Summary: Iron-sulfur cluster assembly protein
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Iron-sulfur cluster assembly protein Provide feedback
This family has an alpha/beta topology, with 13 conserved hydrophobic residues at its core and a putative active site containing a highly conserved cysteine [1]. Members of this family are involved in a range of physiological functions. The family includes PaaJ (PhaH) O84984 from Pseudomonas putida. PaaJ forms a complex with PaaG (PhaF) O84982 PaaI (PhaG) O84983 and PaaK (PhaI) O84985 which hydroxylates phenylacetic acid to 2-hydroxyphenylacetic acid [2]. It also includes PaaD P76080 from Escherichia coli, a member of a multicomponent oxygenase involved in phenylacetyl-CoA hydroxylation [3]. Furthermore, several members of this family are shown to be involved in iron-sulfur (FeS) cluster assembly. Iron-sulfur (FeS) clusters are inorganic co-factors that are are able to transfer electrons and act as catalysts [4]. They are involved in diverse cellular processes including cellular respiration, DNA replication and repair, antibiotic resistance, and dinitrogen fixation [5]. The biogenesis of such clusters from elemental iron and sulfur is an enzymatic process that requires a set of specialised proteins. Proteins containing this domain include the chloroplast protein HCF101 (high chlorophyll fluorescence 101), Q6STH5 which has been described as an essential and specific factor for assembly of [4Fe-4S]-cluster-containing protein complexes such as the membrane complex Photosystem I (PSI) and the heterodimeric FTR (ferredoxin-thioredoxin reductase) complex [4] and is involved in the assembly of [4Fe-4S] clusters and their transfer to apoproteins [4]. The mature HCF101 protein contains this domain at the N-terminal as well as eight cysteine residues along the sequence. All cysteine residues are conserved among higher plants, but of the two cysteine residues located in this domain only Cys128 is highly conserved and is present in the highly conserved P-loop domain of the plant HCF101 (CKGGVGKS) [4]. SufT protein from Staphylococcus aureus is composed of this domain solely and is shown to be involved in the maturation of FeS proteins [5]. Given all this data, it is hypothesised that this domain might play a role in FeS cluster assembly.
Literature references
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Almeida MS, Herrmann T, Peti W, Wilson IA, Wuthrich K;, Protein Sci. 2005;14:2880-2886.: NMR structure of the conserved hypothetical protein TM0487 from Thermotoga maritima: implications for 216 homologous DUF59 proteins. PUBMED:16199668 EPMC:16199668
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Olivera ER, Minambres B, Garcia B, Muniz C, Moreno MA, Ferrandez A, Diaz E, Garcia JL, Luengo JM; , Proc Natl Acad Sci U S A 1998;95:6419-6424.: Molecular characterization of the phenylacetic acid catabolic pathway in Pseudomonas putida U: the phenylacetyl-CoA catabolon. PUBMED:9600981 EPMC:9600981
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Ferrandez A, Minambres B, Garcia B, Olivera ER, Luengo JM, Garcia JL, Diaz E; , J Biol Chem 1998;273:25974-25986.: Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway. PUBMED:9748275 EPMC:9748275
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Schwenkert S, Netz DJ, Frazzon J, Pierik AJ, Bill E, Gross J, Lill R, Meurer J;, Biochem J. 2009;425:207-214.: Chloroplast HCF101 is a scaffold protein for [4Fe-4S] cluster assembly. PUBMED:19817716 EPMC:19817716
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Mashruwala AA, Bhatt S, Poudel S, Boyd ES, Boyd JM;, PLoS Genet. 2016;12:e1006233.: The DUF59 Containing Protein SufT Is Involved in the Maturation of Iron-Sulfur (FeS) Proteins during Conditions of High FeS Cofactor Demand in Staphylococcus aureus. PUBMED:27517714 EPMC:27517714
Internal database links
SCOOP: | NifU |
This tab holds annotation information from the InterPro database.
InterPro entry IPR002744
This domain (previously known as DUF59) is found in proteins that are mostly defined as members of the MIP18 family. This includes iron-sulfur cluster carrier proteins, where the domain is found in the N terminus. This domain is also found in protein AE7 from Arabidopsis and its homologues. Protein AE7 is thought to be a central member of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) pathway, however protein AE7-like 1 and 2 (also containing this domain) are probably not involved in this pathway [ PUBMED:23104832 ]. MIP18 family protein YHR122W (CIA2) from S. cerevisiae is a component of the CIA machinery, and acts at a late step of Fe-S cluster assembly [ PUBMED:22678362 ]. The SufT protein from Staphylococcus aureus is composed of this domain solely and is involved in the maturation of FeS proteins [ PUBMED:27517714 ].
Domain organisation
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Pfam Clan
Alignments
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Seed (39) |
Full (16223) |
Representative proteomes | UniProt (66791) |
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RP15 (2037) |
RP35 (7426) |
RP55 (16402) |
RP75 (27653) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (39) |
Full (16223) |
Representative proteomes | UniProt (66791) |
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RP15 (2037) |
RP35 (7426) |
RP55 (16402) |
RP75 (27653) |
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Raw Stockholm | |||||||
Gzipped |
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.
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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
Seed source: | Enright A |
Previous IDs: | DUF59; Iron-sulfur; |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Enright A |
Number in seed: | 39 |
Number in full: | 16223 |
Average length of the domain: | 74.6 aa |
Average identity of full alignment: | 25 % |
Average coverage of the sequence by the domain: | 32.25 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 75 | ||||||||||||
Family (HMM) version: | 22 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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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 FeS_assembly_P domain has been found. There are 30 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.