NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|306966146|ref|NP_001182465|]
View 

charged multivesicular body protein 5 isoform 2 [Homo sapiens]

Protein Classification

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 super family cl21588
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
1-165 3.47e-64

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.


The actual alignment was detected with superfamily member PTZ00464:

Pssm-ID: 328813  Cd Length: 211  Bit Score: 195.81  E-value: 3.47e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306966146   1 MNRLFGKAKpKAPPPSLTDCIGTVDSRAESIDKKISRLDAELVKYKDQIKKMReGPAKNMVKQKALRVLKQKRMYEQQRD 80
Cdd:PTZ00464   1 MNRLFGKKN-KTPKPTLEDASKRIGGRSEVVDARINKIDAELMKLKEQIQRTR-GMTQSRHKQRAMQLLQQKRMYQNQQD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306966146  81 NLAQQSFNMEQANYTIQSLKDTKTTVDAMKLGVKEMKKAYKQVKIDQIEDLQDQLEDMMEDANEIQEALSRSYGTPE-LD 159
Cdd:PTZ00464  79 MMMQQQFNMDQLQFTTESVKDTKVQVDAMKQAAKTLKKQFKKLNVDKVEDLQDELADLYEDTQEIQEIMGRAYDVPDdID 158

                 ....*.
gi 306966146 160 EDDLEA 165
Cdd:PTZ00464 159 EDEMLG 164
 
Name Accession Description Interval E-value
PTZ00464 PTZ00464
SNF-7-like protein; Provisional
1-165 3.47e-64

SNF-7-like protein; Provisional


Pssm-ID: 240425  Cd Length: 211  Bit Score: 195.81  E-value: 3.47e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306966146   1 MNRLFGKAKpKAPPPSLTDCIGTVDSRAESIDKKISRLDAELVKYKDQIKKMReGPAKNMVKQKALRVLKQKRMYEQQRD 80
Cdd:PTZ00464   1 MNRLFGKKN-KTPKPTLEDASKRIGGRSEVVDARINKIDAELMKLKEQIQRTR-GMTQSRHKQRAMQLLQQKRMYQNQQD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306966146  81 NLAQQSFNMEQANYTIQSLKDTKTTVDAMKLGVKEMKKAYKQVKIDQIEDLQDQLEDMMEDANEIQEALSRSYGTPE-LD 159
Cdd:PTZ00464  79 MMMQQQFNMDQLQFTTESVKDTKVQVDAMKQAAKTLKKQFKKLNVDKVEDLQDELADLYEDTQEIQEIMGRAYDVPDdID 158

                 ....*.
gi 306966146 160 EDDLEA 165
Cdd:PTZ00464 159 EDEMLG 164
Snf7 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
13-165 1.30e-38

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: 308778  Cd Length: 170  Bit Score: 129.29  E-value: 1.30e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306966146   13 PPPSLTDCIGTVDSRAESIDKKISRLDAELVKYKDQIKKMRegpaknmvkqkALRVLKQKRMYEQQRDNLAQQSFNMEQA 92
Cdd:pfam03357   2 AILSLRKAIRKLDKKQESLEKKIEKLELEIKKLAKKGNKDA-----------ALLLLKQKKRYEKQLDQLDGQLANLEQQ 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 306966146   93 NYTIQSLKDTKTTVDAMKLGVKEMKKAYKQVKIDQIEDLQDQLEDMMEDANEIQEALSRSYGT-PELDEDDLEA 165
Cdd:pfam03357  71 RMAIENAKSNQEVLNAMKQGAKAMKAMNKLMDIDKIDDLMDEIEDQMEKADEISEMLSDPLDDaDEEDEEELEA 144
 
Name Accession Description Interval E-value
PTZ00464 PTZ00464
SNF-7-like protein; Provisional
1-165 3.47e-64

SNF-7-like protein; Provisional


Pssm-ID: 240425  Cd Length: 211  Bit Score: 195.81  E-value: 3.47e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306966146   1 MNRLFGKAKpKAPPPSLTDCIGTVDSRAESIDKKISRLDAELVKYKDQIKKMReGPAKNMVKQKALRVLKQKRMYEQQRD 80
Cdd:PTZ00464   1 MNRLFGKKN-KTPKPTLEDASKRIGGRSEVVDARINKIDAELMKLKEQIQRTR-GMTQSRHKQRAMQLLQQKRMYQNQQD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306966146  81 NLAQQSFNMEQANYTIQSLKDTKTTVDAMKLGVKEMKKAYKQVKIDQIEDLQDQLEDMMEDANEIQEALSRSYGTPE-LD 159
Cdd:PTZ00464  79 MMMQQQFNMDQLQFTTESVKDTKVQVDAMKQAAKTLKKQFKKLNVDKVEDLQDELADLYEDTQEIQEIMGRAYDVPDdID 158

                 ....*.
gi 306966146 160 EDDLEA 165
Cdd:PTZ00464 159 EDEMLG 164
Snf7 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
13-165 1.30e-38

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: 308778  Cd Length: 170  Bit Score: 129.29  E-value: 1.30e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306966146   13 PPPSLTDCIGTVDSRAESIDKKISRLDAELVKYKDQIKKMRegpaknmvkqkALRVLKQKRMYEQQRDNLAQQSFNMEQA 92
Cdd:pfam03357   2 AILSLRKAIRKLDKKQESLEKKIEKLELEIKKLAKKGNKDA-----------ALLLLKQKKRYEKQLDQLDGQLANLEQQ 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 306966146   93 NYTIQSLKDTKTTVDAMKLGVKEMKKAYKQVKIDQIEDLQDQLEDMMEDANEIQEALSRSYGT-PELDEDDLEA 165
Cdd:pfam03357  71 RMAIENAKSNQEVLNAMKQGAKAMKAMNKLMDIDKIDDLMDEIEDQMEKADEISEMLSDPLDDaDEEDEEELEA 144
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
25-164 2.71e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 311715 [Multi-domain]  Cd Length: 545  Bit Score: 37.14  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306966146   25 DSRAESIDKKISRLDAELVKYKDQIKKMregpaknMVKQKALRVL-----KQKRMYEQQRDNLAQQSFNMEQANYTI-QS 98
Cdd:pfam07888 181 ERQRKELESRISELKEELRHSREKHEEL-------EEKQKEEQDLseeltQEKDALLEQRAEHEARIRELEEDIKTLtQR 253
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 306966146   99 LKDTKTTVDAMKLGVKEMKKAYKQVKIDQiEDLQDQLEDMMEDANEIQEALSRSYGTPELDEDDLE 164
Cdd:pfam07888 254 VLERETELERMKERVKKAGAQRKEEEAER-EQLQAENEALLEELRSLQERLNASERKVEGLGEELS 318
PTZ00446 PTZ00446
vacuolar sorting protein SNF7-like; Provisional
35-150 8.21e-03

vacuolar sorting protein SNF7-like; Provisional


Pssm-ID: 240422  Cd Length: 191  Bit Score: 35.09  E-value: 8.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306966146  35 ISRLDAELVKYKDQIKKMrEGPAKNMVKQKALR----VLKQKRMYEQQRDNLAQQSFNMEQANYTIQSLKDTKTTVDAMK 110
Cdd:PTZ00446  36 IDALEKKQVQVEKKIKQL-EIEAKQKVEQNQMSnakiLLKRKKLYEQEIENILNNRLTLEDNMINLENMHLHKIAVNALS 114
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 306966146 111 LGVKEMKKAYKQVKIDQIEDLQDQLEDMMEDANEIQEALS 150
Cdd:PTZ00446 115 YAANTHKKLNNEINTQKVEKIIDTIQENKDIQEEINQALS 154
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH