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Conserved domains on  [gi|17506771|ref|NP_490974|]
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Doa4-Independent Degradation, homologous to yeast Did2 [Caenorhabditis elegans]

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 ...
16-181 7.26e-11

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: 58.03  E-value: 7.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506771    16 DLKFAAKQLEKNAQRCEKDEKVEKDKLTAAIKKGNKEVAQVHAENAIRKKNEAVNYIKMAARIDAVAARVQTAATQKRVT 95
Cdd:pfam03357   5 SLRKAIRKLDKKQESLEKKIEKLELEIKKLAKKGNKDAALLLLKQKKRYEKQLDQLDGQLANLEQQRMAIENAKSNQEVL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506771    96 ASMSGVVKAMESAMKSMNLEKVQQLMDRFERDFEDLDVTTKTMEKTMDGTTVLNAPKSQ--VDALIAEAADKagIELNQE 173
Cdd:pfam03357  85 NAMKQGAKAMKAMNKLMDIDKIDDLMDEIEDQMEKADEISEMLSDPLDDADEEDEEELEaeLDALLDEIGDE--ELLPVK 162

                  ....*...
gi 17506771   174 LPsNVPTA 181
Cdd:pfam03357 163 LP-SAPSG 169
 
Name Accession Description Interval E-value
Snf7 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
16-181 7.26e-11

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: 58.03  E-value: 7.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506771    16 DLKFAAKQLEKNAQRCEKDEKVEKDKLTAAIKKGNKEVAQVHAENAIRKKNEAVNYIKMAARIDAVAARVQTAATQKRVT 95
Cdd:pfam03357   5 SLRKAIRKLDKKQESLEKKIEKLELEIKKLAKKGNKDAALLLLKQKKRYEKQLDQLDGQLANLEQQRMAIENAKSNQEVL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506771    96 ASMSGVVKAMESAMKSMNLEKVQQLMDRFERDFEDLDVTTKTMEKTMDGTTVLNAPKSQ--VDALIAEAADKagIELNQE 173
Cdd:pfam03357  85 NAMKQGAKAMKAMNKLMDIDKIDDLMDEIEDQMEKADEISEMLSDPLDDADEEDEEELEaeLDALLDEIGDE--ELLPVK 162

                  ....*...
gi 17506771   174 LPsNVPTA 181
Cdd:pfam03357 163 LP-SAPSG 169
Did4 COG5491
Archaeal division protein CdvB, Snf7/Vps24/ESCRT-III family [Cell cycle control, cell division, ...
21-205 8.88e-11

Archaeal division protein CdvB, Snf7/Vps24/ESCRT-III family [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227778  Cd Length: 204  Bit Score: 58.67  E-value: 8.88e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506771  21 AKQLEKNAQRCEKDEKVEKDKLTAAIKKGNKEvaqvhAENAIRKKNEAVNYIKMAARIDAVAARVQTAATQKRVTASMSG 100
Cdd:COG5491   2 RSSLERQAKKLVRELKQEAKKGQVLLNEIAKK-----APNRRRLAEELYKLRKARSRLDASISRLQSLDTMLFEKVVMRQ 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506771 101 VVKAMESAMKSMN-LEKVQQLMDRFERDFEDLDVTT---KTMEKTMDGTTVLNA--PKSQVDALIAEAADKAGIELNqEL 174
Cdd:COG5491  77 VSGDMAKAAMYMNeLESIRRIMQLFETQFLALELVQlrlETMDELMDVVVGDPVleDLEELDELVNKVLPEIGLELD-ES 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 17506771 175 PSNVPTAL---PTGTQAVSE-------------DKDLTERLAALRNM 205
Cdd:COG5491 156 EQSLPANVvenGSVPAAVSPearkileeaekiaEDRLQERLRELPAL 202
 
Name Accession Description Interval E-value
Snf7 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
16-181 7.26e-11

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: 58.03  E-value: 7.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506771    16 DLKFAAKQLEKNAQRCEKDEKVEKDKLTAAIKKGNKEVAQVHAENAIRKKNEAVNYIKMAARIDAVAARVQTAATQKRVT 95
Cdd:pfam03357   5 SLRKAIRKLDKKQESLEKKIEKLELEIKKLAKKGNKDAALLLLKQKKRYEKQLDQLDGQLANLEQQRMAIENAKSNQEVL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506771    96 ASMSGVVKAMESAMKSMNLEKVQQLMDRFERDFEDLDVTTKTMEKTMDGTTVLNAPKSQ--VDALIAEAADKagIELNQE 173
Cdd:pfam03357  85 NAMKQGAKAMKAMNKLMDIDKIDDLMDEIEDQMEKADEISEMLSDPLDDADEEDEEELEaeLDALLDEIGDE--ELLPVK 162

                  ....*...
gi 17506771   174 LPsNVPTA 181
Cdd:pfam03357 163 LP-SAPSG 169
Did4 COG5491
Archaeal division protein CdvB, Snf7/Vps24/ESCRT-III family [Cell cycle control, cell division, ...
21-205 8.88e-11

Archaeal division protein CdvB, Snf7/Vps24/ESCRT-III family [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227778  Cd Length: 204  Bit Score: 58.67  E-value: 8.88e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506771  21 AKQLEKNAQRCEKDEKVEKDKLTAAIKKGNKEvaqvhAENAIRKKNEAVNYIKMAARIDAVAARVQTAATQKRVTASMSG 100
Cdd:COG5491   2 RSSLERQAKKLVRELKQEAKKGQVLLNEIAKK-----APNRRRLAEELYKLRKARSRLDASISRLQSLDTMLFEKVVMRQ 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506771 101 VVKAMESAMKSMN-LEKVQQLMDRFERDFEDLDVTT---KTMEKTMDGTTVLNA--PKSQVDALIAEAADKAGIELNqEL 174
Cdd:COG5491  77 VSGDMAKAAMYMNeLESIRRIMQLFETQFLALELVQlrlETMDELMDVVVGDPVleDLEELDELVNKVLPEIGLELD-ES 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 17506771 175 PSNVPTAL---PTGTQAVSE-------------DKDLTERLAALRNM 205
Cdd:COG5491 156 EQSLPANVvenGSVPAAVSPearkileeaekiaEDRLQERLRELPAL 202
 
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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