ECM31/YBR176W Domains/Motifs and Signal Peptides Help

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 Ecm31p domain/motif information see the external links section.


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Shared domains/motifs


This table lists proteins that share domains/motifs in common with those found in Ecm31p , 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 Ecm31p domain/motif information see the external links section.

Last updated on 2013-12-16

Other Saccharomyces cerevisiae proteins that contain motifs found in Ecm31p
Protein Motifs in common with Ecm31p Other motifs in this protein (but not in Ecm31p )
Cdc19p Gene3D G3DSA:3.20.20.60: no description
SUPERFAMILY SSF51621: Phosphoenolpyruvate/pyruvate domain
TIGRFAMs TIGR01064: pyruv_kin: pyruvate kinase
Gene3D G3DSA:2.40.33.10: no description
Gene3D G3DSA:3.40.1380.20: no description
PANTHER PTHR11817:SF0: SUBFAMILY NOT NAMED
PANTHER PTHR11817: PYRUVATE KINASE
SUPERFAMILY SSF52935: PK C-terminal domain-like
SUPERFAMILY SSF50800: PK beta-barrel domain-like
Pfam PF00224: PK
Pfam PF02887: PK_C
PRINTS PR01050: PYRUVTKNASE
Icl1p Gene3D G3DSA:3.20.20.60: no description
SUPERFAMILY SSF51621: Phosphoenolpyruvate/pyruvate domain
PIR superfamily PIRSF001362: Isocitrate lyase
Pfam PF00463: ICL
PANTHER PTHR21631:SF3: ISOCITRATE LYASE
PANTHER PTHR21631: ISOCITRATE LYASE/MALATE SYNTHASE
TIGRFAMs TIGR01346: isocit_lyase: isocitrate lyase
Pyk2p Gene3D G3DSA:3.20.20.60: no description
SUPERFAMILY SSF51621: Phosphoenolpyruvate/pyruvate domain
Gene3D G3DSA:2.40.33.10: no description
Gene3D G3DSA:3.40.1380.20: no description
PRINTS PR01050: PYRUVTKNASE
PANTHER PTHR11817:SF0: SUBFAMILY NOT NAMED
PANTHER PTHR11817: PYRUVATE KINASE
Pfam PF00224: PK
Pfam PF02887: PK_C
SUPERFAMILY SSF52935: PK C-terminal domain-like
SUPERFAMILY SSF50800: PK beta-barrel domain-like
TIGRFAMs TIGR01064: pyruv_kin: pyruvate kinase
Icl2p SUPERFAMILY SSF51621: Phosphoenolpyruvate/pyruvate domain
Gene3D G3DSA:3.20.20.60: no description
PIR superfamily PIRSF001362: Isocitrate lyase
Pfam PF00463: ICL
PANTHER PTHR21631:SF3: ISOCITRATE LYASE
PANTHER PTHR21631: ISOCITRATE LYASE/MALATE SYNTHASE
TIGRFAMs TIGR01346: isocit_lyase: isocitrate lyase

Unique domains/motifs


This table lists domains/motifs that are unique to Ecm31p . 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 Ecm31p domain/motif information see the external links section.

Last updated on 2013-12-16

Domain/motifs that are unique to Ecm31p
Database source Accession number Description
PIR superfamily PIRSF000388 3-methyl-2-oxobutanoate hydroxymethyltransferase
PANTHER PTHR20881 3-METHYL-2-OXOBUTANOATE HYDROXYMETHYLTRANSFERASE
Pfam PF02548 Pantoate_transf
TIGRFAMs TIGR00222 panB: 3-methyl-2-oxobutanoate hydroxymethyltransfe

Transmembrane Domains


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.

There are no transmembrane domains predicted for Ecm31p .

Signal Peptide(s)


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.

There are no signal peptide(s) predicted for Ecm31p .


The following external links can be used to directly search external databases for domain/motif information for Ecm31p .