0  structures 96  species 0  interactions 150  sequences 3  architectures

Family: DAP3 (PF10236)

Summary

Mitochondrial ribosomal death-associated protein 3 Add an annotation

This is a family of conserved proteins which were originally described as death-associated-protein-3 (DAP-3). The proteins carry a P-loop DNA-binding motif, and induce apoptosis [1]. DAP3 has been shown to be a pro-apoptotic factor in the mitochondrial matrix [2] and to be crucial for mitochondrial biogenesis and so has also been designated as MRP-S29 (mitochondrial ribosomal protein subunit 29).


Literature references

  1. Kissil JL, Cohen O, Raveh T, Kimchi A; , EMBO J. 1999;18:353-362.: Structure-function analysis of an evolutionary conserved protein, DAP3, which mediates TNF-alpha- and Fas-induced cell death. PUBMED:9889192

  2. Berger T, Brigl M, Herrmann JM, Vielhauer V, Luckow B, Schlondorff D, Kretzler M; , J Cell Sci. 2000;113:3603-3612.: The apoptosis mediator mDAP-3 is a novel member of a conserved family of mitochondrial proteins. PUBMED:11017876


InterPro entry IPR019368

Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in accordance with the genetic information. Incoming amino acid monomers enter the ribosomal A site in the form of aminoacyl-tRNAs complexed with elongation factor Tu (EF-Tu) and GTP. The growing polypeptide chain, situated in the P site as peptidyl-tRNA, is then transferred to aminoacyl-tRNA and the new peptidyl-tRNA, extended by one residue, is translocated to the P site with the aid the elongation factor G (EF-G) and GTP as the deacylated tRNA is released from the ribosome through one or more exit sites PUBMED:11297922, PUBMED:11290319. About 2/3 of the mass of the ribosome consists of RNA and 1/3 of protein. The proteins are named in accordance with the subunit of the ribosome which they belong to - the small (S1 to S31) and the large (L1 to L44). Usually they decorate the rRNA cores of the subunits.

Many of ribosomal proteins, particularly those of the large subunit, are composed of a globular, surfaced-exposed domain with long finger-like projections that extend into the rRNA core to stabilise its structure. Most of the proteins interact with multiple RNA elements, often from different domains. In the large subunit, about 1/3 of the 23S rRNA nucleotides are at least in van der Waal's contact with protein, and L22 interacts with all six domains of the 23S rRNA. Proteins S4 and S7, which initiate assembly of the 16S rRNA, are located at junctions of five and four RNA helices, respectively. In this way proteins serve to organise and stabilise the rRNA tertiary structure. While the crucial activities of decoding and peptide transfer are RNA based, proteins play an active role in functions that may have evolved to streamline the process of protein synthesis. In addition to their function in the ribosome, many ribosomal proteins have some function 'outside' the ribosome PUBMED:11290319, PUBMED:11114498.

This entry represents a family of conserved proteins which were originally described as death-associated-protein-3 (DAP-3). The proteins carry a P-loop DNA-binding motif, and induce apoptosis PUBMED:9889192. DAP3 has been shown to be a pro-apoptotic factor in the mitochondrial matrix PUBMED:11017876 and to be crucial for mitochondrial biogenesis and so has also been designated as MRP-S29 (mitochondrial ribosomal protein subunit 29).

Clan

This family is a member of clan AAA (CL0023), which contains the following 142 members:

6PF2K AAA AAA-ATPase_like AAA_2 AAA_3 AAA_5 AAA_PrkA ABC_ATPase ABC_tran Adeno_IVa2 Adenylsucc_synt ADK AFG1_ATPase AIG1 APS_kinase Arch_ATPase Arf ArgK ArsA_ATPase ATP-synt_ab ATP_bind_1 ATP_bind_2 Bac_DnaA CbiA CoaE CobA_CobO_BtuR CobU cobW CPT CTP_synth_N Cytidylate_kin DAP3 DEAD DEAD_2 DLIC DNA_pack_C DNA_pack_N DNA_pol3_delta DnaB_C dNK DUF1253 DUF1611 DUF2075 DUF2478 DUF258 DUF265 DUF699 DUF815 DUF853 DUF87 DUF889 Dynamin_N Exonuc_V_gamma FeoB_N Fer4_NifH Flavi_DEAD FTHFS FtsK_SpoIIIE G-alpha Gal-3-0_sulfotr GBP GSPII_E GTP_EFTU Gtr1_RagA Guanylate_kin GvpD HDA2-3 Helicase_C Herpes_Helicase Herpes_ori_bp Herpes_TK IIGP IPPT IPT IstB KaiC KAP_NTPase Kinesin KTI12 LpxK MCM Mg_chelatase MipZ Miro MMR_HSR1 MobB MutS_V Myosin_head NACHT NB-ARC NOG1 ParA Parvo_NS1 PAXNEB PduV-EutP PhoH Podovirus_Gp16 Polyoma_lg_T_C Pox_A32 PPK2 PPV_E1_C PRK Rad17 Rad51 Ras RecA Rep_fac_C ResIII RHD3 RNA12 RNA_helicase RuvB_N SecA_DEAD Septin Sigma54_activat SKI SMC_N SNF2_N Spore_IV_A SRP54 SRPRB Sulfotransfer_1 Sulfotransfer_2 Sulphotransf Terminase_1 Terminase_3 Terminase_6 Terminase_GpA Thymidylate_kin TIP49 TK TniB Torsin TraG TrwB_AAD_bind UPF0079 UvrD-helicase Viral_helicase1 VirC1 YhjQ Zeta_toxin Zot

External database links

Domain organisation

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Alignments

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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.

You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.

Pfam alignments:
Full length sequences

External links

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Trees

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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: KOGs (KOG3928)
Previous IDs: none
Type: Family
Author: KOGs, Finn RD, Coggill PC
Number in seed: 31
Number in full: 150
Average length of the domain: 281.80 aa
Average identity of full alignment: 22 %
Average coverage of the sequence by the domain: 62.08 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 23.1 23.1
Trusted cut-off 23.1 23.2
Noise cut-off 23.0 22.6
Model length: 309
Family (HMM) version: 2
Download: download the raw HMM for this family

Species distribution

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