Summary: Haemadin
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Haemadin Edit Wikipedia article
| Haemadin | |||||||||
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crystal structure of the human alpha-thrombin-haemadin complex: an exosite ii-binding inhibitor |
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| Identifiers | |||||||||
| Symbol | Haemadin | ||||||||
| Pfam | PF09065 | ||||||||
| InterPro | IPR015150 | ||||||||
| SCOP | 1e0f | ||||||||
| SUPERFAMILY | 1e0f | ||||||||
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In molecular biology, haemadin is an anticoagulant peptide synthesised by the Indian leech, Haemadipsa sylvestris. It adopts a secondary structure consisting of five short beta-strands (beta1-beta5), which are arranged in two antiparallel distorted sheets formed by strands beta1-beta4-beta5 and beta2-beta3 facing each other. This beta-sandwich is stabilised by six enclosed cysteines arranged in a [1-2, 3-5, 4-6] disulfide pairing resulting in a disulfide-rich hydrophobic core that is largely inaccessible to bulk solvent. The close proximity of disulfide bonds [3-5] and [4-6] organises haemadin into four distinct loops. The N-terminal segment of this domain binds to the active site of thrombin, inhibiting it.[1]
[edit] References
- ^ Richardson JL, Kroger B, Hoeffken W, Sadler JE, Pereira P, Huber R, Bode W, Fuentes-Prior P (November 2000). "Crystal structure of the human alpha-thrombin-haemadin complex: an exosite II-binding inhibitor". EMBO J. 19 (21): 5650–60. doi:10.1093/emboj/19.21.5650. PMC 305786. PMID 11060016.
This article incorporates text from the public domain Pfam and InterPro IPR015150
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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.
Haemadin Provide feedback
Members of this family adopt a secondary structure consisting of five short beta-strands (beta1-beta5), which are arranged in two antiparallel distorted sheets formed by strands beta1-beta4-beta5 and beta2-beta3 facing each other. This beta-sandwich is stabilised by six enclosed cysteines arranged in a [1-2, 3-5, 4-6] disulphide pairing resulting in a disulphide-rich hydrophobic core that is largely inaccessible to bulk solvent. The close proximity of disulfide bonds [3-5] and [4-6] organises haemadin into four distinct loops. The N-terminal segment of this domain binds to the active site of thrombin, inhibiting it [1].
Literature references
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Richardson JL, Kroger B, Hoeffken W, Sadler JE, Pereira P, Huber R, Bode W, Fuentes-Prior P; , EMBO J. 2000;19:5650-5660.: Crystal structure of the human alpha-thrombin-haemadin complex: an exosite II-binding inhibitor. PUBMED:11060016 EPMC:11060016
External database links
| PANDIT: | PF09065 |
| Pseudofam: | PF09065 |
| SCOP: | 1e0f |
| SYSTERS: | Haemadin |
This tab holds annotation information from the InterPro database.
InterPro entry IPR015150
Members of this family adopt a secondary structure consisting of five short beta-strands (beta1-beta5), which are arranged in two antiparallel distorted sheets formed by strands beta1-beta4-beta5 and beta2-beta3 facing each other. This beta-sandwich is stabilised by six enclosed cysteines arranged in a [1-2, 3-5, 4-6] disulphide pairing resulting in a disulphide-rich hydrophobic core that is largely inaccessible to bulk solvent. The close proximity of disulphide bonds [3-5] and [4-6] organises haemadin into four distinct loops. The N-terminal segment of this domain binds to the active site of thrombin, inhibiting it [PUBMED:11060016].
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...
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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 (2) |
Full (2) |
Representative proteomes | NCBI (3) |
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| RP15 (0) |
RP35 (0) |
RP55 (0) |
RP75 (0) |
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| PP/heatmap | 1 | |||||||
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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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 (2) |
Full (2) |
Representative proteomes | NCBI (3) |
Meta (0) |
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| RP15 (0) |
RP35 (0) |
RP55 (0) |
RP75 (0) |
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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: | pdb_1e0f |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Sammut SJ |
| Number in seed: | 2 |
| Number in full: | 2 |
| Average length of the domain: | 27.00 aa |
| Average identity of full alignment: | 100 % |
| Average coverage of the sequence by the domain: | 46.55 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 27 | ||||||||||||
| Family (HMM) version: | 5 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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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 Haemadin 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