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Conserved domains on  [gi|257471797|pdb|3GGZ|D]
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Chain D, Increased sodium tolerance protein 1

Protein Classification

IST1 family protein( domain architecture ID 10506161)

IST1 family protein such as increased sodium tolerance protein 1 (IST1), an ESCRT-III-like protein involved in specific functions of the ESCRT machinery

CATH:  1.20.1260.60
Gene Ontology:  GO:0015031|GO:0099638|GO:0042030
SCOP:  4007386
TCDB:  3.A.31

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ist1 pfam03398
Regulator of Vps4 activity in the MVB pathway; ESCRT-I, -II, and -III are endosomal sorting ...
 13-183 6.75e-72

Regulator of Vps4 activity in the MVB pathway; ESCRT-I, -II, and -III are endosomal sorting complexes required for transporting proteins and carry out cargo sorting and vesicle formation in the multivesicular bodies, MVBs, pathway. These complexes are transiently recruited from the cytoplasm to the endosomal membrane where they bind transmembrane proteins previously marked for degradation by mono-ubiquitination. Assembly of ESCRT-III, a complex composed of at least four subunits (Vps2, Vps24, Vps20, Snf7), is intimately linked with MVB vesicle formation, its disassembly being an essential step in the MVB vesicle formation, a reaction that is carried out by Vps4, an AAA-type ATPase. The family Ist1 is a regulator of Vps4 activity; by interacting with Did2 and Vps4, Ist1 appears to regulate the recruitment and oligomerization of Vps4. Together Ist1, Did2, and Vta1 form a network of interconnected regulatory proteins that modulate Vps4 activity, thereby regulating the flow of cargo through the MVB pathway.


:

Pssm-ID: 460910  Cd Length: 164  Bit Score: 214.63  E-value: 6.75e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3GGZ_D         13 KTCLKMCIQRLRYAQEKQQAIAKQSRRQVAQLLLTNKEQKAHYRVETLIHDDIHIELLEILELYCELLLARVQVINDIST 92
Cdd:pfam03398   1 KTQLKLAIQRLKLLQNKKEALAKQARRDIAQLLENGKEERARIRVEHIIREDNLIEALEILELYCELLLARLGLLEQQKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3GGZ_D         93 eeqlvkehMDDGINEAIRSLIYAILFVDEVKELSQLKDLMAWKINVEFVNGVIADHID-VPEKIIKKCSPSVPKEELVDL 171
Cdd:pfam03398  81 --------CPPGLKEAVSSLIYAAPRCSELPELQQLRDLLAEKYGKEFAKAAVENPDNgVNEKVVEKLSVKPPSKELVDK 152

                         170
                  ....*....|..
3GGZ_D        172 YLKEIAKTYDVP 183
Cdd:pfam03398 153 YLKEIAKEYGVP 164
 
Name Accession Description Interval E-value
Ist1 pfam03398
Regulator of Vps4 activity in the MVB pathway; ESCRT-I, -II, and -III are endosomal sorting ...
 13-183 6.75e-72

Regulator of Vps4 activity in the MVB pathway; ESCRT-I, -II, and -III are endosomal sorting complexes required for transporting proteins and carry out cargo sorting and vesicle formation in the multivesicular bodies, MVBs, pathway. These complexes are transiently recruited from the cytoplasm to the endosomal membrane where they bind transmembrane proteins previously marked for degradation by mono-ubiquitination. Assembly of ESCRT-III, a complex composed of at least four subunits (Vps2, Vps24, Vps20, Snf7), is intimately linked with MVB vesicle formation, its disassembly being an essential step in the MVB vesicle formation, a reaction that is carried out by Vps4, an AAA-type ATPase. The family Ist1 is a regulator of Vps4 activity; by interacting with Did2 and Vps4, Ist1 appears to regulate the recruitment and oligomerization of Vps4. Together Ist1, Did2, and Vta1 form a network of interconnected regulatory proteins that modulate Vps4 activity, thereby regulating the flow of cargo through the MVB pathway.


Pssm-ID: 460910  Cd Length: 164  Bit Score: 214.63  E-value: 6.75e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3GGZ_D         13 KTCLKMCIQRLRYAQEKQQAIAKQSRRQVAQLLLTNKEQKAHYRVETLIHDDIHIELLEILELYCELLLARVQVINDIST 92
Cdd:pfam03398   1 KTQLKLAIQRLKLLQNKKEALAKQARRDIAQLLENGKEERARIRVEHIIREDNLIEALEILELYCELLLARLGLLEQQKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3GGZ_D         93 eeqlvkehMDDGINEAIRSLIYAILFVDEVKELSQLKDLMAWKINVEFVNGVIADHID-VPEKIIKKCSPSVPKEELVDL 171
Cdd:pfam03398  81 --------CPPGLKEAVSSLIYAAPRCSELPELQQLRDLLAEKYGKEFAKAAVENPDNgVNEKVVEKLSVKPPSKELVDK 152

                         170
                  ....*....|..
3GGZ_D        172 YLKEIAKTYDVP 183
Cdd:pfam03398 153 YLKEIAKEYGVP 164
 
Name Accession Description Interval E-value
Ist1 pfam03398
Regulator of Vps4 activity in the MVB pathway; ESCRT-I, -II, and -III are endosomal sorting ...
 13-183 6.75e-72

Regulator of Vps4 activity in the MVB pathway; ESCRT-I, -II, and -III are endosomal sorting complexes required for transporting proteins and carry out cargo sorting and vesicle formation in the multivesicular bodies, MVBs, pathway. These complexes are transiently recruited from the cytoplasm to the endosomal membrane where they bind transmembrane proteins previously marked for degradation by mono-ubiquitination. Assembly of ESCRT-III, a complex composed of at least four subunits (Vps2, Vps24, Vps20, Snf7), is intimately linked with MVB vesicle formation, its disassembly being an essential step in the MVB vesicle formation, a reaction that is carried out by Vps4, an AAA-type ATPase. The family Ist1 is a regulator of Vps4 activity; by interacting with Did2 and Vps4, Ist1 appears to regulate the recruitment and oligomerization of Vps4. Together Ist1, Did2, and Vta1 form a network of interconnected regulatory proteins that modulate Vps4 activity, thereby regulating the flow of cargo through the MVB pathway.


Pssm-ID: 460910  Cd Length: 164  Bit Score: 214.63  E-value: 6.75e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3GGZ_D         13 KTCLKMCIQRLRYAQEKQQAIAKQSRRQVAQLLLTNKEQKAHYRVETLIHDDIHIELLEILELYCELLLARVQVINDIST 92
Cdd:pfam03398   1 KTQLKLAIQRLKLLQNKKEALAKQARRDIAQLLENGKEERARIRVEHIIREDNLIEALEILELYCELLLARLGLLEQQKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3GGZ_D         93 eeqlvkehMDDGINEAIRSLIYAILFVDEVKELSQLKDLMAWKINVEFVNGVIADHID-VPEKIIKKCSPSVPKEELVDL 171
Cdd:pfam03398  81 --------CPPGLKEAVSSLIYAAPRCSELPELQQLRDLLAEKYGKEFAKAAVENPDNgVNEKVVEKLSVKPPSKELVDK 152

                         170
                  ....*....|..
3GGZ_D        172 YLKEIAKTYDVP 183
Cdd:pfam03398 153 YLKEIAKEYGVP 164
 
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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