PEP1/YBL017C Domains/Motifs and Signal Peptides

This page contains a summary of information for Saccharomyces cerevisiae proteins which share domains/motifs in common with the target protein, listed above. Coordinate information for proteins with predicted transmembrane domains and signal peptides is also listed.

To directly search external databases for Pep1p domain/motif information see the external links section.

Proteome Browser

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Shared domains/motifs

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This table lists proteins that share domains/motifs in common with those found in Pep1p , and a list of domains/motifs that are not shared. Domains/Motifs were determined by comparing the Saccharomyces cerevisiae protein sequence against the sequences in the Interpro database, using the Interpro scan (iprscan) program. The Interpro database integrates motif and domain information from PROSITE, PRINTS, Pfam, ProDom, SMART, TIGRFAMs, PIR SUPERFAMILY, Gene3D, and PANTHER databases.

To directly search external databases for Pep1p domain/motif information see the external links section.

Last updated on 2013-05-06

Other Saccharomyces cerevisiae proteins that contain motifs found in Pep1p
Protein	Motifs in common with Pep1p	Other motifs in this protein (but not in Pep1p )
Ycr099cp	PANTHER PTHR12106:SF6: VACUOLAR PROTEIN SORTING/TARGETING PROTEIN PEP1 PANTHER PTHR12106: SORTILIN RELATED	none
Ycr100cp	Gene3D G3DSA:2.120.10.10: no description SUPERFAMILY SSF110296: Oligoxyloglucan reducing end-specific cellobiohydrolase PANTHER PTHR12106:SF6: VACUOLAR PROTEIN SORTING/TARGETING PROTEIN PEP1 PANTHER PTHR12106: SORTILIN RELATED	none
Ycr101cp	SUPERFAMILY SSF110296: Oligoxyloglucan reducing end-specific cellobiohydrolase Gene3D G3DSA:2.130.10.140: no description	PANTHER PTHR25121:SF8: SUBFAMILY NOT NAMED PANTHER PTHR25121: FAMILY NOT NAMED
Vth1p	SUPERFAMILY SSF110296: Oligoxyloglucan reducing end-specific cellobiohydrolase SUPERFAMILY SSF50939: Sialidases PANTHER PTHR12106:SF6: VACUOLAR PROTEIN SORTING/TARGETING PROTEIN PEP1 PANTHER PTHR12106: SORTILIN RELATED Gene3D G3DSA:2.130.10.140: no description Gene3D G3DSA:2.120.10.10: no description SMART SM00602: no description	none
Vth2p	Gene3D G3DSA:2.130.10.140: no description Gene3D G3DSA:2.120.10.10: no description PANTHER PTHR12106:SF6: VACUOLAR PROTEIN SORTING/TARGETING PROTEIN PEP1 PANTHER PTHR12106: SORTILIN RELATED SUPERFAMILY SSF110296: Oligoxyloglucan reducing end-specific cellobiohydrolase SUPERFAMILY SSF50939: Sialidases SMART SM00602: no description	none
Ynr065cp	SMART SM00602: no description PANTHER PTHR12106:SF6: VACUOLAR PROTEIN SORTING/TARGETING PROTEIN PEP1 PANTHER PTHR12106: SORTILIN RELATED Gene3D G3DSA:2.120.10.10: no description SUPERFAMILY SSF110296: Oligoxyloglucan reducing end-specific cellobiohydrolase	none
Ynr066cp	SMART SM00602: no description Gene3D G3DSA:2.130.10.140: no description Gene3D G3DSA:2.120.10.10: no description SUPERFAMILY SSF110296: Oligoxyloglucan reducing end-specific cellobiohydrolase	PANTHER PTHR25121:SF7: SUBFAMILY NOT NAMED PANTHER PTHR25121: FAMILY NOT NAMED

Unique domains/motifs

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This table lists domains/motifs that are unique to Pep1p . Domains/Motifs were determined by comparing the Saccharomyces cerevisiae protein sequence against the sequences in the Interpro database, using the Interpro scan (iprscan) program. The Interpro database integrates motif and domain information from PROSITE, PRINTS, Pfam, ProDom, SMART, TIGRFAMs, PIR SUPERFAMILY, Gene3D, and PANTHER databases.

To directly search external databases for Pep1p domain/motif information see the external links section.

Last updated on 2013-05-06

There are no unique domains/motifs predicted for Pep1p .

Transmembrane Domains

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This table lists coordinates for transmembrane domain(s), as predicted by version 2.0 using TMHMM, an application available at The Center for Biological Sequence Analysis at the Technical University of Denmark DTU.

Predicted Transmembane Domain(s) (Click on image for expanded interactive view)	Amino Acid Coordinate(s)

	1393 - 1415

Signal Peptide(s)

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This table lists coordinates for signal peptide(s), as predicted using version 3.0 of SignalP, an application available at The Center for Biological Sequence Analysis at the Technical University of Denmark DTU. Cleavage typically occurs on the carboxy side of the predicted site.

Predicted Signal Peptide(s) (Click on image for expanded interactive view)	Amino Acid Coordinate(s)

	1 - 21

External Links

Jump to: top | Shared domains | Unique domains | Transmembrane domains | Signal peptide(s)

The following external links can be used to directly search external databases for domain/motif information for Pep1p .