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0  structures 422  species 0  interactions 1516  sequences 41  architectures

Family: Arm_2 (PF04826)

Summary: Armadillo-like

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 "Armadillo repeats". More...

Armadillo repeats 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.

Armadillo-like Provide feedback

This domain contains armadillo-like repeats [1]. Proteins containing this domain interact with numerous other proteins, through these interactions they are involved in a wide variety of processes including carcinogenesis [2] control of cellular ageing and survival [1] regulation of circadian rhythm [3] and lysosomal sorting of G protein-coupled receptors [4].

Literature references

  1. Heese K, Yamada T, Akatsu H, Yamamoto T, Kosaka K, Nagai Y, Sawada T;, J Cell Biochem. 2004;91:1030-1042.: Characterizing the new transcription regulator protein p60TRP. PUBMED:15034937 EPMC:15034937

  2. Zhou X, Yang G, Huang R, Chen X, Hu G;, FEBS Lett. 2007;581:4943-4948.: SVH-B interacts directly with p53 and suppresses the transcriptional activity of p53. PUBMED:17904127 EPMC:17904127

  3. Matsuki T, Kiyama A, Kawabuchi M, Okada M, Nagai K;, Brain Res. 2001;916:1-10.: A novel protein interacts with a clock-related protein, rPer1. PUBMED:11597585 EPMC:11597585

  4. Whistler JL, Enquist J, Marley A, Fong J, Gladher F, Tsuruda P, Murray SR, Von Zastrow M;, Science. 2002;297:615-620.: Modulation of postendocytic sorting of G protein-coupled receptors. PUBMED:12142540 EPMC:12142540


Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR006911

This domain contains armadillo-like repeats [ PUBMED:15034937 ]. Proteins containing this domain interact with numerous other proteins, through these interactions they are involved in a wide variety of processes including carcinogenesis [ PUBMED:17904127 ], control of cellular ageing and survival [ PUBMED:15034937 ], regulation of circadian rhythm [ PUBMED:11597585 ] and lysosomal sorting of G protein-coupled receptors [ PUBMED:12142540 ].

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 TPR (CL0020), which has the following description:

Tetratricopeptide-like repeats are found in a numerous and diverse proteins involved in such functions as cell cycle regulation, transcriptional control, mitochondrial and peroxisomal protein transport, neurogenesis and protein folding.

The clan contains the following 176 members:

Adaptin_N Alkyl_sulf_dimr ANAPC3 ANAPC5 ANAPC8 APC_rep API5 Arm Arm_2 Arm_3 Arm_vescicular Atx10homo_assoc B56 BAF250_C BTAD CAS_CSE1 ChAPs CHIP_TPR_N CID CLASP_N Clathrin Clathrin-link Clathrin_H_link Clathrin_propel Cnd1 Cnd3 Coatomer_E Cohesin_HEAT Cohesin_load ComR_TPR COPI_C CPL CRM1_C CRM1_repeat CRM1_repeat_3 Cse1 CTK3 DHR-2 DIL DNA_alkylation Dopey_N Drf_FH3 Drf_GBD DUF1822 DUF2019 DUF2225 DUF3385 DUF3458_C DUF3808 DUF3856 DUF4042 DUF5588 DUF5691 DUF6340 DUF6377 DUF924 EAD11 EST1 EST1_DNA_bind FAT Fis1_TPR_C Fis1_TPR_N Foie-gras_1 GUN4_N HAT HEAT HEAT_2 HEAT_EZ HEAT_PBS HEAT_UF HemY_N HrpB1_HrpK HSM3_C HSM3_N IBB IBN_N IFRD Importin_rep Importin_rep_2 Importin_rep_3 Importin_rep_4 Importin_rep_5 Importin_rep_6 Insc_C KAP Leuk-A4-hydro_C LRV LRV_FeS MA3 MIF4G MIF4G_like MIF4G_like_2 MMS19_C Mo25 MRP-S27 Mtf2 NARP1 Neurochondrin Nipped-B_C Nro1 NSF Paf67 ParcG PC_rep PHAT PI3Ka PknG_TPR PPP5 PPR PPR_1 PPR_2 PPR_3 PPR_long PPTA Proteasom_PSMB PUF Rapsyn_N RIX1 RNPP_C RPM2 RPN7 Sel1 SHNi-TPR SNAP SPO22 SRP_TPR_like ST7 Suf SusD-like SusD-like_2 SusD-like_3 SusD_RagB SYCP2_ARLD TAF6_C TAL_effector TAtT Tcf25 TIP120 TOM20_plant TPR_1 TPR_10 TPR_11 TPR_12 TPR_14 TPR_15 TPR_16 TPR_17 TPR_18 TPR_19 TPR_2 TPR_20 TPR_21 TPR_22 TPR_3 TPR_4 TPR_5 TPR_6 TPR_7 TPR_8 TPR_9 TPR_MalT TTC7_N UNC45-central Upf2 V-ATPase_H_C V-ATPase_H_N Vac14_Fab1_bd Vitellogenin_N Vps39_1 W2 WSLR Wzy_C_2 Xpo1 YcaO_C YfiO Zmiz1_N

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
(8)
Full
(1516)
Representative proteomes UniProt
(2423)
RP15
(158)
RP35
(424)
RP55
(1118)
RP75
(1670)
Jalview View  View  View  View  View  View  View 
HTML View  View           
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
(8)
Full
(1516)
Representative proteomes UniProt
(2423)
RP15
(158)
RP35
(424)
RP55
(1118)
RP75
(1670)
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
(8)
Full
(1516)
Representative proteomes UniProt
(2423)
RP15
(158)
RP35
(424)
RP55
(1118)
RP75
(1670)
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_2700 (release 7.6)
Previous IDs: DUF634;
Type: Repeat
Sequence Ontology: SO:0001068
Author: Kerrison ND , Eberhardt R
Number in seed: 8
Number in full: 1516
Average length of the domain: 188.10 aa
Average identity of full alignment: 28 %
Average coverage of the sequence by the domain: 35.10 %

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 20.4 20.4
Trusted cut-off 20.4 20.4
Noise cut-off 20.3 20.3
Model length: 224
Family (HMM) version: 15
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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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
B0BNC7 View 3D Structure Click here
B1WBW4 View 3D Structure Click here
D3ZV39 View 3D Structure Click here
D4A542 View 3D Structure Click here
D4A548 View 3D Structure Click here
E9PWM3 View 3D Structure Click here
F6NIY4 View 3D Structure Click here
I1KHS7 View 3D Structure Click here
O48700 View 3D Structure Click here
Q3UZB0 View 3D Structure Click here
Q54P24 View 3D Structure Click here
Q5H9R4 View 3D Structure Click here
Q5JY77 View 3D Structure Click here
Q5T9G4 View 3D Structure Click here
Q5U310 View 3D Structure Click here
Q5U4C1 View 3D Structure Click here
Q5XID7 View 3D Structure Click here
Q642B5 View 3D Structure Click here
Q66HF0 View 3D Structure Click here
Q6A058 View 3D Structure Click here
Q6P1M9 View 3D Structure Click here
Q6PB60 View 3D Structure Click here
Q6PI77 View 3D Structure Click here
Q71HP2 View 3D Structure Click here
Q7L311 View 3D Structure Click here
Q7L4S7 View 3D Structure Click here
Q80X86 View 3D Structure Click here
Q8BHS6 View 3D Structure Click here
Q8BUY8 View 3D Structure Click here
Q8K3A6 View 3D Structure Click here
Q8N2F6 View 3D Structure Click here
Q920R4 View 3D Structure Click here
Q96D09 View 3D Structure Click here
Q9CX83 View 3D Structure Click here
Q9D0L7 View 3D Structure Click here
Q9P291 View 3D Structure Click here
Q9U1V2 View 3D Structure Click here
Q9UH62 View 3D Structure Click here

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;