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2263  structures 9380  species 0  interactions 440379  sequences 2901  architectures

Clan: HUP (CL0039)

Summary

HUP - HIGH-signature proteins, UspA, and PP-ATPase. Add an annotation

The HUP class contains the HIGH-signature proteins, UspA superfamily and the PP-ATPase superfamily [1]. The HIGH superfamily has the HIGH Nucleotidyl transferases and the class I tRNA synthetases both of which have the HIGH and the KMSKS motif [1],[2]. The PP-loop ATPase named after the ATP PyroPhosphatase domain, was initially identified as a conserved amino acid sequence motif in four distinct groups of enzymes that catalyse the hydrolysis of the alpha-beta phosphate bond of ATP, namely GMP synthetases, argininosuccinate synthetases, asparagine synthetases, and ATP sulfurylases [3]. The USPA superfamily contains USPA, ETFP and Photolyases [1]

This clan contains 32 families and the total number of domains in the clan is 440379. The clan was built by A Bateman and V Anantharaman.

Literature references

  1. Aravind L, Anantharaman V, Koonin EV; , Proteins 2002;48:1-14.: Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP, photolyase, and PP-ATPase nucleotide-binding domains: implications for protein evolution in the RNA. PUBMED:12012333 EPMC:12012333
  2. Wolf YI, Aravind L, Grishin NV, Koonin EV; , Genome Res 1999;9:689-710.: Evolution of aminoacyl-tRNA synthetases--analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events. PUBMED:10447505 EPMC:10447505
  3. Bork P, Koonin EV; , Proteins 1994;20:347-355.: A P-loop-like motif in a widespread ATP pyrophosphatase domain: implications for the evolution of sequence motifs and enzyme activity. PUBMED:7731953 EPMC:7731953

Members

This clan contains the following 32 member families:

Arginosuc_synth Asn_synthase ATP-sulfurylase ATP_bind_3 BshC CDPS Citrate_ly_lig CTP_transf_like Diphthami_syn_2 DNA_photolyase DPRP ETF FAD_syn HIGH_NTase1 HIGH_NTase1_ass NAD_synthase Pantoate_ligase PAPS_reduct QueC QueH ThiI tRNA-synt_1 tRNA-synt_1_2 tRNA-synt_1b tRNA-synt_1c tRNA-synt_1d tRNA-synt_1e tRNA-synt_1f tRNA-synt_1g tRNA_Me_trans UDPG_MGDP_dh_C Usp

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
Usp (PF00582) 62462 (14.2%) View
tRNA-synt_1 (PF00133) 46827 (10.6%) View
CTP_transf_like (PF01467) 34489 (7.8%) View
tRNA-synt_1b (PF00579) 26965 (6.1%) View
tRNA-synt_1c (PF00749) 24704 (5.6%) View
tRNA-synt_1g (PF09334) 23206 (5.3%) View
ETF (PF01012) 21131 (4.8%) View
Asn_synthase (PF00733) 20644 (4.7%) View
NAD_synthase (PF02540) 20589 (4.7%) View
UDPG_MGDP_dh_C (PF03720) 17233 (3.9%) View
PAPS_reduct (PF01507) 16149 (3.7%) View
ATP_bind_3 (PF01171) 14925 (3.4%) View
tRNA-synt_1e (PF01406) 13610 (3.1%) View
tRNA-synt_1d (PF00750) 13516 (3.1%) View
DNA_photolyase (PF00875) 12432 (2.8%) View
tRNA_Me_trans (PF03054) 10646 (2.4%) View
Arginosuc_synth (PF00764) 9901 (2.2%) View
continued
Pfam family Num. domains Alignment
tRNA-synt_1_2 (PF13603) 9249 (2.1%) View
FAD_syn (PF06574) 8344 (1.9%) View
Pantoate_ligase (PF02569) 7618 (1.7%) View
QueC (PF06508) 4942 (1.1%) View
ATP-sulfurylase (PF01747) 4764 (1.1%) View
Diphthami_syn_2 (PF01902) 3421 (0.8%) View
ThiI (PF02568) 3098 (0.7%) View
DPRP (PF04244) 2049 (0.5%) View
tRNA-synt_1f (PF01921) 1974 (0.4%) View
HIGH_NTase1 (PF05636) 1723 (0.4%) View
QueH (PF02677) 1624 (0.4%) View
BshC (PF10079) 1301 (0.3%) View
Citrate_ly_lig (PF08218) 575 (0.1%) View
CDPS (PF16715) 235 (0.1%) View
HIGH_NTase1_ass (PF16581) 33 (0.0%) View
Total: 32 Total: 440379 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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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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