Summary: ATP synthase A chain

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Wikipedia: MT-ATP6
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MT-ATP6 Edit Wikipedia article

"ATP6" redirects here. For the nuclear genes, see V-ATPase and ATPase.

ATP synthase A chain

Identifiers

Symbol

ATP-synt_A

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

ATP synthase F0 subunit 6

Identifiers

Symbols

ATP6; ATPase6; MTATP6

External IDs

OMIM: 516060 MGI: 99927 HomoloGene: 5012 GeneCards: ATP6 Gene

EC number

3.6.3.14

Gene Ontology
Molecular function	• hydrogen ion transmembrane transporter activity • ATPase activity • transmembrane transporter activity
Cellular component	• mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) • mitochondrial inner membrane • mitochondrial proton-transporting ATP synthase complex • integral to membrane
Biological process	• ATP catabolic process • ATP synthesis coupled proton transport • respiratory electron transport chain • mitochondrial ATP synthesis coupled proton transport • small molecule metabolic process • response to hyperoxia
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

n/a

RefSeq (protein)

YP_003024031.1

NP_904333.1

Location (UCSC)

Chr MT:
0.01 – 0.01 Mb

PubMed search

[1]

[2]

ATP synthase F0 subunit 6 (or subunit/chain A) (human mitochondrial gene name ATP6) is a subunit of F0 complex of transmembrane F-type ATP synthase.^[1]

[edit] Function

This subunit is a key component of the proton channel, and may play a direct role in the translocation of protons across the membrane. Catalysis in the F1 complex depends upon the rotation of the central stalk and F0 c-ring, which in turn is driven by the flux of protons through the membrane via the interface between the F0 c-ring and subunit A. The peripheral stalk links subunit A to the external surface of the F1 domain, and is thought to act as a stator to counter the tendency of subunit A and the F1alpha(3)beta(3) catalytic portion to rotate with the central rotary element.^[2]

3D structure of E. coli homologue of this subunit was modelled based on electron microscopy data (chain M of PDB 1c17). It forms a transmembrane 4-α-bundle.

[edit] Clinical significance

ATP6 is a gene associated with neuropathy, ataxia, and retinitis pigmentosa.^[3]

[edit] References

^ Anderson S, Bankier AT, Barrell BG, de Bruijn MH, Coulson AR, Drouin J, Eperon IC, Nierlich DP, Roe BA, Sanger F, Schreier PH, Smith AJ, Staden R, Young IG (April 1981). "Sequence and organization of the human mitochondrial genome". Nature 290 (5806): 457–65. doi:10.1038/290457a0. PMID 7219534.
^ Walker JE, Runswick MJ, Neuhaus D, Montgomery MG, Carbajo RJ, Kellas FA (2005). "Structure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit". J. Mol. Biol. 351 (4): 824–838. doi:10.1016/j.jmb.2005.06.012. PMID 16045926.
^ Baracca A, Sgarbi G, Mattiazzi M, Casalena G, Pagnotta E, Valentino ML, Moggio M, Lenaz G, Carelli V, Solaini G (July 2007). "Biochemical phenotypes associated with the mitochondrial ATP6 gene mutations at nt8993". Biochim. Biophys. Acta 1767 (7): 913–9. doi:10.1016/j.bbabio.2007.05.005. PMID 17568559.

[edit] Further reading

Torroni A, Achilli A, Macaulay V, et al. (2006). "Harvesting the fruit of the human mtDNA tree.". Trends Genet. 22 (6): 339–45. doi:10.1016/j.tig.2006.04.001. PMID 16678300.
Ingman M, Kaessmann H, Pääbo S, Gyllensten U (2001). "Mitochondrial genome variation and the origin of modern humans.". Nature 408 (6813): 708–13. doi:10.1038/35047064. PMID 11130070.
Manfredi G, Fu J, Ojaimi J, et al. (2002). "Rescue of a deficiency in ATP synthesis by transfer of MTATP6, a mitochondrial DNA-encoded gene, to the nucleus.". Nat. Genet. 30 (4): 394–9. doi:10.1038/ng851. PMID 11925565.
Torigoe T, Izumi H, Ishiguchi H, et al. (2002). "Enhanced expression of the human vacuolar H+-ATPase c subunit gene (ATP6L) in response to anticancer agents.". J. Biol. Chem. 277 (39): 36534–43. doi:10.1074/jbc.M202605200. PMID 12133827.
Mishmar D, Ruiz-Pesini E, Golik P, et al. (2003). "Natural selection shaped regional mtDNA variation in humans.". Proc. Natl. Acad. Sci. U.S.A. 100 (1): 171–6. doi:10.1073/pnas.0136972100. PMC 140917. PMID 12509511. //www.ncbi.nlm.nih.gov/pmc/articles/PMC140917/.
Ingman M, Gyllensten U (2003). "Mitochondrial genome variation and evolutionary history of Australian and New Guinean aborigines.". Genome Res. 13 (7): 1600–6. doi:10.1101/gr.686603. PMC 403733. PMID 12840039. //www.ncbi.nlm.nih.gov/pmc/articles/PMC403733/.
Kong QP, Yao YG, Sun C, et al. (2003). "Phylogeny of east Asian mitochondrial DNA lineages inferred from complete sequences.". Am. J. Hum. Genet. 73 (3): 671–6. doi:10.1086/377718. PMC 1180693. PMID 12870132. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1180693/.
Temperley RJ, Seneca SH, Tonska K, et al. (2004). "Investigation of a pathogenic mtDNA microdeletion reveals a translation-dependent deadenylation decay pathway in human mitochondria.". Hum. Mol. Genet. 12 (18): 2341–8. doi:10.1093/hmg/ddg238. PMID 12915481.
Reuter TY, Medhurst AL, Waisfisz Q, et al. (2003). "Yeast two-hybrid screens imply involvement of Fanconi anemia proteins in transcription regulation, cell signaling, oxidative metabolism, and cellular transport.". Exp. Cell Res. 289 (2): 211–21. doi:10.1016/S0014-4827(03)00261-1. PMID 14499622.
Dubot A, Godinot C, Dumur V, et al. (2004). "GUG is an efficient initiation codon to translate the human mitochondrial ATP6 gene.". Biochem. Biophys. Res. Commun. 313 (3): 687–93. doi:10.1016/j.bbrc.2003.12.013. PMID 14697245.
Coble MD, Just RS, O'Callaghan JE, et al. (2004). "Single nucleotide polymorphisms over the entire mtDNA genome that increase the power of forensic testing in Caucasians.". Int. J. Legal Med. 118 (3): 137–46. doi:10.1007/s00414-004-0427-6. PMID 14760490.
Carrozzo R, Rizza T, Stringaro A, et al. (2004). "Maternally-inherited Leigh syndrome-related mutations bolster mitochondrial-mediated apoptosis.". J. Neurochem. 90 (2): 490–501. doi:10.1111/j.1471-4159.2004.02505.x. PMID 15228605.

[edit] External links

GeneReviews/NCBI/NIH/UW entry on Mitochondrial DNA-Associated Leigh Syndrome and NARP
MT-ATP6+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)

v t e Mitochondrial proteins

Outer membrane	fatty acid degradation (Carnitine palmitoyltransferase I, Long fatty acyl CoA synthetase) tryptophan metabolism (Kynureninase) monoamine neurotransmitter metabolism (Monoamine oxidase)

Intermembrane space	Adenylate kinase - Creatine kinase

Inner membrane	oxidative phosphorylation (Coenzyme Q - cytochrome c reductase, Cytochrome c, NADH dehydrogenase, Succinate dehydrogenase) pyrimidine metabolism (Dihydroorotate dehydrogenase) mitochondrial shuttle (Malate-aspartate shuttle, Glycerol phosphate shuttle) other (Glutamate aspartate transporter, Glycerol-3-phosphate dehydrogenase, ATP synthase, Carnitine palmitoyltransferase II, Uncoupling protein)

Matrix	citric acid cycle (Citrate synthase, Aconitase, Isocitrate dehydrogenase, Oxoglutarate dehydrogenase, Succinyl coenzyme A synthetase, Fumarase, Malate dehydrogenase) anaplerotic reactions (Aspartate transaminase, Glutamate dehydrogenase, Pyruvate dehydrogenase complex) urea cycle (Carbamoyl phosphate synthetase I, Ornithine transcarbamylase, N-Acetylglutamate synthase) alcohol metabolism (ALDH2) PMPCB

Other/to be sorted	steroidogenesis (Cholesterol side-chain cleavage enzyme, Steroid 11-beta-hydroxylase, Aldosterone synthase), Frataxin Mitochondrial membrane transport protein (Mitochondrial permeability transition pore, Mitochondrial carrier)

Mitochondrial DNA	Complex I (MT-ND1, MT-ND2, MT-ND3, MT-ND4, MT-ND4L, MT-ND5, MT-ND6) - Complex III (MT-CYB) - Complex IV (MT-CO1, MT-CO2, MT-CO3) ATP synthase (MT-ATP6, MT-ATP8) tRNA (MT-TA, MT-TC, MT-TD, MT-TE, MT-TF, MT-TG, MT-TH, MT-TI, MT-TK, MT-TL1, MT-TL2, MT-TM, MT-TN, MT-TP, MT-TQ, MT-TR, MT-TS1, MT-TS2, MT-TT, MT-TV, MT-TW, MT-TY)

see also mitochondrial diseases B strc: edmb (perx), skel (ctrs), epit, cili, mito, nucl (chro)

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.

ATP synthase A chain Provide feedback

No Pfam abstract.

External database links

PANDIT:	PF00119
PRINTS:	PR00123
PROSITE:	PDOC00420
Pseudofam:	PF00119
SCOP:	1c17
SYSTERS:	ATP-synt_A

This tab holds annotation information from the InterPro database.

InterPro entry IPR000568

Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP.

There are several different types of transmembrane ATPases, which can differ in function (ATP hydrolysis and/or synthesis), structure (e.g., F-, V- and A-ATPases, which contain rotary motors) and in the type of ions they transport [PUBMED:15473999, PUBMED:15078220]. The different types include:

F-ATPases (F1F0-ATPases), which are found in mitochondria, chloroplasts and bacterial plasma membranes where they are the prime producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).
V-ATPases (V1V0-ATPases), which are primarily found in eukaryotic vacuoles and catalyse ATP hydrolysis to transport solutes and lower pH in organelles.
A-ATPases (A1A0-ATPases), which are found in Archaea and function like F-ATPases (though with respect to their structure and some inhibitor responses, A-ATPases are more closely related to the V-ATPases).
P-ATPases (E1E2-ATPases), which are found in bacteria and in eukaryotic plasma membranes and organelles, and function to transport a variety of different ions across membranes.
E-ATPases, which are cell-surface enzymes that hydrolyse a range of NTPs, including extracellular ATP.

F-ATPases (also known as F1F0-ATPase, or H(+)-transporting two-sector ATPase) (EC) are composed of two linked complexes: the F1 ATPase complex is the catalytic core and is composed of 5 subunits (alpha, beta, gamma, delta, epsilon), while the F0 ATPase complex is the membrane-embedded proton channel that is composed of at least 3 subunits (A-C), nine in mitochondria (A-G, F6, F8). Both the F1 and F0 complexes are rotary motors that are coupled back-to-back. In the F1 complex, the central gamma subunit forms the rotor inside the cylinder made of the alpha(3)beta(3) subunits, while in the F0 complex, the ring-shaped C subunits forms the rotor. The two rotors rotate in opposite directions, but the F0 rotor is usually stronger, using the force from the proton gradient to push the F1 rotor in reverse in order to drive ATP synthesis [PUBMED:11309608]. These ATPases can also work in reverse to hydrolyse ATP to create a proton gradient.

This entry represents subunit A (or subunit 6) found in the F0 complex of F-ATPases. This subunit is a key component of the proton channel, and may play a direct role in the translocation of protons across the membrane. Catalysis in the F1 complex depends upon the rotation of the central stalk and F0 c-ring, which in turn is driven by the flux of protons through the membrane via the interface between the F0 c-ring and subunit A. The peripheral stalk links subunit A to the external surface of the F1 domain, and is thought to act as a stator to counter the tendency of subunit A and the F1 alpha(3)beta(3) catalytic portion to rotate with the central rotary element [PUBMED:16045926].

More information about this protein can be found at Protein of the Month: ATP Synthases [PUBMED:].

Gene Ontology

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

Cellular component	proton-transporting ATP synthase complex, coupling factor F(o) (GO:0045263)
Molecular function	hydrogen ion transmembrane transporter activity (GO:0015078)
Biological process	ATP synthesis coupled proton transport (GO:0015986)

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 (30)	Full (17567)	Representative proteomes				NCBI (15216)	Meta (2921)
	Seed (30)	Full (17567)	RP15 (343)	RP35 (689)	RP55 (893)	RP75 (1063)	NCBI (15216)	Meta (2921)
Jalview	View	View	View	View	View	View	View	View
HTML	View		View	View	View	View
PP/heatmap	₁		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 (30)	Full (17567)	Representative proteomes				NCBI (15216)	Meta (2921)
	Seed (30)	Full (17567)	RP15 (343)	RP35 (689)	RP55 (893)	RP75 (1063)	NCBI (15216)	Meta (2921)
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 (30)	Full (17567)	Representative proteomes				NCBI (15216)	Meta (2921)
	Seed (30)	Full (17567)	RP15 (343)	RP35 (689)	RP55 (893)	RP75 (1063)	NCBI (15216)	Meta (2921)
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:

Prosite

Previous IDs:

none

Type:

Domain

Author:

Sonnhammer ELL

Number in seed:

30

Number in full:

17567

Average length of the domain:

204.40 aa

Average identity of full alignment:

33 %

Average coverage of the sequence by the domain:

91.02 %

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	21.7	21.7
Trusted cut-off	21.7	21.7
Noise cut-off	21.4	21.6

Model length:

215

Family (HMM) version:

15

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

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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
highlight species that are represented in the seed alignment
expand/collapse the tree or expand it to a given depth
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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 ATP-synt_A 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.

Loading structure mapping...

Archea	Eukaryota
Bacteria	Other sequences
Viruses	Unclassified
Viroids	Unclassified sequence

Family: ATP-synt_A (PF00119)

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Summary: ATP synthase A chain

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MT-ATP6 Edit Wikipedia article

Contents

[edit] Function

[edit] Clinical significance

[edit] References

[edit] Further reading

[edit] External links

ATP synthase A chain Provide feedback

External database links

InterPro entry IPR000568

Gene Ontology

Domain organisation

Alignments

Alignment types

Viewing

Reformatting

Downloading

View options

Format an alignment

Download options

External links

HMM logo

Trees

Curation and family details

Curation

HMM information

Species distribution

Sunburst controls

Weight segments by...

Change the size of the sunburst

Colour assignments

Selections

Currently selected:

How the sunburst is generated

Colouring and labels

Anomalies in the taxonomy tree

Missing taxonomic levels

Unmapped species names

Sub-species

Too many species/sequences

Tree controls

Annotation

Download tree

Selected sequences

Species trees

Interactive tree

Structures