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Conserved domains on  [gi|18414711|ref|NP_568143|]
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SNF7 family protein [Arabidopsis thaliana]

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
PTZ00464 super family cl21588
SNF-7-like protein; Provisional
 1-182 1.06e-68

SNF-7-like protein; Provisional


The actual alignment was detected with superfamily member PTZ00464:

Pssm-ID: 473916 [Multi-domain]  Cd Length: 211  Bit Score: 210.06  E-value: 1.06e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414711    1 MKRIFGAKNnKEPPPSIQDASDRINKRGDSVEEKVKRLDAELCKYKDQIKRTRpGPALEAIKARAMRVLKQKKMYEGQRD 80
Cdd:PTZ00464   1 MNRLFGKKN-KTPKPTLEDASKRIGGRSEVVDARINKIDAELMKLKEQIQRTR-GMTQSRHKQRAMQLLQQKRMYQNQQD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414711   81 MLYNQTFNLDQVSFAAEGLKDAQQTMTALKSANKELKGMMKTVKIQDIDNLQDDMMDLMDESSEIQETLGRSYNVPDDID 160
Cdd:PTZ00464  79 MMMQQQFNMDQLQFTTESVKDTKVQVDAMKQAAKTLKKQFKKLNVDKVEDLQDELADLYEDTQEIQEIMGRAYDVPDDID 158

                        170       180
                 ....*....|....*....|..
gi 18414711  161 EDDLLGELDALEADMGNETEAD 182
Cdd:PTZ00464 159 EDEMLGELDALDFDMEKEADAS 180
 
Name Accession Description Interval E-value
PTZ00464 PTZ00464
SNF-7-like protein; Provisional
 1-182 1.06e-68

SNF-7-like protein; Provisional


Pssm-ID: 240425 [Multi-domain]  Cd Length: 211  Bit Score: 210.06  E-value: 1.06e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414711    1 MKRIFGAKNnKEPPPSIQDASDRINKRGDSVEEKVKRLDAELCKYKDQIKRTRpGPALEAIKARAMRVLKQKKMYEGQRD 80
Cdd:PTZ00464   1 MNRLFGKKN-KTPKPTLEDASKRIGGRSEVVDARINKIDAELMKLKEQIQRTR-GMTQSRHKQRAMQLLQQKRMYQNQQD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414711   81 MLYNQTFNLDQVSFAAEGLKDAQQTMTALKSANKELKGMMKTVKIQDIDNLQDDMMDLMDESSEIQETLGRSYNVPDDID 160
Cdd:PTZ00464  79 MMMQQQFNMDQLQFTTESVKDTKVQVDAMKQAAKTLKKQFKKLNVDKVEDLQDELADLYEDTQEIQEIMGRAYDVPDDID 158

                        170       180
                 ....*....|....*....|..
gi 18414711  161 EDDLLGELDALEADMGNETEAD 182
Cdd:PTZ00464 159 EDEMLGELDALDFDMEKEADAS 180
Snf7 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
 12-186 9.80e-48

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: 155.09  E-value: 9.80e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414711    12 EPPPSIQDASDRINKRGDSVEEKVKRLDAELCKYKDQIKrtrpgpaleaiKARAMRVLKQKKMYEGQRDMLYNQTFNLDQ 91
Cdd:pfam03357   1 EAIRSLRKAIRKLDKKQESLEKKIEKLELEIKKLAKKGN-----------KDAALLLLKQKKRYEKQLDQLDGQLSNLEQ 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414711    92 VSFAAEGLKDAQQTMTALKSANKELKGMMKTVKIQDIDNLQDDMMDLMDESSEIQETLGRSYNVPDDIDEDDLLGELDAL 171
Cdd:pfam03357  70 QRMAIENAKSNQEVLNAMKQGAKAMKAMNKLMDIDKIDKLMDEIEDQMEKADEISEMLSDPLDDADEEDEEELDAELDAL 149

                         170
                  ....*....|....*..
gi 18414711   172 EADMGNET--EADGVPS 186
Cdd:pfam03357 150 LDEIGDEEsvELPSAPS 166
 
Name Accession Description Interval E-value
PTZ00464 PTZ00464
SNF-7-like protein; Provisional
 1-182 1.06e-68

SNF-7-like protein; Provisional


Pssm-ID: 240425 [Multi-domain]  Cd Length: 211  Bit Score: 210.06  E-value: 1.06e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414711    1 MKRIFGAKNnKEPPPSIQDASDRINKRGDSVEEKVKRLDAELCKYKDQIKRTRpGPALEAIKARAMRVLKQKKMYEGQRD 80
Cdd:PTZ00464   1 MNRLFGKKN-KTPKPTLEDASKRIGGRSEVVDARINKIDAELMKLKEQIQRTR-GMTQSRHKQRAMQLLQQKRMYQNQQD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414711   81 MLYNQTFNLDQVSFAAEGLKDAQQTMTALKSANKELKGMMKTVKIQDIDNLQDDMMDLMDESSEIQETLGRSYNVPDDID 160
Cdd:PTZ00464  79 MMMQQQFNMDQLQFTTESVKDTKVQVDAMKQAAKTLKKQFKKLNVDKVEDLQDELADLYEDTQEIQEIMGRAYDVPDDID 158

                        170       180
                 ....*....|....*....|..
gi 18414711  161 EDDLLGELDALEADMGNETEAD 182
Cdd:PTZ00464 159 EDEMLGELDALDFDMEKEADAS 180
Snf7 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
 12-186 9.80e-48

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: 155.09  E-value: 9.80e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414711    12 EPPPSIQDASDRINKRGDSVEEKVKRLDAELCKYKDQIKrtrpgpaleaiKARAMRVLKQKKMYEGQRDMLYNQTFNLDQ 91
Cdd:pfam03357   1 EAIRSLRKAIRKLDKKQESLEKKIEKLELEIKKLAKKGN-----------KDAALLLLKQKKRYEKQLDQLDGQLSNLEQ 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414711    92 VSFAAEGLKDAQQTMTALKSANKELKGMMKTVKIQDIDNLQDDMMDLMDESSEIQETLGRSYNVPDDIDEDDLLGELDAL 171
Cdd:pfam03357  70 QRMAIENAKSNQEVLNAMKQGAKAMKAMNKLMDIDKIDKLMDEIEDQMEKADEISEMLSDPLDDADEEDEEELDAELDAL 149

                         170
                  ....*....|....*..
gi 18414711   172 EADMGNET--EADGVPS 186
Cdd:pfam03357 150 LDEIGDEEsvELPSAPS 166
PTZ00446 PTZ00446
vacuolar sorting protein SNF7-like; Provisional
 8-172 4.58e-05

vacuolar sorting protein SNF7-like; Provisional


Pssm-ID: 240422 [Multi-domain]  Cd Length: 191  Bit Score: 42.79  E-value: 4.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414711    8 KNNKEPPPSI---QDASDRINKRGDSVEEKVKRLDAELckyKDQIKRTRpgpaleaiKARAMRVLKQKKMYEGQRDMLYN 84
Cdd:PTZ00446  20 KNNDEIYKAIlknREAIDALEKKQVQVEKKIKQLEIEA---KQKVEQNQ--------MSNAKILLKRKKLYEQEIENILN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414711   85 QTFNLDQVSFAAEGLKDAQQTMTALKSANKELKGMMKTVKIQDIDNLQDDMMDLMDESSEIQETLgrSYNVPDDIDEDDL 164
Cdd:PTZ00446  89 NRLTLEDNMINLENMHLHKIAVNALSYAANTHKKLNNEINTQKVEKIIDTIQENKDIQEEINQAL--SFNLLNNVDDDEI 166


                 ....*...
gi 18414711  165 LGELDALE 172
Cdd:PTZ00446 167 DKELDLLK 174
 
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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