COR1/YBL045C 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 Cor1p 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 Cor1p , 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 Cor1p domain/motif information see the external links section.

Last updated on 2013-05-06

Other Saccharomyces cerevisiae proteins that contain motifs found in Cor1p
Protein	Motifs in common with Cor1p	Other motifs in this protein (but not in Cor1p )
Cym1p	Gene3D G3DSA:3.30.830.10: no description Pfam PF05193: Peptidase_M16_C Pfam PF00675: Peptidase_M16 SUPERFAMILY SSF63411: LuxS/MPP-like metallohydrolase PANTHER PTHR11851: METALLOPROTEASE	Pfam PF08367: M16C_assoc PANTHER PTHR11851:SF68: METALLOPROTEASE 1-RELATED
Mas2p	Gene3D G3DSA:3.30.830.10: no description Pfam PF05193: Peptidase_M16_C Pfam PF00675: Peptidase_M16 SUPERFAMILY SSF63411: LuxS/MPP-like metallohydrolase PANTHER PTHR11851: METALLOPROTEASE	PANTHER PTHR11851:SF49: MITOCHONDRIAL PROCESSING PEPTIDASE ALPHA SUBUNIT
Mas1p	Gene3D G3DSA:3.30.830.10: no description SUPERFAMILY SSF63411: LuxS/MPP-like metallohydrolase PANTHER PTHR11851:SF58: MITOCHONDRIAL PROCESSING PEPTIDASE BETA SUBUNIT PANTHER PTHR11851: METALLOPROTEASE Pfam PF00675: Peptidase_M16 Pfam PF05193: Peptidase_M16_C	none
Ste23p	SUPERFAMILY SSF63411: LuxS/MPP-like metallohydrolase Pfam PF00675: Peptidase_M16 Pfam PF05193: Peptidase_M16_C Gene3D G3DSA:3.30.830.10: no description PANTHER PTHR11851: METALLOPROTEASE	PANTHER PTHR11851:SF64: INSULIN-DEGRADING ENZYME (INSULYSIN) (INSULINASE) (INSULIN PROTEASE)
Yol098cp	Pfam PF05193: Peptidase_M16_C Pfam PF00675: Peptidase_M16 Gene3D G3DSA:3.30.830.10: no description PANTHER PTHR11851: METALLOPROTEASE SUPERFAMILY SSF63411: LuxS/MPP-like metallohydrolase	PANTHER PTHR11851:SF68: METALLOPROTEASE 1-RELATED
Axl1p	Gene3D G3DSA:3.30.830.10: no description Pfam PF00675: Peptidase_M16 Pfam PF05193: Peptidase_M16_C SUPERFAMILY SSF63411: LuxS/MPP-like metallohydrolase PANTHER PTHR11851: METALLOPROTEASE	PANTHER PTHR11851:SF64: INSULIN-DEGRADING ENZYME (INSULYSIN) (INSULINASE) (INSULIN PROTEASE)
Qcr2p	PANTHER PTHR11851: METALLOPROTEASE Gene3D G3DSA:3.30.830.10: no description SUPERFAMILY SSF63411: LuxS/MPP-like metallohydrolase Pfam PF00675: Peptidase_M16 Pfam PF05193: Peptidase_M16_C	PANTHER PTHR11851:SF45: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN 2

Unique domains/motifs

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This table lists domains/motifs that are unique to Cor1p . 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 Cor1p domain/motif information see the external links section.

Last updated on 2013-05-06

There are no unique domains/motifs predicted for Cor1p .

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 Cor1p .

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 Cor1p .

External Links

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The following external links can be used to directly search external databases for domain/motif information for Cor1p .