VPS16 family protein similar to Homo sapiens vacuolar protein sorting-associated protein 16 homolog that plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways
Vps16, C-terminal region; This protein forms part of the Class C vacuolar protein sorting (Vps) ...
373-691
6.98e-170
Vps16, C-terminal region; This protein forms part of the Class C vacuolar protein sorting (Vps) complex. Vps16 is essential for vacuolar protein sorting, which is essential for viability in plants, but not yeast. The Class C Vps complex is required for SNARE-mediated membrane fusion at the lysosome-like yeast vacuole. It is thought to play essential roles in membrane docking and fusion at the Golgi-to-endosome and endosome-to-vacuole stages of transport. The role of VPS16 in this complex is not known.
:
Pssm-ID: 282668 Cd Length: 320 Bit Score: 488.96 E-value: 6.98e-170
Vps16, N-terminal region; This protein forms part of the Class C vacuolar protein sorting (Vps) ...
4-301
2.34e-133
Vps16, N-terminal region; This protein forms part of the Class C vacuolar protein sorting (Vps) complex. Vps16 is essential for vacuolar protein sorting, which is essential for viability in plants, but not yeast. The Class C Vps complex is required for SNARE-mediated membrane fusion at the lysosome-like yeast vacuole. It is thought to play essential roles in membrane docking and fusion at the Golgi-to-endosome and endosome-to-vacuole stages of transport. The role of VPS16 in this complex is not known.
The actual alignment was detected with superfamily member pfam04841:
Pssm-ID: 252829 Cd Length: 408 Bit Score: 398.80 E-value: 2.34e-133
Vps16, C-terminal region; This protein forms part of the Class C vacuolar protein sorting (Vps) ...
373-691
6.98e-170
Vps16, C-terminal region; This protein forms part of the Class C vacuolar protein sorting (Vps) complex. Vps16 is essential for vacuolar protein sorting, which is essential for viability in plants, but not yeast. The Class C Vps complex is required for SNARE-mediated membrane fusion at the lysosome-like yeast vacuole. It is thought to play essential roles in membrane docking and fusion at the Golgi-to-endosome and endosome-to-vacuole stages of transport. The role of VPS16 in this complex is not known.
Pssm-ID: 282668 Cd Length: 320 Bit Score: 488.96 E-value: 6.98e-170
Vps16, N-terminal region; This protein forms part of the Class C vacuolar protein sorting (Vps) ...
4-301
2.34e-133
Vps16, N-terminal region; This protein forms part of the Class C vacuolar protein sorting (Vps) complex. Vps16 is essential for vacuolar protein sorting, which is essential for viability in plants, but not yeast. The Class C Vps complex is required for SNARE-mediated membrane fusion at the lysosome-like yeast vacuole. It is thought to play essential roles in membrane docking and fusion at the Golgi-to-endosome and endosome-to-vacuole stages of transport. The role of VPS16 in this complex is not known.
Pssm-ID: 252829 Cd Length: 408 Bit Score: 398.80 E-value: 2.34e-133
Vps16, C-terminal region; This protein forms part of the Class C vacuolar protein sorting (Vps) ...
373-691
6.98e-170
Vps16, C-terminal region; This protein forms part of the Class C vacuolar protein sorting (Vps) complex. Vps16 is essential for vacuolar protein sorting, which is essential for viability in plants, but not yeast. The Class C Vps complex is required for SNARE-mediated membrane fusion at the lysosome-like yeast vacuole. It is thought to play essential roles in membrane docking and fusion at the Golgi-to-endosome and endosome-to-vacuole stages of transport. The role of VPS16 in this complex is not known.
Pssm-ID: 282668 Cd Length: 320 Bit Score: 488.96 E-value: 6.98e-170
Vps16, N-terminal region; This protein forms part of the Class C vacuolar protein sorting (Vps) ...
4-301
2.34e-133
Vps16, N-terminal region; This protein forms part of the Class C vacuolar protein sorting (Vps) complex. Vps16 is essential for vacuolar protein sorting, which is essential for viability in plants, but not yeast. The Class C Vps complex is required for SNARE-mediated membrane fusion at the lysosome-like yeast vacuole. It is thought to play essential roles in membrane docking and fusion at the Golgi-to-endosome and endosome-to-vacuole stages of transport. The role of VPS16 in this complex is not known.
Pssm-ID: 252829 Cd Length: 408 Bit Score: 398.80 E-value: 2.34e-133
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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(labeled illustration) Four types of hits can be shown, as available,
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specific hits meet or exceed a domain-specific e-value threshold
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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