Summary: A-macroglobulin TED domain
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This is the Wikipedia entry entitled "Alpha-2-Macroglobulin". More...
Alpha-2-Macroglobulin Edit Wikipedia article
Alpha-2 macroglobulin is a large plasma protein found in the blood. It is produced by the liver, and is a major component of the alpha-2 band in protein electrophoresis.
Alpha-2 macroglobulin levels are increased in nephrotic syndrome, a condition where the kidneys start to leak out some of the smaller blood proteins. Because of its size, α2-macroglobulin is retained in the bloodstream. Increased production of all proteins means α2-macroglobulin concentration increases. (This increase has little adverse affect on the health, but is used as a diagnostic clue.)
A rare variant (polymorphism) of α2-macroglobulin leads to increased risk of Alzheimer's disease, although the mechanism is unknown.
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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
A-macroglobulin TED domain Provide feedback
This entry corresponds to the TED domain of the complement components such as C3, C4 and C5. This domain contains a short highly conserved region of proteinase-binding alpha-macro-globulins contains the cysteine and a glutamine of a thiol-ester bond that is cleaved at the moment of proteinase binding, and mediates the covalent binding of the alpha-macro-globulin to the proteinase. The GCGEQ motif is highly conserved.
Literature references
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Huang W, Dolmer K, Liao X, Gettins PG; , J Biol Chem 2000;275:1089-1094.: NMR solution structure of the receptor binding domain of human alpha(2)-macroglobulin. PUBMED:10625650 EPMC:10625650
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Xiao T, DeCamp DL, Spran SR; , Protein Sci 2000;9:1889-1897.: Structure of a rat alpha 1-macroglobulin receptor-binding domain dimer. PUBMED:11106161 EPMC:11106161
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Szakonyi G, Guthridge JM, Li D, Young K, Holers VM, Chen XS; , Science 2001;292:1725-1728.: Structure of complement receptor 2 in complex with its C3d ligand. PUBMED:11387479 EPMC:11387479
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Zanotti G, Bassetto A, Battistutta R, Folli C, Arcidiaco P, Stoppini M, Berni R; , Biochim Biophys Acta 2000;1478:232-238.: Structure at 1.44 A resolution of an N-terminally truncated form of the rat serum complement C3d fragment. PUBMED:10825534 EPMC:10825534
Internal database links
SCOOP: | A2M_recep Prenyltrans SQHop_cyclase_C SQHop_cyclase_N |
Similarity to PfamA using HHSearch: | SQHop_cyclase_C SQHop_cyclase_C |
External database links
PROSITE: | PDOC00440 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR011626
This entry corresponds to the TED domain of the complement components such as C3, C4 and C5. This domain contains a short highly conserved region of proteinase-binding alpha-macro-globulins contains the cysteine and a glutamine of a thiol-ester bond that is cleaved at the moment of proteinase binding, and mediates the covalent binding of the alpha-macro-globulin to the proteinase. The GCGEQ motif is highly conserved [ PUBMED:10625650 , PUBMED:11106161 , PUBMED:11387479 , PUBMED:10825534 ].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Cellular component | extracellular space (GO:0005615) |
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 6_Hairpin (CL0059), which has the following description:
This Clan includes CAZy clans GH-L, GH-M and GH-G. The members of this clan share a common structure composed of 6 helical hairpins. Most members of this superfamily are glycosyl hydrolase enzymes.
The clan contains the following 30 members:
Bac_rhamnosid6H C5-epim_C Cobalamin_bind DUF608 GDE_C GlcNAc_2-epim Glyco_hydro81C Glyco_hydro_100 Glyco_hydro_125 Glyco_hydro_127 Glyco_hydro_15 Glyco_hydro_36 Glyco_hydro_47 Glyco_hydro_48 Glyco_hydro_63 Glyco_hydro_65m Glyco_hydro_76 Glyco_hydro_8 Glyco_hydro_88 Glyco_hydro_9 Glycoamylase LANC_like Ldi Pec_lyase Prenyltrans SQHop_cyclase_C SQHop_cyclase_N TED_complement Terpene_synth TrehalaseAlignments
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 and the UniProtKB 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 (21) |
Full (8285) |
Representative proteomes | UniProt (22010) |
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RP15 (1262) |
RP35 (3077) |
RP55 (6868) |
RP75 (9754) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
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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 (21) |
Full (8285) |
Representative proteomes | UniProt (22010) |
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RP15 (1262) |
RP35 (3077) |
RP55 (6868) |
RP75 (9754) |
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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: | Prosite |
Previous IDs: | A2M3; A2M_comp; |
Type: | Repeat |
Sequence Ontology: | SO:0001068 |
Author: |
Studholme DJ |
Number in seed: | 21 |
Number in full: | 8285 |
Average length of the domain: | 249.8 aa |
Average identity of full alignment: | 28 % |
Average coverage of the sequence by the domain: | 18.96 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 313 | ||||||||||||
Family (HMM) version: | 17 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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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 TED_complement domain has been found. There are 142 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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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.