0  structures 40  species 0  interactions 110  sequences 1  architecture

Family: YopJ (PF03421)

Summary

YopJ Serine/Threonine acetyltransferase Add an annotation

The Yersinia effector YopJ inhibits the innate immune response by blocking MAP kinase and NFkappaB signaling pathways. YopJ is a serine/threonine acetyltransferase which regulates signalling pathways by blocking phosphorylation [1]. This family was previously incorrectly annotated in Pfam as being a peptidase family.


Literature references

  1. Mukherjee S, Keitany G, Li Y, Wang Y, Ball HL, Goldsmith EJ, Orth K; , Science. 2006;312:1211-1214.: Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation. PUBMED:16728640

  2. Yoon S, Liu Z, Eyobo Y, Orth K; , J Biol Chem. 2003;278:2131-2135.: Yersinia effector YopJ inhibits yeast MAPK signaling pathways by an evolutionarily conserved mechanism. PUBMED:12433923


InterPro entry IPR005083

The infection of mammalian host cells by Yersinia sp. causes a rapid induction of the mitogen-activated protein kinase (MAPK; including the ERK, JNK and p38 pathways) and nuclear factor kappaB (NF-kappaB) signalling pathways that would typically result in cytokine production and initiation of the innate immune response. However, these pathways are rapidly inhibited promoting apoptosis.

This entry contains YopJ and related proteins. It has been shown that YopJ is a serine/threonine acetyltransferase PUBMED:17412595. It acetylates the serine and threonine residues in the phosphorylation sites of MAPK kinases and nuclear factor kappaB, preventing their activation by phosphorylation and the inhibition of these signalling pathways PUBMED:17116858.

Serine and threonine acetylation is yet another complication to the control of signalling pathways and may be a may be a widespread mode of biochemical regulation of endogenous processes in eukaryotic cells. Although, at the present time there are no predicted eukaryotic orthologs of YopJ based on primary sequence analysis, it could well be they have not as yet been identified.

Clan

This family is a member of clan Peptidase_CE (CL0134), which contains the following 3 members:

Peptidase_C48 Peptidase_C5 YopJ

External database links

Domain organisation

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Alignments

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The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.

You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.

Pfam alignments:
Full length sequences

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MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER2.

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Trees

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Curation and family details

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Curation View help on the curation process

Seed source: Bateman A
Previous IDs: Peptidase_C55;
Type: Family
Author: Bateman A, Mistry J
Number in seed: 17
Number in full: 110
Average length of the domain: 170.40 aa
Average identity of full alignment: 31 %
Average coverage of the sequence by the domain: 52.43 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 19.9 19.9
Trusted cut-off 20.4 21.5
Noise cut-off 18.0 19.0
Model length: 178
Family (HMM) version: 9
Download: download the raw HMM for this family

Species distribution

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