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197  structures 5983  species 0  interactions 32886  sequences 513  architectures

Family: Cation_ATPase_C (PF00689)

Summary: Cation transporting ATPase, C-terminus

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 "P-type ATPase". More...

P-type ATPase Edit Wikipedia article

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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Cation transporting ATPase, C-terminus Provide feedback

Members of this families are involved in Na+/K+, H+/K+, Ca++ and Mg++ transport. This family represents 5 transmembrane helices.

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR006068

P-ATPases (also known as E1-E2 ATPases) ([intenz:3.6.3.-]) are found in bacteria and in a number of eukaryotic plasma membranes and organelles [ PUBMED:9419228 ]. P-ATPases function to transport a variety of different compounds, including ions and phospholipids, across a membrane using ATP hydrolysis for energy. There are many different classes of P-ATPases, which transport specific types of ion: H + , Na + , K + , Mg 2+ , Ca 2+ , Ag + and Ag 2+ , Zn 2+ , Co 2+ , Pb 2+ , Ni 2+ , Cd 2+ , Cu + and Cu 2+ . P-ATPases can be composed of one or two polypeptides, and can usually assume two main conformations called E1 and E2.

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 conserved C-terminal region found in several classes of cation-transporting P-type ATPases, including those that transport H + ( EC ), Na + ( EC ), Ca 2+ ( EC ), Na + /K + ( EC ), and H + /K + ( EC ). In the H + /K + - and Na + /K + -exchange P-ATPases, this domain is found in the catalytic alpha chain.

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 (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB 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.

  Seed
(134)
Full
(32886)
Representative proteomes UniProt
(83893)
RP15
(4687)
RP35
(13509)
RP55
(27047)
RP75
(40506)
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PP/heatmap 1            

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

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

Format an alignment

  Seed
(134)
Full
(32886)
Representative proteomes UniProt
(83893)
RP15
(4687)
RP35
(13509)
RP55
(27047)
RP75
(40506)
Alignment:
Format:
Order:
Sequence:
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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
(134)
Full
(32886)
Representative proteomes UniProt
(83893)
RP15
(4687)
RP35
(13509)
RP55
(27047)
RP75
(40506)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped 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.

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 View help on the curation process

Seed source: Pfam-B_137 (release 2.1)
Previous IDs: Na_K_ATPase_C;
Type: Family
Sequence Ontology: SO:0100021
Author: Bateman A , Griffiths-Jones SR
Number in seed: 134
Number in full: 32886
Average length of the domain: 181.9 aa
Average identity of full alignment: 23 %
Average coverage of the sequence by the domain: 18.47 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 27.3 27.3
Trusted cut-off 27.3 27.3
Noise cut-off 27.2 27.2
Model length: 182
Family (HMM) version: 24
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

Selections

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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...

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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 Cation_ATPase_C domain has been found. There are 197 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
A0A044RCX5 View 3D Structure Click here
A0A044T5F9 View 3D Structure Click here
A0A044TSZ2 View 3D Structure Click here
A0A044VJL5 View 3D Structure Click here
A0A077Z2V2 View 3D Structure Click here
A0A077Z5K8 View 3D Structure Click here
A0A077Z6Q6 View 3D Structure Click here
A0A077Z709 View 3D Structure Click here
A0A077ZCT9 View 3D Structure Click here
A0A077ZDB7 View 3D Structure Click here
A0A077ZMV6 View 3D Structure Click here
A0A096SBT9 View 3D Structure Click here
A0A0A2V0I6 View 3D Structure Click here
A0A0A2V1Y5 View 3D Structure Click here
A0A0A2V3C8 View 3D Structure Click here
A0A0A2VJ88 View 3D Structure Click here
A0A0B4LG94 View 3D Structure Click here
A0A0D2E684 View 3D Structure Click here
A0A0D2F121 View 3D Structure Click here
A0A0D2F7A4 View 3D Structure Click here
A0A0D2F8I7 View 3D Structure Click here
A0A0D2GBY3 View 3D Structure Click here
A0A0D2H2Q9 View 3D Structure Click here
A0A0D2HFT6 View 3D Structure Click here
A0A0H3GJR1 View 3D Structure Click here
A0A0H3GQU9 View 3D Structure Click here
A0A0H3GUA3 View 3D Structure Click here
A0A0K0E519 View 3D Structure Click here
A0A0K0E843 View 3D Structure Click here
A0A0K0EB63 View 3D Structure Click here
A0A0K0ED38 View 3D Structure Click here
A0A0K0EH84 View 3D Structure Click here
A0A0K0EHT4 View 3D Structure Click here
A0A0K0EK19 View 3D Structure Click here
A0A0K0EKG1 View 3D Structure Click here
A0A0K0ELU3 View 3D Structure Click here
A0A0K0J331 View 3D Structure Click here
A0A0N4U5K0 View 3D Structure Click here
A0A0N4UCS4 View 3D Structure Click here
A0A0N4UG53 View 3D Structure Click here