Summary: Polysaccharide biosynthesis protein
Polysaccharide biosynthesis protein Provide feedback
This is a family of diverse bacterial polysaccharide biosynthesis proteins including the CapD protein (P39853)  WalL protein (O86159) mannosyl-transferase (O05349)  and several putative epimerases (e.g. WbiI O69130).
Lin WS, Cunneen T, Lee CY; , J Bacteriol 1994;176:7005-7016.: Sequence analysis and molecular characterization of genes required for the biosynthesis of type 1 capsular polysaccharide in Staphylococcus aureus. PUBMED:7961465 EPMC:7961465
Fallarino A, Mavrangelos C, Stroeher UH, Manning PA; , J Bacteriol 1997;179:2147-2153.: Identification of additional genes required for O-antigen biosynthesis in Vibrio cholerae O1. PUBMED:9079898 EPMC:9079898
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR003869This domain is found in diverse bacterial polysaccharide biosynthesis proteins including the CapD protein from Staphylococcus aureus [PUBMED:7961465], the WalL protein, mannosyl-transferase [PUBMED:9079898], and several putative epimerases. The CapD protein is required for biosynthesis of type 1 capsular polysaccharide.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Biological process||biosynthetic process (GO:0009058)|
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This example describes an architecture with one
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We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Pfam-B_1536 (release 5.5)|
|Author:||Mian N, Bateman A|
|Number in seed:||77|
|Number in full:||3666|
|Average length of the domain:||278.60 aa|
|Average identity of full alignment:||42 %|
|Average coverage of the sequence by the domain:||55.79 %|
|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:||10|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Polysacc_synt_2 domain has been found. There are 14 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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