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Conserved domains on  [gi|961513275|ref|NP_001304828|]
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charged multivesicular body protein 7 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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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 ...
133-292 3.22e-20

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 pfam03357:

Pssm-ID: 328813  Cd Length: 170  Bit Score: 86.15  E-value: 3.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961513275  133 QLMQSEQLLSRKVESLSQEAERCKEEARRACRAGKKQLALRSLKAKQRTEKRIEALHAKLDTVQGILDRIYASQTDQMVF 212
Cdd:pfam03357   5 SLRKAIRKLDKKQESLEKKIEKLELEIKKLAKKGNKDAALLLLKQKKRYEKQLDQLDGQLANLEQQRMAIENAKSNQEVL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961513275  213 NAYQAGVGALKLSMKDVTVEKAESLVDQIQELCDTQDEVSQTLAGGVTNGLDFDSEELEKELDILLQDTTKE---PLDLP 289
Cdd:pfam03357  85 NAMKQGAKAMKAMNKLMDIDKIDDLMDEIEDQMEKADEISEMLSDPLDDADEEDEEELEAELDALLDEIGDEellPVKLP 164

                  ...
gi 961513275  290 DNP 292
Cdd:pfam03357 165 SAP 167
 
Name Accession Description Interval E-value
Snf7 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
133-292 3.22e-20

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: 86.15  E-value: 3.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961513275  133 QLMQSEQLLSRKVESLSQEAERCKEEARRACRAGKKQLALRSLKAKQRTEKRIEALHAKLDTVQGILDRIYASQTDQMVF 212
Cdd:pfam03357   5 SLRKAIRKLDKKQESLEKKIEKLELEIKKLAKKGNKDAALLLLKQKKRYEKQLDQLDGQLANLEQQRMAIENAKSNQEVL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961513275  213 NAYQAGVGALKLSMKDVTVEKAESLVDQIQELCDTQDEVSQTLAGGVTNGLDFDSEELEKELDILLQDTTKE---PLDLP 289
Cdd:pfam03357  85 NAMKQGAKAMKAMNKLMDIDKIDDLMDEIEDQMEKADEISEMLSDPLDDADEEDEEELEAELDALLDEIGDEellPVKLP 164

                  ...
gi 961513275  290 DNP 292
Cdd:pfam03357 165 SAP 167
PTZ00464 PTZ00464
SNF-7-like protein; Provisional
141-285 2.24e-06

SNF-7-like protein; Provisional


Pssm-ID: 240425  Cd Length: 211  Bit Score: 47.50  E-value: 2.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961513275 141 LSRKVESLSQEAERCKEEARRACRAGK---KQLALRSLKAKQRTEKRIEALHAKLDTVQGILDRIYASQTDQMVFNAYQA 217
Cdd:PTZ00464  30 VDARINKIDAELMKLKEQIQRTRGMTQsrhKQRAMQLLQQKRMYQNQQDMMMQQQFNMDQLQFTTESVKDTKVQVDAMKQ 109
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961513275 218 GVGALKLSMKDVTVEKAESLVDQIQELCDTQDEVSQTLAGGVTNGLDFDSEELEKELDILLQDTTKEP 285
Cdd:PTZ00464 110 AAKTLKKQFKKLNVDKVEDLQDELADLYEDTQEIQEIMGRAYDVPDDIDEDEMLGELDALDFDMEKEA 177
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
133-202 2.18e-04

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 224755 [Multi-domain]  Cd Length: 225  Bit Score: 41.92  E-value: 2.18e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961513275 133 QLMQSEQLLSRKVESLSQEAERCKEEARRACRAGKKQLALRSLKAKQRTEKRIEALHAKLDTVQGILDRI 202
Cdd:COG1842   49 QAIARQKQLERKLEEAQARAEKLEEKAELALQAGNEDLAREALEEKQSLEDLAKALEAELQQAEEQVEKL 118
 
Name Accession Description Interval E-value
Snf7 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
133-292 3.22e-20

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: 86.15  E-value: 3.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961513275  133 QLMQSEQLLSRKVESLSQEAERCKEEARRACRAGKKQLALRSLKAKQRTEKRIEALHAKLDTVQGILDRIYASQTDQMVF 212
Cdd:pfam03357   5 SLRKAIRKLDKKQESLEKKIEKLELEIKKLAKKGNKDAALLLLKQKKRYEKQLDQLDGQLANLEQQRMAIENAKSNQEVL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961513275  213 NAYQAGVGALKLSMKDVTVEKAESLVDQIQELCDTQDEVSQTLAGGVTNGLDFDSEELEKELDILLQDTTKE---PLDLP 289
Cdd:pfam03357  85 NAMKQGAKAMKAMNKLMDIDKIDDLMDEIEDQMEKADEISEMLSDPLDDADEEDEEELEAELDALLDEIGDEellPVKLP 164

                  ...
gi 961513275  290 DNP 292
Cdd:pfam03357 165 SAP 167
PTZ00464 PTZ00464
SNF-7-like protein; Provisional
141-285 2.24e-06

SNF-7-like protein; Provisional


Pssm-ID: 240425  Cd Length: 211  Bit Score: 47.50  E-value: 2.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961513275 141 LSRKVESLSQEAERCKEEARRACRAGK---KQLALRSLKAKQRTEKRIEALHAKLDTVQGILDRIYASQTDQMVFNAYQA 217
Cdd:PTZ00464  30 VDARINKIDAELMKLKEQIQRTRGMTQsrhKQRAMQLLQQKRMYQNQQDMMMQQQFNMDQLQFTTESVKDTKVQVDAMKQ 109
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961513275 218 GVGALKLSMKDVTVEKAESLVDQIQELCDTQDEVSQTLAGGVTNGLDFDSEELEKELDILLQDTTKEP 285
Cdd:PTZ00464 110 AAKTLKKQFKKLNVDKVEDLQDELADLYEDTQEIQEIMGRAYDVPDDIDEDEMLGELDALDFDMEKEA 177
PTZ00446 PTZ00446
vacuolar sorting protein SNF7-like; Provisional
141-286 2.21e-05

vacuolar sorting protein SNF7-like; Provisional


Pssm-ID: 240422  Cd Length: 191  Bit Score: 44.33  E-value: 2.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961513275 141 LSRKVESLSQEAERCKEEARRACRAGKKQLALRSLKAKQRTEKRIEALHAKLDTVQGILDRIYASQTDQMVFNAYQAGVG 220
Cdd:PTZ00446  39 LEKKQVQVEKKIKQLEIEAKQKVEQNQMSNAKILLKRKKLYEQEIENILNNRLTLEDNMINLENMHLHKIAVNALSYAAN 118
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 961513275 221 ALKLSMKDVTVEKAESLVDQIQELCDTQDEVSQTLAGGVTNGLDFDseELEKELDILLQDTTKEPL 286
Cdd:PTZ00446 119 THKKLNNEINTQKVEKIIDTIQENKDIQEEINQALSFNLLNNVDDD--EIDKELDLLKEQTMEEKL 182
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
133-202 2.18e-04

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 224755 [Multi-domain]  Cd Length: 225  Bit Score: 41.92  E-value: 2.18e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961513275 133 QLMQSEQLLSRKVESLSQEAERCKEEARRACRAGKKQLALRSLKAKQRTEKRIEALHAKLDTVQGILDRI 202
Cdd:COG1842   49 QAIARQKQLERKLEEAQARAEKLEEKAELALQAGNEDLAREALEEKQSLEDLAKALEAELQQAEEQVEKL 118
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
133-193 1.75e-03

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 281941 [Multi-domain]  Cd Length: 218  Bit Score: 38.90  E-value: 1.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961513275  133 QLMQSEQLLSRKVESLSQEAERCKEEARRACRAGKKQLALRSLKAKQRTEKRIEALHAKLD 193
Cdd:pfam04012  48 QVIARQKQLERKLEEQKEQAKKLENKARAALTKGNEELAREALAEIATLEKLAEALETQLT 108
 
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.
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