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Conserved domains on  [gi|1799657593|ref|NP_001364879|]
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X-linked retinitis pigmentosa GTPase regulator-interacting protein 1 isoform 5 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RPGR1_C pfam18111
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain ...
440-605 2.15e-83

Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain of retinitis pigmentosa G-protein regulator (RPGR) interacting protein-1 present in Homo sapiens. A mutation in RPGR interacting protein-1 can be observed in the eye disease Leber congenital amaurosis. The domain is commonly known as the RPGR-interacting domain (RID) and is thought to have a C2-like fold.


:

Pssm-ID: 465655  Cd Length: 166  Bit Score: 258.50  E-value: 2.15e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799657593 440 DSEKMCIEIVSLAFYPEAEVMSDENIKQVYVEYKFYDLPLSETETPVSLRKPRAGEEIHFHFSKVIDLDPQEQQGRRRFL 519
Cdd:pfam18111   1 DSDTIRIEIISLQLLNESEVMQDDNIQQLFVEYRFLGRPEEETETPVSLPKPKTGQELYYNFSKVIDVDKEKNSARREIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799657593 520 FDMLNGQDPDQGHLKFTVVSDPLDEEKKECEEVGYAYLQLWQILESGRDILEQELDIVSPEDLATPIGRLKVSLQAAAVL 599
Cdd:pfam18111  81 RSMLLPEDPNQGNLKFTVVSEPLDTEDGECEEIGYAYVDLKQILQSGRDIIEQDLDVKDARDENEQIGKLKVSVEALAAL 160

                  ....*.
gi 1799657593 600 HAIYKE 605
Cdd:pfam18111 161 RAIYSE 166
 
Name Accession Description Interval E-value
RPGR1_C pfam18111
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain ...
440-605 2.15e-83

Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain of retinitis pigmentosa G-protein regulator (RPGR) interacting protein-1 present in Homo sapiens. A mutation in RPGR interacting protein-1 can be observed in the eye disease Leber congenital amaurosis. The domain is commonly known as the RPGR-interacting domain (RID) and is thought to have a C2-like fold.


Pssm-ID: 465655  Cd Length: 166  Bit Score: 258.50  E-value: 2.15e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799657593 440 DSEKMCIEIVSLAFYPEAEVMSDENIKQVYVEYKFYDLPLSETETPVSLRKPRAGEEIHFHFSKVIDLDPQEQQGRRRFL 519
Cdd:pfam18111   1 DSDTIRIEIISLQLLNESEVMQDDNIQQLFVEYRFLGRPEEETETPVSLPKPKTGQELYYNFSKVIDVDKEKNSARREIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799657593 520 FDMLNGQDPDQGHLKFTVVSDPLDEEKKECEEVGYAYLQLWQILESGRDILEQELDIVSPEDLATPIGRLKVSLQAAAVL 599
Cdd:pfam18111  81 RSMLLPEDPNQGNLKFTVVSEPLDTEDGECEEIGYAYVDLKQILQSGRDIIEQDLDVKDARDENEQIGKLKVSVEALAAL 160

                  ....*.
gi 1799657593 600 HAIYKE 605
Cdd:pfam18111 161 RAIYSE 166
 
Name Accession Description Interval E-value
RPGR1_C pfam18111
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain ...
440-605 2.15e-83

Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain of retinitis pigmentosa G-protein regulator (RPGR) interacting protein-1 present in Homo sapiens. A mutation in RPGR interacting protein-1 can be observed in the eye disease Leber congenital amaurosis. The domain is commonly known as the RPGR-interacting domain (RID) and is thought to have a C2-like fold.


Pssm-ID: 465655  Cd Length: 166  Bit Score: 258.50  E-value: 2.15e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799657593 440 DSEKMCIEIVSLAFYPEAEVMSDENIKQVYVEYKFYDLPLSETETPVSLRKPRAGEEIHFHFSKVIDLDPQEQQGRRRFL 519
Cdd:pfam18111   1 DSDTIRIEIISLQLLNESEVMQDDNIQQLFVEYRFLGRPEEETETPVSLPKPKTGQELYYNFSKVIDVDKEKNSARREIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799657593 520 FDMLNGQDPDQGHLKFTVVSDPLDEEKKECEEVGYAYLQLWQILESGRDILEQELDIVSPEDLATPIGRLKVSLQAAAVL 599
Cdd:pfam18111  81 RSMLLPEDPNQGNLKFTVVSEPLDTEDGECEEIGYAYVDLKQILQSGRDIIEQDLDVKDARDENEQIGKLKVSVEALAAL 160

                  ....*.
gi 1799657593 600 HAIYKE 605
Cdd:pfam18111 161 RAIYSE 166
 
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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