Summary: Ankyrin repeat
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This is the Wikipedia entry entitled "Ankyrin". More...
Ankyrin Edit Wikipedia article
| ANK1, erythrocytic | |||||||
|---|---|---|---|---|---|---|---|
 Ribbon diagram of a fragment of the membrane-binding domain of ankyrin R.[1] | |||||||
| Identifiers | |||||||
| Symbol | ANK1 | ||||||
| Alt. symbols | AnkyrinR, Band2.1 | ||||||
| NCBI gene | 286 | ||||||
| HGNC | 492 | ||||||
| OMIM | 182900 | ||||||
| PDB | 1N11 | ||||||
| RefSeq | NM_000037 | ||||||
| UniProt | P16157 | ||||||
| Other data | |||||||
| Locus | Chr. 8 p21.1-11.2 | ||||||
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| Ankyrin repeat | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Ank | ||||||||
| Pfam | PF00023 | ||||||||
| InterPro | IPR002110 | ||||||||
| SMART | SM00248 | ||||||||
| PROSITE | PDOC50088 | ||||||||
| SCOP2 | 1awc / SCOPe / SUPFAM | ||||||||
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| ANK2, neuronal | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | ANK2 | ||||||
| Alt. symbols | AnkyrinB | ||||||
| NCBI gene | 287 | ||||||
| HGNC | 493 | ||||||
| OMIM | 106410 | ||||||
| RefSeq | NM_001148 | ||||||
| UniProt | Q01484 | ||||||
| Other data | |||||||
| Locus | Chr. 4 q25-q27 | ||||||
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| ANK3, node of Ranvier | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | ANK3 | ||||||
| Alt. symbols | AnkyrinG | ||||||
| NCBI gene | 288 | ||||||
| HGNC | 494 | ||||||
| OMIM | 600465 | ||||||
| RefSeq | NM_020987 | ||||||
| UniProt | Q12955 | ||||||
| Other data | |||||||
| Locus | Chr. 10 q21 | ||||||
| |||||||
Ankyrins are a family of proteins that mediate the attachment of integral membrane proteins to the spectrin-actin based membrane cytoskeleton.[2] Ankyrins have binding sites for the beta subunit of spectrin and at least 12 families of integral membrane proteins. This linkage is required to maintain the integrity of the plasma membranes and to anchor specific ion channels, ion exchangers and ion transporters in the plasma membrane. The name is derived from the Greek word ἄγκυÏα (ankyra) for "anchor".
Structure
Ankyrins contain four functional domains: an N-terminal domain that contains 24 tandem ankyrin repeats, a central domain that binds to spectrin, a death domain that binds to proteins involved in apoptosis, and a C-terminal regulatory domain that is highly variable between different ankyrin proteins.[2]
Membrane protein recognition
The 24 tandem ankyrin repeats are responsible for the recognition of a wide range of membrane proteins. These 24 repeats contain 3 structurally distinct binding sites ranging from repeat 1-14. These binding sites are quasi-independent of each other and can be used in combination. The interactions the sites use to bind to membrane proteins are non-specific and consist of: hydrogen bonding, hydrophobic interactions and electrostatic interactions. These non-specific interactions give ankyrin the property to recognise a large range of proteins as the sequence doesn't have to be conserved, just the properties of the amino acids. The quasi-independence means that if a binding site is not used, it won't have a large effect on the overall binding. These two properties in combination give rise to large repertoire of proteins ankyrin can recognise.
Subtypes
Ankyrins are encoded by three genes (ANK1, ANK2 and ANK3) in mammals. Each gene in turn produces multiple proteins through alternative splicing.
ANK1
The ANK1 gene encodes the AnkyrinR proteins. AnkyrinR was first characterized in human erythrocytes, where this ankyrin was referred to as erythrocyte ankyrin or band2.1.[3] AnkyrinR enables erythrocytes to resist shear forces experienced in the circulation. Individuals with reduced or defective ankyrinR have a form of hemolytic anemia termed hereditary spherocytosis.[4] In erythrocytes, AnkyrinR links the membrane skeleton to the Cl−/HCO3− anion exchanger.[5]
Ankyrin 1 links membrane receptor CD44 to the inositol triphosphate receptor and the cytoskeleton.[6]
It has been suggested that Ankyrin 1 interacts with KAHRP (shown via selective pull-downs, SPR and ELISA).[7]
ANK2
Subsequently, ankyrinB proteins (products of the ANK2 gene[8]) were identified in brain and muscle. AnkyrinB and AnkyrinG proteins are required for the polarized distribution of many membrane proteins including the Na+/K+ ATPase, the voltage gated Na+ channel and the Na+/Ca2+ exchanger.
ANK3
AnkyrinG proteins (products of the ANK3 gene[9]) were identified in epithelial cells and neurons. A large-scale genetic analysis conducted in 2008 shows the possibility that ANK3 is involved in bipolar disorder.[10][11]
See also
- DARPin (designed ankyrin repeat protein), an engineered antibody mimetic based on the structure of ankyrin repeats
References
- ^ PDB: 1N11​; Michaely P, Tomchick DR, Machius M, Anderson RG (December 2002). "Crystal structure of a 12 ANK repeat stack from human ankyrinR". The EMBO Journal. 21 (23): 6387–96. doi:10.1093/emboj/cdf651. PMC 136955. PMID 12456646.
- ^ a b Bennett V, Baines AJ (July 2001). "Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues". Physiological Reviews. 81 (3): 1353–92. doi:10.1152/physrev.2001.81.3.1353. PMID 11427698.
- ^ Bennett V, Stenbuck PJ (April 1979). "Identification and partial purification of ankyrin, the high affinity membrane attachment site for human erythrocyte spectrin". The Journal of Biological Chemistry. 254 (7): 2533–41. doi:10.1016/S0021-9258(17)30254-5. PMID 372182.
- ^ Lux SE, Tse WT, Menninger JC, John KM, Harris P, Shalev O, Chilcote RR, Marchesi SL, Watkins PC, Bennett V (June 1990). "Hereditary spherocytosis associated with deletion of human erythrocyte ankyrin gene on chromosome 8". Nature. 345 (6277): 736–9. Bibcode:1990Natur.345..736L. doi:10.1038/345736a0. PMID 2141669. S2CID 4334791.
- ^ Bennett V, Stenbuck PJ (August 1979). "The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes". Nature. 280 (5722): 468–73. Bibcode:1979Natur.280..468B. doi:10.1038/280468a0. PMID 379653. S2CID 4268702.
- ^ Singleton PA, Bourguignon LY (April 2004). "CD44 interaction with ankyrin and IP3 receptor in lipid rafts promotes hyaluronan-mediated Ca2+ signaling leading to nitric oxide production and endothelial cell adhesion and proliferation". Experimental Cell Research. 295 (1): 102–18. doi:10.1016/j.yexcr.2003.12.025. PMID 15051494.
- ^ Weng H, Guo X, Papoin J, Wang J, Coppel R, Mohandas N, An X (January 2014). "Interaction of Plasmodium falciparum knob-associated histidine-rich protein (KAHRP) with erythrocyte ankyrin R is required for its attachment to the erythrocyte membrane". Biochimica et Biophysica Acta (BBA) - Biomembranes. 1838 (1 Pt B): 185–92. doi:10.1016/j.bbamem.2013.09.014. PMC 4403245. PMID 24090929.
- ^ Schott JJ, Charpentier F, Peltier S, Foley P, Drouin E, Bouhour JB, Donnelly P, Vergnaud G, Bachner L, Moisan JP (November 1995). "Mapping of a gene for long QT syndrome to chromosome 4q25-27". American Journal of Human Genetics. 57 (5): 1114–22. PMC 1801360. PMID 7485162.
- ^ Kapfhamer D, Miller DE, Lambert S, Bennett V, Glover TW, Burmeister M (May 1995). "Chromosomal localization of the ankyrinG gene (ANK3/Ank3) to human 10q21 and mouse 10". Genomics. 27 (1): 189–91. doi:10.1006/geno.1995.1023. PMID 7665168.
- ^ Ferreira MA, O'Donovan MC, Meng YA, Jones IR, Ruderfer DM, Jones L, et al. (September 2008). "Collaborative genome-wide association analysis supports a role for ANK3 and CACNA1C in bipolar disorder". Nature Genetics. 40 (9): 1056–8. doi:10.1038/ng.209. PMC 2703780. PMID 18711365.
- ^ "Channeling Mental Illness: GWAS Links Ion Channels, Bipolar Disorder". Schizophrenia Research Forum: News. schizophreniaforum.org. 2008-08-19. Archived from the original on 2010-12-18. Retrieved 2008-08-21.
External links
- Ankyrins at the US National Library of Medicine Medical Subject Headings (MeSH)
- Proteopedia 1n11 Ankyrin-R
This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
This is the Wikipedia entry entitled "Ankyrin repeat". More...
Ankyrin repeat Edit Wikipedia article
 | This article possibly contains original research. (July 2015) |
| Ankyrin repeat domain | |||||||||||
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| Identifiers | |||||||||||
| Symbol | Ank | ||||||||||
| Pfam | PF00023 | ||||||||||
| InterPro | IPR002110 | ||||||||||
| SMART | SM00248 | ||||||||||
| PROSITE | PDOC50088 | ||||||||||
| SCOP2 | 1awc / SCOPe / SUPFAM | ||||||||||
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The ankyrin repeat is a 33-residue motif in proteins consisting of two alpha helices separated by loops, first discovered in signaling proteins in yeast Cdc10 and Drosophila Notch. Domains consisting of ankyrin tandem repeats mediate protein–protein interactions and are among the most common structural motifs in known proteins. They appear in bacterial, archaeal, and eukaryotic proteins, but are far more common in eukaryotes. Ankyrin repeat proteins, though absent in most viruses, are common among poxviruses. Most proteins that contain the motif have four to six repeats, although its namesake ankyrin contains 24, and the largest known number of repeats is 34, predicted in a protein expressed by Giardia lamblia.[2]
Ankyrin repeats typically fold together to form a single, linear solenoid structure called ankyrin repeat domains. These domains are one of the most common protein–protein interaction platforms in nature. They occur in a large number of functionally diverse proteins, mainly from eukaryotes. The few known examples from prokaryotes and viruses may be the result of horizontal gene transfers.[3] The repeat has been found in proteins of diverse function such as transcriptional initiators, cell cycle regulators, cytoskeletal, ion transporters, and signal transducers. The ankyrin fold appears to be defined by its structure rather than its function, since there is no specific sequence or structure that is universally recognised by it.
Considering the atomic structures of individual ankyrin repeats, the loop is often a type 1 beta bulge loop, while both alpha-helices commonly have a Schellman loop at their N-terminus.
Role in protein folding
The ankyrin-repeat sequence motif has been studied using multiple sequence alignment to determine conserved amino acid residues critical for folding and stability. The residues on the wide lateral surface of ankyrin repeat structures are variable, often hydrophobic, and involved mainly in mediating protein–protein interactions. An artificial protein design based on a consensus sequence derived from sequence alignment has been synthesized and found to fold stably, representing the first designed protein with multiple repeats.[4] More extensive design strategies have used combinatorial sequences to "evolve" ankyrin-repeats that recognize particular protein targets, a technique that has been presented as an alternative to antibody design for applications requiring high-affinity binding.[5] A structure-based study involving a range of ankyrin proteins of known structures, shows that consensus-based ankyrin proteins are very stable since they maximize the energetic gap between the folding and unfolding structures, encoding a densely connected network of favourable interactions among conserved sequence motifs, like the TPLX motif.[6] The same study shows that insertions in the canonical framework of ankyrin repeats are enriched in conflictive interactions, that are related to function. The same applies to interactions surrounding deletion hotspots. These might be related to complex folding/unfolding transitions that are important to the partner recognition and interaction.
Ankyrin-repeat proteins present an unusual problem in the study of protein folding, which has largely focused on globular proteins that form well-defined tertiary structure stabilized by long-range, nonlocal residue-residue contacts. Ankyrin repeats, by contrast, contain very few such contacts (that is, they have a low contact order). Most studies have found that ankyrin repeats fold in a two-state folding mechanism, suggesting a high degree of folding cooperativity despite the local inter-residue contacts and the evident need for successful folding with varying numbers of repeats. Some evidence, based on synthesis of truncated versions of natural repeat proteins,[7] and on the examination of phi values,[8] suggests that the C-terminus forms the folding nucleation site.
Clinical significance
Ankyrin-repeat proteins have been associated with a number of human diseases. These proteins include the cell cycle inhibitor p16, which is associated with cancer, and the Notch protein (a key component of cell signalling pathways) which can cause the neurological disorder CADASIL when the repeat domain is disrupted by mutations.[2]
A specialized family of ankyrin proteins known as muscle ankyrin repeat proteins (MARPs) are involved with the repair and regeneration of muscle tissue following damage due to injury and stress.[9]
A natural variation between glutamine and lysine at position 703 in the 11th ankyrin repeat of ANKK1, known as the TaqI A1 allele,[10] has been credited with encouraging addictive behaviours such as obesity, alcoholism, nicotine dependency and the Eros love style[citation needed] while discouraging juvenile delinquency and neuroticism-anxiety.[11][failed verification] The variation may affect the specificity of protein interactions made by the ANKK1 protein kinase through this repeat[citation needed].
Human proteins containing this repeat
ABTB1; ABTB2; ACBD6; ACTBL1; ANK1; ANK2; ANK3; ANKAR; ANKDD1A; ANKEF1; ANKFY1; ANKHD1; ANKIB1; ANKK1; ANKMY1; ANKMY2; ANKRA2; ANKRD1; ANKRD10; ANKRD11; ANKRD12; ANKRD13; ANKRD13A; ANKRD13B; ANKRD13C; ANKRD13D; ANKRD15; ANKRD16; ANKRD17; ANKRD18A; ANKRD18B; ANKRD19; ANKRD2; ANKRD20A1; ANKRD20A2; ANKRD20A3; ANKRD20A4; ANKRD21; ANKRD22; ANKRD23; ANKRD24; ANKRD25; ANKRD26; ANKRD27; ANKRD28; ANKRD30A; ANKRD30B; ANKRD30BL; ANKRD32; ANKRD33; ANKRD35; ANKRD36; ANKRD36B; ANKRD37; ANKRD38; ANKRD39; ANKRD40; ANKRD41; ANKRD42; ANKRD43; ANKRD44; ANKRD45; ANKRD46; ANKRD47; ANKRD49; ANKRD50; ANKRD52; ANKRD53; ANKRD54; ANKRD55; ANKRD56; ANKRD57; ANKRD58; ANKRD60; ANKRD6; ANKRD7; ANKRD9; ANKS1A; ANKS3; ANKS4B; ANKS6; ANKZF1; ASB1; ASB10; ASB11; ASB12; ASB13; ASB14; ASB15; ASB16; ASB2; ASB3; ASB4; ASB5; ASB6; ASB7; ASB8; ASB9; ASZ1; BARD1; BAT4; BAT8; BCL3; BCOR; BCORL1; BTBD11; CAMTA1; CAMTA2; CASKIN1; CASKIN2; CCM1; CDKN2A; CDKN2B; CDKN2C; CDKN2D; CENTB1; CENTB2; CENTB5; CENTG1; CENTG2; CENTG3; CLIP3; CLIP4; CLPB; CTGLF1; CTGLF2; CTGLF3; CTGLF4; CTGLF5; CTTNBP2; DAPK1; DDEF1; DDEF2; DDEFL1; DGKI; DGKZ; DP58; DYSFIP1; DZANK; EHMT1; EHMT2; ESPN; FANK1; FEM1A; FEM1B; GABPB2; GIT1; GIT2; GLS; GLS2; HACE1; HECTD1; IBTK; ILK; INVS; KIDINS220; KRIT1; LRRK1; MAIL; MIB1; MIB2; MPHOSPH8; MTPN; MYO16; NFKB1; NFKB2; NFKBIA; NFKBIB; NFKBIE; NFKBIL1; NFKBIL2; NOTCH1; NOTCH2; NOTCH3; NOTCH4; NRARP; NUDT12; OSBPL1A; OSTF1; PLA2G6; POTE14; POTE15; POTE8; PPP1R12A; PPP1R12B; PPP1R12C; PPP1R13B; PPP1R13L; PPP1R16A; PPP1R16B; PSMD10; RAI14; RFXANK; RIPK4; RNASEL; SHANK1; SHANK2; SHANK3; SNCAIP; TA-NFKBH; TEX14; TNKS; TNKS2; TNNI3K; TP53BP2; TRP7; TRPA1; TRPC3; TRPC4; TRPC5; TRPC6; TRPC7; TRPV1; TRPV2; TRPV3; TRPV4; TRPV5; TRPV6; UACA; USH1G; ZDHHC13; ZDHHC17;
See also
- DARPin (designed ankyrin repeat protein), an engineered antibody mimetic based on the structure of ankyrin repeats
References
- ^ PDB: 1N11​; Michaely P, Tomchick DR, Machius M, Anderson RG (December 2002). "Crystal structure of a 12 ANK repeat stack from human ANK1". EMBO J. 21 (23): 6387–96. doi:10.1093/emboj/cdf651. PMC 136955. PMID 12456646.
- ^ a b Mosavi L, Cammett T, Desrosiers D, Peng Z (2004). "The ankyrin repeat as molecular architecture for protein recognition". Protein Sci. 13 (6): 1435–48. doi:10.1110/ps.03554604. PMC 2279977. PMID 15152081. Archived from the original on 2004-09-07.
- ^ Bork P (December 1993). "Hundreds of ankyrin-like repeats in functionally diverse proteins: mobile modules that cross phyla horizontally?". Proteins. 17 (4): 363–74. doi:10.1002/prot.340170405. PMID 8108379. S2CID 35224626.
- ^ Mosavi LK, Minor DL, Peng ZY (Dec 2002). "Consensus-derived structural determinants of the ankyrin repeat motif". Proc Natl Acad Sci USA. 99 (25): 16029–34. Bibcode:2002PNAS...9916029M. doi:10.1073/pnas.252537899. PMC 138559. PMID 12461176.
- ^ Binz HK, Amstutz P, Kohl A, et al. (May 2004). "High-affinity binders selected from designed ankyrin repeat protein libraries". Nat. Biotechnol. 22 (5): 575–82. doi:10.1038/nbt962. PMID 15097997. S2CID 1191035.
- ^ Parra RG, Espada R, Verstraete N, Ferreiro DU, et al. (Dec 2015). "Structural and Energetic Characterization of the Ankyrin Repeat Protein Family". PLOS Comput. Biol. 12 (11): 575–82. Bibcode:2015PLSCB..11E4659P. doi:10.1371/journal.pcbi.1004659. PMC 4687027. PMID 26691182.
- ^ Zhang B, Peng Z (Jun 2000). "A minimum folding unit in the ankyrin repeat protein p16(INK4)". J Mol Biol. 299 (4): 1121–32. doi:10.1006/jmbi.2000.3803. PMID 10843863.
- ^ Tang KS, Fersht AR, Itzhaki LS (Jan 2003). "Sequential unfolding of ankyrin repeats in tumor suppressor p16". Structure. 11 (1): 67–73. doi:10.1016/S0969-2126(02)00929-2. PMID 12517341.
- ^ Miller MK, Bang ML, Witt CC, et al. (Nov 2003). "The muscle ankyrin repeat proteins: CARP, ankrd2/Arpp and DARP as a family of titin filament-based stress response molecules". J Mol Biol. 333 (5): 951–64. doi:10.1016/j.jmb.2003.09.012. PMID 14583192.
- ^ Neville MJ, Johnstone EC, Walton RT (Jun 2004). "Identification and characterization of ANKK1: a novel kinase gene closely linked to DRD2 on chromosome band 11q23.1". Hum. Mutat. 23 (6): 540–5. doi:10.1002/humu.20039. PMID 15146457. S2CID 22242611.
- ^ "NCBI Gene summary for DRD2". (interim reference)
External links
- Eukaryotic Linear Motif resource motif class LIG_TNKBM_1
- Ankyrin+repeat at the US National Library of Medicine Medical Subject Headings (MeSH)
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.
Ankyrin repeat Provide feedback
Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity [2].
Literature references
-
Lux SE, John KM, Bennett V; , Nature 1990;345:736-739.: Hereditary spherocytosis associated with deletion of human erythrocyte ankyrin gene on chromosome 8. PUBMED:2141669 EPMC:2141669
-
Michaely P, Tomchick DR, Machius M, Anderson RG;, EMBO J. 2002;21:6387-6396.: Crystal structure of a 12 ANK repeat stack from human ankyrinR. PUBMED:12456646 EPMC:12456646
-
Michaely P, Bennett V;, Trends Cell Biol. 1992;2:127-129.: The ANK repeat: a ubiquitous motif involved in macromolecular recognition. PUBMED:14731966 EPMC:14731966
Internal database links
| SCOOP: | Ank_2 Ank_3 Ank_4 Ank_5 |
| Similarity to PfamA using HHSearch: | Ank_2 Ank_2 Ank_3 Ank_4 Ank_4 Ank_5 |
External database links
| HOMSTRAD: | ANK |
| MIM: | 182900 |
| SCOP: | 1awc |
This tab holds annotation information from the InterPro database.
InterPro entry IPR002110
The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes. The few known examples from prokaryotes and viruses may be the result of horizontal gene transfers. The repeat has been found in proteins of diverse function such as transcriptional initiators, cell-cycle regulators [ PUBMED:31000436 ], cytoskeletal, ion transporters and signal transducers [ PUBMED:29769718 , PUBMED:8108379 ]. The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it.
The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures [ PUBMED:8875926 , PUBMED:9353127 , PUBMED:9461436 , PUBMED:9865693 ]. Each repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 o angle. The repeats stack together to form an L-shaped structure [ PUBMED:8875926 , PUBMED:12461176 ].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Molecular function | protein binding (GO:0005515) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan Ank (CL0465), which has the following description:
The ankyrin repeat is a short sequence region that is about 30-34 amino-acids in length. Multiple copies of the repeat composed of two beta strands and two alpha helices combine to form long arrays. In general these repeats are involved in protein-protein interactions. This superfamily also includes some families that are arrays of several repeats.
The clan contains the following 8 members:
Ank Ank_2 Ank_3 Ank_4 Ank_5 AnkUBD DUF3420 DUF3447Alignments
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 and the UniProtKB sequence database. More...
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| Seed (1062) |
Full (28509) |
Representative proteomes | UniProt (52743) |
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| RP15 (6448) |
RP35 (12640) |
RP55 (22523) |
RP75 (30270) |
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| PP/heatmap | 1 | ||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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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 (1062) |
Full (28509) |
Representative proteomes | UniProt (52743) |
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| RP15 (6448) |
RP35 (12640) |
RP55 (22523) |
RP75 (30270) |
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| Raw Stockholm | |||||||
| Gzipped | |||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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: | Swissprot_feature_table |
| Previous IDs: | ank; |
| Type: | Repeat |
| Sequence Ontology: | SO:0001068 |
| Author: |
Bateman A  , Sonnhammer ELL
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| Number in seed: | 1062 |
| Number in full: | 28509 |
| Average length of the domain: | 33.50 aa |
| Average identity of full alignment: | 31 % |
| Average coverage of the sequence by the domain: | 4.18 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 33 | ||||||||||||
| Family (HMM) version: | 33 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Colour assignments
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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 Ank domain has been found. There are 479 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.
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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.
