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Conserved domains on  [gi|767973431|ref|XP_011536314|]
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RILP-like protein 2 isoform X2 [Homo sapiens]

Protein Classification

ATP-binding protein; ENTH domain-containing protein( domain architecture ID 10199244)

ATPase similar to histidine kinase domains| ENTH (Epsin N-Terminal Homology) domain-containing protein may be involved in clathrin-mediated endocytosis; similar to epsin that plays an important role as accessory proteins in clathrin-mediated endocytosis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RILP pfam11461
Rab interacting lysosomal protein; RILP contains a domain which contains two coiled-coil ...
 134-202 7.47e-27

Rab interacting lysosomal protein; RILP contains a domain which contains two coiled-coil regions and is found mainly in the cytosol. RILP is recruited onto late endosomal and lysosomal membranes by Rab7 and acts as a downstream effector of Rab7. This recruitment process is important for phagosome maturation and fusion with late endosomes and lysosomes.


:

Pssm-ID: 463282 [Multi-domain]  Cd Length: 69  Bit Score: 97.28  E-value: 7.47e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973431  134 TLQELRDVLQERNKLKSQLLVVQEELQCYKSGLIPPREGPGGRREKDAVVTSAKNAgRNKEEKTIIKKL 202
Cdd:pfam11461   1 TLQELRDVLQERNELKAQLFLLQEELAYYKSGLLNEEEIPSLRLESPSPRTKPQRS-KIKQEESGIKRL 68
RILP-like cd14445
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in ...
 25-106 3.45e-24

Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in Rab interacting lysosomal protein-like 1 and 2, and appears to be conserved in Bilateria. The Rilp-like proteins regulate the concentration of ciliary membrane proteins in the primary cilium. Rilpl2 interacts with myosin-Va and has been linked to the regulation of cellular morphology in neurons; it forms a complex with Rac1 and activates Rac1-Pak signaling, dependent on myosin-Va.


:

Pssm-ID: 271220 [Multi-domain]  Cd Length: 89  Bit Score: 91.12  E-value: 3.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973431  25 PEGALGKSPFQLTAEDVYDISYLLGRELMALGS---DPRVTQLQFKVVRVLEMLEALVNEGS---LALEELKMERDHLRK 98
Cdd:cd14445    2 AESALDKSPSELTVVDVYDIASAIGKEFERLIDrygPEAVAGLMPKVVRVLELLEALASRNErenLEIEELRLEVDRLEL 81


                 ....*...
gi 767973431  99 EVEGLRRQ 106
Cdd:cd14445   82 EKRERAQK 89
 
Name Accession Description Interval E-value
RILP pfam11461
Rab interacting lysosomal protein; RILP contains a domain which contains two coiled-coil ...
 134-202 7.47e-27

Rab interacting lysosomal protein; RILP contains a domain which contains two coiled-coil regions and is found mainly in the cytosol. RILP is recruited onto late endosomal and lysosomal membranes by Rab7 and acts as a downstream effector of Rab7. This recruitment process is important for phagosome maturation and fusion with late endosomes and lysosomes.


Pssm-ID: 463282 [Multi-domain]  Cd Length: 69  Bit Score: 97.28  E-value: 7.47e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973431  134 TLQELRDVLQERNKLKSQLLVVQEELQCYKSGLIPPREGPGGRREKDAVVTSAKNAgRNKEEKTIIKKL 202
Cdd:pfam11461   1 TLQELRDVLQERNELKAQLFLLQEELAYYKSGLLNEEEIPSLRLESPSPRTKPQRS-KIKQEESGIKRL 68
RILP-like cd14445
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in ...
 25-106 3.45e-24

Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in Rab interacting lysosomal protein-like 1 and 2, and appears to be conserved in Bilateria. The Rilp-like proteins regulate the concentration of ciliary membrane proteins in the primary cilium. Rilpl2 interacts with myosin-Va and has been linked to the regulation of cellular morphology in neurons; it forms a complex with Rac1 and activates Rac1-Pak signaling, dependent on myosin-Va.


Pssm-ID: 271220 [Multi-domain]  Cd Length: 89  Bit Score: 91.12  E-value: 3.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973431  25 PEGALGKSPFQLTAEDVYDISYLLGRELMALGS---DPRVTQLQFKVVRVLEMLEALVNEGS---LALEELKMERDHLRK 98
Cdd:cd14445    2 AESALDKSPSELTVVDVYDIASAIGKEFERLIDrygPEAVAGLMPKVVRVLELLEALASRNErenLEIEELRLEVDRLEL 81


                 ....*...
gi 767973431  99 EVEGLRRQ 106
Cdd:cd14445   82 EKRERAQK 89
 
Name Accession Description Interval E-value
RILP pfam11461
Rab interacting lysosomal protein; RILP contains a domain which contains two coiled-coil ...
 134-202 7.47e-27

Rab interacting lysosomal protein; RILP contains a domain which contains two coiled-coil regions and is found mainly in the cytosol. RILP is recruited onto late endosomal and lysosomal membranes by Rab7 and acts as a downstream effector of Rab7. This recruitment process is important for phagosome maturation and fusion with late endosomes and lysosomes.


Pssm-ID: 463282 [Multi-domain]  Cd Length: 69  Bit Score: 97.28  E-value: 7.47e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973431  134 TLQELRDVLQERNKLKSQLLVVQEELQCYKSGLIPPREGPGGRREKDAVVTSAKNAgRNKEEKTIIKKL 202
Cdd:pfam11461   1 TLQELRDVLQERNELKAQLFLLQEELAYYKSGLLNEEEIPSLRLESPSPRTKPQRS-KIKQEESGIKRL 68
RILP-like cd14445
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in ...
 25-106 3.45e-24

Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in Rab interacting lysosomal protein-like 1 and 2, and appears to be conserved in Bilateria. The Rilp-like proteins regulate the concentration of ciliary membrane proteins in the primary cilium. Rilpl2 interacts with myosin-Va and has been linked to the regulation of cellular morphology in neurons; it forms a complex with Rac1 and activates Rac1-Pak signaling, dependent on myosin-Va.


Pssm-ID: 271220 [Multi-domain]  Cd Length: 89  Bit Score: 91.12  E-value: 3.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973431  25 PEGALGKSPFQLTAEDVYDISYLLGRELMALGS---DPRVTQLQFKVVRVLEMLEALVNEGS---LALEELKMERDHLRK 98
Cdd:cd14445    2 AESALDKSPSELTVVDVYDIASAIGKEFERLIDrygPEAVAGLMPKVVRVLELLEALASRNErenLEIEELRLEVDRLEL 81


                 ....*...
gi 767973431  99 EVEGLRRQ 106
Cdd:cd14445   82 EKRERAQK 89
 
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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