Summary: Glycosyl transferase family 41
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Glycosyl transferase family 41 Provide feedback
This family of glycosyltransferases includes O-linked beta-N-acetylglucosamine (O-GlcNAc) transferase, an enzyme which catalyses the addition of O-GlcNAc to serine and threonine residues [1,2]. In addition to its function as an O-GlcNAc transferase, human OGT, O15294 also appears to proteolytically cleave the epigenetic cell-cycle regulator HCF-1 [3].
Literature references
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Clarke AJ, Hurtado-Guerrero R, Pathak S, Schuttelkopf AW, Borodkin V, Shepherd SM, Ibrahim AF, van Aalten DM;, EMBO J. 2008;27:2780-2788.: Structural insights into mechanism and specificity of O-GlcNAc transferase. PUBMED:18818698 EPMC:18818698
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Martinez-Fleites C, Macauley MS, He Y, Shen DL, Vocadlo DJ, Davies GJ;, Nat Struct Mol Biol. 2008;15:764-765.: Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation. PUBMED:18536723 EPMC:18536723
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Capotosti F, Guernier S, Lammers F, Waridel P, Cai Y, Jin J, Conaway JW, Conaway RC, Herr W;, Cell. 2011;144:376-388.: O-GlcNAc Transferase Catalyzes Site-Specific Proteolysis of HCF-1. PUBMED:21295698 EPMC:21295698
Internal database links
SCOOP: | Glyco_trans_1_4 |
External database links
CAZY: | GT41 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR029489
This entry represents the C-terminal domain of the O-linked beta-N-acetylglucosamine transferase (OGT, also known as UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase), which catalyses the transfer of a single GlcNAc to the Ser or Thr of nucleocytoplasmic proteins [PUBMED:18948359]. OGTs have two known domains: the N-terminal tetratricopeptide repeat domain and the C-terminal glycosyltransferase domain [PUBMED:18536723]. Deletions of the C-terminal domain result in a complete loss of the enzyme activity [PUBMED:10753899].
In animals, OGT is an essential protein that modifies transcription factors, nuclear pore proteins, kinases, and many other proteins. Abnormalities in OGT activities have been associated with type 2 diabetes [PUBMED:18288188].
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan GT-B (CL0113), which has the following description:
This is the GT-B clan that contains diverse glycosyltransferases that possess a Rossmann like fold [1].
The clan contains the following 47 members:
A-2_8-polyST AGT ALG11_N Alg14 Asp1 Capsule_synth DUF1205 DUF1972 DUF3492 DUF354 Epimerase_2 FucT_N Glyco_tran_28_C Glyco_trans_1_2 Glyco_trans_1_3 Glyco_trans_1_4 Glyco_trans_4_2 Glyco_trans_4_3 Glyco_trans_4_4 Glyco_trans_4_5 Glyco_transf_10 Glyco_transf_20 Glyco_transf_28 Glyco_transf_4 Glyco_transf_41 Glyco_transf_5 Glyco_transf_52 Glyco_transf_56 Glyco_transf_9 Glyco_transf_90 Glycogen_syn Glycos_transf_1 Glycos_transf_N Glyphos_transf LpxB MGDG_synth Mito_fiss_Elm1 NodZ O-FucT Phosphorylase PIGA PM0188 PS_pyruv_trans SUA5 Sucrose_synth T4-Gluco-transf UDPGTAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
Seed (13) |
Full (6148) |
Representative proteomes | UniProt (18667) |
NCBI (30985) |
Meta (1683) |
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RP15 (927) |
RP35 (3119) |
RP55 (5534) |
RP75 (9114) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
Seed (13) |
Full (6148) |
Representative proteomes | UniProt (18667) |
NCBI (30985) |
Meta (1683) |
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---|---|---|---|---|---|---|---|---|---|
RP15 (927) |
RP35 (3119) |
RP55 (5534) |
RP75 (9114) |
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Raw Stockholm | |||||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
Seed source: | Jackhmmer:O15294 |
Previous IDs: | none |
Type: | Family |
Sequence Ontology: | SO:0100021 |
Author: |
Eberhardt R |
Number in seed: | 13 |
Number in full: | 6148 |
Average length of the domain: | 218.60 aa |
Average identity of full alignment: | 16 % |
Average coverage of the sequence by the domain: | 42.38 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 543 | ||||||||||||
Family (HMM) version: | 7 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Selections
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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...
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Interactions
Structures
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 Glyco_transf_41 domain has been found. There are 99 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 sequence.
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