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Conserved domains on  [gi|62955661|ref|NP_001017844|]
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charged multivesicular body protein 4c [Danio rerio]

Protein Classification

Snf7 family protein( domain architecture ID 10505749)

Snf7 family protein may be involved in protein sorting and transport from the endosome to the vacuole/lysosome

Gene Ontology:  GO:0007034
PubMed:  32875105

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Snf7 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
 42-173 1.35e-37

Snf7; This family of proteins are involved in protein sorting and transport from the endosome to the vacuole/lysosome in eukaryotic cells. Vacuoles/lysosomes play an important role in the degradation of both lipids and cellular proteins. In order to perform this degradative function, vacuoles/lysosomes contain numerous hydrolases which have been transported in the form of inactive precursors via the biosynthetic pathway and are proteolytically activated upon delivery to the vacuole/lysosome. The delivery of transmembrane proteins, such as activated cell surface receptors to the lumen of the vacuole/lysosome, either for degradation/downregulation, or in the case of hydrolases, for proper localization, requires the formation of multivesicular bodies (MVBs). These late endosomal structures are formed by invaginating and budding of the limiting membrane into the lumen of the compartment. During this process, a subset of the endosomal membrane proteins is sorted into the forming vesicles. Mature MVBs fuse with the vacuole/lysosome, thereby releasing cargo containing vesicles into its hydrolytic lumen for degradation. Endosomal proteins that are not sorted into the intralumenal MVB vesicles are either recycled back to the plasma membrane or Golgi complex, or remain in the limiting membrane of the MVB and are thereby transported to the limiting membrane of the vacuole/lysosome as a consequence of fusion. Therefore, the MVB sorting pathway plays a critical role in the decision between recycling and degradation of membrane proteins. A few archaeal sequences are also present within this family.


:

Pssm-ID: 460896 [Multi-domain]  Cd Length: 168  Bit Score: 129.28  E-value: 1.35e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955661    42 EAINRLRETEAMLTKKQEYLESRIEQEIV-IAKKNGTKNKRAALQALKRKKRFEQQLTQIDGTLSTIEFQRESLENATTN 120
Cdd:pfam03357   1 EAIRSLRKAIRKLDKKQESLEKKIEKLELeIKKLAKKGNKDAALLLLKQKKRYEKQLDQLDGQLSNLEQQRMAIENAKSN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 62955661   121 TEVLKNMGYAAKAIKGVHEKIDLDKIDSLMQDITEQQEVAQEISDAISKPFGD 173
Cdd:pfam03357  81 QEVLNAMKQGAKAMKAMNKLMDIDKIDKLMDEIEDQMEKADEISEMLSDPLDD 133
 
Name Accession Description Interval E-value
Snf7 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
 42-173 1.35e-37

Snf7; This family of proteins are involved in protein sorting and transport from the endosome to the vacuole/lysosome in eukaryotic cells. Vacuoles/lysosomes play an important role in the degradation of both lipids and cellular proteins. In order to perform this degradative function, vacuoles/lysosomes contain numerous hydrolases which have been transported in the form of inactive precursors via the biosynthetic pathway and are proteolytically activated upon delivery to the vacuole/lysosome. The delivery of transmembrane proteins, such as activated cell surface receptors to the lumen of the vacuole/lysosome, either for degradation/downregulation, or in the case of hydrolases, for proper localization, requires the formation of multivesicular bodies (MVBs). These late endosomal structures are formed by invaginating and budding of the limiting membrane into the lumen of the compartment. During this process, a subset of the endosomal membrane proteins is sorted into the forming vesicles. Mature MVBs fuse with the vacuole/lysosome, thereby releasing cargo containing vesicles into its hydrolytic lumen for degradation. Endosomal proteins that are not sorted into the intralumenal MVB vesicles are either recycled back to the plasma membrane or Golgi complex, or remain in the limiting membrane of the MVB and are thereby transported to the limiting membrane of the vacuole/lysosome as a consequence of fusion. Therefore, the MVB sorting pathway plays a critical role in the decision between recycling and degradation of membrane proteins. A few archaeal sequences are also present within this family.


Pssm-ID: 460896 [Multi-domain]  Cd Length: 168  Bit Score: 129.28  E-value: 1.35e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955661    42 EAINRLRETEAMLTKKQEYLESRIEQEIV-IAKKNGTKNKRAALQALKRKKRFEQQLTQIDGTLSTIEFQRESLENATTN 120
Cdd:pfam03357   1 EAIRSLRKAIRKLDKKQESLEKKIEKLELeIKKLAKKGNKDAALLLLKQKKRYEKQLDQLDGQLSNLEQQRMAIENAKSN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 62955661   121 TEVLKNMGYAAKAIKGVHEKIDLDKIDSLMQDITEQQEVAQEISDAISKPFGD 173
Cdd:pfam03357  81 QEVLNAMKQGAKAMKAMNKLMDIDKIDKLMDEIEDQMEKADEISEMLSDPLDD 133
PTZ00446 PTZ00446
vacuolar sorting protein SNF7-like; Provisional
 42-168 2.73e-06

vacuolar sorting protein SNF7-like; Provisional


Pssm-ID: 240422 [Multi-domain]  Cd Length: 191  Bit Score: 46.64  E-value: 2.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955661   42 EAINRLRETEAMLTKKQEYLESRIEQEIVIAKKNGTKNKRAALQAL-KRKKRFEQQLTQIDGTLSTIEFQRESLENATTN 120
Cdd:PTZ00446  27 KAILKNREAIDALEKKQVQVEKKIKQLEIEAKQKVEQNQMSNAKILlKRKKLYEQEIENILNNRLTLEDNMINLENMHLH 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 62955661  121 TEVLKNMGYAAKAIKGVHEKIDLDKIDSLMQDITEQQEVAQEISDAIS 168
Cdd:PTZ00446 107 KIAVNALSYAANTHKKLNNEINTQKVEKIIDTIQENKDIQEEINQALS 154
 
Name Accession Description Interval E-value
Snf7 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
 42-173 1.35e-37

Snf7; This family of proteins are involved in protein sorting and transport from the endosome to the vacuole/lysosome in eukaryotic cells. Vacuoles/lysosomes play an important role in the degradation of both lipids and cellular proteins. In order to perform this degradative function, vacuoles/lysosomes contain numerous hydrolases which have been transported in the form of inactive precursors via the biosynthetic pathway and are proteolytically activated upon delivery to the vacuole/lysosome. The delivery of transmembrane proteins, such as activated cell surface receptors to the lumen of the vacuole/lysosome, either for degradation/downregulation, or in the case of hydrolases, for proper localization, requires the formation of multivesicular bodies (MVBs). These late endosomal structures are formed by invaginating and budding of the limiting membrane into the lumen of the compartment. During this process, a subset of the endosomal membrane proteins is sorted into the forming vesicles. Mature MVBs fuse with the vacuole/lysosome, thereby releasing cargo containing vesicles into its hydrolytic lumen for degradation. Endosomal proteins that are not sorted into the intralumenal MVB vesicles are either recycled back to the plasma membrane or Golgi complex, or remain in the limiting membrane of the MVB and are thereby transported to the limiting membrane of the vacuole/lysosome as a consequence of fusion. Therefore, the MVB sorting pathway plays a critical role in the decision between recycling and degradation of membrane proteins. A few archaeal sequences are also present within this family.


Pssm-ID: 460896 [Multi-domain]  Cd Length: 168  Bit Score: 129.28  E-value: 1.35e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955661    42 EAINRLRETEAMLTKKQEYLESRIEQEIV-IAKKNGTKNKRAALQALKRKKRFEQQLTQIDGTLSTIEFQRESLENATTN 120
Cdd:pfam03357   1 EAIRSLRKAIRKLDKKQESLEKKIEKLELeIKKLAKKGNKDAALLLLKQKKRYEKQLDQLDGQLSNLEQQRMAIENAKSN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 62955661   121 TEVLKNMGYAAKAIKGVHEKIDLDKIDSLMQDITEQQEVAQEISDAISKPFGD 173
Cdd:pfam03357  81 QEVLNAMKQGAKAMKAMNKLMDIDKIDKLMDEIEDQMEKADEISEMLSDPLDD 133
PTZ00446 PTZ00446
vacuolar sorting protein SNF7-like; Provisional
 42-168 2.73e-06

vacuolar sorting protein SNF7-like; Provisional


Pssm-ID: 240422 [Multi-domain]  Cd Length: 191  Bit Score: 46.64  E-value: 2.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955661   42 EAINRLRETEAMLTKKQEYLESRIEQEIVIAKKNGTKNKRAALQAL-KRKKRFEQQLTQIDGTLSTIEFQRESLENATTN 120
Cdd:PTZ00446  27 KAILKNREAIDALEKKQVQVEKKIKQLEIEAKQKVEQNQMSNAKILlKRKKLYEQEIENILNNRLTLEDNMINLENMHLH 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 62955661  121 TEVLKNMGYAAKAIKGVHEKIDLDKIDSLMQDITEQQEVAQEISDAIS 168
Cdd:PTZ00446 107 KIAVNALSYAANTHKKLNNEINTQKVEKIIDTIQENKDIQEEINQALS 154
PTZ00464 PTZ00464
SNF-7-like protein; Provisional
 80-211 8.40e-05

SNF-7-like protein; Provisional


Pssm-ID: 240425 [Multi-domain]  Cd Length: 211  Bit Score: 42.50  E-value: 8.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955661   80 KRAALQALKRKKRFEQQLTQIDGTLSTIEFQRESLENATTNTEVLKNMGYAAKAIKGVHEKIDLDKIDSLMQDITEQQEV 159
Cdd:PTZ00464  60 KQRAMQLLQQKRMYQNQQDMMMQQQFNMDQLQFTTESVKDTKVQVDAMKQAAKTLKKQFKKLNVDKVEDLQDELADLYED 139

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 62955661  160 AQEISDAISKPFG---DQFDEDELLAELAELEQEDLEESMKSMGRLPSAPTHKLP 211
Cdd:PTZ00464 140 TQEIQEIMGRAYDvpdDIDEDEMLGELDALDFDMEKEADASYLADALAVPGTKLP 194
 
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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