Summary: Dolichyl-phosphate-mannose-protein mannosyltransferase
Dolichyl-phosphate-mannose-protein mannosyltransferase Provide feedback
This is a family of Dolichyl-phosphate-mannose-protein mannosyltransferase proteins EC:184.108.40.206. These proteins are responsible for O-linked glycosylation of proteins, they catalyse the reaction:- Dolichyl phosphate D-mannose + protein <=> dolichyl phosphate + O-D-mannosyl-protein. Also in this family is Q94891 Drosophila rotated abdomen protein which is a putative mannosyltransferase . This family appears to be distantly related to PF02516 (A Bateman pers. obs.).
Martin-Blanco E, Garcia-Bellido A; , Proc Natl Acad Sci U S A 1996;93:6048-6052.: Mutations in the rotated abdomen locus affect muscle development and reveal an intrinsic asymmetry in Drosophila. PUBMED:8650217 EPMC:8650217
Lussier M, Gentzsch M, Sdicu AM, Bussey H, Tanner W; , J Biol Chem 1995;270:2770-2775.: Protein O-glycosylation in yeast. The PMT2 gene specifies a second protein O-mannosyltransferase that functions in addition to the PMT1-encoded activity. PUBMED:7852348 EPMC:7852348
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR003342
The biosynthesis of disaccharides, oligosaccharides and polysaccharides involves the action of hundreds of different glycosyltransferases. These enzymes catalyse the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. A classification of glycosyltransferases using nucleotide diphospho-sugar, nucleotide monophospho-sugar and sugar phosphates (EC) and related proteins into distinct sequence based families has been described [PUBMED:9334165]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site. The same three-dimensional fold is expected to occur within each of the families. Because 3-D structures are better conserved than sequences, several of the families defined on the basis of sequence similarities may have similar 3-D structures and therefore form 'clans'.
Dolichyl-phosphate-mannose-protein mannosyltransferase proteins EC belong to the glycosyltransferase family 39 (CAZY) and are responsible for O-linked glycosylation of proteins. They catalyse the reaction:
The transfer of mannose to seryl and threonyl residues of secretory proteins is catalyzed by a family of protein mannosyltransferases in Saccharomyces cerevisiae coded for by seven genes (PMT1-7). Protein O-glycosylation is essential for cell wall rigidity and cell integrity and this protein modification is vital for S. cerevisiae [PUBMED:8918452].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||membrane (GO:0016020)|
|Molecular function||mannosyltransferase activity (GO:0000030)|
|Biological process||protein O-linked glycosylation (GO:0006493)|
- the number of sequences which exhibit this architecture
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This example describes an architecture with one
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This is the GT-C clan that contains diverse glycosyltransferases that possess 8-13 predicted transmembrane segments .
The clan contains the following 21 members:ALG3 Alg6_Alg8 Arabinose_trans DIE2_ALG10 DUF1420 DUF2029 DUF2079 DUF2142 DUF2723 EpsG Glucan_synthase Glyco_transf_22 Mannosyl_trans Mannosyl_trans2 Oleosin PIG-U PMT PMT_2 PTPS_related STT3 YfhO
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
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- alignment generated by searching the NCBI sequence database using the family HMM
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Curation and family details
|Seed source:||Pfam-B_556 (release 5.2)|
|Author:||Bashton M, Bateman A|
|Number in seed:||22|
|Number in full:||2315|
|Average length of the domain:||228.90 aa|
|Average identity of full alignment:||21 %|
|Average coverage of the sequence by the domain:||38.08 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||13|
|Download:||download the raw HMM for this family|
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