Please note: this site relies heavily on the use of javascript. Without a javascript-enabled browser, this site will not function correctly. Please enable javascript and reload the page, or switch to a different browser.
37  structures 3275  species 2  interactions 3610  sequences 26  architectures

Family: YjeF_N (PF03853)

Summary: YjeF-related protein N-terminus

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 "YjeF N terminal protein domain". More...

YjeF N terminal protein domain Edit Wikipedia article

YjeF_N
PDB 1jzt EBI.jpg
crystal structure of yeast ynu0, ynl200c
Identifiers
Symbol YjeF_N
Pfam PF03853
InterPro IPR004443
SCOP 1jzt
SUPERFAMILY 1jzt

In molecular biology, the YjeF N terminal is a protein domain found in the N-terminal of the protein, EDC3. The YjeF N-terminal domains occur either as single proteins or fusions with other domains and are commonly associated with enzymes. They help assemble the processing body (P-body) in preparation for mRNAdecay. Structural homology indicated it may have some similarity to the enzyme family, hydrolase.

Function[edit]

At the cellular level, the YjeF-N terminal domain is vital to the assembly of the processing body (P-body). This aids mRNA decay and is thought to bring together different complexes to aggregate mRNPs.[1] At the organism level, in bacteria and archaea, YjeF N-terminal domains are often fused to a YjeF C-terminal domain with high structural homology to the members of a ribokinase-like superfamily or belong to operons that encode enzymes of diverse functions. Examples of such include:

  • pyridoxal phosphate biosynthetic protein PdxJ;
  • phosphopanteine-protein transferase;
  • ATP/GTP hydrolase;
  • and pyruvate-formate lyase 1-activating enzyme.

In plants, the YjeF N-terminal domain is fused to a C-terminal putative pyridoxamine 5'-phosphate oxidase. In eukaryotes, proteins that consist of (Sm)-FDF-YjeF N-terminal domains may be involved in RNA processing.[2][3]

Structure[edit]

The YjeF N-terminal domains represent a novel version of the Rossmann fold, one of the most common protein folds in nature. The YjeF N-terminal domain is a three-layer alpha-beta-alpha sandwich with a central beta-sheet surrounded by alpha helices. The conservation of the acidic residues in the predicted active site of the YjeF N-terminal domains shows some similarities to the amino acids found in the active sites of diverse hydrolases.[2][3]

References[edit]

  1. ^ Ling SH, Decker CJ, Walsh MA, She M, Parker R, Song H (2008). "Crystal structure of human Edc3 and its functional implications.". Mol Cell Biol 28 (19): 5965–76. doi:10.1128/MCB.00761-08. PMC 2547010. PMID 18678652. 
  2. ^ a b Anantharaman V, Aravind L (July 2004). "Novel conserved domains in proteins with predicted roles in eukaryotic cell-cycle regulation, decapping and RNA stability". BMC Genomics 5 (1): 45. doi:10.1186/1471-2164-5-45. PMC 503384. PMID 15257761. 
  3. ^ a b Jha KN, Shumilin IA, Digilio LC, Chertihin O, Zheng H, Schmitz G, Visconti PE, Flickinger CJ, Minor W, Herr JC (May 2008). "Biochemical and structural characterization of apolipoprotein A-I binding protein, a novel phosphoprotein with a potential role in sperm capacitation". Endocrinology 149 (5): 2108–20. doi:10.1210/en.2007-0582. PMC 2329272. PMID 18202122. 

This article incorporates text from the public domain Pfam and InterPro IPR004443

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.

YjeF-related protein N-terminus Provide feedback

YjeF-N domain is a novel version of the Rossmann fold with a set of catalytic residues and structural features that are different from the conventional dehydrogenases [1]. YjeF-N domain is fused to Ribokinases in bacteria (YjeF), where they may be phosphatases, and to divergent Sm and the FDF domain in eukaryotes (Dcp3p and FLJ21128) [1] where they may be involved in decapping and catalyze hydrolytic RNA-processing reactions [1].

Literature references

  1. Anantharaman V, Aravind L;, BMC Genomics. 2004;5:45.: Novel conserved domains in proteins with predicted roles in eukaryotic cell-cycle regulation, decapping and RNA stability. PUBMED:15257761 EPMC:15257761


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR004443

The YjeF N-terminal domains occur either as single proteins or fusions with other domains and are commonly associated with enzymes. In bacteria and archaea, YjeF N-terminal domains are often fused to a YjeF C-terminal domain with high structural homology to the members of a ribokinase-like superfamily (see PROSITEDOC)and/or belong to operons that encode enzymes of diverse functions: pyridoxal phosphate biosynthetic protein PdxJ; phosphopanteine-protein transferase; ATP/GTP hydrolase; and pyruvate-formate lyase 1-activating enzyme. In plants, the YjeF N-terminal domain is fused to a C-terminal putative pyridoxamine 5'-phosphate oxidase. In eukaryotes, proteins that consist of (Sm)-FDF-YjeF N-terminal domains may be involved in RNA processing [PUBMED:15257761, PUBMED:18202122].

The YjeF N-terminal domains represent a novel version of the Rossmann fold, one of the most common protein folds in nature observed in numerous enzyme families, that has acquired a set of catalytic residues and structural features that distinguish them from the conventional dehydrogenases. The YjeF N-terminal domain is comprised of a three-layer alpha-beta-alpha sandwich with a central beta-sheet surrounded by helices. The conservation of the acidic residues in the predicted active site of the YjeF N-terminal domains is reminiscent of the presence of such residues in the active sites of diverse hydrolases [PUBMED:15257761, PUBMED:18202122].

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

Loading domain graphics...

Pfam Clan

This family is a member of clan NADP_Rossmann (CL0063), which contains the following 180 members:

2-Hacid_dh_C 3Beta_HSD 3HCDH_N adh_short adh_short_C2 ADH_zinc_N ADH_zinc_N_2 AdoHcyase_NAD AdoMet_MTase AlaDh_PNT_C Amino_oxidase ApbA AviRa Bac_GDH Bin3 CheR CMAS CmcI CoA_binding CoA_binding_2 CoA_binding_3 Cons_hypoth95 DAO DapB_N DFP DNA_circ_N DNA_methylase DOT1 DREV dTMP_synthase DUF1442 DUF1776 DUF2431 DUF268 DUF3321 DUF43 DUF633 DUF938 DXP_redisom_C DXP_reductoisom Eco57I ELFV_dehydrog Eno-Rase_FAD_bd Eno-Rase_NADH_b Enoyl_reductase Epimerase F420_oxidored FAD_binding_2 FAD_binding_3 FAD_oxidored Fibrillarin FMO-like FmrO FtsJ G-7-MTase G6PD_N GCD14 GDI GFO_IDH_MocA GIDA GidB GLF Glyco_hydro_4 GMC_oxred_N Gp_dh_N GRAS GRDA HI0933_like HIM1 IlvN K_oxygenase KR LCM Ldh_1_N Lycopene_cycl Malic_M Mannitol_dh Met_10 Methyltrans_Mon Methyltrans_SAM Methyltransf_10 Methyltransf_11 Methyltransf_12 Methyltransf_15 Methyltransf_16 Methyltransf_17 Methyltransf_18 Methyltransf_19 Methyltransf_2 Methyltransf_20 Methyltransf_21 Methyltransf_22 Methyltransf_23 Methyltransf_24 Methyltransf_25 Methyltransf_26 Methyltransf_27 Methyltransf_28 Methyltransf_29 Methyltransf_3 Methyltransf_30 Methyltransf_31 Methyltransf_32 Methyltransf_4 Methyltransf_5 Methyltransf_7 Methyltransf_8 Methyltransf_9 Methyltransf_PK MethyltransfD12 MetW Mg-por_mtran_C Mqo MT-A70 MTS Mur_ligase N2227 N6-adenineMlase N6_Mtase N6_N4_Mtase NAD_binding_10 NAD_binding_11 NAD_binding_2 NAD_binding_3 NAD_binding_4 NAD_binding_5 NAD_binding_7 NAD_binding_8 NAD_binding_9 NAD_Gly3P_dh_N NAS NmrA NNMT_PNMT_TEMT NodS Nol1_Nop2_Fmu Nol1_Nop2_Fmu_2 NSP13 OCD_Mu_crystall PARP_regulatory PCMT PDH Polysacc_synt_2 Pox_MCEL Prenylcys_lyase PrmA PRMT5 Pyr_redox Pyr_redox_2 Pyr_redox_3 RmlD_sub_bind Rossmann-like rRNA_methylase RrnaAD Rsm22 RsmJ Saccharop_dh SAM_MT SE Semialdhyde_dh Shikimate_DH Spermine_synth Strep_67kDa_ant TehB THF_DHG_CYH_C Thi4 ThiF TPMT TrkA_N TRM TRM13 tRNA_U5-meth_tr Trp_halogenase TylF Ubie_methyltran UDPG_MGDP_dh_N UPF0020 UPF0146 V_cholerae_RfbT XdhC_C YjeF_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 using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics 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
(82)
Full
(3610)
Representative proteomes NCBI
(3081)
Meta
(755)
RP15
(398)
RP35
(764)
RP55
(1032)
RP75
(1227)
Jalview View  View  View  View  View  View  View  View 
HTML View  View  View  View  View  View     
PP/heatmap 1 View  View  View  View  View     
Pfam viewer View  View             

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

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

Format an alignment

  Seed
(82)
Full
(3610)
Representative proteomes NCBI
(3081)
Meta
(755)
RP15
(398)
RP35
(764)
RP55
(1032)
RP75
(1227)
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
(82)
Full
(3610)
Representative proteomes NCBI
(3081)
Meta
(755)
RP15
(398)
RP35
(764)
RP55
(1032)
RP75
(1227)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   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.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

Pfam alignments:

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: TIGRFAMs
Previous IDs: none
Type: Domain
Author: TIGRFAMs, Griffiths-Jones SR
Number in seed: 82
Number in full: 3610
Average length of the domain: 164.50 aa
Average identity of full alignment: 29 %
Average coverage of the sequence by the domain: 35.13 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 24.9 24.9
Trusted cut-off 24.9 25.0
Noise cut-off 24.7 24.6
Model length: 169
Family (HMM) version: 10
Download: download the raw HMM for this family

Species distribution

Sunburst controls

Show

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...

Loading sunburst data...

Tree controls

Hide

The tree shows the occurrence of this domain across different species. More...

Loading...

Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.

Interactions

There are 2 interactions for this family. More...

YjeF_N Carb_kinase

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 YjeF_N domain has been found. There are 37 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 seqence.

Loading structure mapping...