Summary: Transglutaminase-like superfamily
Transglutaminase-like superfamily Provide feedback
This family includes animal transglutaminases and other bacterial proteins of unknown function. Sequence conservation in this superfamily primarily involves three motifs that centre around conserved cysteine, histidine, and aspartate residues that form the catalytic triad in the structurally characterised transglutaminase, the human blood clotting factor XIIIa' . On the basis of the experimentally demonstrated activity of the Methanobacterium phage pseudomurein endoisopeptidase  it is proposed that many, if not all, microbial homologues of the transglutaminases are proteases and that the eukaryotic transglutaminases have evolved from an ancestral protease. 
Yee VC, Pedersen LC, Le Trong I, Bishop PD, Stenkamp RE, Teller DC; , Proc Natl Acad Sci USA 1994;91:7296-7300.: Three-dimensional structure of a transglutaminase: human blood coagulation factor XIII. PUBMED:7913750 EPMC:7913750
Makarova KS, Aravind L, Koonin EV; , Protein Sci 1999;8:1714-1719.: A superfamily of archaeal, bacterial, and eukaryotic proteins homologous to animal transglutaminases [In Process Citation] PUBMED:10452618 EPMC:10452618
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR002931
This domain is found in many proteins known to have transglutaminase activity, i.e. which cross-link proteins through an acyl-transfer reaction between the gamma-carboxamide group of peptide-bound glutamine and the epsilon-amino group of peptide-bound lysine, resulting in a epsilon-(gamma-glutamyl)lysine isopeptide bond. Tranglutaminases have been found in a diverse range of species, from bacteria through to mammals. The enzymes require calcium binding and their activity leads to post-translational modification of proteins through acyl-transfer reactions, involving peptidyl glutamine residues as acyl donors and a variety of primary amines as acyl acceptors, with the generation of proteinase resistant isopeptide bonds [PUBMED:12366374].
Sequence conservation in this superfamily primarily involves three motifs that centre around conserved cysteine, histidine, and aspartate residues that form the catalytic triad in the structurally characterised transglutaminase, the human blood clotting factor XIIIa' [PUBMED:7913750]. On the basis of the experimentally demonstrated activity of the Methanobacterium phage psiM2 pseudomurein endoisopeptidase [PUBMED:9791169], it is proposed that many, if not all, microbial homologs of the transglutaminases are proteases and that the eukaryotic transglutaminases have evolved from an ancestral protease [PUBMED:10452618].
A subunit of plasma Factor XIII revealed that each Factor XIIIA subunit is composed of four domains (termed N-terminal beta-sandwich, core domain (containing the catalytic and the regulatory sites), and C-terminal beta-barrels 1 and 2) and that two monomers assemble into the native dimer through the surfaces in domains 1 and 2, in opposite orientation. This organisation in four domains is highly conserved during evolution among transglutaminase isoforms [PUBMED:12366374].
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
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This clan includes peptidases with the papain-like fold.
The clan contains the following 60 members:Acetyltransf_2 Amidase_5 Amidase_6 CHAP DUF1175 DUF1287 DUF1460 DUF2272 DUF3335 DUF553 DUF830 EDR1 Guanylate_cyc_2 LRAT NLPC_P60 OTU Peptidase_C1 Peptidase_C10 Peptidase_C12 Peptidase_C16 Peptidase_C1_2 Peptidase_C2 Peptidase_C21 Peptidase_C23 Peptidase_C27 Peptidase_C28 Peptidase_C31 Peptidase_C32 Peptidase_C33 Peptidase_C34 Peptidase_C36 Peptidase_C39 Peptidase_C39_2 Peptidase_C42 Peptidase_C47 Peptidase_C48 Peptidase_C5 Peptidase_C54 Peptidase_C58 Peptidase_C6 Peptidase_C65 Peptidase_C7 Peptidase_C70 Peptidase_C71 Peptidase_C78 Peptidase_C8 Peptidase_C9 Peptidase_C93 Peptidase_C98 Phytochelatin Rad4 Transglut_core Transglut_core2 Transglut_core3 Transglut_i_TM Transpep_BrtH UCH UCH_1 Viral_protease YopJ
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Number in seed:||87|
|Number in full:||6914|
|Average length of the domain:||111.30 aa|
|Average identity of full alignment:||20 %|
|Average coverage of the sequence by the domain:||20.05 %|
|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:||14|
|Download:||download the raw HMM for this family|
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There are 3 interactions 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 Transglut_core domain has been found. There are 45 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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