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0  structures 578  species 0  interactions 2113  sequences 37  architectures

Family: B9-C2 (PF07162)

Summary: Ciliary basal body-associated, B9 protein

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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.

Ciliary basal body-associated, B9 protein Provide feedback

The B9-C2 domain is found in proteins associated with the ciliary basal body. B9 domains were identified as a specific family of C2 domains [1]. There are three sub-families represented by this family, notably, Mks1-Xbx7, Stumpy-Tza1 and Tza2 groups of proteins. Mutations in human Mks1 result in the developmental disorder Mechler-Gruber syndrome [2]; mutations in mouse Stumpy lead to perinatal hydrocephalus and severe polycystic kidney disease [3]. All the three distinct types of B9-C2 proteins cooperatively localise to the basal body or centrosome of cilia.

Literature references

  1. Zhang D, Aravind L;, Gene. 2010;469:18-30.: Identification of novel families and classification of the C2 domain superfamily elucidate the origin and evolution of membrane targeting activities in eukaryotes. PUBMED:20713135 EPMC:20713135

  2. Kyttala M, Tallila J, Salonen R, Kopra O, Kohlschmidt N, Paavola-Sakki P, Peltonen L, Kestila M;, Nat Genet. 2006;38:155-157.: MKS1, encoding a component of the flagellar apparatus basal body proteome, is mutated in Meckel syndrome. PUBMED:16415886 EPMC:16415886

  3. Town T, Breunig JJ, Sarkisian MR, Spilianakis C, Ayoub AE, Liu X, Ferrandino AF, Gallagher AR, Li MO, Rakic P, Flavell RA;, Proc Natl Acad Sci U S A. 2008;105:2853-2858.: The stumpy gene is required for mammalian ciliogenesis. PUBMED:18287022 EPMC:18287022


This tab holds annotation information from the InterPro database.

InterPro entry IPR010796

The C2 domain is one of the most prevalent eukaryotic lipid-binding domains deployed in diverse functional contexts. Distinct versions of the C2 domain have been recognized, the classical C2, the PI3K-type, the tensin-type, the B9-type, the DOCK-type, the NT-type and the Aida-type. Despite their limited sequence similarity, all C2 domains contain at their core a compact beta-sandwich composed of two four-stranded beta-sheets with highly variable inter-strand regions that might contain one or more alpha-helices. One feature that is highly conserved in the C2 domains is the pair of hydrophobic residues on the upper part of the beta-sheet, which are involved in imparting a curvature of the sheet that allows formation of a concave ligand-binding area [ PUBMED:20713135 ].

This entry represents the B9-type C2 domain containing proteins, found in ciliary basal body associated proteins. Although its function is unknown, a cilia-specific role has been suggested for the poorly characterised B9-type C2 domain [ PUBMED:16415886 , PUBMED:17127412 , PUBMED:18337471 ].

Some proteins known to contain a B9-type C2 domain are listed below:

  • Mammalian Meckel syndrome 1 (MKS1) protein, which may be related to the ciliary basal body.
  • Mammalian protein B9D1 and B9D2.
  • Caenorhabditis elegans X-box promoter element regulated protein 7 (xbx-7). It corresponds to mammalian MKS1.
  • Caenorhabditis elegans ciliary transition zone associate protein 1 (tza-1). It corresponds to mammalian B9D2.
  • Caenorhabditis elegans ciliary transition zone associate protein 2 (tza-2). It corresponds to mammalian B9D1.
  • Paramecium tetraurelia ICIS-1 (Involved in Cilia Stability-1), the B9D2 homologue.

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 C2 (CL0154), which has the following description:

This superfamily includes C2 domains and C2-like domains.

The clan contains the following 18 members:

Aida_C2 Anillin B9-C2 C2 C2-C2_1 CC2D2AN-C2 CEP76-C2 DOCK-C2 IcmF_C MNNL NT-C2 PI3K_C2 PTEN_C2 pYEATS RPGR1_C SPATA6 Spond_N YEATS

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...

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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.

  Seed
(122)
Full
(2113)
Representative proteomes UniProt
(3626)
RP15
(552)
RP35
(949)
RP55
(1663)
RP75
(2154)
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PP/heatmap 1 View           

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

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

Format an alignment

  Seed
(122)
Full
(2113)
Representative proteomes UniProt
(3626)
RP15
(552)
RP35
(949)
RP55
(1663)
RP75
(2154)
Alignment:
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Sequence:
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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
(122)
Full
(2113)
Representative proteomes UniProt
(3626)
RP15
(552)
RP35
(949)
RP55
(1663)
RP75
(2154)
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_12595 (release 10.0)
Previous IDs: B9;
Type: Domain
Sequence Ontology: SO:0000417
Author: Vella Briffa B , Coggill P
Number in seed: 122
Number in full: 2113
Average length of the domain: 158.7 aa
Average identity of full alignment: 30 %
Average coverage of the sequence by the domain: 47.14 %

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 27.0 27.0
Trusted cut-off 27.3 27.7
Noise cut-off 26.9 26.9
Model length: 168
Family (HMM) version: 14
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
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Viroids Viroids Unclassified sequence Unclassified sequence

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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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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
A0A044SJ57 View 3D Structure Click here
A0A044TFH6 View 3D Structure Click here
A0A077Z2Q0 View 3D Structure Click here
A0A077ZF55 View 3D Structure Click here
A0A077ZF88 View 3D Structure Click here
A0A0H5SJE0 View 3D Structure Click here
A0A0H5SKR1 View 3D Structure Click here
A0A0K0E9R3 View 3D Structure Click here
A0A0K0EJU4 View 3D Structure Click here
A0A0K0EQK7 View 3D Structure Click here
A0A0N4U3P7 View 3D Structure Click here
A0A0N4UGW3 View 3D Structure Click here
A0A158Q3M8 View 3D Structure Click here
A0A2K6W579 View 3D Structure Click here
A0A2R8RPF9 View 3D Structure Click here
A0A3P7EC62 View 3D Structure Click here
A0A3Q0KFN5 View 3D Structure Click here
A0A5K4EE15 View 3D Structure Click here
A0A5K4F2L8 View 3D Structure Click here
A0A5K4F453 View 3D Structure Click here
A0A5K4F5M6 View 3D Structure Click here
A0A5S6P8D1 View 3D Structure Click here
A0A5S6P8F2 View 3D Structure Click here
A0A5S6PSN9 View 3D Structure Click here
A0A679L8Q5 View 3D Structure Click here
A4I0K7 View 3D Structure Click here
A4I175 View 3D Structure Click here
A4I7J2 View 3D Structure Click here
G4LXE7 View 3D Structure Click here
M9MRD5 View 3D Structure Click here
P0C5J2 View 3D Structure Click here
P0C5J3 View 3D Structure Click here
Q21191 View 3D Structure Click here
Q387L3 View 3D Structure Click here
Q388F8 View 3D Structure Click here
Q3UK10 View 3D Structure Click here
Q499Q5 View 3D Structure Click here
Q4CVC7 View 3D Structure Click here
Q4D074 View 3D Structure Click here
Q4DKV6 View 3D Structure Click here