that support protein-lipid and play a role in mediating membrane localization through IP binding. However, the Phospholipid Binding Properties of PH domains is not conserved in the TgISP1. Unlike PH domains, ISP1 is cysteine rich. The cysteine-rich nature of the ISPs and the number of surface-exposed cysteines may result in redox instability and may also facilitate higher order multimerization. A disulfide bond between beta 2 and beta 3 is likely a structural feature of the ISP1, as both cysteines appear broadly conserved.


Pssm-ID: 436320  Cd Length: 107  Bit Score: 109.07  E-value: 8.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597015   34 FKKRLKNNIQIVVLLQDGTKLPCNLQANFQEKTLCISCHQKVRMINFSDIRSLLYGEEQLKRVETQANLINDNCCLALHL 113
Cdd:pfam18161   2 WIRRLKSGNSIKVLLPDGSELQCTLHYNFKDNYLELSCDDKVRVIKFSDIKCILHTKSELTRVETEANLLKDPKVIAIHL 81

                          90       100
                  ....*....|....*....|....*
gi 258597015  114 DDSGNCIPIKFGSVKEKNLFIFIMK 138
Cdd:pfam18161  82 IESGNCIPLSFDNPGEKRIFLDFLQ 106
ISP3_C pfam18045
ISP3 C-terminal; This is the C-terminal domain of ISP3 protein, which plays a role in asexual ...
 30-139 6.51e-24

ISP3 C-terminal; This is the C-terminal domain of ISP3 protein, which plays a role in asexual daughter cell formation, for example in T.gondii. The domain consists of a seven-stranded antiparallel beta-sandwich bordered on one end by a interstrand loop (open end) and capped at the other end by an amphipathic C-terminal helix (closed end). The loop between beta 5 and beta 6 is extended and variable. The domain adopts a pleckstrin homology (PH) fold, despite having neglible sequence similarity. PH domains are often found in proteins that support protein-lipid and play a role in mediating membrane localization through IP binding. However, the Phospholipid Binding Properties of PH domains is not conserved in the ISP3. Unlike PH domains, ISP3 is cysteine rich. The cysteine-rich nature of the ISP3s and the number of surface-exposed cysteines may result in redox instability and may also facilitate higher order multimerization. There are no disulfide bonds in ISP3 unlike in ISP1. It is worth noting that ISP1 and ISP3 share low sequence identity but contain the same secondary core elements.


Pssm-ID: 407882  Cd Length: 110  Bit Score: 89.05  E-value: 6.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597015   30 EINEFKKRLKNNIQIVVLLQDGTKLPCNLQANFQEKTLCISCHQKVRMINFSDIRSLLYGEEQLKRVETQANLINDNCCL 109
Cdd:pfam18045   1 EEQNFMNKYQNGLTVIVLFPDGTKLSCTLKIDLEESCVRLACDKKVRVIDFADVKKILHTKDEESLIQTDGNLLNYPTVV 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 258597015  110 ALHLDDSGNCIPIKFGSVKEKNLFIFIMKD 139
Cdd:pfam18045  81 AFRLLSTGKAIAFSFSDTREKRMFYNFLSP 110
 
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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