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192  structures 498  species 0  interactions 181267  sequences 1522  architectures

Family: Spectrin (PF00435)

Summary: Spectrin repeat

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 "Spectrin repeat". More...

Spectrin repeat Edit Wikipedia article

Spectrin repeat
Identifiers
SymbolSpectrin
PfamPF00435
InterProIPR002017
PROSITEPDOC50083
SCOP21aj3 / SCOPe / SUPFAM
OPM superfamily79
OPM protein2spc

Spectrin repeats[1] are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The spectrin repeat forms a three-helix bundle.

Human proteins containing this domain

ACTN1; ACTN2; ACTN3; ACTN4; AKAP6; C14orf49; CATX-15; DMD; DRP2; DST; KALRN; MACF1; MCF2L; SPNB4; SPTA1; SPTAN1; SPTB; SPTBN1; SPTBN2; SPTBN3; SPTBN4; SPTBN5; SYNE1; SYNE2; TRIO; UTRN;

References

  1. ^ Harrison SC, Yan Y, Winograd E, Viel A, Cronin T, Branton D (1993). "Crystal structure of the repetitive segments of spectrin". Science. 262 (5142): 2027–2030. PMID 8266097.{{cite journal}}: CS1 maint: multiple names: authors list (link)

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.

Spectrin repeat Provide feedback

Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference [2]. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.

Literature references

  1. Hartwig JH; , Protein Profile 1995;2:732-732.: Actin-binding proteins. 1: Spectrin super family. PUBMED:7584474 EPMC:7584474

  2. Yan Y, Winograd E, Viel A, Cronin T, Harrison SC, Branton D; , Science 1993;262:2027-2030.: Crystal structure of the repetitive segments of spectrin. PUBMED:8266097 EPMC:8266097


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR002017

Spectrin repeats [ PUBMED:8266097 ] are found in several proteins involved in cytoskeletal structure. These include spectrin alpha and beta subunits [ PUBMED:12672815 , PUBMED:15062087 ], alpha-actinin [ PUBMED:10481917 ] and dystrophin. The spectrin repeat forms a three-helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C.

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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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
(80)
Full
(181267)
Representative proteomes UniProt
(277615)
RP15
(19677)
RP35
(46103)
RP55
(125085)
RP75
(181507)
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HTML View             
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
(80)
Full
(181267)
Representative proteomes UniProt
(277615)
RP15
(19677)
RP35
(46103)
RP55
(125085)
RP75
(181507)
Alignment:
Format:
Order:
Sequence:
Gaps:
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
(80)
Full
(181267)
Representative proteomes UniProt
(277615)
RP15
(19677)
RP35
(46103)
RP55
(125085)
RP75
(181507)
Raw Stockholm Download   Download   Download   Download   Download   Download    
Gzipped 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_1 (release 1.0)
Previous IDs: spectrin;
Type: Domain
Sequence Ontology: SO:0000417
Author: Bateman A , Finn RD , Stabach P
Number in seed: 80
Number in full: 181267
Average length of the domain: 104.8 aa
Average identity of full alignment: 17 %
Average coverage of the sequence by the domain: 32.83 %

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 29.9 24.2
Trusted cut-off 29.9 24.2
Noise cut-off 29.8 24.1
Model length: 105
Family (HMM) version: 24
Download: download the raw HMM for this family

Species distribution

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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 Spectrin domain has been found. There are 192 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
A0A044S1Q4 View 3D Structure Click here
A0A044UCE8 View 3D Structure Click here
A0A044UFL9 View 3D Structure Click here
A0A077YWU8 View 3D Structure Click here
A0A077Z6Z1 View 3D Structure Click here
A0A077Z7I5 View 3D Structure Click here
A0A077Z838 View 3D Structure Click here
A0A077Z8F4 View 3D Structure Click here
A0A077ZAL9 View 3D Structure Click here
A0A077ZEI5 View 3D Structure Click here
A0A0G2JY25 View 3D Structure Click here
A0A0G2K677 View 3D Structure Click here
A0A0G2K8W9 View 3D Structure Click here
A0A0G2L1F5 View 3D Structure Click here
A0A0H5S196 View 3D Structure Click here
A0A0H5S2L4 View 3D Structure Click here
A0A0K0E9W1 View 3D Structure Click here
A0A0K0EEA2 View 3D Structure Click here
A0A0K0ELE0 View 3D Structure Click here
A0A0K0ELT0 View 3D Structure Click here
A0A0K0ERA4 View 3D Structure Click here
A0A0K0ERH2 View 3D Structure Click here
A0A0N4UP00 View 3D Structure Click here
A0A0R4I9W4 View 3D Structure Click here
A0A0R4IBE3 View 3D Structure Click here
A0A140UHX6 View 3D Structure Click here
A0A158Q4A0 View 3D Structure Click here
A0A158Q6N4 View 3D Structure Click here
A0A286YB77 View 3D Structure Click here
A0A2K6VYN4 View 3D Structure Click here
A0A2R8Q1V1 View 3D Structure Click here
A0A2R8QBL5 View 3D Structure Click here
A0A2R8QDC7 View 3D Structure Click here
A0A2R8QPA3 View 3D Structure Click here
A0A2R8RHL8 View 3D Structure Click here
A0A3P7DAV0 View 3D Structure Click here
A0A3P7E3A4 View 3D Structure Click here
A0A3P7FFE4 View 3D Structure Click here
A0A3P7FFR0 View 3D Structure Click here
A0A3P7GDS3 View 3D Structure Click here