NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|157786724|ref|NP_001099326|]
View 

charged multivesicular body protein 6 [Rattus norvegicus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 18-177 7.29e-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: 126.20  E-value: 7.29e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786724   18 RAILQLKQQRDKLRQYQKRVTQQLERERALARQLLRDGRKERAKLLLKKKRYREQLLDRTENQISSLEAMVQSIEFTQIE 97
Cdd:pfam03357   1 EAIRSLRKAIRKLDKKQESLEKKIEKLELEIKKLAKKGNKDAALLLLKQKKRYEKQLDQLDGQLSNLEQQRMAIENAKSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786724   98 MKVMEGLQVGNECLNKMHQVMSIEEVERILDETQEAVEYQRQIDELLAGSF---TQEDEDAILEELNAITQE-----QIE 169
Cdd:pfam03357  81 QEVLNAMKQGAKAMKAMNKLMDIDKIDKLMDEIEDQMEKADEISEMLSDPLddaDEEDEEELDAELDALLDEigdeeSVE 160


                  ....*...
gi 157786724  170 LPEVPSEP 177
Cdd:pfam03357 161 LPSAPSGE 168
 
Name Accession Description Interval E-value
Snf7 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
 18-177 7.29e-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: 126.20  E-value: 7.29e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786724   18 RAILQLKQQRDKLRQYQKRVTQQLERERALARQLLRDGRKERAKLLLKKKRYREQLLDRTENQISSLEAMVQSIEFTQIE 97
Cdd:pfam03357   1 EAIRSLRKAIRKLDKKQESLEKKIEKLELEIKKLAKKGNKDAALLLLKQKKRYEKQLDQLDGQLSNLEQQRMAIENAKSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786724   98 MKVMEGLQVGNECLNKMHQVMSIEEVERILDETQEAVEYQRQIDELLAGSF---TQEDEDAILEELNAITQE-----QIE 169
Cdd:pfam03357  81 QEVLNAMKQGAKAMKAMNKLMDIDKIDKLMDEIEDQMEKADEISEMLSDPLddaDEEDEEELDAELDALLDEigdeeSVE 160


                  ....*...
gi 157786724  170 LPEVPSEP 177
Cdd:pfam03357 161 LPSAPSGE 168
PTZ00446 PTZ00446
vacuolar sorting protein SNF7-like; Provisional
 9-169 7.64e-07

vacuolar sorting protein SNF7-like; Provisional


Pssm-ID: 240422 [Multi-domain]  Cd Length: 191  Bit Score: 47.41  E-value: 7.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786724   9 KQSRVTEQDRAILQLKQQRDKLRQYQKRVTQQLERERALARQLLRDGRKERAKLLLKKKRYREQLLDRTENQISSLEAMV 88
Cdd:PTZ00446  18 KKKNNDEIYKAILKNREAIDALEKKQVQVEKKIKQLEIEAKQKVEQNQMSNAKILLKRKKLYEQEIENILNNRLTLEDNM 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786724  89 QSIEFTQIEMKVMEGLQVGNECLNKMHQVMSIEEVERILDETQEAVEYQRQIDELLAGSFTQE-DEDAILEELNAITQEQ 167
Cdd:PTZ00446  98 INLENMHLHKIAVNALSYAANTHKKLNNEINTQKVEKIIDTIQENKDIQEEINQALSFNLLNNvDDDEIDKELDLLKEQT 177


                 ..
gi 157786724 168 IE 169
Cdd:PTZ00446 178 ME 179
 
Name Accession Description Interval E-value
Snf7 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
 18-177 7.29e-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: 126.20  E-value: 7.29e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786724   18 RAILQLKQQRDKLRQYQKRVTQQLERERALARQLLRDGRKERAKLLLKKKRYREQLLDRTENQISSLEAMVQSIEFTQIE 97
Cdd:pfam03357   1 EAIRSLRKAIRKLDKKQESLEKKIEKLELEIKKLAKKGNKDAALLLLKQKKRYEKQLDQLDGQLSNLEQQRMAIENAKSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786724   98 MKVMEGLQVGNECLNKMHQVMSIEEVERILDETQEAVEYQRQIDELLAGSF---TQEDEDAILEELNAITQE-----QIE 169
Cdd:pfam03357  81 QEVLNAMKQGAKAMKAMNKLMDIDKIDKLMDEIEDQMEKADEISEMLSDPLddaDEEDEEELDAELDALLDEigdeeSVE 160


                  ....*...
gi 157786724  170 LPEVPSEP 177
Cdd:pfam03357 161 LPSAPSGE 168
PTZ00446 PTZ00446
vacuolar sorting protein SNF7-like; Provisional
 9-169 7.64e-07

vacuolar sorting protein SNF7-like; Provisional


Pssm-ID: 240422 [Multi-domain]  Cd Length: 191  Bit Score: 47.41  E-value: 7.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786724   9 KQSRVTEQDRAILQLKQQRDKLRQYQKRVTQQLERERALARQLLRDGRKERAKLLLKKKRYREQLLDRTENQISSLEAMV 88
Cdd:PTZ00446  18 KKKNNDEIYKAILKNREAIDALEKKQVQVEKKIKQLEIEAKQKVEQNQMSNAKILLKRKKLYEQEIENILNNRLTLEDNM 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786724  89 QSIEFTQIEMKVMEGLQVGNECLNKMHQVMSIEEVERILDETQEAVEYQRQIDELLAGSFTQE-DEDAILEELNAITQEQ 167
Cdd:PTZ00446  98 INLENMHLHKIAVNALSYAANTHKKLNNEINTQKVEKIIDTIQENKDIQEEINQALSFNLLNNvDDDEIDKELDLLKEQT 177


                 ..
gi 157786724 168 IE 169
Cdd:PTZ00446 178 ME 179
PTZ00464 PTZ00464
SNF-7-like protein; Provisional
 1-175 8.76e-04

SNF-7-like protein; Provisional


Pssm-ID: 240425 [Multi-domain]  Cd Length: 211  Bit Score: 38.64  E-value: 8.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786724   1 MGNLFGRKKQSRVTEQDRAILQLKQQRD-------KLRQYQKRVTQQLERERALARQLLrdgrKERAKLLLKKKRYREQL 73
Cdd:PTZ00464   1 MNRLFGKKNKTPKPTLEDASKRIGGRSEvvdarinKIDAELMKLKEQIQRTRGMTQSRH----KQRAMQLLQQKRMYQNQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786724  74 LDRTENQ---ISSLEAMVQSIEFTQIEMKVMeglQVGNECLNKMHQVMSIEEVERILDETQEAVEYQRQIDELLAGSFTQ 150
Cdd:PTZ00464  77 QDMMMQQqfnMDQLQFTTESVKDTKVQVDAM---KQAAKTLKKQFKKLNVDKVEDLQDELADLYEDTQEIQEIMGRAYDV 153

                        170       180
                 ....*....|....*....|....*...
gi 157786724 151 E---DEDAILEELNAITQEQIELPEVPS 175
Cdd:PTZ00464 154 PddiDEDEMLGELDALDFDMEKEADASY 181
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH