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0  structures 1975  species 0  interactions 4774  sequences 33  architectures

Family: Rick_17kDa_Anti (PF05433)

Summary: Glycine zipper 2TM domain

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Glycine zipper 2TM domain Provide feedback

This family includes a putative two transmembrane alpha-helical region that contains glycine zipper motifs [2]. This family includes several Rickettsia genus specific 17 kDa surface antigen proteins [1].

Literature references

  1. Anderson BE, Baumstark BR, Bellini WJ; , J Bacteriol 1988;170:4493-4500.: Expression of the gene encoding the 17-kilodalton antigen from Rickettsia rickettsii: transcription and posttranslational modification. PUBMED:3139629 EPMC:3139629

  2. Kim S, Jeon TJ, Oberai A, Yang D, Schmidt JJ, Bowie JU;, Proc Natl Acad Sci U S A. 2005;102:14278-14283.: Transmembrane glycine zippers: physiological and pathological roles in membrane proteins. PUBMED:16179394 EPMC:16179394

Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR008816

This domain includes a putative two transmembrane alpha-helical region that contains glycine zipper motifs [ PUBMED:16179394 ]. The domain is found in several Rickettsia genus specific 17kDa surface antigen proteins [ PUBMED:3139629 ].

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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Pfam Clan

This family is a member of clan Glycine-zipper (CL0500), which has the following description:

This superfamily is characterised by having long glycine-zipper motifs, characteristically GxxxGxxxG [1], often with several contiguous copies. The x following the G is frequently found to be an alanine. This sequence region can be found in both symmetric and non-symmetrical membrane structures, and is relatively common. The fact that such a large fraction of the relatively few known membrane channel structures use the glycine zipper suggests that the sequence motif plays a special role in forming these homo-oligomeric bundles [1].

The clan contains the following 11 members:

17kDa_Anti_2 DUF1269 DUF3482 DUF456 DUF5061 DUF883_C Gly-zipper_Omp Gly-zipper_OmpA Gly-zipper_YMGG Rick_17kDa_Anti Romo1


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.

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

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

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Representative proteomes UniProt

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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.

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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...


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_13382 (Rel 8.0) & Pfam-B_6 (Rel 24.0)
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Moxon SJ , Bateman A
Number in seed: 77
Number in full: 4774
Average length of the domain: 42.10 aa
Average identity of full alignment: 39 %
Average coverage of the sequence by the domain: 24.51 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild --amino -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 24.2 24.2
Trusted cut-off 24.2 24.2
Noise cut-off 24.1 24.1
Model length: 42
Family (HMM) version: 18
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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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

trRosetta Structure

The structural model below was generated by the Baker group with the trRosetta software using the Pfam UniProt multiple sequence alignment.

The InterPro website shows the contact map for the Pfam SEED alignment. Hovering or clicking on a contact position will highlight its connection to other residues in the alignment, as well as on the 3D structure.

Improved protein structure prediction using predicted inter-residue orientations. Jianyi Yang, Ivan Anishchenko, Hahnbeom Park, Zhenling Peng, Sergey Ovchinnikov, David Baker Proceedings of the National Academy of Sciences Jan 2020, 117 (3) 1496-1503; DOI: 10.1073/pnas.1914677117;