URN1/YPR152C 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 Urn1p 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 Urn1p , 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 Urn1p domain/motif information see the external links section.

Last updated on 2013-05-06

Other Saccharomyces cerevisiae proteins that contain motifs found in Urn1p
Protein Motifs in common with Urn1p Other motifs in this protein (but not in Urn1p )
Rsp5p Gene3D G3DSA:2.20.70.10: no description
SUPERFAMILY SSF51045: WW domain
Pfam PF00397: WW
SMART SM00456: Domain with 2 conserved Trp (W) residues
Gene3D G3DSA:2.60.40.150: no description
Gene3D G3DSA:3.30.2160.10: no description
SUPERFAMILY SSF56204: Hect, E3 ligase catalytic domain
SUPERFAMILY SSF49562: C2 domain (Calcium/lipid-binding domain, CaLB)
PANTHER PTHR11254:SF81: E3 UBIQUITIN--PROTEIN LIGASE RSP5(YEAST)-RELATED
PANTHER PTHR11254: HECT DOMAIN UBIQUITIN-PROTEIN LIGASE
Pfam PF00632: HECT
Pfam PF00168: C2
SMART SM00239: Protein kinase C conserved region
SMART SM00119: Domain Homologous to E6-AP Carboxyl Terminus
Wwm1p SMART SM00456: Domain with 2 conserved Trp (W) residues
Pfam PF00397: WW
SUPERFAMILY SSF51045: WW domain
Gene3D G3DSA:2.20.70.10: no description
none
Set2p SUPERFAMILY SSF51045: WW domain
SMART SM00456: Domain with 2 conserved Trp (W) residues
SUPERFAMILY SSF82199: SET domain
Pfam PF08236: SRI
Pfam PF00856: SET
SMART SM00570: associated with SET domains
SMART SM00317: SET (Su(var)3-9, Enhancer-of-zeste, Trithora
SMART SM00508: Cysteine-rich motif following a subset of SE
Gene3D G3DSA:2.170.270.10: no description
PANTHER PTHR22884:SF36: HUNTINGTIN INTERACTING PROTEIN 1
PANTHER PTHR22884: SET DOMAIN PROTEINS
Ess1p Gene3D G3DSA:2.20.70.10: no description
SMART SM00456: Domain with 2 conserved Trp (W) residues
SUPERFAMILY SSF51045: WW domain
Pfam PF00397: WW
PANTHER PTHR10657:SF4: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1 (ROTAMASE PIN1)(PPIASE PIN1)
PANTHER PTHR10657: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE
Gene3D G3DSA:3.10.50.40: no description
SUPERFAMILY SSF54534: FKBP-like
Pfam PF00639: Rotamase
Prp40p SUPERFAMILY SSF51045: WW domain
SUPERFAMILY SSF81698: FF domain
SMART SM00456: Domain with 2 conserved Trp (W) residues
SMART SM00441: Contains two conserved F residues
PANTHER PTHR11864: PRE-MRNA-PROCESSING PROTEIN PRP40
Pfam PF01846: FF
Pfam PF00397: WW
Gene3D G3DSA:2.20.70.10: no description
Gene3D G3DSA:1.10.10.440: no description
none

Unique domains/motifs


This table lists domains/motifs that are unique to Urn1p . 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 Urn1p domain/motif information see the external links section.

Last updated on 2013-05-06

There are no unique domains/motifs predicted for Urn1p .

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 Urn1p .

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 Urn1p .


The following external links can be used to directly search external databases for domain/motif information for Urn1p .