RAD52/YML032C 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 Rad52p 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 Rad52p , 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 Rad52p domain/motif information see the external links section.

Last updated on 2013-05-06

Other Saccharomyces cerevisiae proteins that contain motifs found in Rad52p
Protein	Motifs in common with Rad52p	Other motifs in this protein (but not in Rad52p )
Mrps5p	SUPERFAMILY SSF54768: dsRNA-binding domain-like	Gene3D G3DSA:3.30.160.20: no description Gene3D G3DSA:3.30.230.10: no description PANTHER PTHR13718:SF2: 30S RIBOSOMAL PROTEIN S5 PANTHER PTHR13718: RIBOSOMAL S SUBUNIT Pfam PF00333: Ribosomal_S5 Pfam PF03719: Ribosomal_S5_C SUPERFAMILY SSF54211: Ribosomal protein S5 domain 2-like
Rad59p	SUPERFAMILY SSF54768: dsRNA-binding domain-like PANTHER PTHR12132: DNA REPAIR AND RECOMBINATION PROTEIN RAD52, RAD59 Pfam PF04098: Rad52_Rad22	PIR superfamily PIRSF022936: DNA repair protein RAD59, fungal type PANTHER PTHR12132:SF2: GB DEF: DNA REPAIR PROTEIN RAD59
Rps2p	SUPERFAMILY SSF54768: dsRNA-binding domain-like	TIGRFAMs TIGR01020: rpsE_arch: ribosomal protein S5 SUPERFAMILY SSF54211: Ribosomal protein S5 domain 2-like Pfam PF00333: Ribosomal_S5 Pfam PF03719: Ribosomal_S5_C Gene3D G3DSA:3.30.160.20: no description Gene3D G3DSA:3.30.230.10: no description PANTHER PTHR13718:SF4: 40S RIBOSOMAL PROTEIN S2 PANTHER PTHR13718: RIBOSOMAL S SUBUNIT
Mrpl3p	SUPERFAMILY SSF54768: dsRNA-binding domain-like	SMART SM00535: Ribonuclease III family SMART SM00358: Double-stranded RNA binding motif Pfam PF00636: Ribonuclease_3 Pfam PF00035: dsrm SUPERFAMILY SSF69065: RNase III domain-like Gene3D G3DSA:1.10.1520.10: no description Gene3D G3DSA:3.30.160.20: no description PANTHER PTHR11207: RIBONUCLEASE III
Rnt1p	SUPERFAMILY SSF54768: dsRNA-binding domain-like	SUPERFAMILY SSF69065: RNase III domain-like Pfam PF00636: Ribonuclease_3 Pfam PF00035: dsrm Gene3D G3DSA:1.10.1520.10: no description Gene3D G3DSA:3.30.160.20: no description PANTHER PTHR11207: RIBONUCLEASE III SMART SM00535: Ribonuclease III family SMART SM00358: Double-stranded RNA binding motif

Unique domains/motifs

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This table lists domains/motifs that are unique to Rad52p . 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 Rad52p domain/motif information see the external links section.

Last updated on 2013-05-06

Domain/motifs that are unique to Rad52p
Database source	Accession number	Description
PANTHER	PTHR12132:SF1	DNA REPAIR AND RECOMBINATION PROTEIN RAD52
TIGRFAMs	TIGR00607	rad52: recombination protein rad52

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 Rad52p .

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 Rad52p .

External Links

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The following external links can be used to directly search external databases for domain/motif information for Rad52p .