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Conserved domains on  [gi|1907105976|ref|XP_036014795|]
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X-linked retinitis pigmentosa GTPase regulator-interacting protein 1 isoform X5 [Mus musculus]

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 ...
842-1007 2.37e-73

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: 239.24  E-value: 2.37e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105976  842 DSEKMCIEIVSLAFCPEADVMSDETIQQVYVEYKFCDLPLSETETPMSLRKPRAGEEIHFHFSKVIDLDPVEHQSRRQFL 921
Cdd:pfam18111    1 DSDTIRIEIISLQLLNESEVMQDDNIQQLFVEYRFLGRPEEETETPVSLPKPKTGQELYYNFSKVIDVDKEKNSARREIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105976  922 FAMLHAQDSDEGRFKFTVVSDPLDEEKKECQDIGYAYLELWQIFQSGKDILEQELEIVSPRNQAIQIGRLKVSLQAAAAL 1001
Cdd:pfam18111   81 RSMLLPEDPNQGNLKFTVVSEPLDTEDGECEEIGYAYVDLKQILQSGRDIIEQDLDVKDARDENEQIGKLKVSVEALAAL 160

                   ....*.
gi 1907105976 1002 HGIYKE 1007
Cdd:pfam18111  161 RAIYSE 166
HOOK super family cl38191
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
219-523 7.24e-04

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


The actual alignment was detected with superfamily member pfam05622:

Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 43.52  E-value: 7.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105976  219 ECTQKAAELRASI---KENVE----LIRLKKLLQERNTSLAATEAQltrvqeaYEDLLQKNQGiLDTAHNAFLSQVNELK 291
Cdd:pfam05622  125 ESSDKVKKLEATVetyKKKLEdlgdLRRQVKLLEERNAEYMQRTLQ-------LEEELKKANA-LRGQLETYKRQVQELH 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105976  292 AELSEESKKAVSlrtqlgdvsiLQITLKEFQVRVEDLEKERKLLSDSYDRLLEnMLDSSHQPLDSSHQPHWSTELTGKQL 371
Cdd:pfam05622  197 GKLSEESKKADK----------LEFEYKKLEEKLEALQKEKERLIIERDTLRE-TNEELRCAQLQQAELSQADALLSPSS 265
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105976  372 PPQVCPLLDQMGTALEETKVFRQATNKA----QDGKLKFQDTDILYQHEQEEESLQSTAT-VASSPEELCELAAQPTLLP 446
Cdd:pfam05622  266 DPGDNLAAEIMPAEIREKLIRLQHENKMlrlgQEGSYRERLTELQQLLEDANRRKNELETqNRLANQRILELQQQVEELQ 345
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105976  447 QTDQRESSepKAQDENDLSQVLSELQVSHAETTLELEKTRDML---------LLQRKINmcyqeELEATLTKADRENRDH 517
Cdd:pfam05622  346 KALQEQGS--KAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIeelepkqdsNLAQKID-----ELQEALRKKDEDMKAM 418

                   ....*.
gi 1907105976  518 EEKLER 523
Cdd:pfam05622  419 EERYKK 424
 
Name Accession Description Interval E-value
RPGR1_C pfam18111
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain ...
842-1007 2.37e-73

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: 239.24  E-value: 2.37e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105976  842 DSEKMCIEIVSLAFCPEADVMSDETIQQVYVEYKFCDLPLSETETPMSLRKPRAGEEIHFHFSKVIDLDPVEHQSRRQFL 921
Cdd:pfam18111    1 DSDTIRIEIISLQLLNESEVMQDDNIQQLFVEYRFLGRPEEETETPVSLPKPKTGQELYYNFSKVIDVDKEKNSARREIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105976  922 FAMLHAQDSDEGRFKFTVVSDPLDEEKKECQDIGYAYLELWQIFQSGKDILEQELEIVSPRNQAIQIGRLKVSLQAAAAL 1001
Cdd:pfam18111   81 RSMLLPEDPNQGNLKFTVVSEPLDTEDGECEEIGYAYVDLKQILQSGRDIIEQDLDVKDARDENEQIGKLKVSVEALAAL 160

                   ....*.
gi 1907105976 1002 HGIYKE 1007
Cdd:pfam18111  161 RAIYSE 166
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
219-523 7.24e-04

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 43.52  E-value: 7.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105976  219 ECTQKAAELRASI---KENVE----LIRLKKLLQERNTSLAATEAQltrvqeaYEDLLQKNQGiLDTAHNAFLSQVNELK 291
Cdd:pfam05622  125 ESSDKVKKLEATVetyKKKLEdlgdLRRQVKLLEERNAEYMQRTLQ-------LEEELKKANA-LRGQLETYKRQVQELH 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105976  292 AELSEESKKAVSlrtqlgdvsiLQITLKEFQVRVEDLEKERKLLSDSYDRLLEnMLDSSHQPLDSSHQPHWSTELTGKQL 371
Cdd:pfam05622  197 GKLSEESKKADK----------LEFEYKKLEEKLEALQKEKERLIIERDTLRE-TNEELRCAQLQQAELSQADALLSPSS 265
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105976  372 PPQVCPLLDQMGTALEETKVFRQATNKA----QDGKLKFQDTDILYQHEQEEESLQSTAT-VASSPEELCELAAQPTLLP 446
Cdd:pfam05622  266 DPGDNLAAEIMPAEIREKLIRLQHENKMlrlgQEGSYRERLTELQQLLEDANRRKNELETqNRLANQRILELQQQVEELQ 345
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105976  447 QTDQRESSepKAQDENDLSQVLSELQVSHAETTLELEKTRDML---------LLQRKINmcyqeELEATLTKADRENRDH 517
Cdd:pfam05622  346 KALQEQGS--KAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIeelepkqdsNLAQKID-----ELQEALRKKDEDMKAM 418

                   ....*.
gi 1907105976  518 EEKLER 523
Cdd:pfam05622  419 EERYKK 424
 
Name Accession Description Interval E-value
RPGR1_C pfam18111
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain ...
842-1007 2.37e-73

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: 239.24  E-value: 2.37e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105976  842 DSEKMCIEIVSLAFCPEADVMSDETIQQVYVEYKFCDLPLSETETPMSLRKPRAGEEIHFHFSKVIDLDPVEHQSRRQFL 921
Cdd:pfam18111    1 DSDTIRIEIISLQLLNESEVMQDDNIQQLFVEYRFLGRPEEETETPVSLPKPKTGQELYYNFSKVIDVDKEKNSARREIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105976  922 FAMLHAQDSDEGRFKFTVVSDPLDEEKKECQDIGYAYLELWQIFQSGKDILEQELEIVSPRNQAIQIGRLKVSLQAAAAL 1001
Cdd:pfam18111   81 RSMLLPEDPNQGNLKFTVVSEPLDTEDGECEEIGYAYVDLKQILQSGRDIIEQDLDVKDARDENEQIGKLKVSVEALAAL 160

                   ....*.
gi 1907105976 1002 HGIYKE 1007
Cdd:pfam18111  161 RAIYSE 166
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
219-523 7.24e-04

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 43.52  E-value: 7.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105976  219 ECTQKAAELRASI---KENVE----LIRLKKLLQERNTSLAATEAQltrvqeaYEDLLQKNQGiLDTAHNAFLSQVNELK 291
Cdd:pfam05622  125 ESSDKVKKLEATVetyKKKLEdlgdLRRQVKLLEERNAEYMQRTLQ-------LEEELKKANA-LRGQLETYKRQVQELH 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105976  292 AELSEESKKAVSlrtqlgdvsiLQITLKEFQVRVEDLEKERKLLSDSYDRLLEnMLDSSHQPLDSSHQPHWSTELTGKQL 371
Cdd:pfam05622  197 GKLSEESKKADK----------LEFEYKKLEEKLEALQKEKERLIIERDTLRE-TNEELRCAQLQQAELSQADALLSPSS 265
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105976  372 PPQVCPLLDQMGTALEETKVFRQATNKA----QDGKLKFQDTDILYQHEQEEESLQSTAT-VASSPEELCELAAQPTLLP 446
Cdd:pfam05622  266 DPGDNLAAEIMPAEIREKLIRLQHENKMlrlgQEGSYRERLTELQQLLEDANRRKNELETqNRLANQRILELQQQVEELQ 345
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105976  447 QTDQRESSepKAQDENDLSQVLSELQVSHAETTLELEKTRDML---------LLQRKINmcyqeELEATLTKADRENRDH 517
Cdd:pfam05622  346 KALQEQGS--KAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIeelepkqdsNLAQKID-----ELQEALRKKDEDMKAM 418

                   ....*.
gi 1907105976  518 EEKLER 523
Cdd:pfam05622  419 EERYKK 424
 
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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