The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 36: Dolichol-phosphate mannosyltransferase subunit 1

Please note: GO annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

There are 12 GO terms relating to "molecular function"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Dolichyl-phosphate beta-D-mannosyltransferase activity GO:0004582
Catalysis of the reaction: GDP-mannose + dolichyl phosphate = GDP + dolichyl D-mannosyl phosphate.
8 A5GFZ5 (/ISS) A5GFZ5 (/ISS) O70152 (/ISS) Q1JQ93 (/ISS) Q4QR31 (/ISS) Q54LP3 (/ISS) Q6DEJ9 (/ISS) Q9VIU7 (/ISS)
Dolichyl-phosphate-mannose-protein mannosyltransferase activity GO:0004169
Catalysis of the reaction: dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein.
7 A5GFZ5 (/ISS) A5GFZ5 (/ISS) O70152 (/ISS) Q1JQ93 (/ISS) Q4QR31 (/ISS) Q54LP3 (/ISS) Q6DEJ9 (/ISS)
Dolichyl-phosphate beta-D-mannosyltransferase activity GO:0004582
Catalysis of the reaction: GDP-mannose + dolichyl phosphate = GDP + dolichyl D-mannosyl phosphate.
4 D4A8N1 (/IDA) O60762 (/IDA) O60762 (/IDA) O60762 (/IDA)
Dolichyl-phosphate-mannose-protein mannosyltransferase activity GO:0004169
Catalysis of the reaction: dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein.
3 O60762 (/IDA) O60762 (/IDA) O60762 (/IDA)
Protein binding GO:0005515
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
3 O60762 (/IPI) O60762 (/IPI) O60762 (/IPI)
Dolichyl-phosphate beta-D-mannosyltransferase activity GO:0004582
Catalysis of the reaction: GDP-mannose + dolichyl phosphate = GDP + dolichyl D-mannosyl phosphate.
2 O14466 (/ISO) O70152 (/ISO)
Dolichyl-phosphate-mannose-protein mannosyltransferase activity GO:0004169
Catalysis of the reaction: dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein.
1 O70152 (/ISO)
Dolichyl-phosphate beta-D-mannosyltransferase activity GO:0004582
Catalysis of the reaction: GDP-mannose + dolichyl phosphate = GDP + dolichyl D-mannosyl phosphate.
1 O70152 (/IMP)
Mannose binding GO:0005537
Interacting selectively and non-covalently with mannose, a monosaccharide hexose, stereoisomeric with glucose, that occurs naturally only in polymerized forms called mannans.
1 D4A8N1 (/IDA)
Mannose binding GO:0005537
Interacting selectively and non-covalently with mannose, a monosaccharide hexose, stereoisomeric with glucose, that occurs naturally only in polymerized forms called mannans.
1 O70152 (/ISO)
Alcohol binding GO:0043178
Interacting selectively and non-covalently with an alcohol, any of a class of alkyl compounds containing a hydroxyl group.
1 D4A8N1 (/IDA)
Alcohol binding GO:0043178
Interacting selectively and non-covalently with an alcohol, any of a class of alkyl compounds containing a hydroxyl group.
1 O70152 (/ISO)

There are 24 GO terms relating to "biological process"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
GPI anchor biosynthetic process GO:0006506
The chemical reactions and pathways resulting in the formation of a glycosylphosphatidylinositol (GPI) anchor that attaches some membrane proteins to the lipid bilayer of the cell membrane. The phosphatidylinositol group is linked via the C-6 hydroxyl residue of inositol to a carbohydrate chain which is itself linked to the protein via an ethanolamine phosphate group, its amino group forming an amide linkage with the C-terminal carboxyl of the protein. Some GPI anchors have variants on this canonical linkage.
7 A5GFZ5 (/ISS) A5GFZ5 (/ISS) O70152 (/ISS) Q1JQ93 (/ISS) Q4QR31 (/ISS) Q54LP3 (/ISS) Q6DEJ9 (/ISS)
Protein mannosylation GO:0035268
The addition of a mannose residue to a protein acceptor molecule.
7 A5GFZ5 (/ISS) A5GFZ5 (/ISS) O70152 (/ISS) Q1JQ93 (/ISS) Q4QR31 (/ISS) Q54LP3 (/ISS) Q6DEJ9 (/ISS)
Protein O-linked mannosylation GO:0035269
The transfer of mannose from dolichyl activated mannose to the hydroxyl group of a seryl or threonyl residue of a protein acceptor molecule, to form an O-linked protein-sugar linkage.
7 A5GFZ5 (/ISS) A5GFZ5 (/ISS) O70152 (/ISS) Q1JQ93 (/ISS) Q4QR31 (/ISS) Q54LP3 (/ISS) Q6DEJ9 (/ISS)
Dolichol metabolic process GO:0019348
The chemical reactions and pathways involving dolichols, any 2,3-dihydropolyprenol derived from four or more linked isoprene units.
4 D4A8N1 (/IDA) O60762 (/IDA) O60762 (/IDA) O60762 (/IDA)
GPI anchor biosynthetic process GO:0006506
The chemical reactions and pathways resulting in the formation of a glycosylphosphatidylinositol (GPI) anchor that attaches some membrane proteins to the lipid bilayer of the cell membrane. The phosphatidylinositol group is linked via the C-6 hydroxyl residue of inositol to a carbohydrate chain which is itself linked to the protein via an ethanolamine phosphate group, its amino group forming an amide linkage with the C-terminal carboxyl of the protein. Some GPI anchors have variants on this canonical linkage.
3 O60762 (/IDA) O60762 (/IDA) O60762 (/IDA)
Protein N-linked glycosylation via asparagine GO:0018279
The glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.
3 O60762 (/TAS) O60762 (/TAS) O60762 (/TAS)
Protein mannosylation GO:0035268
The addition of a mannose residue to a protein acceptor molecule.
3 O60762 (/IDA) O60762 (/IDA) O60762 (/IDA)
Protein O-linked mannosylation GO:0035269
The transfer of mannose from dolichyl activated mannose to the hydroxyl group of a seryl or threonyl residue of a protein acceptor molecule, to form an O-linked protein-sugar linkage.
3 O60762 (/IDA) O60762 (/IDA) O60762 (/IDA)
Protein glycosylation GO:0006486
A protein modification process that results in the addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid, e.g. the addition of glycan chains to proteins.
1 Q9VIU7 (/ISS)
Protein N-linked glycosylation GO:0006487
A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the N4 atom of peptidyl-asparagine, the omega-N of arginine, or the N1' atom peptidyl-tryptophan.
1 A0A1D8PEA2 (/IMP)
Dolichol-linked oligosaccharide biosynthetic process GO:0006488
The chemical reactions and pathways resulting in the formation of dolichol-linked oligosaccharide, usually by a stepwise addition of glycosyl chains to endoplasmic reticulum membrane-bound dolichol-P.
1 A0A1D8PEA2 (/IMP)
Dolichol-linked oligosaccharide biosynthetic process GO:0006488
The chemical reactions and pathways resulting in the formation of dolichol-linked oligosaccharide, usually by a stepwise addition of glycosyl chains to endoplasmic reticulum membrane-bound dolichol-P.
1 O14466 (/ISO)
Protein O-linked glycosylation GO:0006493
A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the hydroxyl group of peptidyl-serine, peptidyl-threonine, peptidyl-hydroxylysine, or peptidyl-hydroxyproline, or via the phenol group of peptidyl-tyrosine, forming an O-glycan.
1 A0A1D8PEA2 (/IMP)
Protein O-linked glycosylation GO:0006493
A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the hydroxyl group of peptidyl-serine, peptidyl-threonine, peptidyl-hydroxylysine, or peptidyl-hydroxyproline, or via the phenol group of peptidyl-tyrosine, forming an O-glycan.
1 O14466 (/ISO)
GPI anchor biosynthetic process GO:0006506
The chemical reactions and pathways resulting in the formation of a glycosylphosphatidylinositol (GPI) anchor that attaches some membrane proteins to the lipid bilayer of the cell membrane. The phosphatidylinositol group is linked via the C-6 hydroxyl residue of inositol to a carbohydrate chain which is itself linked to the protein via an ethanolamine phosphate group, its amino group forming an amide linkage with the C-terminal carboxyl of the protein. Some GPI anchors have variants on this canonical linkage.
1 O70152 (/IMP)
GPI anchor biosynthetic process GO:0006506
The chemical reactions and pathways resulting in the formation of a glycosylphosphatidylinositol (GPI) anchor that attaches some membrane proteins to the lipid bilayer of the cell membrane. The phosphatidylinositol group is linked via the C-6 hydroxyl residue of inositol to a carbohydrate chain which is itself linked to the protein via an ethanolamine phosphate group, its amino group forming an amide linkage with the C-terminal carboxyl of the protein. Some GPI anchors have variants on this canonical linkage.
1 O70152 (/ISO)
Fungal-type cell wall biogenesis GO:0009272
A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of a fungal-type cell wall. The fungal-type cell wall contains beta-glucan and may contain chitin.
1 A0A1D8PEA2 (/IMP)
Dolichol metabolic process GO:0019348
The chemical reactions and pathways involving dolichols, any 2,3-dihydropolyprenol derived from four or more linked isoprene units.
1 O70152 (/IMP)
Dolichol metabolic process GO:0019348
The chemical reactions and pathways involving dolichols, any 2,3-dihydropolyprenol derived from four or more linked isoprene units.
1 O70152 (/ISO)
GDP-mannose metabolic process GO:0019673
The chemical reactions and pathways involving GDP-mannose, a substance composed of mannose in glycosidic linkage with guanosine diphosphate.
1 D4A8N1 (/IDA)
GDP-mannose metabolic process GO:0019673
The chemical reactions and pathways involving GDP-mannose, a substance composed of mannose in glycosidic linkage with guanosine diphosphate.
1 O70152 (/ISO)
Protein mannosylation GO:0035268
The addition of a mannose residue to a protein acceptor molecule.
1 O70152 (/ISO)
Protein O-linked mannosylation GO:0035269
The transfer of mannose from dolichyl activated mannose to the hydroxyl group of a seryl or threonyl residue of a protein acceptor molecule, to form an O-linked protein-sugar linkage.
1 O70152 (/ISO)
Muscle structure development GO:0061061
The progression of a muscle structure over time, from its formation to its mature state. Muscle structures are contractile cells, tissues or organs that are found in multicellular organisms.
1 Q6DEJ9 (/IMP)

There are 18 GO terms relating to "cellular component"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
7 A5GFZ5 (/ISS) A5GFZ5 (/ISS) O70152 (/ISS) Q1JQ93 (/ISS) Q4QR31 (/ISS) Q54LP3 (/ISS) Q6DEJ9 (/ISS)
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
3 O60762 (/HDA) O60762 (/HDA) O60762 (/HDA)
Endoplasmic reticulum GO:0005783
The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
3 O60762 (/IDA) O60762 (/IDA) O60762 (/IDA)
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
3 O60762 (/IDA) O60762 (/IDA) O60762 (/IDA)
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
3 O60762 (/TAS) O60762 (/TAS) O60762 (/TAS)
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
3 O60762 (/HDA) O60762 (/HDA) O60762 (/HDA)
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
3 O60762 (/IDA) O60762 (/IDA) O60762 (/IDA)
Dolichol-phosphate-mannose synthase complex GO:0033185
A protein complex that possesses dolichyl-phosphate beta-D-mannosyltransferase activity; contains a catalytic subunit, a regulatory subunit, and a third subunit that stabilizes the complex. In human and several other metazoa, the subunits are named DPM1, DPM2 and DPM3, respectively.
3 O60762 (/IDA) O60762 (/IDA) O60762 (/IDA)
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
2 O14466 (/ISO) O70152 (/ISO)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
1 O14466 (/HDA)
Endoplasmic reticulum GO:0005783
The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
1 O14466 (/HDA)
Endoplasmic reticulum GO:0005783
The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
1 O70152 (/ISO)
Endoplasmic reticulum GO:0005783
The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
1 Q54LP3 (/ISS)
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
1 A0A1D8PEA2 (/IDA)
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
1 O70152 (/ISO)
Dolichol-phosphate-mannose synthase complex GO:0033185
A protein complex that possesses dolichyl-phosphate beta-D-mannosyltransferase activity; contains a catalytic subunit, a regulatory subunit, and a third subunit that stabilizes the complex. In human and several other metazoa, the subunits are named DPM1, DPM2 and DPM3, respectively.
1 O70152 (/ISO)
Intracellular membrane-bounded organelle GO:0043231
Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
1 D4A8N1 (/IDA)
Intracellular membrane-bounded organelle GO:0043231
Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
1 O70152 (/ISO)
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