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Conserved domains on  [gi|28827795|ref|NP_789782|]
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charged multivesicular body protein 4b [Homo sapiens]

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

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 ...
 24-198 1.28e-45

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: 149.31  E-value: 1.28e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827795    24 EAIQRLRDTEEMLSKKQEFLEKKIEQ-ELTAAKKHGTKNKRAALQALKRKKRYEKQLAQIDGTLSTIEFQREALENANTN 102
Cdd:pfam03357   1 EAIRSLRKAIRKLDKKQESLEKKIEKlELEIKKLAKKGNKDAALLLLKQKKRYEKQLDQLDGQLSNLEQQRMAIENAKSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827795   103 TEVLKNMGYAAKAMKAAHDNMDIDKVDELMQDIADQQELAEEISTAISKPVGFGEEFDedelmaelEELEQEELDKNLLE 182
Cdd:pfam03357  81 QEVLNAMKQGAKAMKAMNKLMDIDKIDKLMDEIEDQMEKADEISEMLSDPLDDADEED--------EEELDAELDALLDE 152

                         170
                  ....*....|....*.
gi 28827795   183 ISGPETVPLPNVPSIA 198
Cdd:pfam03357 153 IGDEESVELPSAPSGE 168
 
Name Accession Description Interval E-value
Snf7 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
 24-198 1.28e-45

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: 149.31  E-value: 1.28e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827795    24 EAIQRLRDTEEMLSKKQEFLEKKIEQ-ELTAAKKHGTKNKRAALQALKRKKRYEKQLAQIDGTLSTIEFQREALENANTN 102
Cdd:pfam03357   1 EAIRSLRKAIRKLDKKQESLEKKIEKlELEIKKLAKKGNKDAALLLLKQKKRYEKQLDQLDGQLSNLEQQRMAIENAKSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827795   103 TEVLKNMGYAAKAMKAAHDNMDIDKVDELMQDIADQQELAEEISTAISKPVGFGEEFDedelmaelEELEQEELDKNLLE 182
Cdd:pfam03357  81 QEVLNAMKQGAKAMKAMNKLMDIDKIDKLMDEIEDQMEKADEISEMLSDPLDDADEED--------EEELDAELDALLDE 152

                         170
                  ....*....|....*.
gi 28827795   183 ISGPETVPLPNVPSIA 198
Cdd:pfam03357 153 IGDEESVELPSAPSGE 168
PTZ00464 PTZ00464
SNF-7-like protein; Provisional
 20-213 1.60e-10

SNF-7-like protein; Provisional


Pssm-ID: 240425 [Multi-domain]  Cd Length: 211  Bit Score: 58.67  E-value: 1.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827795   20 PTPQEAIQRLRDTEEMLSKKQefleKKIEQELTAAKKHGTKN--------KRAALQALKRKKRYEKQLAQIDGTLSTIEF 91
Cdd:PTZ00464  14 PTLEDASKRIGGRSEVVDARI----NKIDAELMKLKEQIQRTrgmtqsrhKQRAMQLLQQKRMYQNQQDMMMQQQFNMDQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827795   92 QREALENANTNTEVLKNMGYAAKAMKAAHDNMDIDKVDELMQDIADQQELAEEISTAISKPVGFGEEFDEDELMAELEEL 171
Cdd:PTZ00464  90 LQFTTESVKDTKVQVDAMKQAAKTLKKQFKKLNVDKVEDLQDELADLYEDTQEIQEIMGRAYDVPDDIDEDEMLGELDAL 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 28827795  172 EQEELdknlLEISGPETVPLPNVPSIALPSKPAKKKEEEDDD 213
Cdd:PTZ00464 170 DFDME----KEADASYLADALAVPGTKLPDVPTDEKQQAEGQ 207
 
Name Accession Description Interval E-value
Snf7 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
 24-198 1.28e-45

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: 149.31  E-value: 1.28e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827795    24 EAIQRLRDTEEMLSKKQEFLEKKIEQ-ELTAAKKHGTKNKRAALQALKRKKRYEKQLAQIDGTLSTIEFQREALENANTN 102
Cdd:pfam03357   1 EAIRSLRKAIRKLDKKQESLEKKIEKlELEIKKLAKKGNKDAALLLLKQKKRYEKQLDQLDGQLSNLEQQRMAIENAKSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827795   103 TEVLKNMGYAAKAMKAAHDNMDIDKVDELMQDIADQQELAEEISTAISKPVGFGEEFDedelmaelEELEQEELDKNLLE 182
Cdd:pfam03357  81 QEVLNAMKQGAKAMKAMNKLMDIDKIDKLMDEIEDQMEKADEISEMLSDPLDDADEED--------EEELDAELDALLDE 152

                         170
                  ....*....|....*.
gi 28827795   183 ISGPETVPLPNVPSIA 198
Cdd:pfam03357 153 IGDEESVELPSAPSGE 168
PTZ00464 PTZ00464
SNF-7-like protein; Provisional
 20-213 1.60e-10

SNF-7-like protein; Provisional


Pssm-ID: 240425 [Multi-domain]  Cd Length: 211  Bit Score: 58.67  E-value: 1.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827795   20 PTPQEAIQRLRDTEEMLSKKQefleKKIEQELTAAKKHGTKN--------KRAALQALKRKKRYEKQLAQIDGTLSTIEF 91
Cdd:PTZ00464  14 PTLEDASKRIGGRSEVVDARI----NKIDAELMKLKEQIQRTrgmtqsrhKQRAMQLLQQKRMYQNQQDMMMQQQFNMDQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827795   92 QREALENANTNTEVLKNMGYAAKAMKAAHDNMDIDKVDELMQDIADQQELAEEISTAISKPVGFGEEFDEDELMAELEEL 171
Cdd:PTZ00464  90 LQFTTESVKDTKVQVDAMKQAAKTLKKQFKKLNVDKVEDLQDELADLYEDTQEIQEIMGRAYDVPDDIDEDEMLGELDAL 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 28827795  172 EQEELdknlLEISGPETVPLPNVPSIALPSKPAKKKEEEDDD 213
Cdd:PTZ00464 170 DFDME----KEADASYLADALAVPGTKLPDVPTDEKQQAEGQ 207
PTZ00446 PTZ00446
vacuolar sorting protein SNF7-like; Provisional
 24-150 9.24e-07

vacuolar sorting protein SNF7-like; Provisional


Pssm-ID: 240422 [Multi-domain]  Cd Length: 191  Bit Score: 47.80  E-value: 9.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28827795   24 EAIQRLRDTEEMLSKKQEFLEKKIEQ-ELTAAKKHGTKNKRAALQALKRKKRYEKQLAQIDGTLSTIEFQREALENANTN 102
Cdd:PTZ00446  27 KAILKNREAIDALEKKQVQVEKKIKQlEIEAKQKVEQNQMSNAKILLKRKKLYEQEIENILNNRLTLEDNMINLENMHLH 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 28827795  103 TEVLKNMGYAAKAMKAAHDNMDIDKVDELMQDIADQQELAEEISTAIS 150
Cdd:PTZ00446 107 KIAVNALSYAANTHKKLNNEINTQKVEKIIDTIQENKDIQEEINQALS 154
 
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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