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Conserved domains on  [gi|556503347|ref|NP_001273301|]
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vacuolar protein sorting-associated protein VTA1 homolog isoform c [Homo sapiens]

Protein Classification

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 ...
 8-94 1.41e-36

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: 124.98  E-value: 1.41e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503347    8 WLITLKKQLGDNEAITQEIVGCAHLENYALKMFLYADNEDRAGRFHKNMIKSFYTASLLIDVITVFGELTDENVKHRKYA 87
Cdd:pfam04652  47 KLEQFKKELGDNEAITDEVAAQAYVENFALKLFNRADKEDRAGRATKQTAKTFYAAATFFEVLQIFGELDEEIAKKIKYA 126


                  ....*..
gi 556503347   88 RWKATYI 94
Cdd:pfam04652 127 KWKAARI 133
Vta1_C pfam18097
Vta1 C-terminal domain; This is the C-terminal domain of Vta1 proteins pfam04652. Structural ...
 181-218 3.12e-17

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: 72.31  E-value: 3.12e-17
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 556503347  181 PEDFARAQKYCKYAGSALQYEDVSTAVQNLQKALKLLT 218
Cdd:pfam18097   1 PDQIAQAQKHAKYAVSALQFDDVETAIKNLLKALKLLT 38
 
Name Accession Description Interval E-value
Vta1 pfam04652
Vta1 like; Vta1 (VPS20-associated protein 1) is a positive regulator of Vps4. Vps4 is an ...
 8-94 1.41e-36

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: 124.98  E-value: 1.41e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503347    8 WLITLKKQLGDNEAITQEIVGCAHLENYALKMFLYADNEDRAGRFHKNMIKSFYTASLLIDVITVFGELTDENVKHRKYA 87
Cdd:pfam04652  47 KLEQFKKELGDNEAITDEVAAQAYVENFALKLFNRADKEDRAGRATKQTAKTFYAAATFFEVLQIFGELDEEIAKKIKYA 126


                  ....*..
gi 556503347   88 RWKATYI 94
Cdd:pfam04652 127 KWKAARI 133
Vta1_C pfam18097
Vta1 C-terminal domain; This is the C-terminal domain of Vta1 proteins pfam04652. Structural ...
 181-218 3.12e-17

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: 72.31  E-value: 3.12e-17
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 556503347  181 PEDFARAQKYCKYAGSALQYEDVSTAVQNLQKALKLLT 218
Cdd:pfam18097   1 PDQIAQAQKHAKYAVSALQFDDVETAIKNLLKALKLLT 38
PRK11788 PRK11788
tetratricopeptide repeat protein; Provisional
 177-215 5.48e-03

tetratricopeptide repeat protein; Provisional


Pssm-ID: 236983 [Multi-domain]  Cd Length: 389  Bit Score: 37.10  E-value: 5.48e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 556503347 177 VRLTPEDFAR--AQKYCKYAGSALQYEDVSTAVQNLQKALK 215
Cdd:PRK11788 168 EKLGGDSLRVeiAHFYCELAQQALARGDLDAARALLKKALA 208
 
Name Accession Description Interval E-value
Vta1 pfam04652
Vta1 like; Vta1 (VPS20-associated protein 1) is a positive regulator of Vps4. Vps4 is an ...
 8-94 1.41e-36

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: 124.98  E-value: 1.41e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503347    8 WLITLKKQLGDNEAITQEIVGCAHLENYALKMFLYADNEDRAGRFHKNMIKSFYTASLLIDVITVFGELTDENVKHRKYA 87
Cdd:pfam04652  47 KLEQFKKELGDNEAITDEVAAQAYVENFALKLFNRADKEDRAGRATKQTAKTFYAAATFFEVLQIFGELDEEIAKKIKYA 126


                  ....*..
gi 556503347   88 RWKATYI 94
Cdd:pfam04652 127 KWKAARI 133
Vta1_C pfam18097
Vta1 C-terminal domain; This is the C-terminal domain of Vta1 proteins pfam04652. Structural ...
 181-218 3.12e-17

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: 72.31  E-value: 3.12e-17
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 556503347  181 PEDFARAQKYCKYAGSALQYEDVSTAVQNLQKALKLLT 218
Cdd:pfam18097   1 PDQIAQAQKHAKYAVSALQFDDVETAIKNLLKALKLLT 38
PRK11788 PRK11788
tetratricopeptide repeat protein; Provisional
 177-215 5.48e-03

tetratricopeptide repeat protein; Provisional


Pssm-ID: 236983 [Multi-domain]  Cd Length: 389  Bit Score: 37.10  E-value: 5.48e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 556503347 177 VRLTPEDFAR--AQKYCKYAGSALQYEDVSTAVQNLQKALK 215
Cdd:PRK11788 168 EKLGGDSLRVeiAHFYCELAQQALARGDLDAARALLKKALA 208
 
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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