To directly search external databases for Rpl35ap domain/motif information see the external links section.
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This table lists proteins that share domains/motifs in common with those found in Rpl35ap , 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 Rpl35ap domain/motif information see the external links section.
Last updated on 2013-05-06
| Other Saccharomyces cerevisiae proteins that contain motifs found in Rpl35ap | ||
|---|---|---|
| Protein | Motifs in common with Rpl35ap | Other motifs in this protein (but not in Rpl35ap ) |
| Rpl35bp | Gene3D G3DSA:1.10.287.310: no description PANTHER PTHR13872:SF2: 60S RIBOSOMAL PROTEIN L35 PANTHER PTHR13872: 60S RIBOSOMAL PROTEIN L35 SUPERFAMILY SSF46561: Ribosomal protein L29 (L29p) TIGRFAMs TIGR00012: L29: ribosomal protein L29 Pfam PF00831: Ribosomal_L29 |
none |
| Stt3p | PANTHER PTHR13872: 60S RIBOSOMAL PROTEIN L35 |
Pfam PF02516: STT3 PANTHER PTHR13872:SF15: SUBFAMILY NOT NAMED |
This table lists domains/motifs that are unique to Rpl35ap . 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 Rpl35ap domain/motif information see the external links section.
Last updated on 2013-05-06
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.
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.
The following external links can be used to directly search external databases for domain/motif information for Rpl35ap .


