Please note: this site relies heavily on the use of javascript. Without a javascript-enabled browser, this site will not function correctly. Please enable javascript and reload the page, or switch to a different browser.
5  structures 61  species 0  interactions 1108  sequences 1  architecture

Family: HDV_ag (PF01517)

Summary: Hepatitis delta virus delta antigen

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 "Hepatitis D". More...

Hepatitis D Edit Wikipedia article

Hepatitis D
Virus classification
Group: Group V ((-)ssRNA)
Order: Unassigned
Family: Unassigned
Genus: Deltavirus
Species: Hepatitis delta virus
Hepatitis D
Classification and external resources
ICD-10 B17.0, B18.0
ICD-9 070.31
DiseasesDB 5792
MeSH D003699

Hepatitis D, also referred to as hepatitis D virus (HDV) and classified as Hepatitis delta virus, is a disease caused by a small circular enveloped RNA virus. It is one of five known hepatitis viruses: A, B, C, D, and E. HDV is considered to be a subviral satellite because it can propagate only in the presence of the hepatitis B virus (HBV).[1] Transmission of HDV can occur either via simultaneous infection with HBV (coinfection) or superimposed on chronic hepatitis B or hepatitis B carrier state (superinfection).

Both superinfection and coinfection with HDV results in more severe complications compared to infection with HBV alone. These complications include a greater likelihood of experiencing liver failure in acute infections and a rapid progression to liver cirrhosis, with an increased chance of developing liver cancer in chronic infections.[2] In combination with hepatitis B virus, hepatitis D has the highest mortality rate of all the hepatitis infections, at 20%.



Hepatitis D virus was first reported in the mid-1977 as a nuclear antigen in patients infected with HBV who had severe liver disease[3] This nuclear antigen was then thought to be a hepatitis B antigen and was called the delta antigen. Subsequent experiments in chimpanzees showed that the hepatitis delta antigen (HDAg) was a structural part of a pathogen that required HBV infection to replicate[4] The entire genome was cloned and sequenced in 1986. It was subsequently placed in its own genus: Deltavirus.[5][6]

Structure and genome[edit]

Hepatitis delta virus delta antigen
PDB 1a92 EBI.jpg
oligomerization domain of hepatitis delta antigen
Symbol HDV_ag
Pfam PF01517
InterPro IPR002506
SCOP 1a92

The HDV is a small, spherical virus with a 36 nm diameter. It has an outer coat containing three HBV envelope proteins (called large, medium, and small hepatitis B surface antigens), and host lipids surrounding an inner nucleocapsid. The nucleocapsid contains single-stranded, circular RNA of 1679 nucleotides and about 200 molecules of hepatitis D antigen (HDAg) for each genome. The central region of HDAg has been shown to bind RNA.[7] Several interactions are also mediated by a coiled-coil region at the N terminus of HDAg.[8] The hepatitis D circular genome is unique to animal viruses because of its high GC nucleotide content. The HDV genome exists as an enveloped, negative sense, single-stranded, closed circular RNA. Its nucleotide sequence is 70% self-complementary, allowing the genome to form a partially double-stranded, rod-like RNA structure.[9] With a genome of approximately 1700 nucleotides, HDV is the smallest "virus" known to infect animals. It has been proposed that HDV may have originated from a class of plant pathogens called viroids, which are much smaller than viruses.[10][11]

Life cycle[edit]

The receptor that HDV recognizes on human hepatocytes has not been identified; however it is thought to be the same as the HBV receptor because both viruses have the same outer coat.[12] HDV recognizes its receptor via the N-terminal domain of the large hepatitis B surface antigen, HBsAg.[13] Mapping by mutagenesis of this domain has shown that amino acid residues 9–15 make up the receptor binding site.[14] After entering the hepatocyte, the virus is uncoated and the nucleocapsid translocated to the nucleus due to a signal in HDAg[15] Since the nucleocapsid does not contain an RNA polymerase to replicate the virus’ genome, the virus makes use of the cellular RNA polymerases. Initially just RNA pol II,[16][17] now RNA polymerases I and III have also been shown to be involved in HDV replication[18] Normally RNA polymerase II utilizes DNA as a template and produces mRNA. Consequently, if HDV indeed utilizes RNA polymerase II during replication, it would be the only known animal pathogen capable of using a DNA-dependent polymerase as an RNA-dependent polymerase.

The RNA polymerases treat the RNA genome as double stranded DNA due to the folded rod-like structure it is in. Three forms of RNA are made; circular genomic RNA, circular complementary antigenomic RNA, and a linear polyadenylated antigenomic RNA, which is the mRNA containing the open reading frame for the HDAg. Synthesis of antigenomic RNA occurs in the nucleolus, mediated by RNA Pol I, whereas synthesis of genomic RNA takes place in the nucleoplasm, mediated by RNA Pol II.[19] HDV RNA is synthesized first as linear RNA that contains many copies of the genome. The genomic and antigenomic RNA contain a sequence of 85 nucleotides, the Hepatitis delta virus ribozyme, that acts as a ribozyme, which self-cleaves the linear RNA into monomers. These monomers are then ligated to form circular RNA.[20][21]

There are eight reported genotypes of HDV with unexplained variations in their geographical distribution and pathogenicity.

Delta antigens[edit]

A significant difference between viroids and HDV is that, while viroids produce no proteins, HDV is known to produce one protein, namely HDAg. It comes in two forms; a 27kDa large-HDAg, and a small-HDAg of 24kDa. The N-terminals of the two forms are identical, they differ by 19 more amino acids in the C-terminal of the large HDAg.[22] Both isoforms are produced from the same reading frame which contains an UAG stop codon at codon 196, which normally produces only the small-HDAg. However, editing by cellular enzyme adenosine deaminase-1 changes the stop codon to UCG, allowing the large-HDAg to be produced.[22][23] Despite having 90% identical sequences, these two proteins play diverging roles during the course of an infection. HDAg-S is produced in the early stages of an infection and enters the nucleus and supports viral replication. HDAg-L, in contrast, is produced during the later stages of an infection, acts as an inhibitor of viral replication, and is required for assembly of viral particles.[24][25][26] Thus RNA editing by the cellular enzymes is critical to the virus’ life cycle because it regulates the balance between viral replication and virion assembly.


The routes of transmission of hepatitis D are similar to those for hepatitis B. Infection is largely restricted to persons at high risk of hepatitis B infection, particularly injecting drug users and persons receiving clotting factor concentrates. Worldwide more than 15 million people are co-infected. HDV is rare in most developed countries, and is mostly associated with intravenous drug use. However, HDV is much more common in the immediate Mediterranean region, sub-Saharan Africa, the Middle East, and the northern part of South America.[27] In all, about 20 million people may be infected with HDV.[28]

Treatment and prevention[edit]

The vaccine for hepatitis B protects against hepatitis D virus because of the latter's dependence on the presence of hepatitis B virus for it to replicate.[29][30]

Low quality evidence suggests that interferon alpha can be effective in reducing the severity of the infection and the effect of the disease during the time the drug is given, but the benefit generally stops when the drug is discontinued, indicating that it does not cure the disease.[31] Interferon is effective only in ~20% of cases.[32]


Three genotypes (I–III) were originally described. Genotype I has been isolated in Europe, North America, Africa and some Asia. Genotype II has been found in Japan, Taiwan, and Yakutia (Russia). Genotype III has been found exclusively in South America (Peru, Colombia, and Venezuela). Some genomes from Taiwan and the Okinawa islands have been difficult to type but have been placed in genotype 2. However it is now known that there are at least 8 genotypes of this virus (HDV-1 to HDV-8).[33] Phylogenetic studies suggest an African origin for this pathogen.[34]

An analysis of 36 strains of genotype 3 estimated that the most recent common ancestor of these strains originated around 1930.[35] This genotype spread exponentially from early 1950s to the 1970s in South America. The substitution rate was estimated to be 1.07×10−3 substitutions per site per year.

Genotype 8 has also been isolated from South America. This genotype is usually only found in Africa and may have been imported into South America during the slave trade.[36]

Genotypes, with the exception of type 1, appear to be restricted to certain geographical areas: HDV-2 (previously HDV-IIa) is found in Japan, Taiwan and Yakoutia, Russia; HDV-4 (previously HDV-IIb) in Japan and Taiwan; HDV-3 in the Amazonian region; HDV-5, HDV-6, HDV-7 and HDV-8 in Africa.[37]

See also[edit]


  1. ^ Makino S, Chang MF, Shieh CK et al. (1987). "Molecular cloning and sequencing of a human hepatitis delta (delta) virus RNA". Nature 329 (6137): 343–6. doi:10.1038/329343a0. PMID 3627276. 
  2. ^ Fattovich G, Giustina G, Christensen E et al. (March 2000). "Influence of hepatitis delta virus infection on morbidity and mortality in compensated cirrhosis type B". Gut 46 (3): 420–6. doi:10.1136/gut.46.3.420. PMC 1727859. PMID 10673308. 
  3. ^ Rizzetto, M; Canese MG, Arico S, Criello O, Trepo C, Bonino F, Verme G (1977). "Immunofluorescence detection of new antigen-antibody system (delta/anti-delta) associated to hepatitis B virus in liver and in serum of HBsAg carriers". Gut 18 (12): 997–1003. doi:10.1136/gut.18.12.997. PMC 1411847. PMID 75123. 
  4. ^ Rizzetto, M; Canese, MG, Purcell, RH, London, WT, Sly, LD, Gerin, JL (1981 Nov–Dec). "Experimental HBV and delta infections of chimpanzees: occurrence and significance of intrahepatic immune complexes of HBcAg and delta antigen". Hepatology (Baltimore, Md.) 1 (6): 567–74. doi:10.1002/hep.1840010602. PMID 7030907. 
  5. ^ Wang, KS; Choo, QL, Weiner, AJ, Ou, JH, Najarian, RC, Thayer, RM, Mullenbach, GT, Denniston, KJ, Gerin, JL, Houghton, M (1986 Oct 9–15). "Structure, sequence and expression of the hepatitis delta (delta) viral genome". Nature 323 (6088): 508–14. doi:10.1038/323508a0. PMID 3762705. 
  6. ^ Fauquet, CM; Mayo MA, Maniloff J, Desselberger U, Ball LA (2005). "Deltavirus". Eight Report of the International Committee on Taxonomy of Viruses. London: 735–8. 
  7. ^ Poisson F, Roingeard P, Baillou A, Dubois F, Bonelli F, Calogero RA, Goudeau A (November 1993). "Characterization of RNA-binding domains of hepatitis delta antigen". J. Gen. Virol. 74 (Pt 11): 2473–8. doi:10.1099/0022-1317-74-11-2473. PMID 8245865. 
  8. ^ Zuccola HJ, Rozzelle JE, Lemon SM, Erickson BW, Hogle JM (July 1998). "Structural basis of the oligomerization of hepatitis delta antigen". Structure 6 (7): 821–30. doi:10.1016/S0969-2126(98)00084-7. PMID 9687364. 
  9. ^ Saldanha JA, Thomas HC, Monjardino JP (July 1990). "Cloning and sequencing of RNA of hepatitis delta virus isolated from human serum". J. Gen. Virol. 71 (7): 1603–6. doi:10.1099/0022-1317-71-7-1603. PMID 2374010. 
  10. ^ Elena SF, Dopazo J, Flores R, Diener TO, Moya A (July 1991). "Phylogeny of viroids, viroidlike satellite RNAs, and the viroidlike domain of hepatitis delta virus RNA". Proc. Natl. Acad. Sci. U.S.A. 88 (13): 5631–4. doi:10.1073/pnas.88.13.5631. PMC 51931. PMID 1712103. 
  11. ^ Sureau, C (2006). "The role of the HBV envelope proteins in the HDV replication cycle". Current topics in microbiology and immunology. Current Topics in Microbiology and Immunology 307: 113–31. doi:10.1007/3-540-29802-9_6. ISBN 978-3-540-29801-4. PMID 16903223. 
  12. ^ Barrera, A; Guerra, B, Notvall, L, Lanford, RE (August 2005). "Mapping of the Hepatitis B Virus Pre-S1 Domain Involved in Receptor Recognition". Journal of Virology 79 (15): 9786–98. doi:10.1128/JVI.79.15.9786-9798.2005. PMC 1181564. PMID 16014940. 
  13. ^ Engelke, M; Mills, K, Seitz, S, Simon, P, Gripon, P, Schnölzer, M, Urban, S (April 2006). "Characterization of a hepatitis B and hepatitis delta virus receptor binding site". Hepatology (Baltimore, Md.) 43 (4): 750–60. doi:10.1002/hep.21112. PMID 16557545. 
  14. ^ Schulze, A; Schieck, A, Ni, Y, Mier, W, Urban, S (February 2010). "Fine Mapping of Pre-S Sequence Requirements for Hepatitis B Virus Large Envelope Protein-Mediated Receptor Interaction". Journal of Virology 84 (4): 1989–2000. doi:10.1128/JVI.01902-09. PMC 2812397. PMID 20007265. 
  15. ^ Xia, YP; Yeh, CT, Ou, JH, Lai, MM (February 1992). "Characterization of nuclear targeting signal of hepatitis delta antigen: nuclear transport as a protein complex". Journal of Virology 66 (2): 914–21. PMC 240792. PMID 1731113. 
  16. ^ Lehmann E, Brueckner F, Cramer P (November 2007). "Molecular basis of RNA-dependent RNA polymerase II activity". Nature 450 (7168): 445–9. doi:10.1038/nature06290. PMID 18004386. 
  17. ^ Filipovska J, Konarska MM (January 2000). "Specific HDV RNA-templated transcription by pol II in vitro". RNA 6 (1): 41–54. doi:10.1017/S1355838200991167. PMC 1369892. PMID 10668797. 
  18. ^ Greco-Stewart, VS; Schissel, E, Pelchat, M (2009-03-30). "The hepatitis delta virus RNA genome interacts with the human RNA polymerases I and III". Virology 386 (1): 12–5. doi:10.1016/j.virol.2009.02.007. PMID 19246067. 
  19. ^ Li, YJ; Macnaughton, T, Gao, L, Lai, MM (July 2006). "RNA-Templated Replication of Hepatitis Delta Virus: Genomic and Antigenomic RNAs Associate with Different Nuclear Bodies". Journal of Virology 80 (13): 6478–86. doi:10.1128/JVI.02650-05. PMC 1488965. PMID 16775335. 
  20. ^ Branch, AD; Benenfeld, BJ, Baroudy, BM, Wells, FV, Gerin, JL, Robertson, HD (1989-02-03). "An ultraviolet-sensitive RNA structural element in a viroid-like domain of the hepatitis delta virus". Science 243 (4891): 649–52. doi:10.1126/science.2492676. PMID 2492676. 
  21. ^ Wu, HN; Lin, YJ, Lin, FP, Makino, S, Chang, MF, Lai, MM (March 1989). "Human hepatitis delta virus RNA subfragments contain an autocleavage activity". Proceedings of the National Academy of Sciences of the United States of America 86 (6): 1831–5. doi:10.1073/pnas.86.6.1831. PMC 286798. PMID 2648383. 
  22. ^ a b Weiner, AJ; Choo, QL, Wang, KS, Govindarajan, S, Redeker, AG, Gerin, JL, Houghton, M (February 1988). "A single antigenomic open reading frame of the hepatitis delta virus encodes the epitope(s) of both hepatitis delta antigen polypeptides p24 delta and p27 delta". Journal of Virology 62 (2): 594–9. PMC 250573. PMID 2447291. 
  23. ^ Jayan, GC; Casey, JL (December 2002). "Inhibition of Hepatitis Delta Virus RNA Editing by Short Inhibitory RNA-Mediated Knockdown of ADAR1 but Not ADAR2 Expression". Journal of Virology 76 (23): 12399–404. doi:10.1128/JVI.76.23.12399-12404.2002. PMC 136899. PMID 12414985. 
  24. ^ Sato S, Cornillez-Ty C, Lazinski DW (August 2004). "By Inhibiting Replication, the Large Hepatitis Delta Antigen Can Indirectly Regulate Amber/W Editing and Its Own Expression". J. Virol. 78 (15): 8120–34. doi:10.1128/JVI.78.15.8120-8134.2004. PMC 446097. PMID 15254184. 
  25. ^ Taylor, JM (2006). "Structure and replication of hepatitis delta virus RNA". Current topics in microbiology and immunology. Current Topics in Microbiology and Immunology 307: 1–23. doi:10.1007/3-540-29802-9_1. ISBN 978-3-540-29801-4. PMID 16903218. 
  26. ^ Chang, MF; Chen, CJ, Chang, SC (February 1994). "Mutational analysis of delta antigen: effect on assembly and replication of hepatitis delta virus". Journal of Virology 68 (2): 646–53. PMC 236498. PMID 8289368. 
  27. ^ Radjef N, Gordien E, Ivaniushina V et al. (March 2004). "Molecular Phylogenetic Analyses Indicate a Wide and Ancient Radiation of African Hepatitis Delta Virus, Suggesting a Deltavirus Genus of at Least Seven Major Clades". J. Virol. 78 (5): 2537–44. doi:10.1128/JVI.78.5.2537-2544.2004. PMC 369207. PMID 14963156. 
  28. ^ Taylor JM (January 2006). "Hepatitis delta virus". Virology 344 (1): 71–6. doi:10.1016/j.virol.2005.09.033. PMID 16364738. 
  29. ^ U.S. National Library of Medicine "Delta Agent (hepatitis D)"
  30. ^ Tayor, J. M. (2009). Desk Encyclopedia of Human and Medical Virology. Boston: Academic Press. p. 121. ISBN 0-12-375147-0. 
  31. ^ Abbas, Z.; Khan, MA.; Salih, M.; Jafri, W. (2011). "Interferon alpha for chronic hepatitis D". In Abbas, Zaigham. Cochrane Database Syst Rev (12): CD006002. doi:10.1002/14651858.CD006002.pub2. PMID 22161394. 
  32. ^ Pascarella S, Negro F (2011) Hepatitis D virus: an update. Liver Int 31(1):7-21 doi: 10.1111/j.1478-3231.2010.02320.x.
  33. ^ Celik I, Karataylı E, Cevik E, et al. (December 2011). "Complete genome sequences and phylogenetic analysis of hepatitis delta viruses isolated from nine Turkish patients". Arch. Virol. 156 (12): 2215–20. doi:10.1007/s00705-011-1120-y. PMID 21984217. 
  34. ^ Radjef, N.; Gordien, E.; Ivaniushina, V.; Gault, E.; Anaïs, P.; Drugan, T.; Trinchet, J. C; Roulot, D.; Tamby, M.; Milinkovitch, M. C.; Dény, P. (2004). "Molecular phylogenetic analyses indicate a wide and ancient radiation of African hepatitis delta virus, suggesting a deltavirus genus of at least seven major clades". J Virol 78 (5): 2537–44. doi:10.1128/JVI.78.5.2537-2544.2004. PMC 369207. PMID 14963156. 
  35. ^ Alvarado-Mora, M. V.; Romano, C. M.; Gomes-Gouvêa, M. S.; Gutierrez, M. F.; Carrilho, F. J.; Pinho, J. R. (2011). "Dynamics of hepatitis D (delta) virus genotype 3 in the Amazon region of South America". Infect Genet Evol (Elsevier) 11 (6): 1462–8. doi:10.1016/j.meegid.2011.05.020. PMID 21645647. 
  36. ^ Barros, L. M.; Gomes-Gouvêa, M. S.; Pinho, J. R.; Alvarado-Mora, M. V.; Dos Santos, A.; Mendes-Corrêa, M. C.; Caldas, A. J.; Sousa, M. T.; Santos, M. D.; Ferreira, A. S. (2011). "Hepatitis Delta virus genotype 8 infection in Northeast Brazil: inheritance from African slaves?". Virus Res 160 (1–2): 333–9. doi:10.1016/j.virusres.2011.07.006. PMID 21798297. 
  37. ^ Le Gal, F.; Gault, E.; Ripault, M. P.; Serpaggi, J.; Trinchet, J. C.; Gordien, E.; Dény, P. (2006). "Eighth Major Clade for Hepatitis Delta Virus". Emerg Infect Dis 12 (9): 1447–50. doi:10.3201/eid1209.060112. PMC 3294742. PMID 17073101. 

External links[edit]

This article incorporates text from the public domain Pfam and InterPro IPR002506

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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.

Hepatitis delta virus delta antigen Provide feedback

The hepatitis delta virus (HDV) encodes a single protein, the hepatitis delta antigen (HDAg). The central region of this protein has been shown to bind RNA [1]. Several interactions are also mediated by a coiled-coil region at the N terminus of the protein [2].

Literature references

  1. Poisson F, Roingeard P, Baillou A, Dubois F, Bonelli F, Calogero RA, Goudeau A; , J Gen Virol 1993;74:2473-2478.: Characterization of RNA-binding domains of hepatitis delta antigen. PUBMED:8245865 EPMC:8245865

  2. Zuccola HJ, Rozzelle JE, Lemon SM, Erickson BW, Hogle JM; , Structure 1998;6:821-830.: Structural basis of the oligomerization of hepatitis delta antigen. PUBMED:9687364 EPMC:9687364

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR002506

The Hepatitis delta virus (HDV) encodes a single protein, the hepatitis delta antigen (HDAg). The central region of this protein has been shown to bind RNA [PUBMED:8245865]. Several interactions are also mediated by a coiled-coil region at the N terminus of the protein [PUBMED:9687364].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

Loading domain graphics...


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...

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.

Representative proteomes NCBI
Jalview View  View          View   
HTML View  View             
PP/heatmap 1 View             
Pfam viewer View  View             

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

Key: ✓ available, x not generated, not available.

Format an alignment

Representative proteomes NCBI

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.

Representative proteomes NCBI
Raw Stockholm Download   Download           Download    
Gzipped 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...


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 View help on the curation process

Seed source: Pfam-B_808 (release 4.0)
Previous IDs: none
Type: Family
Author: Bateman A
Number in seed: 4
Number in full: 1108
Average length of the domain: 117.60 aa
Average identity of full alignment: 80 %
Average coverage of the sequence by the domain: 89.58 %

HMM information View help on HMM parameters

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 26.0 25.9
Noise cut-off 21.9 21.2
Model length: 194
Family (HMM) version: 13
Download: download the raw HMM for this family

Species distribution

Sunburst controls


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...

Loading sunburst data...

Tree controls


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


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.


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 HDV_ag domain has been found. There are 5 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.

Loading structure mapping...