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Conserved domains on  [gi|24655474|ref|NP_647640|]
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vesicle trafficking 1 [Drosophila melanogaster]

Protein Classification

VTA1 family vacuolar protein sorting-associated protein( domain architecture ID 15904302)

VTA1 family vacuolar protein sorting-associated protein such as Saccharomyces cerevisiae VTA1 that plays a role in the formation of the multivesicular body (MVB) and is required for the sorting of lipids to form intralumenal vesicles and for fluid-phase transport to the vacuole

Gene Ontology:  GO:0005771|GO:0045324
PubMed:  28379137|18194651

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Vta1 pfam04652
Vta1 like; Vta1 (VPS20-associated protein 1) is a positive regulator of Vps4. Vps4 is an ...
 18-148 4.73e-60

Vta1 like; Vta1 (VPS20-associated protein 1) is a positive regulator of Vps4. Vps4 is an ATPase that is required in the multivesicular body (MVB) sorting pathway to dissociate the endosomal sorting complex required for transport (ESCRT). Vta1 promotes correct assembly of Vps4 and stimulates its ATPase activity through its conserved Vta1/SBP1/LIP5 region.


:

Pssm-ID: 461380  Cd Length: 133  Bit Score: 188.16  E-value: 4.73e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655474    18 KLAQEHDTRDVVIAYWARLYALQVGLKAS--TQTGEETKLLLGIMDWLEQMKKQYAENEAITNEVAAQAHIENYALKLFL 95
Cdd:pfam04652   1 KRAQELEKADPVVAYYCRLYAVQQILKLGlhKKDKEVRAFLTKLLDKLEQFKKELGDNEAITDEVAAQAYVENFALKLFN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 24655474    96 YADKQDREENFGKNVVKAFYSSGVLYDILQTFGELSEEALHNRKYAKWKAAYI 148
Cdd:pfam04652  81 RADKEDRAGRATKQTAKTFYAAATFFEVLQIFGELDEEIAKKIKYAKWKAARI 133
Vta1_C pfam18097
Vta1 C-terminal domain; This is the C-terminal domain of Vta1 proteins pfam04652. Structural ...
 275-311 9.01e-15

Vta1 C-terminal domain; This is the C-terminal domain of Vta1 proteins pfam04652. Structural and functional analysis indicate that this C-terminal domain promotes the ATP-dependent double ring assembly of Vps4. Furthermore, it has been shown that it is necessary and sufficient for protein dimerization. Mutations in Lys-299 and Lys-302 completely abolished the ability of Vta1 to stimulate the ATPase activity of Vps4 while mutation in Lys-322 had no effect.


:

Pssm-ID: 465647  Cd Length: 38  Bit Score: 66.92  E-value: 9.01e-15
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 24655474   275 PDQMITAQKYCKYAGSALNYDDVKTAIENLQKALKLL 311
Cdd:pfam18097   1 PDQIAQAQKHAKYAVSALQFDDVETAIKNLLKALKLL 37
 
Name Accession Description Interval E-value
Vta1 pfam04652
Vta1 like; Vta1 (VPS20-associated protein 1) is a positive regulator of Vps4. Vps4 is an ...
 18-148 4.73e-60

Vta1 like; Vta1 (VPS20-associated protein 1) is a positive regulator of Vps4. Vps4 is an ATPase that is required in the multivesicular body (MVB) sorting pathway to dissociate the endosomal sorting complex required for transport (ESCRT). Vta1 promotes correct assembly of Vps4 and stimulates its ATPase activity through its conserved Vta1/SBP1/LIP5 region.


Pssm-ID: 461380  Cd Length: 133  Bit Score: 188.16  E-value: 4.73e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655474    18 KLAQEHDTRDVVIAYWARLYALQVGLKAS--TQTGEETKLLLGIMDWLEQMKKQYAENEAITNEVAAQAHIENYALKLFL 95
Cdd:pfam04652   1 KRAQELEKADPVVAYYCRLYAVQQILKLGlhKKDKEVRAFLTKLLDKLEQFKKELGDNEAITDEVAAQAYVENFALKLFN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 24655474    96 YADKQDREENFGKNVVKAFYSSGVLYDILQTFGELSEEALHNRKYAKWKAAYI 148
Cdd:pfam04652  81 RADKEDRAGRATKQTAKTFYAAATFFEVLQIFGELDEEIAKKIKYAKWKAARI 133
Vta1_C pfam18097
Vta1 C-terminal domain; This is the C-terminal domain of Vta1 proteins pfam04652. Structural ...
 275-311 9.01e-15

Vta1 C-terminal domain; This is the C-terminal domain of Vta1 proteins pfam04652. Structural and functional analysis indicate that this C-terminal domain promotes the ATP-dependent double ring assembly of Vps4. Furthermore, it has been shown that it is necessary and sufficient for protein dimerization. Mutations in Lys-299 and Lys-302 completely abolished the ability of Vta1 to stimulate the ATPase activity of Vps4 while mutation in Lys-322 had no effect.


Pssm-ID: 465647  Cd Length: 38  Bit Score: 66.92  E-value: 9.01e-15
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 24655474   275 PDQMITAQKYCKYAGSALNYDDVKTAIENLQKALKLL 311
Cdd:pfam18097   1 PDQIAQAQKHAKYAVSALQFDDVETAIKNLLKALKLL 37
 
Name Accession Description Interval E-value
Vta1 pfam04652
Vta1 like; Vta1 (VPS20-associated protein 1) is a positive regulator of Vps4. Vps4 is an ...
 18-148 4.73e-60

Vta1 like; Vta1 (VPS20-associated protein 1) is a positive regulator of Vps4. Vps4 is an ATPase that is required in the multivesicular body (MVB) sorting pathway to dissociate the endosomal sorting complex required for transport (ESCRT). Vta1 promotes correct assembly of Vps4 and stimulates its ATPase activity through its conserved Vta1/SBP1/LIP5 region.


Pssm-ID: 461380  Cd Length: 133  Bit Score: 188.16  E-value: 4.73e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655474    18 KLAQEHDTRDVVIAYWARLYALQVGLKAS--TQTGEETKLLLGIMDWLEQMKKQYAENEAITNEVAAQAHIENYALKLFL 95
Cdd:pfam04652   1 KRAQELEKADPVVAYYCRLYAVQQILKLGlhKKDKEVRAFLTKLLDKLEQFKKELGDNEAITDEVAAQAYVENFALKLFN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 24655474    96 YADKQDREENFGKNVVKAFYSSGVLYDILQTFGELSEEALHNRKYAKWKAAYI 148
Cdd:pfam04652  81 RADKEDRAGRATKQTAKTFYAAATFFEVLQIFGELDEEIAKKIKYAKWKAARI 133
Vta1_C pfam18097
Vta1 C-terminal domain; This is the C-terminal domain of Vta1 proteins pfam04652. Structural ...
 275-311 9.01e-15

Vta1 C-terminal domain; This is the C-terminal domain of Vta1 proteins pfam04652. Structural and functional analysis indicate that this C-terminal domain promotes the ATP-dependent double ring assembly of Vps4. Furthermore, it has been shown that it is necessary and sufficient for protein dimerization. Mutations in Lys-299 and Lys-302 completely abolished the ability of Vta1 to stimulate the ATPase activity of Vps4 while mutation in Lys-322 had no effect.


Pssm-ID: 465647  Cd Length: 38  Bit Score: 66.92  E-value: 9.01e-15
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 24655474   275 PDQMITAQKYCKYAGSALNYDDVKTAIENLQKALKLL 311
Cdd:pfam18097   1 PDQIAQAQKHAKYAVSALQFDDVETAIKNLLKALKLL 37
 
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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