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1091  structures 7426  species 0  interactions 114280  sequences 1081  architectures

Clan: Bet_v_1_like (CL0209)

Summary

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 25 families and the total number of domains in the clan is 114280. 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

Members

This clan contains the following 25 member families:

AHSA1 Aromatic_hydrox AtaL Bet_v_1 COXG DAPG_hydrolase DUF220 DUF2505 DUF3074 DUF3211 DUF3284 Fungal_KA1 IP_trans KshA_C LigXa_C Lipoprotein_18 PaO Polyketide_cyc Polyketide_cyc2 PRELI Ring_hydroxyl_A START START_2 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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Alignments

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

Pfam family Num. domains Alignment
AHSA1 (PF08327) 19009 (16.6%) View
Polyketide_cyc2 (PF10604) 18864 (16.5%) View
START (PF01852) 17672 (15.5%) View
Polyketide_cyc (PF03364) 10174 (8.9%) View
Ring_hydroxyl_A (PF00848) 9381 (8.2%) View
VASt (PF16016) 6693 (5.9%) View
Bet_v_1 (PF00407) 5453 (4.8%) View
PRELI (PF04707) 5142 (4.5%) View
IP_trans (PF02121) 4604 (4.0%) View
VanA_C (PF19112) 3511 (3.1%) View
COXG (PF06240) 3176 (2.8%) View
KshA_C (PF19298) 1542 (1.3%) View
PaO (PF08417) 1503 (1.3%) View
continued
Pfam family Num. domains Alignment
Lipoprotein_18 (PF06804) 1395 (1.2%) View
DUF2505 (PF10698) 1108 (1.0%) View
DUF3074 (PF11274) 1039 (0.9%) View
START_2 (PF19569) 794 (0.7%) View
LigXa_C (PF19301) 792 (0.7%) View
AtaL (PF08982) 766 (0.7%) View
Fungal_KA1 (PF16797) 547 (0.5%) View
DUF220 (PF02713) 430 (0.4%) View
DAPG_hydrolase (PF18089) 316 (0.3%) View
DUF3284 (PF11687) 206 (0.2%) View
Aromatic_hydrox (PF11723) 121 (0.1%) View
DUF3211 (PF11485) 42 (0.0%) View
Total: 25 Total: 114280 Clan alignment
 

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Family relationships

This diagram shows the relationships between members of this clan. More...

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 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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