To directly search external databases for Ams1p domain/motif information see the external links section.
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This table lists proteins that share domains/motifs in common with those found in Ams1p , 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 Ams1p domain/motif information see the external links section.
Last updated on 2013-05-06
| Other Saccharomyces cerevisiae proteins that contain motifs found in Ams1p | ||
|---|---|---|
| Protein | Motifs in common with Ams1p | Other motifs in this protein (but not in Ams1p ) |
| Gal10p | SUPERFAMILY SSF74650: Galactose mutarotase-like |
Gene3D G3DSA:3.40.50.720: no description Gene3D G3DSA:3.90.25.10: no description Gene3D G3DSA:2.70.98.10: no description TIGRFAMs TIGR01179: galE: UDP-glucose 4-epimerase GalE PANTHER PTHR10366:SF39: UDP-GLUCOSE 4-EPIMERASE PANTHER PTHR10366: NAD DEPENDENT EPIMERASE/DEHYDRATASE Pfam PF01263: Aldose_epim Pfam PF01370: Epimerase Pfam PF13950: Epimerase_Csub SUPERFAMILY SSF51735: NAD(P)-binding Rossmann-fold domains |
| Rot2p | SUPERFAMILY SSF74650: Galactose mutarotase-like |
Pfam PF01055: Glyco_hydro_31 Pfam PF13802: Gal_mutarotas_2 PANTHER PTHR22762:SF7: NEUTRAL ALPHA-GLUCOSIDASE AB PRECURSOR (GLUCOSIDASE II ALPHA SUBUNIT) (ALPHA GLUCOSIDASE 2) PANTHER PTHR22762: ALPHA-GLUCOSIDASE SUPERFAMILY SSF51445: (Trans)glycosidases SUPERFAMILY SSF51011: Glycosyl hydrolase domain |
| Yhr210cp | SUPERFAMILY SSF74650: Galactose mutarotase-like |
Gene3D G3DSA:2.70.98.10: no description PANTHER PTHR10091:SF0: ALDOSE 1-EPIMERASE PANTHER PTHR10091: ALDOSE-1-EPIMERASE Pfam PF01263: Aldose_epim |
| Cda1p | SUPERFAMILY SSF88713: Glycoside hydrolase/deacetylase |
Pfam PF01522: Polysacc_deac_1 Gene3D G3DSA:3.20.20.370: no description PANTHER PTHR10587:SF15: SUBFAMILY NOT NAMED PANTHER PTHR10587: GLYCOSYL TRANSFERASE-RELATED |
| Cda2p | SUPERFAMILY SSF88713: Glycoside hydrolase/deacetylase |
Gene3D G3DSA:3.20.20.370: no description PANTHER PTHR10587:SF15: SUBFAMILY NOT NAMED PANTHER PTHR10587: GLYCOSYL TRANSFERASE-RELATED Pfam PF01522: Polysacc_deac_1 |
| Ymr099cp | SUPERFAMILY SSF74650: Galactose mutarotase-like |
PANTHER PTHR11122:SF9: SUBFAMILY NOT NAMED PANTHER PTHR11122: APOSPORY-ASSOCIATED PROTEIN C-RELATED Gene3D G3DSA:2.70.98.10: no description Pfam PF01263: Aldose_epim |
| Ynr071cp | SUPERFAMILY SSF74650: Galactose mutarotase-like |
PANTHER PTHR10091:SF0: ALDOSE 1-EPIMERASE PANTHER PTHR10091: ALDOSE-1-EPIMERASE Pfam PF01263: Aldose_epim Gene3D G3DSA:2.70.98.10: no description |
This table lists domains/motifs that are unique to Ams1p . 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 Ams1p domain/motif information see the external links section.
Last updated on 2013-05-06
| Domain/motifs that are unique to Ams1p | ||
|---|---|---|
| Database source | Accession number | Description |
| Gene3D | G3DSA:1.20.1270.50 | no description |
| Gene3D | G3DSA:3.20.110.10 | no description |
| PANTHER | PTHR11607 | ALPHA-MANNOSIDASE |
| PANTHER | PTHR11607:SF2 | ALPHA-MANNOSIDASE 2C1 (ALPHA-D-MANNOSIDE MANNOHYDROLASE) |
| Pfam | PF01074 | Glyco_hydro_38 |
| Pfam | PF07748 | Glyco_hydro_38C |
| Pfam | PF09261 | Alpha-mann_mid |
| SMART | SM00872 | Alpha mannosidase, middle domain |
| SUPERFAMILY | SSF88688 | Families 57/38 glycoside transferase middle domain |
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.
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.
The following external links can be used to directly search external databases for domain/motif information for Ams1p .


