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Conserved domains on  [gi|18848237|gb|AAH24115|]
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CHMP family, member 7 [Mus musculus]

Protein Classification

SNF7 family protein( domain architecture ID 229656)

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 super family cl47805
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
 243-390 2.79e-19

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: 460896 [Multi-domain]  Cd Length: 168  Bit Score: 84.60  E-value: 2.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18848237   243 QLMQSEQLLSRKVESLSQESERCKEEARRACRAGKKQLALRSLKAKQRTEKRIEALHAKLDTVQGILDRIYASQTDQMVF 322
Cdd:pfam03357   5 SLRKAIRKLDKKQESLEKKIEKLELEIKKLAKKGNKDAALLLLKQKKRYEKQLDQLDGQLSNLEQQRMAIENAKSNQEVL 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18848237   323 NAYQAGVGALKLSMKDVTVEKAESLVDQIQELCDTQDEVSQTLAGGVTNGLDFDSEELEKELDILLQD 390
Cdd:pfam03357  85 NAMKQGAKAMKAMNKLMDIDKIDKLMDEIEDQMEKADEISEMLSDPLDDADEEDEEELDAELDALLDE 152
 
Name Accession Description Interval E-value
Snf7 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
 243-390 2.79e-19

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: 84.60  E-value: 2.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18848237   243 QLMQSEQLLSRKVESLSQESERCKEEARRACRAGKKQLALRSLKAKQRTEKRIEALHAKLDTVQGILDRIYASQTDQMVF 322
Cdd:pfam03357   5 SLRKAIRKLDKKQESLEKKIEKLELEIKKLAKKGNKDAALLLLKQKKRYEKQLDQLDGQLSNLEQQRMAIENAKSNQEVL 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18848237   323 NAYQAGVGALKLSMKDVTVEKAESLVDQIQELCDTQDEVSQTLAGGVTNGLDFDSEELEKELDILLQD 390
Cdd:pfam03357  85 NAMKQGAKAMKAMNKLMDIDKIDKLMDEIEDQMEKADEISEMLSDPLDDADEEDEEELDAELDALLDE 152
PTZ00464 PTZ00464
SNF-7-like protein; Provisional
 251-395 1.22e-05

SNF-7-like protein; Provisional


Pssm-ID: 240425 [Multi-domain]  Cd Length: 211  Bit Score: 45.96  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18848237  251 LSRKVESLSQESERCKEEARRACRAGK---KQLALRSLKAKQRTEKRIEALHAKLDTVQGILDRIYASQTDQMVFNAYQA 327
Cdd:PTZ00464  30 VDARINKIDAELMKLKEQIQRTRGMTQsrhKQRAMQLLQQKRMYQNQQDMMMQQQFNMDQLQFTTESVKDTKVQVDAMKQ 109

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18848237  328 GVGALKLSMKDVTVEKAESLVDQIQELCDTQDEVSQTLAGGVTNGLDFDSEELEKELDILLQDTTTEP 395
Cdd:PTZ00464 110 AAKTLKKQFKKLNVDKVEDLQDELADLYEDTQEIQEIMGRAYDVPDDIDEDEMLGELDALDFDMEKEA 177
 
Name Accession Description Interval E-value
Snf7 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
 243-390 2.79e-19

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: 84.60  E-value: 2.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18848237   243 QLMQSEQLLSRKVESLSQESERCKEEARRACRAGKKQLALRSLKAKQRTEKRIEALHAKLDTVQGILDRIYASQTDQMVF 322
Cdd:pfam03357   5 SLRKAIRKLDKKQESLEKKIEKLELEIKKLAKKGNKDAALLLLKQKKRYEKQLDQLDGQLSNLEQQRMAIENAKSNQEVL 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18848237   323 NAYQAGVGALKLSMKDVTVEKAESLVDQIQELCDTQDEVSQTLAGGVTNGLDFDSEELEKELDILLQD 390
Cdd:pfam03357  85 NAMKQGAKAMKAMNKLMDIDKIDKLMDEIEDQMEKADEISEMLSDPLDDADEEDEEELDAELDALLDE 152
PTZ00464 PTZ00464
SNF-7-like protein; Provisional
 251-395 1.22e-05

SNF-7-like protein; Provisional


Pssm-ID: 240425 [Multi-domain]  Cd Length: 211  Bit Score: 45.96  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18848237  251 LSRKVESLSQESERCKEEARRACRAGK---KQLALRSLKAKQRTEKRIEALHAKLDTVQGILDRIYASQTDQMVFNAYQA 327
Cdd:PTZ00464  30 VDARINKIDAELMKLKEQIQRTRGMTQsrhKQRAMQLLQQKRMYQNQQDMMMQQQFNMDQLQFTTESVKDTKVQVDAMKQ 109

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18848237  328 GVGALKLSMKDVTVEKAESLVDQIQELCDTQDEVSQTLAGGVTNGLDFDSEELEKELDILLQDTTTEP 395
Cdd:PTZ00464 110 AAKTLKKQFKKLNVDKVEDLQDELADLYEDTQEIQEIMGRAYDVPDDIDEDEMLGELDALDFDMEKEA 177
PTZ00446 PTZ00446
vacuolar sorting protein SNF7-like; Provisional
 251-396 1.53e-05

vacuolar sorting protein SNF7-like; Provisional


Pssm-ID: 240422 [Multi-domain]  Cd Length: 191  Bit Score: 45.49  E-value: 1.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18848237  251 LSRKVESLSQESERCKEEARRACRAGKKQLALRSLKAKQRTEKRIEALHAKLDTVQGILDRIYASQTDQMVFNAYQAGVG 330
Cdd:PTZ00446  39 LEKKQVQVEKKIKQLEIEAKQKVEQNQMSNAKILLKRKKLYEQEIENILNNRLTLEDNMINLENMHLHKIAVNALSYAAN 118

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18848237  331 ALKLSMKDVTVEKAESLVDQIQELCDTQDEVSQTLAGGVTNGLDFDseELEKELDILLQDTTTEPL 396
Cdd:PTZ00446 119 THKKLNNEINTQKVEKIIDTIQENKDIQEEINQALSFNLLNNVDDD--EIDKELDLLKEQTMEEKL 182
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 243-303 4.53e-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: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 38.51  E-value: 4.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18848237   243 QLMQSEQLLSRKVESLSQESERCKEEARRACRAGKKQLALRSLKAKQRTEKRIEALHAKLD 303
Cdd:pfam04012  47 QTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEELAREALAEKKSLEKQAEALETQLA 107
 
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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