NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|93204881|ref|NP_113618|]
View 

rab-interacting lysosomal protein [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
244-308 4.99e-21

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: 86.11  E-value: 4.99e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 93204881   244 SREEFEQILQERNELKAKVFLLKEELAYFQRELLTDHRVPGLLLEAMKVAVRKQRKKIKAKMLGT 308
Cdd:pfam11461   1 TLQELRDVLQERNELKAQLFLLQEELAYYKSGLLNEEEIPSLRLESPSPRTKPQRSKIKQEESGI 65
RILP-like super family cl47118
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in ...
28-79 5.30e-15

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.


The actual alignment was detected with superfamily member cd14445:

Pssm-ID: 271220 [Multi-domain]  Cd Length: 89  Bit Score: 69.93  E-value: 5.30e-15
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 93204881  28 VYHLAGALGTELQDLARRFGPEAAAGLVPLVVRALELLEQAAVGPAPDSLQV 79
Cdd:cd14445  18 VYDIASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEI 69
 
Name Accession Description Interval E-value
RILP pfam11461
Rab interacting lysosomal protein; RILP contains a domain which contains two coiled-coil ...
244-308 4.99e-21

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: 86.11  E-value: 4.99e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 93204881   244 SREEFEQILQERNELKAKVFLLKEELAYFQRELLTDHRVPGLLLEAMKVAVRKQRKKIKAKMLGT 308
Cdd:pfam11461   1 TLQELRDVLQERNELKAQLFLLQEELAYYKSGLLNEEEIPSLRLESPSPRTKPQRSKIKQEESGI 65
RILP-like cd14445
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in ...
28-79 5.30e-15

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: 69.93  E-value: 5.30e-15
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 93204881  28 VYHLAGALGTELQDLARRFGPEAAAGLVPLVVRALELLEQAAVGPAPDSLQV 79
Cdd:cd14445  18 VYDIASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEI 69
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
28-69 6.04e-08

JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.


Pssm-ID: 462875 [Multi-domain]  Cd Length: 150  Bit Score: 51.46  E-value: 6.04e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 93204881    28 VYHLAGALGTELQDLARRFGPEAAAGLVPLVVRALELLEQAA 69
Cdd:pfam09744   1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLA 42
 
Name Accession Description Interval E-value
RILP pfam11461
Rab interacting lysosomal protein; RILP contains a domain which contains two coiled-coil ...
244-308 4.99e-21

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: 86.11  E-value: 4.99e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 93204881   244 SREEFEQILQERNELKAKVFLLKEELAYFQRELLTDHRVPGLLLEAMKVAVRKQRKKIKAKMLGT 308
Cdd:pfam11461   1 TLQELRDVLQERNELKAQLFLLQEELAYYKSGLLNEEEIPSLRLESPSPRTKPQRSKIKQEESGI 65
RILP-like cd14445
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in ...
28-79 5.30e-15

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: 69.93  E-value: 5.30e-15
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 93204881  28 VYHLAGALGTELQDLARRFGPEAAAGLVPLVVRALELLEQAAVGPAPDSLQV 79
Cdd:cd14445  18 VYDIASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEI 69
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
28-69 6.04e-08

JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.


Pssm-ID: 462875 [Multi-domain]  Cd Length: 150  Bit Score: 51.46  E-value: 6.04e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 93204881    28 VYHLAGALGTELQDLARRFGPEAAAGLVPLVVRALELLEQAA 69
Cdd:pfam09744   1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLA 42
 
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