Summary
ATP:guanido phosphotransferase, N-terminal domain
The N-terminal domain has an all-alpha fold.
Literature references
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Fritz-Wolf K, Schnyder T, Wallimann T, Kabsch W; , Nature 1996;381:341-345.: Structure of mitochondrial creatine kinase. PUBMED:8692275
InterPro entry IPR000749
ATP:guanido phosphotransferases are a family of structurally and functionally related enzymes PUBMED:2324092, PUBMED:7819288 that reversibly catalyse the transfer of phosphate between ATP and various phosphogens. The enzymes belonging to this family include:
- Glycocyamine kinase (), which catalyses the transfer of phosphate from ATP to guanidoacetate.
- Arginine kinase (), which catalyses the transfer of phosphate from ATP to arginine.
- Taurocyamine kinase (), an annelid-specific enzyme that catalyses the transfer of phosphate from ATP to taurocyamine.
- Lombricine kinase (), an annelid-specific enzyme that catalyses the transfer of phosphate from ATP to lombricine.
- Smc74, a cercaria-specific enzyme from Schistosoma mansoni PUBMED:2324092.
- Creatine kinase () (CK) PUBMED:3896131, PUBMED:2324105, which catalyses the reversible transfer of high energy phosphate from ATP to creatine, generating phosphocreatine and ADP.
Creatine kinase plays an important role in energy metabolism of vertebrates. There are at least four different, but very closely related, forms of CK. Two isozymes, M (muscle) and B (brain), are cytosolic, while the other two are mitochondrial. In sea urchins there is a flagellar isozyme, which consists of the triplication of a CK-domain. A cysteine residue is implicated in the catalytic activity of these enzymes and the region around this active site residue is highly conserved.
Gene Ontology
| Molecular function | kinase activity (GO:0016301) |
| transferase activity, transferring phosphorus-containing groups (GO:0016772) |
External database links
| PANDIT: | PF02807 |
| PROSITE: | PDOC00103 |
| SCOP: | 1crk |
| SYSTERS: | ATP-gua_PtransN |
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: | Prosite |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Finn RD, Griffiths-Jones SR |
| Number in seed: | 91 |
| Number in full: | 1059 |
| Average length of the domain: | 67.40 aa |
| Average identity of full alignment: | 61 % |
| Average coverage of the sequence by the domain: | 23.67 % |
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: | 76 | ||||||||||||
| Family (HMM) version: | 8 | ||||||||||||
| 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
There is 1 interaction for this family. More...
ATP-gua_PtransStructures
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 sequences and three-dimensional protein structures. The table below shows the structures on which the ATP-gua_PtransN domain has been found.
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