Summary: Phosphoribosyl transferase domain
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Phosphoribosyl transferase domain Provide feedback
This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:22.214.171.124, P07672. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase P51900. Hypoxanthine phosphoribosyl-transferase EC:126.96.36.199 P36766. Ribose-phosphate pyrophosphokinase i EC:188.8.131.52 P09329. Amidophosphoribosyltransferase EC:184.108.40.206 P00496. Orotate phosphoribosyl-transferase EC:220.127.116.11 P11172. Uracil phosphoribosyl-transferase EC:18.104.22.168 P25532. Xanthine-guanine phosphoribosyl-transferase EC:22.214.171.124 P00501. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain .
Islam MR, Kim H, Kang SW, Kim JS, Jeong YM, Hwang HJ, Lee SY, Woo JC, Kim SG;, Plant Mol Biol. 2007;63:465-477.: Functional characterization of a gene encoding a dual domain for uridine kinase and uracil phosphoribosyltransferase in Arabidopsis thaliana. PUBMED:17143579 EPMC:17143579
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR000836
This domain is found in a range of diverse phosphoribosyl transferase enzymes, including: adenine phosphoribosyltransferase (EC), hypoxanthine phosphoribosyltransferase (EC), ribose-phosphate pyrophosphokinase i (EC), amidophosphoribosyltransferase (EC), and orotate phosphoribosyltransferase (EC). In Arabidopsis, at the very N terminus of this domain is the P-Loop NTPase domain [PUBMED:17143579].
|Biological process||nucleoside metabolic process (GO:0009116)|
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This superfamily of phosphoribosyl-transferases (PRTases) and phosphoribosyl-pyrophosphate synthetase-like protein families is characterised by a core fold of three layers, a/b/a with a mixed beta-sheet of six strands. In one of the families consists of two domains of this fold.
The clan contains the following 6 members:Pribosyl_synth Pribosyltran PRTase_1 PRTase_2 PRTase_3 UPRTase
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Curation and family details
|Seed source:||Bateman A|
|Author:||Bateman A, Sonnhammer ELL, Finn RD, Eberhardt R|
|Number in seed:||33|
|Number in full:||125306|
|Average length of the domain:||145.10 aa|
|Average identity of full alignment:||17 %|
|Average coverage of the sequence by the domain:||57.07 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||23|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Pribosyltran domain has been found. There are 402 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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