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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366641   19 ESNQSMNQAQQSLSNRISQLDTQIAQLNFQLqniqKNLQRSNNKQpslrkQALKILNKRKQLENMKDSLDSQSWSMTQAQ 98
Cdd:pfam03357   1 EAIRSLRKAIRKLDKKQESLEKKIEKLELEI----KKLAKKGNKD-----AALLLLKQKKRYEKQLDQLDGQLSNLEQQR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366641   99 LTNDNLQNTMITINALKQTNNAMKAQYGKINIDKLQDMQDEMLDLIEQGDELQEVLAMNNNSGelDDISDAELDAELDAL 178
Cdd:pfam03357  72 MAIENAKSNQEVLNAMKQGAKAMKAMNKLMDIDKIDKLMDEIEDQMEKADEISEMLSDPLDDA--DEEDEEELDAELDAL 149

                  ...
gi 398366641  179 AQE 181
Cdd:pfam03357 150 LDE 152

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366641   19 ESNQSMNQAQQSLSNRISQLDTQIAQLNFQLqniqKNLQRSNNKQpslrkQALKILNKRKQLENMKDSLDSQSWSMTQAQ 98
Cdd:pfam03357   1 EAIRSLRKAIRKLDKKQESLEKKIEKLELEI----KKLAKKGNKD-----AALLLLKQKKRYEKQLDQLDGQLSNLEQQR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366641   99 LTNDNLQNTMITINALKQTNNAMKAQYGKINIDKLQDMQDEMLDLIEQGDELQEVLAMNNNSGelDDISDAELDAELDAL 178
Cdd:pfam03357  72 MAIENAKSNQEVLNAMKQGAKAMKAMNKLMDIDKIDKLMDEIEDQMEKADEISEMLSDPLDDA--DEEDEEELDAELDAL 149

                  ...
gi 398366641  179 AQE 181
Cdd:pfam03357 150 LDE 152

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of uncharacterized proteins from bacteria and archaea; This family corresponds to a group of uncharacterized hypothetical proteins from bacteria and archaea, showing a high sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, members in this family consist of a single MazG-like domain that contains a well conserved divalent ion-binding motif EXX[E/D].

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 398366641 129 NIDKLQDMQDEMLDLIEQGDELQEVLAMNNNSGELDDISD 168
Cdd:cd11540   14 NLDEGADPRKQLLKLVEEVGELSEAIAKNKQEEIKDSIGD 53

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366641   19 ESNQSMNQAQQSLSNRISQLDTQIAQLNFQLqniqKNLQRSNNKQpslrkQALKILNKRKQLENMKDSLDSQSWSMTQAQ 98
Cdd:pfam03357   1 EAIRSLRKAIRKLDKKQESLEKKIEKLELEI----KKLAKKGNKD-----AALLLLKQKKRYEKQLDQLDGQLSNLEQQR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366641   99 LTNDNLQNTMITINALKQTNNAMKAQYGKINIDKLQDMQDEMLDLIEQGDELQEVLAMNNNSGelDDISDAELDAELDAL 178
Cdd:pfam03357  72 MAIENAKSNQEVLNAMKQGAKAMKAMNKLMDIDKIDKLMDEIEDQMEKADEISEMLSDPLDDA--DEEDEEELDAELDAL 149

                  ...
gi 398366641  179 AQE 181
Cdd:pfam03357 150 LDE 152

YlqD protein; The structure of a representative of this family has been solved (pdb:4dci) and found to form a tetrameric structure of prefoldin-like architecture with the beta-barrel core and helical coiled coil tentacles. This suggests that this family may act as molecular chaperones.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366641   26 QAQQSLSNRISQLDTQIAQLNFQLQNIQKNLQRSNNKQPSLRKQALKilNKRKQLENMKDSLDSQ 90
Cdd:pfam11068  20 ELQQQLQAQIQQLDRELQQLEFQGKRAIAEIKKQSIQQIENLQQQFE--QEKSERLEQKNQLLQQ 82

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of uncharacterized proteins from bacteria and archaea; This family corresponds to a group of uncharacterized hypothetical proteins from bacteria and archaea, showing a high sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, members in this family consist of a single MazG-like domain that contains a well conserved divalent ion-binding motif EXX[E/D].

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 398366641 129 NIDKLQDMQDEMLDLIEQGDELQEVLAMNNNSGELDDISD 168
Cdd:cd11540   14 NLDEGADPRKQLLKLVEEVGELSEAIAKNKQEEIKDSIGD 53