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50  structures 2554  species 0  interactions 7970  sequences 70  architectures

Family: V_ATPase_I (PF01496)

Summary: V-type ATPase 116kDa subunit family

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V-ATPase Edit Wikipedia article

V-ATPase schematic
Membrane-spanning region of the V-type sodium ATPase from Enterococcus hirae. Calculated hydrocarbon boundaries of the lipid bilayer are shown by red and blue dots
OPM superfamily5
OPM protein2bl2
PDB 1u7l EBI.jpg
crystal structure of subunit C (vma5p) of the yeast v-atpase
Pfam clanCL0255
PDB 1r5z EBI.jpg
crystal structure of subunit C (yeast subunit d) of v-atpase
PDB 1ho8 EBI.jpg
crystal structure of the regulatory subunit H of the v-type atpase of saccharomyces cerevisiae
Pfam clanCL0020
Pfam clanCL0255

Vacuolar-type H+
(V-ATPase) is a highly conserved evolutionarily ancient enzyme with remarkably diverse functions in eukaryotic organisms.[1] V-ATPases acidify a wide array of intracellular organelles and pump protons across the plasma membranes of numerous cell types. V-ATPases couple the energy of ATP hydrolysis to proton transport across intracellular and plasma membranes of eukaryotic cells. It is generally seen as the polar opposite of ATP synthase because ATP synthase is a proton channel that uses the energy from a proton gradient to produce ATP. V-ATPase however, is a proton pump that uses the energy from ATP hydrolysis to produce a proton gradient.

Roles played by V-ATPases

V-ATPases are found within the membranes of many organelles, such as endosomes, lysosomes, and secretory vesicles, where they play a variety of roles crucial for the function of these organelles. For example, the proton gradient across the yeast vacuolar membrane generated by V-ATPases drives calcium uptake into the vacuole through an H+
antiporter system.[2] In synaptic transmission in neuronal cells, V-ATPase acidifies synaptic vesicles.[3] Norepinephrine enters vesicles by V-ATPase.

V-ATPases are also found in the plasma membranes of a wide variety of cells such as intercalated cells of the kidney, osteoclasts (bone resorbing cells), macrophages, neutrophils, sperm, midgut cells of insects, and certain tumor cells.[4] Plasma membrane V-ATPases are involved in processes such as pH homeostasis, coupled transport, and tumor metastasis. V-ATPases in the acrosomal membrane of sperm acidify the acrosome. This acidification activates proteases required to drill through the plasma membrane of the egg. V-ATPases in the osteoclast plasma membrane pump protons onto the bone surface, which is necessary for bone resorption. In the intercalated cells of the kidney, V-ATPases pump protons into the urine, allowing for bicarbonate reabsorption into the blood.


The yeast V-ATPase is the best characterized. There are at least thirteen subunits identified to form a functional V-ATPase complex, which consists of two domains. The subunits belong to either the Vo domain (membrane associated subunits, lowercase letters on the figure) or the V1 domain (peripherally associated subunits, uppercase letters on the figure).

The V1 includes eight subunits, A-H, with three copies of the catalytic A and B subunits, three copies of the stator subunits E and G, and one copy of the regulatory C and H subunits. In addition, the V1 domain also contains the subunits D and F, which form a central rotor axle.[5] The V1 domain contains tissue-specific subunit isoforms including B, C, E, and G. Mutations to the B1 isoform result in the human disease distal renal tubular acidosis and sensorineural deafness.

The Vo domain contains six different subunits, a, d, c, c', c", and e, with the stoichiometry of the c ring still a matter of debate with a decamer being postulated for the tobacco hornworm (Manduca sexta) V-ATPase. The mammalian Vo domain contains tissue-specific isoforms for subunits a and d, while yeast V-ATPase contains two organelle-specific subunit isoforms of a, Vph1p, and Stv1p. Mutations to the a3 isoform result in the human disease infantile malignant osteopetrosis, and mutations to the a4 isoform result in distal renal tubular acidosis, in some cases with sensorineural deafness.

The V1 domain is responsible for ATP hydrolysis, whereas the Vo domain is responsible for proton translocation. ATP hydrolysis at the catalytic nucleotide binding sites on subunit A drives rotation of a central stalk composed of subunits D and F, which in turn drives rotation of a barrel of c subunits relative to the a subunit. The complex structure of the V-ATPase has been revealed through the structure of the M. Sexta and Yeast complexes that were solved by single-particle cryo-EM and negative staining, respectively.[6][7][8] These structures have revealed that the V-ATPase has a 3-stator network, linked by a collar of density formed by the C, H, and a subunits, which, while dividing the V1 and V0 domains, make no interactions with the central rotor axle formed by the F, D, and d subunits. Rotation of this central rotor axle caused by the hydrolysis of ATP within the catalytic AB domains results in the movement of the barrel of c subunits past the a subunit, which drives proton transport across the membrane. A stoichiometry of two protons translocated for each ATP hydrolyzed has been proposed by Johnson.[9]

In addition to the structural subunits of yeast V-ATPase, associated proteins that are necessary for assembly have been identified. These associated proteins are essential for Vo domain assembly and are termed Vma12p, Vma21p, and Vma22p.[10][11][12][13] Two of the three proteins, Vma12p and Vma22p, form a complex that binds transiently to Vph1p (subunit a) to aid its assembly and maturation.[12][14][15][16] Vma21p coordinates assembly of the Vo subunits as well as escorting the Vo domain into vesicles for transport to the Golgi.[17]


The V1 domain of the V-ATPase is the site of ATP hydrolysis. This soluble domain consists of a hexamer of alternating A and B subunits, a central rotor D, peripheral stators G and E, and regulatory subunits C and H. Hydrolysis of ATP drives a conformational change in the six A|B interfaces and with it rotation of the central rotor D. Unlike with the ATP synthase, the V1 domain is not an active ATPase when dissociated.

Subunit C

In molecular biology, V-ATPase (Vacuolar-ATPase) C represents the C terminal subunit that is part of the V1 complex, and is localised to the interface between the V1 and V0 complexes.[18]

Subunit C function

The C subunit plays an essential role in controlling the assembly of V-ATPase, acting as a flexible stator that holds together the catalytic (V1) and membrane (V0) sectors of the enzyme .[19] The release of subunit C from the ATPase complex results in the dissociation of the V1 and V0 subcomplexes, which is an important mechanism in controlling V-ATPase activity in cells. Essentially, by creating a high electrochemical gradient and low pH, this powers the enzyme to create more ATP.

Subunit G

This subunit, is part of V1, and is important in V-ATPase assembly and activity.

Subunit H

This subunit is only involved in activity and not in assembly.


The Vo domain is responsible for proton translocation. Opposite the F-type ATP synthase, the Vo domain is transporting protons against their own concentration gradient. Rotation of the Vo domain transports the protons in movement coordinated with the V1 domain, which is responsible for ATP hydrolysis. Several subunits are present in the Vo domain to make this a functional proton translocase; they are described below.

Subunit I

In molecular biology, 116kDa subunit (or subunit a) and subunit I are found in the V0 or A0 complex of V- or A-ATPases, respectively. The 116kDa subunit is a transmembrane glycoprotein required for the assembly and proton transport activity of the ATPase complex. Several isoforms of the 116kDa subunit exist, providing a potential role in the differential targeting and regulation of the V-ATPase for specific organelles.

Subunit I function

The function of the 116-kDa subunit is not defined, but its predicted structure consists of 6–8 transmembranous sectors, suggesting that it may function similar to subunit a of FO.

Subunit d

This particular subunit is a non-integral membrane component of the membrane pore domain and is required for proper assembly of the V0 sector. It is thought to be involved in the regulated assembly of V1 subunits onto the membrane sector or alternatively may prevent the passage of protons through V0 pores.

Subunit d2

This subunit is part of the integral membrane V0 complex of vacuolar ATPase, which is responsible for acidifying intracellular compartments in eukaryotic cells. Therefore, they help provide most of the energy required for transport processes in the vacuolar system. They are thought to play a role in coupling of proton transport and ATP hydrolysis and aid the regulation of osteoclast fusion and bone formation.

Subunit c

Similar to the F-type ATP synthase, the transmembrane region of the V-ATPase includes a ring of membrane-spanning subunits that are primarily responsible for proton translocation. Dissimilar from the F-type ATP synthase, however, the V-ATPase has multiple related subunits in the c-ring; in fungi such as yeast there are three related subunits (of varied stoichiometry) and in most other eukaryotes there are two.

V-ATPase assembly

Yeast V-ATPases fail to assemble when any of the genes that encode subunits are deleted except for subunits H and c".[20][21][22] Without subunit H, the assembled V-ATPase is not active.[11][23] and the loss of the c" subunit results in uncoupling of enzymatic activity.[21]

The precise mechanisms by which V-ATPases assembly are still controversial, with evidence suggesting two different possibilities. Mutational analysis and in vitro assays have shown that preassembled Vo and V1 domains can combine to form one complex in a process called independent assembly. Support for independent assembly includes the findings that the assembled Vo domain can be found at the vacuole in the absence of the V1 domain, whereas free V1 domains can be found in the cytoplasm and not at the vacuole.[24][25] In contrast, in vivo pulse-chase experiments have revealed early interactions between Vo and V1 subunits, to be specific, the a and B subunits, suggesting that subunits are added in a step-wise fashion to form a single complex in a concerted assembly process.[26]

V-ATPase evolution

A relatively new technique called ancestral gene resurrection has shed new light on the evolutionary history of the V-ATPase. It has been shown how the V-ATPase structure of the ancestral form consisting of two different proteins evolves into the fungi version with three different proteins.[27][28][29] The V-Type ATPase is similar to the archaeal (so called) A-Type ATP synthase, a fact that supports an archaeal origin of eukaryotes (like Eocyte Hypothesis, see also Lokiarchaeota). The exceptional occurrence of some lineages of archaea with F-type and of some lineages of bacteria with A-type ATPase respectively is regarded as a result of horizontal gene transfer.[30]

Regulation of V-ATPase activity

In vivo regulation of V-ATPase activity is accomplished by reversible dissociation of the V1 domain from the Vo domain. After initial assembly, both the insect Manduca sexta and yeast V-ATPases can reversibly disassemble into free Vo and V1 domains after a 2- to 5-minute deprivation of glucose.[24] Reversible disassembly may be a general mechanism of regulating V-ATPase activity, since it exists in yeast and insects. Reassembly is proposed to be aided by a complex termed RAVE (regulator of H+
-ATPase of vacuolar and endosomal membranes).[31] Dissasembly and reassembly of V-ATPases does not require new protein synthesis but does need an intact microtubular network.[32]

Human diseases


Osteopetrosis is generic name that represents a group of heritable conditions in which there is a defect in osteoclastic bone resorption. Both dominant and recessive osteopetrosis occur in humans.[33][34] Autosomal dominant osteopetrosis shows mild symptoms in adults experiencing frequent bone fractures due to brittle bones.[33] A more severe form of osteopetrosis is termed autosomal recessive infantile malignant osteopetrosis.[34][35][36] Three genes that are responsible for recessive osteopetrosis in humans have been identified. They are all directly involved in the proton generation and secretion pathways that are essential for bone resorption. One gene is carbonic anhydrase II (CAII), which, when mutated, causes osteopetrosis with renal tubular acidosis(type 3).[37] Mutations to the chloride channel ClC7 gene also lead to both dominant and recessive osteopetrosis.[33] Approximately 50% of patients with recessive infantile malignant osteopetrosis have mutations to the a3 subunit isoform of V-ATPase.[35] [38][39] In humans, 26 mutations have been identified in V-ATPase subunit isoform a3, found in osteoclasts, that result in the bone disease autosomal recessive osteopetrosis.[35][34][38][40]

Distal renal tubular acidosis (dRTA)

The importance of V-ATPase activity in renal proton secretion is highlighted by the inherited disease distal renal tubular acidosis. In all cases, renal tubular acidosis results from a failure of the normal renal mechanisms that regulate systemic pH. There are four types of renal tubular acidosis. Type 1 is distal renal tubular acidosis and results from a failure of the cortical collecting duct to acidify the urine below pH 5.[41] Some patients with autosomal recessive dRTA also have sensorineural hearing loss.[42] Inheritance of this type of RTA results from either mutations to V-ATPase subunit isoform B1 or isoform a4 or mutations of band 3 (also called AE1), a Cl-/HCO3- exchanger.[43][42][44][43] Twelve different mutations to V-ATPase isoform B1[45] and twenty-four different mutations in a4 lead to dRTA.[45][42] Reverse transcription polymerase chain reaction studies have shown expression of the a4 subunit in the intercalated cell of the kidney and in the cochlea.[45] dRTA caused by mutations in the a4 subunit gene in some cases can be associated with deafness due to a failure to normally acidify the endolymph of the inner ear.[43]

X-linked myopathy with excessive autophagy (XMEA)

X-linked myopathy with excessive autophagy is a rare genetic disease resulting from mutations in the VMA21 gene.[46] The disease has a childhood onset and results in a slowly progressive muscle weakness, typically beginning in the legs, and some patients can eventually require wheelchair assistance with advanced age. The Vma21 protein assists in assembly of the V-ATPase, and XMEA associated mutations result in decreased activity of the V-ATPase and increased lysosomal pH.[46]


The term Vo has a lowercase letter "o" (not the number "zero") in subscript. The "o" stands for oligomycin. It is worth noting that the human gene notations at NCBI designate it as "zero" rather than the letter "o". For example, the gene for the human c subunit of Vo is listed in NCBI gene database as "ATP6V0C" (with a zero), rather than "ATP6VOC" (with an "o").

See also


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  2. ^ Ohya Y, Umemoto N, Tanida I, Ohta A, Iida H, Anraku Y (July 1991). "Calcium-sensitive cls mutants of Saccharomyces cerevisiae showing a Pet- phenotype are ascribable to defects of vacuolar membrane H(+)-ATPase activity". The Journal of Biological Chemistry. 266 (21): 13971–7. PMID 1830311.
  3. ^ Wienisch M, Klingauf J (August 2006). "Vesicular proteins exocytosed and subsequently retrieved by compensatory endocytosis are nonidentical". Nature Neuroscience. 9 (8): 1019–27. doi:10.1038/nn1739. hdl:11858/00-001M-0000-0012-E436-F. PMID 16845386.
  4. ^ Izumi H, Torigoe T, Ishiguchi H, Uramoto H, Yoshida Y, Tanabe M, Ise T, Murakami T, Yoshida T, Nomoto M, Kohno K (December 2003). "Cellular pH regulators: potentially promising molecular targets for cancer chemotherapy". Cancer Treatment Reviews. 29 (6): 541–9. doi:10.1016/S0305-7372(03)00106-3. PMID 14585264.
  5. ^ Kitagawa N, Mazon H, Heck AJ, Wilkens S (February 2008). "Stoichiometry of the peripheral stalk subunits E and G of yeast V1-ATPase determined by mass spectrometry". The Journal of Biological Chemistry. 283 (6): 3329–37. doi:10.1074/jbc.M707924200. PMID 18055462.
  6. ^ Muench SP, Huss M, Song CF, Phillips C, Wieczorek H, Trinick J, Harrison MA (March 2009). "Cryo-electron microscopy of the vacuolar ATPase motor reveals its mechanical and regulatory complexity". Journal of Molecular Biology. 386 (4): 989–99. doi:10.1016/j.jmb.2009.01.014. PMID 19244615.
  7. ^ Diepholz M, Börsch M, Böttcher B (October 2008). "Structural organization of the V-ATPase and its implications for regulatory assembly and disassembly". Biochemical Society Transactions. 36 (Pt 5): 1027–31. doi:10.1042/BST0361027. PMID 18793183.
  8. ^ Zhang Z, Zheng Y, Mazon H, Milgrom E, Kitagawa N, Kish-Trier E, Heck AJ, Kane PM, Wilkens S (December 2008). "Structure of the yeast vacuolar ATPase". The Journal of Biological Chemistry. 283 (51): 35983–95. doi:10.1074/jbc.M805345200. PMC 2602884. PMID 18955482.
  9. ^ Johnson RG, Beers MF, Scarpa A (September 1982). "H+ ATPase of chromaffin granules. Kinetics, regulation, and stoichiometry". The Journal of Biological Chemistry. 257 (18): 10701–7. PMID 6213624.
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  12. ^ a b Hill KJ, Stevens TH (September 1994). "Vma21p is a yeast membrane protein retained in the endoplasmic reticulum by a di-lysine motif and is required for the assembly of the vacuolar H(+)-ATPase complex". Molecular Biology of the Cell. 5 (9): 1039–50. doi:10.1091/mbc.5.9.1039. PMC 301125. PMID 7841520.
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  14. ^ Hill KJ, Stevens TH (September 1995). "Vma22p is a novel endoplasmic reticulum-associated protein required for assembly of the yeast vacuolar H(+)-ATPase complex". The Journal of Biological Chemistry. 270 (38): 22329–36. doi:10.1074/jbc.270.38.22329. PMID 7673216.
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  24. ^ a b Kane PM (July 1995). "Disassembly and reassembly of the yeast vacuolar H(+)-ATPase in vivo". The Journal of Biological Chemistry. 270 (28): 17025–32. doi:10.1074/jbc.270.28.17025 (inactive 2019-12-13). PMID 7622524.
  25. ^ Sumner JP, Dow JA, Earley FG, Klein U, Jäger D, Wieczorek H (March 1995). "Regulation of plasma membrane V-ATPase activity by dissociation of peripheral subunits". The Journal of Biological Chemistry. 270 (10): 5649–53. doi:10.1074/jbc.270.10.5649. PMID 7890686.
  26. ^ Kane PM, Tarsio M, Liu J (June 1999). "Early steps in assembly of the yeast vacuolar H+-ATPase". The Journal of Biological Chemistry. 274 (24): 17275–83. doi:10.1074/jbc.274.24.17275. PMID 10358087.
  27. ^ Pearson H (9 January 2012). "Resurrecting extinct proteins shows how a machine evolves". News Blog.
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  29. ^ Snapshot view of the V-ATPase molecular machine: animals vs. fungi, University of Oregon (Accessed 2012-01-11)
  30. ^ Hilario E, Gogarten JP (1993). "Horizontal transfer of ATPase genes--the tree of life becomes a net of life" (PDF). Bio Systems. 31 (2–3): 111–9. doi:10.1016/0303-2647(93)90038-E. PMID 8155843.
  31. ^ Kane PM, Smardon AM (August 2003). "Assembly and regulation of the yeast vacuolar H+-ATPase". Journal of Bioenergetics and Biomembranes. 35 (4): 313–21. doi:10.1023/A:1025724814656. PMID 14635777.
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  33. ^ a b c Michigami T, Kageyama T, Satomura K, Shima M, Yamaoka K, Nakayama M, Ozono K (February 2002). "Novel mutations in the a3 subunit of vacuolar H(+)-adenosine triphosphatase in a Japanese patient with infantile malignant osteopetrosis". Bone. 30 (2): 436–9. doi:10.1016/S8756-3282(01)00684-6. PMID 11856654.
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V-type ATPase 116kDa subunit family Provide feedback

This family consists of the 116kDa V-type ATPase (vacuolar (H+)-ATPases) subunits, as well as V-type ATP synthase subunit i. The V-type ATPases family are proton pumps that acidify intracellular compartments in eukaryotic cells for example yeast central vacuoles, clathrin-coated and synaptic vesicles. They have important roles in membrane trafficking processes [1]. The 116kDa subunit (subunit a) in the V-type ATPase is part of the V0 functional domain responsible for proton transport. The a subunit is a transmembrane glycoprotein with multiple putative transmembrane helices it has a hydrophilic amino terminal and a hydrophobic carboxy terminal [1,2]. It has roles in proton transport and assembly of the V-type ATPase complex [1,2]. This subunit is encoded by two homologous gene in yeast VPH1 and STV1 [2].

Literature references

  1. Forgac M; , J Biol Chem 1999;274:12951-12954.: Structure and properties of the vacuolar (H+)-ATPases. PUBMED:10224039 EPMC:10224039

  2. Forgac M; , J Bioenerg Biomembr 1999;31:57-65.: Structure and properties of the clathrin-coated vesicle and yeast vacuolar V-ATPases. PUBMED:10340849 EPMC:10340849

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External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR002490

V-ATPases (also known as V1V0-ATPase or vacuolar ATPase) are found in the eukaryotic endomembrane system, and in the plasma membrane of prokaryotes and certain specialised eukaryotic cells. V-ATPases hydrolyse ATP to drive a proton pump, and are involved in a variety of vital intra- and inter-cellular processes such as receptor mediated endocytosis, protein trafficking, active transport of metabolites, homeostasis and neurotransmitter release [ PUBMED:15629643 ]. V-ATPases are composed of two linked complexes: the V1 complex (subunits A-H) contains the catalytic core that hydrolyses ATP, while the V0 complex (subunits a, c, c', c'', d) forms the membrane-spanning pore. V-ATPases may have an additional role in membrane fusion through binding to t-SNARE proteins [ PUBMED:15907459 ].

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 (ATP synthases, 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 eukaryotes and they function as proton pumps that acidify intracellular compartments and, in some cases, transport protons across the plasma membrane [ PUBMED:20450191 ]. They are also found in bacteria [ PUBMED:9741106 ].
  • 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 [ PUBMED:18937357 , PUBMED:1385979 ].
  • 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.

This entry represents the 116kDa subunit (or subunit a) found in the V0 complex of V-ATPases, respectively. The 116kDa subunit is a transmembrane glycoprotein required for the assembly and proton transport activity of the ATPase complex. Several isoforms of the 116kDa subunit exist, providing a potential role in the differential targeting and regulation of the V-ATPase for specific organelles [ PUBMED:9891027 ].

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...

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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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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.

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

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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.

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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_446 (release 4.0)
Previous IDs: V_ATPase_sub_a;
Type: Family
Sequence Ontology: SO:0100021
Author: Bashton M , Bateman A
Number in seed: 232
Number in full: 7970
Average length of the domain: 468.10 aa
Average identity of full alignment: 27 %
Average coverage of the sequence by the domain: 84.27 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 30.7 30.7
Trusted cut-off 30.9 30.7
Noise cut-off 30.5 30.6
Model length: 816
Family (HMM) version: 21
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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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 V_ATPase_I domain has been found. There are 50 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.

Protein Predicted structure External Information
A0A0G2JW72 View 3D Structure Click here
A0A0R0K2V9 View 3D Structure Click here
A0A0R0K2V9 View 3D Structure Click here
A0A0R0K2V9 View 3D Structure Click here
A0A0R4IN61 View 3D Structure Click here
A0A1D6G8S1 View 3D Structure Click here
A0A1D6JW69 View 3D Structure Click here
A0A1D6MS64 View 3D Structure Click here
A0A1D6N7R7 View 3D Structure Click here
A0A1D6P1Z9 View 3D Structure Click here
A0A1D6PER2 View 3D Structure Click here
A0A1D8PPB0 View 3D Structure Click here
A0A286Y8R2 View 3D Structure Click here
A0A2R8Q419 View 3D Structure Click here
A1ZBF7 View 3D Structure Click here
A4I0M2 View 3D Structure Click here
A4I0M2 View 3D Structure Click here
A4I7Q8 View 3D Structure Click here
B2MZD0 View 3D Structure Click here
B8A655 View 3D Structure Click here
E7F7W2 View 3D Structure Click here
F1QE30 View 3D Structure Click here
F1QEY7 View 3D Structure Click here
F1QW04 View 3D Structure Click here
G3V887 View 3D Structure Click here
G5EEK9 View 3D Structure Click here
G5EGP4 View 3D Structure Click here
G5EGP4 View 3D Structure Click here
I1K7M8 View 3D Structure Click here
I1LJ94 View 3D Structure Click here
I1LPZ3 View 3D Structure Click here
I1LR08 View 3D Structure Click here
I1M4P0 View 3D Structure Click here
K7M9K9 View 3D Structure Click here
K7N1F4 View 3D Structure Click here
O13742 View 3D Structure Click here
P15920 View 3D Structure Click here
P25286 View 3D Structure Click here
P30628 View 3D Structure Click here
P32563 View 3D Structure Click here
P37296 View 3D Structure Click here
Q0IYP2 View 3D Structure Click here
Q10P12 View 3D Structure Click here
Q13488 View 3D Structure Click here
Q4DK78 View 3D Structure Click here
Q4DSC7 View 3D Structure Click here
Q4DY50 View 3D Structure Click here
Q54E04 View 3D Structure Click here
Q57675 View 3D Structure Click here
Q57675 View 3D Structure Click here
Q59R99 View 3D Structure Click here
Q5QLD9 View 3D Structure Click here
Q8IAQ8 View 3D Structure Click here
Q8IAQ8 View 3D Structure Click here
Q8RWZ7 View 3D Structure Click here
Q8W4S4 View 3D Structure Click here
Q920R6 View 3D Structure Click here
Q93050 View 3D Structure Click here
Q9HBG4 View 3D Structure Click here
Q9JHF5 View 3D Structure Click here
Q9SJT7 View 3D Structure Click here
Q9VE75 View 3D Structure Click here
Q9VE77 View 3D Structure Click here
Q9VKF6 View 3D Structure Click here
Q9VKF6 View 3D Structure Click here
Q9XZ10 View 3D Structure Click here
Q9Y487 View 3D Structure Click here
Q9Z1G4 View 3D Structure Click here