LYS4/YDR234W 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 Lys4p domain/motif information see the external links section.

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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 Lys4p , 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 Lys4p domain/motif information see the external links section.

Last updated on 2013-05-06

Other Saccharomyces cerevisiae proteins that contain motifs found in Lys4p
Protein	Motifs in common with Lys4p	Other motifs in this protein (but not in Lys4p )
Leu1p	SUPERFAMILY SSF53732: Aconitase iron-sulfur domain SUPERFAMILY SSF52016: LeuD/IlvD-like PRINTS PR00415: ACONITASE PANTHER PTHR11670: ACONITASE Pfam PF00330: Aconitase Pfam PF00694: Aconitase_C Gene3D G3DSA:3.30.499.10: no description Gene3D G3DSA:3.40.1060.10: no description Gene3D G3DSA:3.20.19.10: no description	PIR superfamily PIRSF001418: 3-isopropylmalate dehydratase, fused small/large subunits TIGRFAMs TIGR00170: leuC: 3-isopropylmalate dehydratase, large subunit TIGRFAMs TIGR00171: leuD: 3-isopropylmalate dehydratase, small subunit PANTHER PTHR11670:SF8: ACONITATE HYDRATASE-RELATED / CITRATE HYDRO-LYASE-RELATED / ACONITASE-RELATED
Aco2p	Pfam PF00330: Aconitase Pfam PF00694: Aconitase_C PANTHER PTHR11670: ACONITASE SUPERFAMILY SSF53732: Aconitase iron-sulfur domain SUPERFAMILY SSF52016: LeuD/IlvD-like PRINTS PR00415: ACONITASE Gene3D G3DSA:3.30.499.10: no description Gene3D G3DSA:3.40.1060.10: no description Gene3D G3DSA:3.20.19.10: no description	TIGRFAMs TIGR01340: aconitase_mito: aconitate hydratase, mitochondrial PANTHER PTHR11670:SF5: ACONITASE, MITOCHONDRIAL
Ilv3p	SUPERFAMILY SSF52016: LeuD/IlvD-like	TIGRFAMs TIGR00110: ilvD: dihydroxy-acid dehydratase Pfam PF00920: ILVD_EDD PANTHER PTHR21000: DIHYDROXY-ACID DEHYDRATASE (DAD) SUPERFAMILY SSF143975: IlvD/EDD N-terminal domain-like
Aco1p	SUPERFAMILY SSF53732: Aconitase iron-sulfur domain SUPERFAMILY SSF52016: LeuD/IlvD-like Gene3D G3DSA:3.30.499.10: no description Gene3D G3DSA:3.40.1060.10: no description Gene3D G3DSA:3.20.19.10: no description Pfam PF00330: Aconitase Pfam PF00694: Aconitase_C PANTHER PTHR11670: ACONITASE PRINTS PR00415: ACONITASE	TIGRFAMs TIGR01340: aconitase_mito: aconitate hydratase, mitochondrial PANTHER PTHR11670:SF5: ACONITASE, MITOCHONDRIAL

Unique domains/motifs

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This table lists domains/motifs that are unique to Lys4p . 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 Lys4p domain/motif information see the external links section.

Last updated on 2013-05-06

Domain/motifs that are unique to Lys4p
Database source	Accession number	Description
PANTHER	PTHR11670:SF7	HOMOACONITASE
TIGRFAMs	TIGR00139	h_aconitase: homoaconitase

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.

There are no transmembrane domains predicted for Lys4p .

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.

There are no signal peptide(s) predicted for Lys4p .

External Links

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The following external links can be used to directly search external databases for domain/motif information for Lys4p .