Summary
Bet V 1 like
The Bet_V_I family is composed of sequences related to the major Birch (Betula verrucose) pollen antigen Betv1. This allergen is known to cause hayfever, dermatitis, asthma and occasionally anaphylactic shock. The other families in this clan share the same structure as Betv1 which is composed of antiparallel beta sheets and alpha helices. There is a cavity between the beta sheet and a long C terminal helix. The cavity appears to play roles in the binding of lipid molecules [1][2][3] which seems a common feature of the families in this clan.
This clan contains 14 families and the total number of domains in the clan is 23609. The clan was built by J Mistry.
Literature references
- Markovic-Housley Z, Degano M, Lamba D, von Roepenack-Lahaye E, Clemens S, Susani M, Ferreira F, Scheiner O, Breiteneder H; , J Mol Biol 2003;325:123-133.: Crystal structure of a hypoallergenic isoform of the major birch pollen allergen Bet v 1 and its likely biological function as a plant steroid carrier. PUBMED:12473456 EPMC:12473456
- Strauss JF 3rd, Kishida T, Christenson LK, Fujimoto T, Hiroi H; , Mol Cell Endocrinol 2003;202:59-65.: START domain proteins and the intracellular trafficking of cholesterol in steroidogenic cells. PUBMED:12770731 EPMC:12770731
- Sha B, Phillips SE, Bankaitis VA, Luo M; , Nature 1998;391:506-510.: Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol-transfer protein. PUBMED:9461221 EPMC:9461221
- Iyer LM, Koonin EV, Aravind L; , Proteins. 2001;43:134-144.: Adaptations of the helix-grip fold for ligand binding and catalysis in the START domain superfamily. PUBMED:11276083 EPMC:11276083
- Radauer C, Lackner P, Breiteneder H; , BMC Evol Biol. 2008;8:286.: The Bet v 1 fold: an ancient, versatile scaffold for binding of large, hydrophobic ligands. PUBMED:18922149 EPMC:18922149
Members
This clan contains the following 14 member families:
AHSA1 Aromatic_hydrox Bet_v_1 COXG DUF1857 DUF2505 DUF3074 DUF3211 DUF3284 IP_trans Polyketide_cyc Polyketide_cyc2 Ring_hydroxyl_A STARTExternal database links
| CATH: | 3.30.530.20 |
| SCOP: | 55961 |
Domain organisation
Below is a listing of the unique domain organisations or architectures from this clan. More...
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Alignments
The table below shows the number of occurrences of each domain throughout the sequence database. More...
| Pfam family | Num. domains | Alignment |
|---|---|---|
| Polyketide_cyc2 (PF10604) | 5359 (22.7%) | View |
| Ring_hydroxyl_A (PF00848) | 4563 (19.3%) | View |
| AHSA1 (PF08327) | 4271 (18.1%) | View |
| Polyketide_cyc (PF03364) | 3012 (12.8%) | View |
| START (PF01852) | 2507 (10.6%) | View |
| Bet_v_1 (PF00407) | 1250 (5.3%) | View |
| COXG (PF06240) | 764 (3.2%) | View |
| IP_trans (PF02121) | 692 (2.9%) | View |
| DUF2505 (PF10698) | 427 (1.8%) | View |
| DUF3284 (PF11687) | 343 (1.5%) | View |
| DUF1857 (PF08982) | 171 (0.7%) | View |
| DUF3074 (PF11274) | 152 (0.6%) | View |
| Aromatic_hydrox (PF11723) | 55 (0.2%) | View |
| DUF3211 (PF11485) | 43 (0.2%) | View |
| Total: 14 | Total: 23609 | Clan alignment |
Please note: Clan alignments can be very large and can cause problems for some browsers. Read the note above before viewing.
Family relationships
This diagram shows the relationships between members of this clan. More...
Species distribution
Tree controls
HideThis tree shows the occurrence of the domains in this clan across different species. More...
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Interactions
There are 9 interactions for this clan. More...
| Interacting families | |
|---|---|
| A | B |
| Bet_v_1 | Bet_v_1 |
| COXG | COXG |
| Ring_hydroxyl_A | Rieske |
| Ring_hydroxyl_A | |
| Ring_hydroxyl_B | |
| Polyketide_cyc | Polyketide_cyc |
| START | START |
| IP_trans | IP_trans |
| AHSA1 | AHSA1 |
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 MSD group, to allow us to map Pfam domains onto UniProt three-dimensional structures. The table below shows the mapping between the Pfam families in this clan, the corresponding UniProt entries, and the region of the three-dimensional structures that are available for that sequence.
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