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Conserved domains on  [gi|23480358|gb|EAA16939|]
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Drosophila melanogaster CG14542 gene product, putative [Plasmodium yoelii yoelii]

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 ...
15-183 4.73e-14

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: 67.66  E-value: 4.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23480358    15 EEKRNLNRSIRELEREIVKLENEKKQIEKNIKLYAKKNDITLVRTLAKDFVKVKQTVTKYSKIKSHLFSMKIKLQSVKSS 94
Cdd:pfam03357   1 EAILSLRKAIRKLDKKQESLEKKIEKLELEIKKLAKKGNKDAALLLLKQKKRYEKQLDQLDGQLANLEQQRMAIENAKSN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23480358    95 EQLSKSLNDINKIITRVNKYIKLKNINKSIYDFQKQNDEVSLKEDMLDDLFDTLNyDIDMAEEEDiIVSKVLDGLGIQMN 174
Cdd:pfam03357  81 QEVLNAMKQGAKAMKAMNKLMDIDKIDDLMDEIEDQMEKADEISEMLSDPLDDAD-EEDEEELEA-ELDALLDEIGDEEL 158
                         170
                  ....*....|.
gi 23480358   175 S--KLDEIPSV 183
Cdd:pfam03357 159 LpvKLPSAPSG 169
 
Name Accession Description Interval E-value
Snf7 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
15-183 4.73e-14

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: 67.66  E-value: 4.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23480358    15 EEKRNLNRSIRELEREIVKLENEKKQIEKNIKLYAKKNDITLVRTLAKDFVKVKQTVTKYSKIKSHLFSMKIKLQSVKSS 94
Cdd:pfam03357   1 EAILSLRKAIRKLDKKQESLEKKIEKLELEIKKLAKKGNKDAALLLLKQKKRYEKQLDQLDGQLANLEQQRMAIENAKSN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23480358    95 EQLSKSLNDINKIITRVNKYIKLKNINKSIYDFQKQNDEVSLKEDMLDDLFDTLNyDIDMAEEEDiIVSKVLDGLGIQMN 174
Cdd:pfam03357  81 QEVLNAMKQGAKAMKAMNKLMDIDKIDDLMDEIEDQMEKADEISEMLSDPLDDAD-EEDEEELEA-ELDALLDEIGDEEL 158
                         170
                  ....*....|.
gi 23480358   175 S--KLDEIPSV 183
Cdd:pfam03357 159 LpvKLPSAPSG 169
Did4 COG5491
Archaeal division protein CdvB, Snf7/Vps24/ESCRT-III family [Cell cycle control, cell division, ...
27-181 1.06e-04

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


Pssm-ID: 227778  Cd Length: 204  Bit Score: 41.72  E-value: 1.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23480358  27 LEREIVKLENEKKQIEKNIKLYAKKN--DITLVRTLAKDFVKVKQTVTKYSKIKSHLFSMKIKLQSVKSSEQLSKSLNDI 104
Cdd:COG5491   5 LERQAKKLVRELKQEAKKGQVLLNEIakKAPNRRRLAEELYKLRKARSRLDASISRLQSLDTMLFEKVVMRQVSGDMAKA 84
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23480358 105 NKIITRVNKYIKL-KNINKSIYDFQKQndeVSLKEDMLDDLFDTLNYDIDMA-EEEDIIVSKVLDGLGIQMNSKLDEIP 181
Cdd:COG5491  85 AMYMNELESIRRImQLFETQFLALELV---QLRLETMDELMDVVVGDPVLEDlEELDELVNKVLPEIGLELDESEQSLP 160
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
1-134 5.65e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 37.60  E-value: 5.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23480358    1 MGGYFSKSLEECLREEKRNLN---RSIRELEREIVKLENEKKQIEKNIK--------------LYAKKNDITLVRTLAKD 63
Cdd:PRK05771  76 KKKVSVKSLEELIKDVEEELEkieKEIKELEEEISELENEIKELEQEIErlepwgnfdldlslLLGFKYVSVFVGTVPED 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23480358   64 FV--------KVKQTVTKYSKIKSHLFSMKIKLQSVKSSEQLSKS-----------------------LNDINKIITRVN 112
Cdd:PRK05771 156 KLeelklesdVENVEYISTDKGYVYVVVVVLKELSDEVEEELKKLgferleleeegtpselireikeeLEEIEKERESLL 235
                        170       180
                 ....*....|....*....|..
gi 23480358  113 KyiKLKNINKSIYDFQKQNDEV 134
Cdd:PRK05771 236 E--ELKELAKKYLEELLALYEY 255
 
Name Accession Description Interval E-value
Snf7 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
15-183 4.73e-14

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: 67.66  E-value: 4.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23480358    15 EEKRNLNRSIRELEREIVKLENEKKQIEKNIKLYAKKNDITLVRTLAKDFVKVKQTVTKYSKIKSHLFSMKIKLQSVKSS 94
Cdd:pfam03357   1 EAILSLRKAIRKLDKKQESLEKKIEKLELEIKKLAKKGNKDAALLLLKQKKRYEKQLDQLDGQLANLEQQRMAIENAKSN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23480358    95 EQLSKSLNDINKIITRVNKYIKLKNINKSIYDFQKQNDEVSLKEDMLDDLFDTLNyDIDMAEEEDiIVSKVLDGLGIQMN 174
Cdd:pfam03357  81 QEVLNAMKQGAKAMKAMNKLMDIDKIDDLMDEIEDQMEKADEISEMLSDPLDDAD-EEDEEELEA-ELDALLDEIGDEEL 158
                         170
                  ....*....|.
gi 23480358   175 S--KLDEIPSV 183
Cdd:pfam03357 159 LpvKLPSAPSG 169
Did4 COG5491
Archaeal division protein CdvB, Snf7/Vps24/ESCRT-III family [Cell cycle control, cell division, ...
27-181 1.06e-04

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


Pssm-ID: 227778  Cd Length: 204  Bit Score: 41.72  E-value: 1.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23480358  27 LEREIVKLENEKKQIEKNIKLYAKKN--DITLVRTLAKDFVKVKQTVTKYSKIKSHLFSMKIKLQSVKSSEQLSKSLNDI 104
Cdd:COG5491   5 LERQAKKLVRELKQEAKKGQVLLNEIakKAPNRRRLAEELYKLRKARSRLDASISRLQSLDTMLFEKVVMRQVSGDMAKA 84
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23480358 105 NKIITRVNKYIKL-KNINKSIYDFQKQndeVSLKEDMLDDLFDTLNYDIDMA-EEEDIIVSKVLDGLGIQMNSKLDEIP 181
Cdd:COG5491  85 AMYMNELESIRRImQLFETQFLALELV---QLRLETMDELMDVVVGDPVLEDlEELDELVNKVLPEIGLELDESEQSLP 160
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
1-134 5.65e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 37.60  E-value: 5.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23480358    1 MGGYFSKSLEECLREEKRNLN---RSIRELEREIVKLENEKKQIEKNIK--------------LYAKKNDITLVRTLAKD 63
Cdd:PRK05771  76 KKKVSVKSLEELIKDVEEELEkieKEIKELEEEISELENEIKELEQEIErlepwgnfdldlslLLGFKYVSVFVGTVPED 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23480358   64 FV--------KVKQTVTKYSKIKSHLFSMKIKLQSVKSSEQLSKS-----------------------LNDINKIITRVN 112
Cdd:PRK05771 156 KLeelklesdVENVEYISTDKGYVYVVVVVLKELSDEVEEELKKLgferleleeegtpselireikeeLEEIEKERESLL 235
                        170       180
                 ....*....|....*....|..
gi 23480358  113 KyiKLKNINKSIYDFQKQNDEV 134
Cdd:PRK05771 236 E--ELKELAKKYLEELLALYEY 255
FapA pfam03961
Flagellar Assembly Protein A; Members of this family include FapA (flagellar assembly protein ...
19-124 6.58e-03

Flagellar Assembly Protein A; Members of this family include FapA (flagellar assembly protein A), found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction.


Pssm-ID: 335555  Cd Length: 451  Bit Score: 37.24  E-value: 6.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23480358    19 NLNRSIRELEREIVKLENEKKQIEKNIKLYAKKNDITLVRTLAKDFVKVKQT----VTKYSKIKSHLFSMKIKLQSVKSS 94
Cdd:pfam03961 332 ELKEKLKELEEELKELEEELEKLKKRLKKLPKKAEGQLPPEKRELLEKLLETknklSEELEELEEELKELKEELESLGAN 411
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 23480358    95 EQLSKS----------LNDINKIITRVNKYIKLKNINKSI 124
Cdd:pfam03961 412 AKISVNktiypgvkihIGNKVLRIKREHGPCTFVLEDGEI 451
 
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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