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122  structures 4610  species 6  interactions 21200  sequences 427  architectures

Clan: SGNH_hydrolase (CL0264)

Summary

SGNH hydrolase superfamily Add an annotation

This superfamily contains a diversity of hydrolytic enzyme activities.

This clan contains 8 families and the total number of domains in the clan is 21200. The clan was built by A Bateman.

Literature references

  1. Akoh CC, Lee GC, Liaw YC, Huang TH, Shaw JF; , Prog Lipid Res. 2004;43:534-552.: GDSL family of serine esterases/lipases. PUBMED:15522763 EPMC:15522763
  2. Lo YC, Lin SC, Shaw JF, Liaw YC; , J Mol Biol. 2003;330:539-551.: Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network. PUBMED:12842470 EPMC:12842470

Members

This clan contains the following 8 member families:

DUF303 DUF459 GSCFA Hema_esterase Lipase_GDSL Lipase_GDSL_2 Lipase_GDSL_3 PC-Esterase

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
Lipase_GDSL_2 (PF13472) 11620 (54.8%) View
Lipase_GDSL (PF00657) 4517 (21.3%) View
DUF303 (PF03629) 2378 (11.2%) View
PC-Esterase (PF13839) 1574 (7.4%) View
Hema_esterase (PF03996) 382 (1.8%) View
GSCFA (PF08885) 313 (1.5%) View
Lipase_GDSL_3 (PF14606) 244 (1.2%) View
DUF459 (PF04311) 172 (0.8%) View
Total: 8 Total: 21200 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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This tree shows the occurrence of the domains in this clan across different species. More...

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Interactions

There are 6 interactions for this clan. More...

Interacting families
A B
DUF303 DUF303
Lipase_GDSL WD40
Lipase_GDSL
Hema_esterase Hema_HEFG
Hema_esterase
Hema_stalk

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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