Summary: Staphylokinase/Streptokinase family
Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.
This is the Wikipedia entry entitled "Streptokinase". More...
The Wikipedia text that you see displayed here is a download from Wikipedia. This means that the information we display is a copy of the information from the Wikipedia database. The button next to the article title ("Edit Wikipedia article") takes you to the edit page for the article directly within Wikipedia. You should be aware you are not editing our local copy of this information. Any changes that you make to the Wikipedia article will not be displayed here until we next download the article from Wikipedia. We currently download new content on a nightly basis.
Does Pfam agree with the content of the Wikipedia entry ?
Pfam has chosen to link families to Wikipedia articles. In some case we have created or edited these articles but in many other cases we have not made any direct contribution to the content of the article. The Wikipedia community does monitor edits to try to ensure that (a) the quality of article annotation increases, and (b) vandalism is very quickly dealt with. However, we would like to emphasise that Pfam does not curate the Wikipedia entries and we cannot guarantee the accuracy of the information on the Wikipedia page.
Editing Wikipedia articles
Before you edit for the first time
Wikipedia is a free, online encyclopedia. Although anyone can edit or contribute to an article, Wikipedia has some strong editing guidelines and policies, which promote the Wikipedia standard of style and etiquette. Your edits and contributions are more likely to be accepted (and remain) if they are in accordance with this policy.
You should take a few minutes to view the following pages:
How your contribution will be recorded
Anyone can edit a Wikipedia entry. You can do this either as a new user or you can register with Wikipedia and log on. When you click on the "Edit Wikipedia article" button, your browser will direct you to the edit page for this entry in Wikipedia. If you are a registered user and currently logged in, your changes will be recorded under your Wikipedia user name. However, if you are not a registered user or are not logged on, your changes will be logged under your computer's IP address. This has two main implications. Firstly, as a registered Wikipedia user your edits are more likely seen as valuable contribution (although all edits are open to community scrutiny regardless). Secondly, if you edit under an IP address you may be sharing this IP address with other users. If your IP address has previously been blocked (due to being flagged as a source of 'vandalism') your edits will also be blocked. You can find more information on this and creating a user account at Wikipedia.
If you have problems editing a particular page, contact us at email@example.com and we will try to help.
The community annotation is a new facility of the Pfam web site. If you have problems editing or experience problems with these pages please contact us.
Streptokinase Edit Wikipedia article
Complex of catalytic domain of human plasmin and streptokinase
|AHFS/Drugs.com||Micromedex Detailed Consumer Information|
|Chemical and physical data|
Streptokinase (SK) is a thrombolytic medication and enzyme. As a medication it is used to break down clots in some cases of myocardial infarction (heart attack), pulmonary embolism, and arterial thromboembolism. The type of heart attack it is used in is an ST elevation myocardial infarction (STEMI). It is given by injection into a vein.
Side effects include nausea, bleeding, low blood pressure, and allergic reactions. A second use in a person's lifetime is not recommended. While no harm has been found with use in pregnancy, it has not been well studied in this group. Streptokinase is in the antithrombotic family of medications and works by turning on the fibrinolytic system.
Streptokinase was discovered in 1933 from beta-hemolytic streptococci. It is on the World Health Organization's List of Essential Medicines, the most effective and safe medicines needed in a health system. The wholesale cost is between 30.00 and US$138.00 per dose as of 2014. It is no longer commercially available in the United States.
If percutaneous coronary intervention (PCI) is not available within 90â€“120 minutes of first contact, streptokinase is recommended intravenously as soon as possible after the onset of a ST elevation myocardial infarction (STEMI). As streptokinase is a bacterial product, the body has the ability to build up an immunity to it. Therefore, it is recommended that this medication should not be used again after four days from the first administration, as it may not be as effective and can also cause an allergic reaction. For this reason, it is usually given only for a person's first heart attack. Further thrombotic events could be treated with tissue plasminogen activator (tPA). Overdose of streptokinase or tPA can be treated with aminocaproic acid.
- Any prior intracranial hemorrhage
- Known structural cerebral vascular lesion (e.g., arteriovenous malformation)
- Known cancer inside the skull (primary or metastatic)
- Ischemic stroke more than 4.5 hours and less than 3 months ago
- Suspected aortic dissection
- Active bleeding or bleeding problem other than menstruation
- Significant closed-head or facial trauma within 3 months
- Intracranial or intraspinal surgery within 2 months
- Severe uncontrolled high blood pressure (unresponsive to emergency therapy)
- For streptokinase, prior treatment within the previous 6 months
- History of chronic, severe, poorly controlled hypertension
- Significant hypertension on presentation (SBP >180 mm Hg or DBP >110 mm Hg)
- History of prior ischemic stroke more than 3 month ago
- Known intracranial pathology not covered in absolute contraindications
- Traumatic or prolonged (>10 min) CPR
- Major surgery less than three weeks ago
- Recent (within 2 to 4 wk) internal bleeding
- Noncompressible vascular punctures
- Active peptic ulcer
- Oral anticoagulant therapy
Mechanism of action
Structure of staphylokinase, a plasminogen activator.
|SCOPe||2sak / SUPFAM|
Streptokinase belongs to a group of medications known as fibrinolytics, and complexes of streptokinase with human plasminogen can hydrolytically activate other unbound plasminogen by activating through bond cleavage to produce plasmin. There are three domains to streptokinase, denoted Î± (residues 1â€“150), Î² (residues 151â€“287), and Î³ (residues 288â€“414). Each domain binds plasminogen, although none can activate plasminogen independently.
Plasmin is produced in the blood to break down fibrin, the major constituent of blood thrombi, thereby dissolving clots once they have fulfilled their purpose of stopping bleeding. Extra production of plasmin caused by streptokinase breaks down unwanted blood clots, for example, in the lungs (pulmonary embolism). The usual activation of plasminogen (Plgn) is by proteolysis of the Arg561â€”Val562 bond. The amino group of Val562 then forms a salt-bridge with Asp740, which triggers a conformational change producing the active protease Plasmin (Pm). When (SK) is present, it binds to Plgn to form a complex (SK. Plgn) that converts substrate Plgn to Pm. Residues 1â€“59 of SK regulate its capacity to induce an active site in bound Pg by a nonproteolytic mechanism and to activate substrate Pg in a fibrin-independent manner. This complex subsequently rearranges to an active complex although the Arg561â€“Val562 bond remains intact. Therefore, another residue must substitute for the free amino group of Val562 and provide a counterion for Asp740 in this active complex. Two candidates for this counterion have been suggested: Ile1 of streptokinase and Lys698 of Plgn. Deletion of Ile1 of SK markedly inhibits its capacity to induce an active site in plasminogen, which supports the hypothesis that establishment of a salt bridge between Ile1 of SK and Asp740 of plasminogen is necessary for SK to induce an active site in plasminogen by a nonproteolytic mechanism. In contrast with the Ile1 substitutions, the Lys698 mutations also decreased the dissociation constant of the SK complex by 15 to 50 fold. These observations suggest that Lys698 is involved in formation of the initial SKÂ·Plgn complex.
Streptokinase (Sk) is naturally produced by Streptococci spp. bacteria, which use this enzyme to break up blood clots so that they can spread from the initial site of infection. It can also activate fibrin.
It is similar, both in function and in structure, to staphylokinase (Sak) found in Staphylococcus aureus. Staphylokinase is considered a virulence factor, although its presence after the establishment of infection actually decreases disease severity. Both enzymes are carried by phages.
After many years of work along with his student Sol Sherry, William S. Tillett discovered streptokinase in 1933. Initially used in treatment of fibrinous pleural exudates, hemothorax and tuberculous meningitis, its role in acute myocardial infarction was serendipitous.
Streptokinase may find a use in helping to prevent postoperative adhesions, a common complication of surgery, especially abdominal surgery (appendectomy, gall stones, hysterectomy, etc.) One study using animal models (rats) found that when used with a PHBV membrane drug-delivery system, it was 90 percent effective in preventing adhesions. However, it has not been shown to be effective in humans in a clinical trial.
It is marketed in Chile as Streptase by Alpes Selection, under license of CSL Behring Germany.
Available in Vietnam under the name Mutose. Available in Cuba, Venezuela, Ecuador and other Latin American countries under the trademark Heberkinasa, commercialized by Heber Biotech, Havana, Cuba. Available in India under the name STPase by Cadila Pharmaceuticals, and Myokinase by Biocon Limited.
- Sikri N, Bardia A (2007). "A history of streptokinase use in acute myocardial infarction". Texas Heart Institute Journal. 34 (3): 318â€“27. PMC 1995058. PMID 17948083.
- WHO Model Formulary 2008 (PDF). World Health Organization. 2009. pp. 291â€“292. ISBN 9789241547659. Archived (PDF) from the original on 13 December 2016. Retrieved 8 December 2016.
- "Streptokinase 1,500,000 iu - Summary of Product Characteristics (SPC) - (eMC)". www.medicines.org.uk. 1 July 2015. Archived from the original on 20 December 2016. Retrieved 14 December 2016.
- "Streptokinase Use During Pregnancy | Drugs.com". www.drugs.com. Archived from the original on 21 December 2016. Retrieved 14 December 2016.
- "WHO Model List of Essential Medicines (19th List)" (PDF). World Health Organization. April 2015. Archived (PDF) from the original on 13 December 2016. Retrieved 8 December 2016.
- "Streptokinase". International Drug Price Indicator Guide. Archived from the original on 8 January 2016. Retrieved 28 November 2015.
- "streptokinase (Intravenous route, Intracoronary route)". Truven Health Analytics. Archived from the original on 8 December 2015. Retrieved 28 November 2015.
- O'Gara PT, Kushner FG, Ascheim DD, Casey DE, Chung MK, de Lemos JA, et al. (January 2013). "2013 ACCF/AHA guideline for the management of ST-elevation myocardial infarction: a report of the American College of Cardiology Foundation/American Heart Association Task Force on Practice Guidelines". Circulation. 127 (4): e362â€“425. doi:10.1161/CIR.0b013e3182742cf6. PMID 23247304.
- Rabijns A, De Bondt HL, De Ranter C (May 1997). "Three-dimensional structure of staphylokinase, a plasminogen activator with therapeutic potential". Nature Structural Biology. 4 (5): 357â€“60. doi:10.1038/nsb0597-357. PMID 9145104.
- Mundada LV, Prorok M, DeFord ME, Figuera M, Castellino FJ, Fay WP (July 2003). "Structure-function analysis of the streptokinase amino terminus (residues 1-59)". The Journal of Biological Chemistry. 278 (27): 24421â€“7. doi:10.1074/jbc.M301825200. PMID 12704199.
- Young KC, Shi GY, Wu DH, Chang LC, Chang BI, Ou CP, Wu HL (January 1998). "Plasminogen activation by streptokinase via a unique mechanism". The Journal of Biological Chemistry. 273 (5): 3110â€“6. doi:10.1074/jbc.273.5.3110. PMID 9446629.
- Loy JA, Lin X, Schenone M, Castellino FJ, Zhang XC, Tang J (December 2001). "Domain interactions between streptokinase and human plasminogen". Biochemistry. 40 (48): 14686â€“95. doi:10.1021/bi011309d. PMID 11724583.
- Wang S, Reed GL, Hedstrom L (April 1999). "Deletion of Ile1 changes the mechanism of streptokinase: evidence for the molecular sexuality hypothesis". Biochemistry. 38 (16): 5232â€“40. doi:10.1021/bi981915h. PMID 10213631.
- Wang X, Lin X, Loy JA, Tang J, Zhang XC (September 1998). "Crystal structure of the catalytic domain of human plasmin complexed with streptokinase". Science. 281 (5383): 1662â€“5. doi:10.1126/science.281.5383.1662. PMID 9733510.
- Wang H, Lottenberg R, Boyle MD (March 1995). "Analysis of the interaction of group A streptococci with fibrinogen, streptokinase and plasminogen". Microbial Pathogenesis. 18 (3): 153â€“66. doi:10.1016/S0882-4010(95)90013-6. PMID 7565010.
- Bokarewa MI, Jin T, Tarkowski A (2006). "Staphylococcus aureus: Staphylokinase". The International Journal of Biochemistry & Cell Biology. 38 (4): 504â€“9. doi:10.1016/j.biocel.2005.07.005. PMID 16111912.
- Kwiecinski J, Jacobsson G, Karlsson M, Zhu X, Wang W, Bremell T, Josefsson E, Jin T (September 2013). "Staphylokinase promotes the establishment of Staphylococcus aureus skin infections while decreasing disease severity". The Journal of Infectious Diseases. 208 (6): 990â€“9. doi:10.1093/infdis/jit288. PMID 23801604.
- Sikri N, Bardia A (2007). "A history of streptokinase use in acute myocardial infarction". Texas Heart Institute Journal. 34 (3): 318â€“27. PMC 1995058. PMID 17948083.
- Yagmurlu A, Barlas M, Gursel I, Gokcora IH (2003). "Reduction of surgery-induced peritoneal adhesions by continuous release of streptokinase from a drug delivery system". European Surgical Research. Europaische Chirurgische Forschung. Recherches Chirurgicales Europeennes. 35 (1): 46â€“9. doi:10.1159/000067035. PMID 12566787.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Staphylokinase/Streptokinase family Provide feedback
No Pfam abstract.
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR004093
This entry represents staphylokinases and streptokinases.
Staphylokinase (also known as SAK) from Staphylococcus aureus is a virulence factor due to its interaction with plasminogen and alpha-defensins in the hosts. The binding of staphylokinase to plasminogen results in the formation of active plasmin, a proteolytic enzyme facilitating bacterial penetration into the surrounding tissues [PUBMED:16111912]. However, once the host tissues are infected, the interaction between staphylokinase and plasminogen decreases disease severity [PUBMED:23801604]. The three-dimensional structure of streptokinase [PUBMED:9145104] is believed to contain two independently folded domains, each with a ubiquitin-like fold.
Streptokinase (SK) can be found in several species of Streptococci. It can bind not only plasminogen, but also host fibrinogen [PUBMED:7565010]. This close interaction with the human fibrinolytic system allows the microbe to acquire unregulatable cell-surface enzymatic activity, promoting further spread from the site of infection. The complexes formed between streptococcal cells, streptokinase, plasminogen and fibrinogen can lyse fibrin clots in the host [PUBMED:7565010]. Streptokinase has been used to treat acute myocardial infarction [PUBMED:17948083].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||extracellular region (GO:0005576)|
|Biological process||pathogenesis (GO:0009405)|
|plasminogen activation (GO:0031639)|
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
The graphic that is shown by default represents the longest sequence with a given architecture. Each row contains the following information:
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- a link to the page in the Pfam site showing information about the sequence that the graphic describes
- the UniProt description of the protein sequence
- the number of residues in the sequence
- the Pfam graphic itself.
Note that you can see the family page for a particular domain by clicking on the graphic. You can also choose to see all sequences which have a given architecture by clicking on the Show link in each row.
Finally, because some families can be found in a very large number of architectures, we load only the first fifty architectures by default. If you want to see more architectures, click the button at the bottom of the page to load the next set.
Loading domain graphics...
This family includes proteins that share the ubiquitin fold. It currently unites four SCOP superfamilies.
The clan contains the following 76 members:APG12 APG5 Atg8 AUX_IAA B1 BILBO1_N Blt1 Caps_synth_GfcC CHIPS CIDE-N Cobl CRIM DCX DIX DUF2407 DUF348 DUF4430 DWNN FERM_f0 FERM_N FERM_N_2 Flg_new Flg_new_2 Formin_GBD_N GABP-alpha IgG_binding_B Kindlin_2_N Lambda_tail_I Mub_B2 MucBP MucBP_2 Multi_ubiq NLE NQRA_SLBB Oxidored_molyb Par3_HAL_N_term PB1 Phenol_monoox PI3K_p85B PI3K_rbd Prok_Ub RA Rad60-SLD Rad60-SLD_2 Ras_bdg_2 RAWUL RBD SAP18 Sde2_N_Ubi SHIRT SLBB SSSPR-51 Staphylokinase TBK1_ULD TGS ThiS ThiS-like TmoB TUG-UBL1 Tugs Ub-Mut7C Ub-RnfH ubiquitin Ubiquitin_2 Ubiquitin_3 Ubiquitin_4 Ubiquitin_5 UBX Ufm1 ULD UN_NPL4 Urm1 USP7_C2 USP7_ICP0_bdg YchF-GTPase_C YukD
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...
There are various ways to view or download the sequence alignments that we store. We provide several sequence viewers and a plain-text Stockholm-format file for download.
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the UniProtKB sequence database using the family HMM
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
You can see the alignments as HTML or in three different sequence viewers:
- a Java applet developed at the University of Dundee. You will need Java installed before running jalview
- an HTML page showing the whole alignment.Please note: full Pfam alignments can be very large. These HTML views are extremely large and often cause problems for browsers. Please use either jalview or the Pfam viewer if you have trouble viewing the HTML version
- an HTML-based representation of the alignment, coloured according to the posterior-probability (PP) values from the HMM. As for the standard HTML view, heatmap alignments can also be very large and slow to render.
You can download (or view in your browser) a text representation of a Pfam alignment in various formats:
You can also change the order in which sequences are listed in the alignment, change how insertions are represented, alter the characters that are used to represent gaps in sequences and, finally, choose whether to download the alignment or to view it in your browser directly.
You may find that large alignments cause problems for the viewers and the reformatting tool, so we also provide all alignments in Stockholm format. You can download either the plain text alignment, or a gzipped version of it.
We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
Format an alignment
We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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...
If you find these logos useful in your own work, please consider citing the following article:
This page displays the phylogenetic tree for this family's seed alignment. 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 alignment.
Note: You can also download the data file for the tree.
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.
|Author:||Bateman A , Griffiths-Jones SR|
|Number in seed:||6|
|Number in full:||23|
|Average length of the domain:||117.70 aa|
|Average identity of full alignment:||40 %|
|Average coverage of the sequence by the domain:||70.99 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||17|
|Download:||download the raw HMM for this family|
Weight segments by...
Change the size of the sunburst
selected sequences to HMM
a FASTA-format file
- 0 sequences
- 0 species
This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the More....
This chart is a modified "sunburst" visualisation of the species tree for this family. It shows each node in the tree as a separate arc, arranged radially with the superkingdoms at the centre and the species arrayed around the outermost ring.
How the sunburst is generated
The tree is built by considering the taxonomic lineage of each sequence that has a match to this family. For each node in the resulting tree, we draw an arc in the sunburst. The radius of the arc, its distance from the root node at the centre of the sunburst, shows the taxonomic level ("superkingdom", "kingdom", etc). The length of the arc represents either the number of sequences represented at a given level, or the number of species that are found beneath the node in the tree. The weighting scheme can be changed using the sunburst controls.
In order to reduce the complexity of the representation, we reduce the number of taxonomic levels that we show. We consider only the following eight major taxonomic levels:
Colouring and labels
Segments of the tree are coloured approximately according to their superkingdom. For example, archeal branches are coloured with shades of orange, eukaryotes in shades of purple, etc. The colour assignments are shown under the sunburst controls. Where space allows, the name of the taxonomic level will be written on the arc itself.
As you move your mouse across the sunburst, the current node will be highlighted. In the top section of the controls panel we show a summary of the lineage of the currently highlighed node. If you pause over an arc, a tooltip will be shown, giving the name of the taxonomic level in the title and a summary of the number of sequences and species below that node in the tree.
Anomalies in the taxonomy tree
There are some situations that the sunburst tree cannot easily handle and for which we have work-arounds in place.
Missing taxonomic levels
Some species in the taxonomic tree may not have one or more of the main eight levels that we display. For example, Bos taurus is not assigned an order in the NCBI taxonomic tree. In such cases we mark the omitted level with, for example, "No order", in both the tooltip and the lineage summary.
Unmapped species names
The tree is built by looking at each sequence in the full alignment for the family. We take the name of the species given by UniProt and try to map that to the full taxonomic tree from NCBI. In some cases, the name chosen by UniProt does not map to any node in the NCBI tree, perhaps because the chosen name is listed as a synonym or a misspelling in the NCBI taxonomy.
So that these nodes are not simply omitted from the sunburst tree, we group them together in a separate branch (or segment of the sunburst tree). Since we cannot determine the lineage for these unmapped species, we show all levels between the superkingdom and the species as "uncategorised".
Since we reduce the species tree to only the eight main taxonomic levels, sequences that are mapped to the sub-species level in the tree would not normally be shown. Rather than leave out these species, we map them instead to their parent species. So, for example, for sequences belonging to one of the Vibrio cholerae sub-species in the NCBI taxonomy, we show them instead as belonging to the species Vibrio cholerae.
Too many species/sequences
For large species trees, you may see blank regions in the outer layers of the sunburst. These occur when there are large numbers of arcs to be drawn in a small space. If an arc is less than approximately one pixel wide, it will not be drawn and the space will be left blank. You may still be able to get some information about the species in that region by moving your mouse across the area, but since each arc will be very small, it will be difficult to accurately locate a particular species.
The tree shows the occurrence of this domain across different species. More...
We show the species tree in one of two ways. For smaller trees we try to show an interactive representation, which allows you to select specific nodes in the tree and view them as an alignment or as a set of Pfam domain graphics.
Unfortunately we have found that there are problems viewing the interactive tree when the it becomes larger than a certain limit. Furthermore, we have found that Internet Explorer can become unresponsive when viewing some trees, regardless of their size. We therefore show a text representation of the species tree when the size is above a certain limit or if you are using Internet Explorer to view the site.
If you are using IE you can still load the interactive tree by clicking the "Generate interactive tree" button, but please be aware of the potential problems that the interactive species tree can cause.
For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.
We also count the number of unique sequences on which each domain is found, which is shown in green. Note that a domain may appear multiple times on the same sequence, leading to the difference between these two numbers.
Finally, we group sequences from the same organism according to the NCBI code that is assigned by UniProt, allowing us to count the number of distinct sequences on which the domain is found. This value is shown in the pink boxes.
We use the NCBI species tree to group organisms according to their taxonomy and this forms the structure of the displayed tree. Note that in some cases the trees are too large (have too many nodes) to allow us to build an interactive tree, but in most cases you can still view the tree in a plain text, non-interactive representation. Those species which are represented in the seed alignment for this domain are highlighted.
You can use the tree controls to manipulate how the interactive tree is displayed:
- show/hide the summary boxes
- highlight species that are represented in the seed alignment
- expand/collapse the tree or expand it to a given depth
- select a sub-tree or a set of species within the tree and view them graphically or as an alignment
- save a plain text representation of the tree
Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.
There are 2 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 Staphylokinase domain has been found. There are 33 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 sequence.
Loading structure mapping...