To directly search external databases for Hch1p 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 Hch1p , 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 Hch1p domain/motif information see the external links section.
Last updated on 2013-05-06
| Other Saccharomyces cerevisiae proteins that contain motifs found in Hch1p | ||
|---|---|---|
| Protein | Motifs in common with Hch1p | Other motifs in this protein (but not in Hch1p ) |
| Aha1p | Pfam PF09229: Aha1_N PANTHER PTHR13009:SF0: SUBFAMILY NOT NAMED PANTHER PTHR13009: HEAT SHOCK PROTEIN 90 (HSP90) CO-CHAPERONE AHA-1 SUPERFAMILY SSF103111: Activator of Hsp90 ATPase, Aha1 SMART SM01000: Activator of Hsp90 ATPase, N-terminal |
Pfam PF08327: AHSA1 Gene3D G3DSA:3.30.530.20: no description SUPERFAMILY SSF55961: Bet v1-like |
This table lists domains/motifs that are unique to Hch1p . 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 Hch1p 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 Hch1p .


