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341  structures 1850  species 11  interactions 5280  sequences 45  architectures

Clan: GlnB-like (CL0089)


GlnB-like superfamily Add an annotation

The members of this clan are characterised by the fact the domains, each comprised of four beta-strand and two alpha helices, tend to form tetrameric structures [1].

This clan contains 9 families and the total number of domains in the clan is 5280. The clan was built by RD Finn.

Literature references

  1. Cho Y, Sharma V, Sacchettini JC; , J Biol Chem 2003;278:8333-8339.: Crystal structure of ATP phosphoribosyltransferase from Mycobacterium tuberculosis. PUBMED:12511575 EPMC:12511575


This clan contains the following 9 member families:

CdAMP_rec CutA1 DUF190 DUF2007 DUF3240 HisG_C Nit_Regul_Hom P-II Rhomboid_N

External database links

Domain organisation

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

Loading domain graphics...


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

Pfam family Num. domains Alignment
P-II (PF00543) 2250 (42.6%) View
HisG_C (PF08029) 885 (16.8%) View
CutA1 (PF03091) 809 (15.3%) View
DUF2007 (PF09413) 516 (9.8%) View
DUF190 (PF02641) 372 (7.0%) View
CdAMP_rec (PF06153) 282 (5.3%) View
Rhomboid_N (PF12122) 98 (1.9%) View
DUF3240 (PF11582) 50 (0.9%) View
Nit_Regul_Hom (PF10126) 18 (0.3%) View
Total: 9 Total: 5280 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 11 interactions for this clan. More...

Interacting families
AA_kinase P-II
ADP_ribosyl_GH P-II
Ammonium_transp P-II
CdAMP_rec CdAMP_rec
CutA1 CutA1
DUF190 DUF190
HisG HisG_C
P-II DUF3539
Rhomboid Rhomboid_N
Rhomboid_N Rhomboid


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...