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Conserved domains on  [gi|530412852|ref|XP_005257725|]
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charged multivesicular body protein 6 isoform X1 [Homo sapiens]

Protein Classification

SNF7 family protein( domain architecture ID 10505749)

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 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
18-177 9.11e-45

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: 147.77  E-value: 9.11e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530412852   18 KAILQLKQQRDKLRQYQKRIAQQLERERALARQLLRDGRKERAKLLLKKKRYQEQLLDRTENQISSLEAMVQSIEFTQIE 97
Cdd:pfam03357   1 EAIRSLRKAIRKLDKKQESLEKKIEKLELEIKKLAKKGNKDAALLLLKQKKRYEKQLDQLDGQLSNLEQQRMAIENAKSN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530412852   98 MKVMEGLQFGNECLNKMHQVMSIEEVERILDETQEAVEYQRQIDELLAGSF---TQEDEDAILEELSAITQE-----QIE 169
Cdd:pfam03357  81 QEVLNAMKQGAKAMKAMNKLMDIDKIDKLMDEIEDQMEKADEISEMLSDPLddaDEEDEEELDAELDALLDEigdeeSVE 160

                  ....*...
gi 530412852  170 LPEVPSEP 177
Cdd:pfam03357 161 LPSAPSGE 168
 
Name Accession Description Interval E-value
Snf7 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
18-177 9.11e-45

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: 147.77  E-value: 9.11e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530412852   18 KAILQLKQQRDKLRQYQKRIAQQLERERALARQLLRDGRKERAKLLLKKKRYQEQLLDRTENQISSLEAMVQSIEFTQIE 97
Cdd:pfam03357   1 EAIRSLRKAIRKLDKKQESLEKKIEKLELEIKKLAKKGNKDAALLLLKQKKRYEKQLDQLDGQLSNLEQQRMAIENAKSN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530412852   98 MKVMEGLQFGNECLNKMHQVMSIEEVERILDETQEAVEYQRQIDELLAGSF---TQEDEDAILEELSAITQE-----QIE 169
Cdd:pfam03357  81 QEVLNAMKQGAKAMKAMNKLMDIDKIDKLMDEIEDQMEKADEISEMLSDPLddaDEEDEEELDAELDALLDEigdeeSVE 160

                  ....*...
gi 530412852  170 LPEVPSEP 177
Cdd:pfam03357 161 LPSAPSGE 168
PTZ00446 PTZ00446
vacuolar sorting protein SNF7-like; Provisional
9-169 4.67e-09

vacuolar sorting protein SNF7-like; Provisional


Pssm-ID: 240422 [Multi-domain]  Cd Length: 191  Bit Score: 54.35  E-value: 4.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530412852   9 KQSRVTEQDKAILQLKQQRDKLRQYQKRIAQQLERERALARQLLRDGRKERAKLLLKKKRYQEQLLDRTENQISSLEAMV 88
Cdd:PTZ00446  18 KKKNNDEIYKAILKNREAIDALEKKQVQVEKKIKQLEIEAKQKVEQNQMSNAKILLKRKKLYEQEIENILNNRLTLEDNM 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530412852  89 QSIEFTQIEMKVMEGLQFGNECLNKMHQVMSIEEVERILDETQEAVEYQRQIDELLAGSFTQE-DEDAILEELSAITQEQ 167
Cdd:PTZ00446  98 INLENMHLHKIAVNALSYAANTHKKLNNEINTQKVEKIIDTIQENKDIQEEINQALSFNLLNNvDDDEIDKELDLLKEQT 177

                 ..
gi 530412852 168 IE 169
Cdd:PTZ00446 178 ME 179
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
13-170 1.18e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530412852  13 VTEQDKAILQLKQQRDKLRQYQKrIAQQLERERALARQLLRDGRKERAKLLLKKKRYQEQLLDRTENQISSLEAMVQSIE 92
Cdd:COG1196  195 LGELERQLEPLERQAEKAERYRE-LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530412852  93 FTQIEMKVmEGLQFGNECLNKMHQVMSIE-----EVERILDETQEAVEYQRQIDELLA-GSFTQEDEDAILEELSAITQE 166
Cdd:COG1196  274 LELEELEL-ELEEAQAEEYELLAELARLEqdiarLEERRRELEERLEELEEELAELEEeLEELEEELEELEEELEEAEEE 352

                 ....
gi 530412852 167 QIEL 170
Cdd:COG1196  353 LEEA 356
 
Name Accession Description Interval E-value
Snf7 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
18-177 9.11e-45

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: 147.77  E-value: 9.11e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530412852   18 KAILQLKQQRDKLRQYQKRIAQQLERERALARQLLRDGRKERAKLLLKKKRYQEQLLDRTENQISSLEAMVQSIEFTQIE 97
Cdd:pfam03357   1 EAIRSLRKAIRKLDKKQESLEKKIEKLELEIKKLAKKGNKDAALLLLKQKKRYEKQLDQLDGQLSNLEQQRMAIENAKSN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530412852   98 MKVMEGLQFGNECLNKMHQVMSIEEVERILDETQEAVEYQRQIDELLAGSF---TQEDEDAILEELSAITQE-----QIE 169
Cdd:pfam03357  81 QEVLNAMKQGAKAMKAMNKLMDIDKIDKLMDEIEDQMEKADEISEMLSDPLddaDEEDEEELDAELDALLDEigdeeSVE 160

                  ....*...
gi 530412852  170 LPEVPSEP 177
Cdd:pfam03357 161 LPSAPSGE 168
PTZ00446 PTZ00446
vacuolar sorting protein SNF7-like; Provisional
9-169 4.67e-09

vacuolar sorting protein SNF7-like; Provisional


Pssm-ID: 240422 [Multi-domain]  Cd Length: 191  Bit Score: 54.35  E-value: 4.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530412852   9 KQSRVTEQDKAILQLKQQRDKLRQYQKRIAQQLERERALARQLLRDGRKERAKLLLKKKRYQEQLLDRTENQISSLEAMV 88
Cdd:PTZ00446  18 KKKNNDEIYKAILKNREAIDALEKKQVQVEKKIKQLEIEAKQKVEQNQMSNAKILLKRKKLYEQEIENILNNRLTLEDNM 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530412852  89 QSIEFTQIEMKVMEGLQFGNECLNKMHQVMSIEEVERILDETQEAVEYQRQIDELLAGSFTQE-DEDAILEELSAITQEQ 167
Cdd:PTZ00446  98 INLENMHLHKIAVNALSYAANTHKKLNNEINTQKVEKIIDTIQENKDIQEEINQALSFNLLNNvDDDEIDKELDLLKEQT 177

                 ..
gi 530412852 168 IE 169
Cdd:PTZ00446 178 ME 179
PTZ00464 PTZ00464
SNF-7-like protein; Provisional
1-175 2.49e-06

SNF-7-like protein; Provisional


Pssm-ID: 240425 [Multi-domain]  Cd Length: 211  Bit Score: 46.73  E-value: 2.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530412852   1 MGNLFGRKKQ--------------SRVTEQDKAILQLKQQRDKLRQyqkriaqQLERERALARQLLrdgrKERAKLLLKK 66
Cdd:PTZ00464   1 MNRLFGKKNKtpkptledaskrigGRSEVVDARINKIDAELMKLKE-------QIQRTRGMTQSRH----KQRAMQLLQQ 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530412852  67 KR-YQEQL--LDRTENQISSLEAMVQSIEFTQIEMKVMeglQFGNECLNKMHQVMSIEEVERILDETQEAVEYQRQIDEL 143
Cdd:PTZ00464  70 KRmYQNQQdmMMQQQFNMDQLQFTTESVKDTKVQVDAM---KQAAKTLKKQFKKLNVDKVEDLQDELADLYEDTQEIQEI 146
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 530412852 144 LAGSFTQE---DEDAILEELSAITQEQIELPEVPS 175
Cdd:PTZ00464 147 MGRAYDVPddiDEDEMLGELDALDFDMEKEADASY 181
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
12-167 4.65e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 41.26  E-value: 4.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530412852    12 RVTEQDKAILQLKQQ-RDKLRQYQKRIaQQLERERALARQLLRDGRKE------------------------RAKLLLKK 66
Cdd:pfam15921  318 QLSDLESTVSQLRSElREAKRMYEDKI-EELEKQLVLANSELTEARTErdqfsqesgnlddqlqklladlhkREKELSLE 396
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530412852    67 KRYQEQLLDRTENQISSLEAMVQSIEFTQIEMKVMEGL--QFGNECLNKMHQVM--------SIEEVERILDETQEAVEY 136
Cdd:pfam15921  397 KEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALlkAMKSECQGQMERQMaaiqgkneSLEKVSSLTAQLESTKEM 476
                          170       180       190
                   ....*....|....*....|....*....|..
gi 530412852   137 QRQ-IDELLAGSFTQEDEDAILEELSAITQEQ 167
Cdd:pfam15921  477 LRKvVEELTAKKMTLESSERTVSDLTASLQEK 508
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
13-170 1.18e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530412852  13 VTEQDKAILQLKQQRDKLRQYQKrIAQQLERERALARQLLRDGRKERAKLLLKKKRYQEQLLDRTENQISSLEAMVQSIE 92
Cdd:COG1196  195 LGELERQLEPLERQAEKAERYRE-LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530412852  93 FTQIEMKVmEGLQFGNECLNKMHQVMSIE-----EVERILDETQEAVEYQRQIDELLA-GSFTQEDEDAILEELSAITQE 166
Cdd:COG1196  274 LELEELEL-ELEEAQAEEYELLAELARLEqdiarLEERRRELEERLEELEEELAELEEeLEELEEELEELEEELEEAEEE 352

                 ....
gi 530412852 167 QIEL 170
Cdd:COG1196  353 LEEA 356
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
11-92 2.24e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.66  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530412852  11 SRVTEQDKAIL-QLKQQRDKLRQYQKRIAQQLERERALARQLlrdgrKERAKLLLKKKRYQEQLLDRTENQISSLEAMVQ 89
Cdd:COG3883  125 SKIADADADLLeELKADKAELEAKKAELEAKLAELEALKAEL-----EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199

                 ...
gi 530412852  90 SIE 92
Cdd:COG3883  200 ELE 202
 
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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