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881  structures 6436  species 22  interactions 83651  sequences 791  architectures

Clan: Bet_v_1_like (CL0209)


Bet v 1 like Add an annotation

The Pfam:PF00407 entry is composed of sequences related to the major Birch (Betula verrucose) pollen antigen Bet v 1. This allergen is known to cause hayfever, dermatitis, asthma and occasionally anaphylactic shock. The other families in this clan share the same structure as Bet v 1, 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 21 families and the total number of domains in the clan is 83651. The clan was built by J Mistry.

Literature references

  1. 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
  2. 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
  3. 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
  4. 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
  5. 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


This clan contains the following 21 member families:

AHSA1 Aromatic_hydrox Bet_v_1 COXG DAPG_hydrolase DUF1857 DUF2505 DUF3074 DUF3211 DUF3284 Fungal_KA1 IP_trans Lipoprotein_18 PaO Polyketide_cyc Polyketide_cyc2 PRELI Ring_hydroxyl_A START VanA_C VASt

External database links

Domain organisation

Below is a listing of the unique domain organisations or architectures from this clan. More...

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The table below shows the number of occurrences of each domain throughout the sequence database. More...

Pfam family Num. domains Alignment
Polyketide_cyc2 (PF10604) 15309 (18.3%) View
AHSA1 (PF08327) 14995 (17.9%) View
START (PF01852) 11235 (13.4%) View
Polyketide_cyc (PF03364) 7974 (9.5%) View
Ring_hydroxyl_A (PF00848) 7916 (9.5%) View
VASt (PF16016) 4613 (5.5%) View
Bet_v_1 (PF00407) 3709 (4.4%) View
PRELI (PF04707) 3673 (4.4%) View
VanA_C (PF19112) 3031 (3.6%) View
IP_trans (PF02121) 2785 (3.3%) View
COXG (PF06240) 2491 (3.0%) View
Pfam family Num. domains Alignment
Lipoprotein_18 (PF06804) 1221 (1.5%) View
PaO (PF08417) 1151 (1.4%) View
DUF2505 (PF10698) 951 (1.1%) View
DUF3074 (PF11274) 889 (1.1%) View
DUF1857 (PF08982) 636 (0.8%) View
Fungal_KA1 (PF16797) 479 (0.6%) View
DAPG_hydrolase (PF18089) 278 (0.3%) View
DUF3284 (PF11687) 191 (0.2%) View
Aromatic_hydrox (PF11723) 89 (0.1%) View
DUF3211 (PF11485) 35 (0.0%) View
Total: 21 Total: 83651 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


This tree shows the occurrence of the domains in this clan across different species. More...



There are 22 interactions for this clan. More...

Interacting families
Aromatic_hydrox Aromatic_hydrox
Bet_v_1 Bet_v_1
DUF1857 DUF1857
IP_trans IP_trans
Lipoprotein_18 Lipoprotein_18
Polyketide_cyc Polyketide_cyc
Polyketide_cyc2 Polyketide_cyc2
PP2C Polyketide_cyc2
Rieske Aromatic_hydrox
Ring_hydroxyl_A Rieske
Ring_hydroxyl_B Ring_hydroxyl_A
YfiO Lipoprotein_18


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.

Loading structure mapping...