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Conserved domains on  [gi|30580371|sp|Q9CR26|]
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RecName: Full=Vacuolar protein sorting-associated protein VTA1 homolog; AltName: Full=SKD1-binding protein 1; Short=SBP1

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 ...
 22-152 2.60e-65

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: 201.25  E-value: 2.60e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30580371    22 RTAQEHDKRDPVVAYYCRLYAMQTGMKIDSKT--PECRKFLSKLMDQLEALKKQLGDNEAVTQEIVGCAHLENYALKMFL 99
Cdd:pfam04652   1 KRAQELEKADPVVAYYCRLYAVQQILKLGLHKkdKEVRAFLTKLLDKLEQFKKELGDNEAITDEVAAQAYVENFALKLFN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 30580371   100 YADNEDRAGRFHKNMIKSFYTASLLIDVITVFGELTDENVKHRKYARWKATYI 152
Cdd:pfam04652  81 RADKEDRAGRATKQTAKTFYAAATFFEVLQIFGELDEEIAKKIKYAKWKAARI 133
Vta1_C pfam18097
Vta1 C-terminal domain; This is the C-terminal domain of Vta1 proteins pfam04652. Structural ...
 268-305 8.19e-16

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: 70.00  E-value: 8.19e-16
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 30580371   268 PEDFARAQKYCKYAGSALQYEDVGTAVQNLQKALRLLT 305
Cdd:pfam18097   1 PDQIAQAQKHAKYAVSALQFDDVETAIKNLLKALKLLT 38
rad23 super family cl36702
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
 183-264 2.07e-03

UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


The actual alignment was detected with superfamily member TIGR00601:

Pssm-ID: 273167 [Multi-domain]  Cd Length: 378  Bit Score: 39.49  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30580371   183 ATSLPTQPPQPSSSSAYDPSNLAPGSYSgiqiPPGAHAPANTpaeVPHSTgvtsnavqPSPQTVPAAPAVDPDLYTASQG 262
Cdd:TIGR00601  79 TGTGKVAPPAATPTSAPTPTPSPPASPA----SGMSAAPASA---VEEKS--------PSEESATATAPESPSTSVPSSG 143


                  ..
gi 30580371   263 DI 264
Cdd:TIGR00601 144 SD 145
 
Name Accession Description Interval E-value
Vta1 pfam04652
Vta1 like; Vta1 (VPS20-associated protein 1) is a positive regulator of Vps4. Vps4 is an ...
 22-152 2.60e-65

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: 201.25  E-value: 2.60e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30580371    22 RTAQEHDKRDPVVAYYCRLYAMQTGMKIDSKT--PECRKFLSKLMDQLEALKKQLGDNEAVTQEIVGCAHLENYALKMFL 99
Cdd:pfam04652   1 KRAQELEKADPVVAYYCRLYAVQQILKLGLHKkdKEVRAFLTKLLDKLEQFKKELGDNEAITDEVAAQAYVENFALKLFN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 30580371   100 YADNEDRAGRFHKNMIKSFYTASLLIDVITVFGELTDENVKHRKYARWKATYI 152
Cdd:pfam04652  81 RADKEDRAGRATKQTAKTFYAAATFFEVLQIFGELDEEIAKKIKYAKWKAARI 133
Vta1_C pfam18097
Vta1 C-terminal domain; This is the C-terminal domain of Vta1 proteins pfam04652. Structural ...
 268-305 8.19e-16

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: 70.00  E-value: 8.19e-16
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 30580371   268 PEDFARAQKYCKYAGSALQYEDVGTAVQNLQKALRLLT 305
Cdd:pfam18097   1 PDQIAQAQKHAKYAVSALQFDDVETAIKNLLKALKLLT 38
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
 183-264 2.07e-03

UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273167 [Multi-domain]  Cd Length: 378  Bit Score: 39.49  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30580371   183 ATSLPTQPPQPSSSSAYDPSNLAPGSYSgiqiPPGAHAPANTpaeVPHSTgvtsnavqPSPQTVPAAPAVDPDLYTASQG 262
Cdd:TIGR00601  79 TGTGKVAPPAATPTSAPTPTPSPPASPA----SGMSAAPASA---VEEKS--------PSEESATATAPESPSTSVPSSG 143


                  ..
gi 30580371   263 DI 264
Cdd:TIGR00601 144 SD 145
PHA01929 PHA01929
putative scaffolding protein
 187-255 3.78e-03

putative scaffolding protein


Pssm-ID: 177328  Cd Length: 306  Bit Score: 38.50  E-value: 3.78e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30580371  187 PTQPPQPSSSSAYDPSNLAPGSYSGIQIPPGAHAPANTPAEVPHstgVTSNA-VQPSPQTVPAAPAVDPD 255
Cdd:PHA01929  25 PTPQPNPVIQPQAPVQPGQPGAPQQLAIPTQQPQPVPTSAMTPH---VVQQApAQPAPAAPPAAGAALPE 91
 
Name Accession Description Interval E-value
Vta1 pfam04652
Vta1 like; Vta1 (VPS20-associated protein 1) is a positive regulator of Vps4. Vps4 is an ...
 22-152 2.60e-65

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: 201.25  E-value: 2.60e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30580371    22 RTAQEHDKRDPVVAYYCRLYAMQTGMKIDSKT--PECRKFLSKLMDQLEALKKQLGDNEAVTQEIVGCAHLENYALKMFL 99
Cdd:pfam04652   1 KRAQELEKADPVVAYYCRLYAVQQILKLGLHKkdKEVRAFLTKLLDKLEQFKKELGDNEAITDEVAAQAYVENFALKLFN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 30580371   100 YADNEDRAGRFHKNMIKSFYTASLLIDVITVFGELTDENVKHRKYARWKATYI 152
Cdd:pfam04652  81 RADKEDRAGRATKQTAKTFYAAATFFEVLQIFGELDEEIAKKIKYAKWKAARI 133
Vta1_C pfam18097
Vta1 C-terminal domain; This is the C-terminal domain of Vta1 proteins pfam04652. Structural ...
 268-305 8.19e-16

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: 70.00  E-value: 8.19e-16
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 30580371   268 PEDFARAQKYCKYAGSALQYEDVGTAVQNLQKALRLLT 305
Cdd:pfam18097   1 PDQIAQAQKHAKYAVSALQFDDVETAIKNLLKALKLLT 38
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
 183-264 2.07e-03

UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273167 [Multi-domain]  Cd Length: 378  Bit Score: 39.49  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30580371   183 ATSLPTQPPQPSSSSAYDPSNLAPGSYSgiqiPPGAHAPANTpaeVPHSTgvtsnavqPSPQTVPAAPAVDPDLYTASQG 262
Cdd:TIGR00601  79 TGTGKVAPPAATPTSAPTPTPSPPASPA----SGMSAAPASA---VEEKS--------PSEESATATAPESPSTSVPSSG 143


                  ..
gi 30580371   263 DI 264
Cdd:TIGR00601 144 SD 145
PHA01929 PHA01929
putative scaffolding protein
 187-255 3.78e-03

putative scaffolding protein


Pssm-ID: 177328  Cd Length: 306  Bit Score: 38.50  E-value: 3.78e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30580371  187 PTQPPQPSSSSAYDPSNLAPGSYSGIQIPPGAHAPANTPAEVPHstgVTSNA-VQPSPQTVPAAPAVDPD 255
Cdd:PHA01929  25 PTPQPNPVIQPQAPVQPGQPGAPQQLAIPTQQPQPVPTSAMTPH---VVQQApAQPAPAAPPAAGAALPE 91
 
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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