Summary
Pyrimidine nucleoside phosphorylase C-terminal domain
This domain is found at the C-terminal end of the large alpha/beta domain making up various pyrimidine nucleoside phosphorylases [1,2]. It has slightly different conformations in different members of this family. For example, in pyrimidine nucleoside phosphorylase (PYNP, P77826) there is an added three-stranded anti-parallel beta sheet as compared to other members of the family, such as E. coli thymidine phosphorylase (TP, P07650) [1]. The domain contains an alpha/ beta hammerhead fold and residues in this domain seem to be important in formation of the homodimer [1].
Literature references
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Pugmire MJ, Ealick SE; , Structure 1998;6:1467-1479.: The crystal structure of pyrimidine nucleoside phosphorylase in a closed conformation. PUBMED:9817849
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Walter MR, Cook WJ, Cole LB, Short SA, Koszalka GW, Krenitsky TA, Ealick SE; , J Biol Chem 1990;265:14016-14022.: Three-dimensional structure of thymidine phosphorylase from Escherichia coli at 2.8 A resolution. PUBMED:2199449
InterPro entry IPR013102
This domain is found at the C-terminal end of the large alpha/beta domain making up various pyrimidine nucleoside phosphorylases PUBMED:9817849, PUBMED:2199449. It has slightly different conformations in different members of this family. For example, in pyrimidine nucleoside phosphorylase (PYNP, ) there is an added three-stranded anti-parallel beta sheet as compared to other members of the family, such as Escherichia coli thymidine phosphorylase (TP, ) PUBMED:9817849. The domain contains an alpha/ beta hammerhead fold and residues in this domain seem to be important in formation of the homodimer PUBMED:9817849.
Clan
This family is a member of clan Hybrid (CL0105), which contains the following 13 members:
Apocytochr_F_C Biotin_lipoyl Complex1_51K DUF2118 DUF2254 GCV_H HlyD NQRA OEP Peptidase_M23 PTS_EIIA_1 PYNP_C QRPTase_NGene Ontology
| Molecular function | transferase activity, transferring pentosyl groups (GO:0016763) |
| Biological process | pyrimidine nucleoside metabolic process (GO:0006213) |
External database links
| PANDIT: | PF07831 |
| SCOP: | 1brw |
| SYSTERS: | PYNP_C |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...
View options
Formatting options
Download options
Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER2.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Pfam-B_1661 (release 14.0) |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Fenech M |
| Number in seed: | 54 |
| Number in full: | 924 |
| Average length of the domain: | 73.70 aa |
| Average identity of full alignment: | 34 % |
| Average coverage of the sequence by the domain: | 16.70 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
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| Model details: |
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| Model length: | 75 | ||||||||||||
| Family (HMM) version: | 6 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
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Interactions
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 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 PYNP_C domain has been found.
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