Summary: Cdc37 Hsp90 binding domain

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Wikipedia: CDC37
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CDC37 Edit Wikipedia article

Cell division cycle 37

PDB rendering based on 1us7.

Available structures

PDB

Ortholog search: PDBe, RCSB

List of PDB id codes
1US7, 2K5B, 2W0G

Identifiers

Symbols

CDC37; P50CDC37

External IDs

OMIM: 605065 MGI: 109531 HomoloGene: 38268 ChEMBL: 1795123 GeneCards: CDC37 Gene

Gene Ontology
Molecular function	• protein binding • protein kinase binding • heat shock protein binding • unfolded protein binding • Hsp90 protein binding
Cellular component	• cytoplasm • cytosol
Biological process	• regulation of cyclin-dependent protein kinase activity • protein targeting • regulation of interferon-gamma-mediated signaling pathway • regulation of type I interferon-mediated signaling pathway
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 19:
10.5 – 10.53 Mb

Chr 9:
21.14 – 21.15 Mb

PubMed search

[1]

[2]

Cdc37 N terminal kinase binding

Identifiers

Symbol

CDC37_N

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe
PDBsum	structure summary

Cdc37 Hsp90 binding domain

complex of hsp90 and p50

Identifiers

Symbol

CDC37_M

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe
PDBsum	structure summary

Cdc37 C terminal domain

complex of hsp90 and p50

Identifiers

Symbol

CDC37_C

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe
PDBsum	structure summary

Hsp90 co-chaperone Cdc37 is a protein that in humans is encoded by the CDC37 gene.^[1]^[2]

The protein encoded by this gene is highly similar to Cdc 37, a cell division cycle control protein of Saccharomyces cerevisiae. This protein is a molecular chaperone with specific function in cell signal transduction. It has been shown to form complex with Hsp90 and a variety of protein kinases including CDK4, CDK6, SRC, RAF1, MOK, as well as eIF-2 alpha kinases. It is thought to play a critical role in directing Hsp90 to its target kinases.^[3]

[edit] Interactions

CDC37 has been shown to interact with IKBKG,^[4]^[5] IKK2,^[5] Cyclin-dependent kinase 4,^[1]^[2]^[6]^[7] Heat shock protein 90kDa alpha (cytosolic), member A1^[8]^[9] and STK11.^[10]

[edit] Domain architecture

CDC37 consists of three structural domains. The N-terminal domain binds to protein kinases.^[11] The central domain is the Hsp90 chaperone (heat shock protein 90) binding domain.^[12] The function of the C-terminal domain is unclear.

[edit] References

^ ^a ^b Dai K, Kobayashi R, Beach D (Oct 1996). "Physical interaction of mammalian CDC37 with CDK4". J Biol Chem 271 (36): 22030–4. doi:10.1074/jbc.271.36.22030. PMID 8703009.
^ ^a ^b Stepanova L, Leng X, Parker SB, Harper JW (Aug 1996). "Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4". Genes Dev 10 (12): 1491–502. doi:10.1101/gad.10.12.1491. PMID 8666233.
^ "Entrez Gene: CDC37 cell division cycle 37 homolog (S. cerevisiae)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11140.
^ Bouwmeester, Tewis; Bauch Angela, Ruffner Heinz, Angrand Pierre-Olivier, Bergamini Giovanna, Croughton Karen, Cruciat Cristina, Eberhard Dirk, Gagneur Julien, Ghidelli Sonja, Hopf Carsten, Huhse Bettina, Mangano Raffaella, Michon Anne-Marie, Schirle Markus, Schlegl Judith, Schwab Markus, Stein Martin A, Bauer Andreas, Casari Georg, Drewes Gerard, Gavin Anne-Claude, Jackson David B, Joberty Gerard, Neubauer Gitte, Rick Jens, Kuster Bernhard, Superti-Furga Giulio (Feb. 2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. (England) 6 (2): 97–105. doi:10.1038/ncb1086. ISSN 1465-7392. PMID 14743216.
^ ^a ^b Chen, Guoqing; Cao Ping, Goeddel David V (Feb. 2002). "TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90". Mol. Cell (United States) 9 (2): 401–10. doi:10.1016/S1097-2765(02)00450-1. ISSN 1097-2765. PMID 11864612.
^ Ewing, Rob M; Chu Peter, Elisma Fred, Li Hongyan, Taylor Paul, Climie Shane, McBroom-Cerajewski Linda, Robinson Mark D, O'Connor Liam, Li Michael, Taylor Rod, Dharsee Moyez, Ho Yuen, Heilbut Adrian, Moore Lynda, Zhang Shudong, Ornatsky Olga, Bukhman Yury V, Ethier Martin, Sheng Yinglun, Vasilescu Julian, Abu-Farha Mohamed, Lambert Jean-Philippe, Duewel Henry S, Stewart Ian I, Kuehl Bonnie, Hogue Kelly, Colwill Karen, Gladwish Katharine, Muskat Brenda, Kinach Robert, Adams Sally-Lin, Moran Michael F, Morin Gregg B, Topaloglou Thodoros, Figeys Daniel (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. (England) 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1847948/.
^ Lamphere, L; Fiore F, Xu X, Brizuela L, Keezer S, Sardet C, Draetta G F, Gyuris J (Apr. 1997). "Interaction between Cdc37 and Cdk4 in human cells". Oncogene (ENGLAND) 14 (16): 1999–2004. doi:10.1038/sj.onc.1201036. ISSN 0950-9232. PMID 9150368.
^ Roe, S Mark; Ali Maruf M U, Meyer Philippe, Vaughan Cara K, Panaretou Barry, Piper Peter W, Prodromou Chrisostomos, Pearl Laurence H (Jan. 2004). "The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)". Cell (United States) 116 (1): 87–98. doi:10.1016/S0092-8674(03)01027-4. ISSN 0092-8674. PMID 14718169.
^ Silverstein, A M; Grammatikakis N, Cochran B H, Chinkers M, Pratt W B (Aug. 1998). "p50(cdc37) binds directly to the catalytic domain of Raf as well as to a site on hsp90 that is topologically adjacent to the tetratricopeptide repeat binding site". J. Biol. Chem. (UNITED STATES) 273 (32): 20090–5. doi:10.1074/jbc.273.32.20090. ISSN 0021-9258. PMID 9685350.
^ Boudeau, Jérôme; Deak Maria, Lawlor Margaret A, Morrice Nick A, Alessi Dario R (Mar. 2003). "Heat-shock protein 90 and Cdc37 interact with LKB1 and regulate its stability". Biochem. J. (England) 370 (Pt 3): 849–57. doi:10.1042/BJ20021813. ISSN 0264-6021. PMC 1223241. PMID 12489981. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1223241/.
^ Kimura Y, Rutherford SL, Miyata Y, Yahara I, Freeman BC, Yue L, Morimoto RI, Lindquist S (July 1997). "Cdc37 is a molecular chaperone with specific functions in signal transduction". Genes Dev. 11 (14): 1775–85. doi:10.1101/gad.11.14.1775. PMID 9242486.
^ Turnbull EL, Martin IV, Fantes PA (August 2005). "Cdc37 maintains cellular viability in Schizosaccharomyces pombe independently of interactions with heat-shock protein 90". FEBS J. 272 (16): 4129–40. doi:10.1111/j.1742-4658.2005.04825.x. PMID 16098195.

[edit] Further reading

Dey B, Lightbody JJ, Boschelli F (1997). "CDC37 is required for p60v-src activity in yeast.". Mol. Biol. Cell 7 (9): 1405–17. PMC 275990. PMID 8885235. //www.ncbi.nlm.nih.gov/pmc/articles/PMC275990/.
Lamphere L, Fiore F, Xu X, et al. (1997). "Interaction between Cdc37 and Cdk4 in human cells.". Oncogene 14 (16): 1999–2004. doi:10.1038/sj.onc.1201036. PMID 9150368.
Kimura Y, Rutherford SL, Miyata Y, et al. (1997). "Cdc37 is a molecular chaperone with specific functions in signal transduction.". Genes Dev. 11 (14): 1775–85. doi:10.1101/gad.11.14.1775. PMID 9242486.
Silverstein AM, Grammatikakis N, Cochran BH, et al. (1998). "p50(cdc37) binds directly to the catalytic domain of Raf as well as to a site on hsp90 that is topologically adjacent to the tetratricopeptide repeat binding site.". J. Biol. Chem. 273 (32): 20090–5. doi:10.1074/jbc.273.32.20090. PMID 9685350.
Grammatikakis N, Lin JH, Grammatikakis A, et al. (1999). "p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function.". Mol. Cell. Biol. 19 (3): 1661–72. PMC 83960. PMID 10022854. //www.ncbi.nlm.nih.gov/pmc/articles/PMC83960/.
O'Keeffe B, Fong Y, Chen D, et al. (2000). "Requirement for a kinase-specific chaperone pathway in the production of a Cdk9/cyclin T1 heterodimer responsible for P-TEFb-mediated tat stimulation of HIV-1 transcription.". J. Biol. Chem. 275 (1): 279–87. doi:10.1074/jbc.275.1.279. PMID 10617616.
Hartson SD, Irwin AD, Shao J, et al. (2000). "p50(cdc37) is a nonexclusive Hsp90 cohort which participates intimately in Hsp90-mediated folding of immature kinase molecules.". Biochemistry 39 (25): 7631–44. doi:10.1021/bi000315r. PMID 10858314.
Shao J, Grammatikakis N, Scroggins BT, et al. (2001). "Hsp90 regulates p50(cdc37) function during the biogenesis of the activeconformation of the heme-regulated eIF2 alpha kinase.". J. Biol. Chem. 276 (1): 206–14. doi:10.1074/jbc.M007583200. PMID 11036079.
Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination.". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863. //www.ncbi.nlm.nih.gov/pmc/articles/PMC310948/.
Rao J, Lee P, Benzeno S, et al. (2001). "Functional interaction of human Cdc37 with the androgen receptor but not with the glucocorticoid receptor.". J. Biol. Chem. 276 (8): 5814–20. doi:10.1074/jbc.M007385200. PMID 11085988.
Simpson JC, Wellenreuther R, Poustka A, et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing.". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC 1083732. PMID 11256614. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1083732/.
Scholz GM, Cartledge K, Hall NE (2001). "Identification and characterization of Harc, a novel Hsp90-associating relative of Cdc37.". J. Biol. Chem. 276 (33): 30971–9. doi:10.1074/jbc.M103889200. PMID 11413142.
Chen G, Cao P, Goeddel DV (2002). "TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90.". Mol. Cell 9 (2): 401–10. doi:10.1016/S1097-2765(02)00450-1. PMID 11864612.
Siligardi G, Panaretou B, Meyer P, et al. (2002). "Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37.". J. Biol. Chem. 277 (23): 20151–9. doi:10.1074/jbc.M201287200. PMID 11916974.
Basso AD, Solit DB, Chiosis G, et al. (2002). "Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function.". J. Biol. Chem. 277 (42): 39858–66. doi:10.1074/jbc.M206322200. PMID 12176997.
Abbas-Terki T, Briand PA, Donzé O, Picard D (2003). "The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.". Biol. Chem. 383 (9): 1335–42. doi:10.1515/BC.2002.152. PMID 12437126.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. //www.ncbi.nlm.nih.gov/pmc/articles/PMC139241/.
Boudeau J, Deak M, Lawlor MA, et al. (2003). "Heat-shock protein 90 and Cdc37 interact with LKB1 and regulate its stability.". Biochem. J. 370 (Pt 3): 849–57. doi:10.1042/BJ20021813. PMC 1223241. PMID 12489981. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1223241/.

PDB gallery

1us7: COMPLEX OF HSP90 AND P50

This article incorporates text from the public domain Pfam and InterPro IPR013855

This article incorporates text from the public domain Pfam and InterPro IPR013874

This article incorporates text from the public domain Pfam and InterPro IPR013873

This article on a gene on chromosome 19 is a stub. You can help Wikipedia by expanding it.

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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.

Cdc37 Hsp90 binding domain Provide feedback

Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domains corresponds to the Hsp90 chaperone (Heat shocked protein 90) binding domain of Cdc37 [2]. It is found between the N terminal Cdc37 domain PF03234 which is predominantly involved in kinase binding, and the C terminal domain of Cdc37 PF08564 whose function is unclear.

Literature references

Kimura Y, Rutherford SL, Miyata Y, Yahara I, Freeman BC, Yue L, Morimoto RI, Lindquist S; , Genes Dev 1997;11:1775-1785.: Cdc37 is a molecular chaperone with specific functions in signal transduction. PUBMED:9242486 EPMC:9242486
Turnbull EL, Martin IV, Fantes PA; , FEBS J 2005;272:4129-4140.: Cdc37 maintains cellular viability in Schizosaccharomyces pombe independently of interactions with heat-shock protein 90. PUBMED:16098195 EPMC:16098195

External database links

PANDIT:	PF08565
Pseudofam:	PF08565
SCOP:	1us7
SYSTERS:	CDC37_M

This tab holds annotation information from the InterPro database.

InterPro entry IPR013874

Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This entry corresponds to the Hsp90 chaperone (heat shock protein 90) binding domain of Cdc37 [PUBMED:16098195]. It is found between the N-terminal Cdc37 domain (INTERPRO), which is predominantly involved in kinase binding, and the C-terminal domain of Cdc37 (INTERPRO) whose function is unclear.

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

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 using the family HMM. We also generate alignments using four representative proteomes (RP) sets, 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.

Alignment types

We make a range of alignments for each Pfam-A family:

seed: the curated alignment from which the HMM for the family is built
full: the alignment generated by searching the sequence database using the HMM
RP15/RP35/RP55/RP75: Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
NCBI: alignment generated by searching the NCBI sequence database using the family HMM
meta: alignment generated by searching the metagenomics sequence database using the family HMM

Viewing

You can see the alignments as HTML or in three different sequence viewers:

jalview: a Java applet developed at the University of Dundee. You will need Java installed before running jalview
HTML: 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
PP/Heatmap: 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.
Pfam viewer: an HTML-based viewer that uses DAS to retrieve alignment fragments on request

Reformatting

You can download (or view in your browser) a text representation of a Pfam alignment in various formats:

Selex
Stockholm
FASTA
MSF

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.

Downloading

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.

View options

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.

	Seed (19)	Full (361)	Representative proteomes				NCBI (346)	Meta (3)
	Seed (19)	Full (361)	RP15 (65)	RP35 (105)	RP55 (170)	RP75 (220)	NCBI (346)	Meta (3)
Jalview	View	View	View	View	View	View	View	View
HTML	View	View	View	View	View	View
PP/heatmap	₁	View	View	View	View	View
Pfam viewer	View	View

¹Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: available, not generated, — not available.

Format an alignment

	Seed (19)	Full (361)	Representative proteomes				NCBI (346)	Meta (3)
	Seed (19)	Full (361)	RP15 (65)	RP35 (105)	RP55 (170)	RP75 (220)	NCBI (346)	Meta (3)
Alignment:
Format:
Order:	Tree Alphabetical
Sequence:	Inserts lower case All upper case
Gaps:
Download/view:	Download View

Download options

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.

	Seed (19)	Full (361)	Representative proteomes				NCBI (346)	Meta (3)
	Seed (19)	Full (361)	RP15 (65)	RP35 (105)	RP55 (170)	RP75 (220)	NCBI (346)	Meta (3)
Raw Stockholm	Download	Download	Download	Download	Download	Download	Download	Download
Gzipped	Download	Download	Download	Download	Download	Download	Download	Download

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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 HMMER3.

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'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.

Curation

Seed source:

Pfam-B_3345 (release 6.5)

Previous IDs:

Cdc37;

Type:

Domain

Author:

Bateman A, Mistry J, Wood V

Number in seed:

19

Number in full:

361

Average length of the domain:

181.10 aa

Average identity of full alignment:

27 %

Average coverage of the sequence by the domain:

44.13 %

HMM information

HMM build commands:

build method: hmmbuild -o /dev/null HMM SEED

search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq

Model details:

Parameter	Sequence	Domain
Gathering cut-off	25.0	25.0
Trusted cut-off	26.3	25.1
Noise cut-off	22.8	24.1

Model length:

173

Family (HMM) version:

6

Download:

download the raw HMM for this family

Species distribution

Sunburst
Tree

Sunburst controls

Show

This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. 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:

superkingdom
kingdom
phylum
class
order
family
genus
species

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".

Sub-species

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.

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Tree controls

Hide

The tree shows the occurrence of this domain across different species. More...

Species trees

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.

Interactive tree

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
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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 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 CDC37_M domain has been found. There are 3 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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Archea	Eukaryota
Bacteria	Other sequences
Viruses	Unclassified
Viroids	Unclassified sequence

Family: CDC37_M (PF08565)

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Summary: Cdc37 Hsp90 binding domain

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Cdc37 Hsp90 binding domain Provide feedback

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InterPro entry IPR013874

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