| Type |
Details |
Score |
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| First Author: |
Senis YA |
| Year: |
2003 |
| Journal: |
Exp Hematol |
| Title: |
Fps/Fes and Fer protein-tyrosinekinases play redundant roles in regulating hematopoiesis. |
| Volume: |
31 |
| Issue: |
8 |
| Pages: |
673-81 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Khajah M |
| Year: |
2013 |
| Journal: |
J Immunol |
| Title: |
Fer kinase limits neutrophil chemotaxis toward end target chemoattractants. |
| Volume: |
190 |
| Issue: |
5 |
| Pages: |
2208-16 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Senis YA |
| Year: |
2003 |
| Journal: |
J Thromb Haemost |
| Title: |
Fps/Fes and Fer non-receptor protein-tyrosine kinases regulate collagen- and ADP-induced platelet aggregation. |
| Volume: |
1 |
| Issue: |
5 |
| Pages: |
1062-70 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Kozak CA |
| Year: |
1983 |
| Journal: |
J Virol |
| Title: |
Genetic mapping of the mouse oncogenes c-Ha-ras-1 and c-fes to chromosome 7. |
| Volume: |
47 |
| Issue: |
1 |
| Pages: |
217-20 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Haigh JJ |
| Year: |
2004 |
| Journal: |
Blood |
| Title: |
Activated Fps/Fes partially rescues the in vivo developmental potential of Flk1-deficient vascular progenitor cells. |
| Volume: |
103 |
| Issue: |
3 |
| Pages: |
912-20 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Zhang C |
| Year: |
2013 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
Design and pharmacology of a highly specific dual FMS and KIT kinase inhibitor. |
| Volume: |
110 |
| Issue: |
14 |
| Pages: |
5689-94 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Lu X |
| Year: |
2001 |
| Journal: |
Mamm Genome |
| Title: |
The murine perilipin gene: the lipid droplet-associated perilipins derive from tissue-specific, mRNA splice variants and define a gene family of ancient origin. |
| Volume: |
12 |
| Issue: |
9 |
| Pages: |
741-9 |
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•
•
•
•
•
|
| Publication |
| First Author: |
Walcz E |
| Year: |
1994 |
| Journal: |
Genomics |
| Title: |
Complete coding sequence, deduced primary structure, chromosomal localization, and structural analysis of murine aggrecan. |
| Volume: |
22 |
| Issue: |
2 |
| Pages: |
364-71 |
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•
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•
•
•
|
| Publication |
| First Author: |
Shapovalova Z |
| Year: |
2007 |
| Journal: |
BMC Dev Biol |
| Title: |
The Fer tyrosine kinase regulates an axon retraction response to Semaphorin 3A in dorsal root ganglion neurons. |
| Volume: |
7 |
|
| Pages: |
133 |
|
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•
•
•
•
|
| Publication |
| First Author: |
Bremner R |
| Year: |
1990 |
| Journal: |
Cell |
| Title: |
Genetic changes in skin tumor progression: correlation between presence of a mutant ras gene and loss of heterozygosity on mouse chromosome 7. |
| Volume: |
61 |
| Issue: |
3 |
| Pages: |
407-17 |
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•
•
•
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| Publication |
| First Author: |
Aponte JL |
| Year: |
2001 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
Point mutations in the murine fumarylacetoacetate hydrolase gene: Animal models for the human genetic disorder hereditary tyrosinemia type 1. |
| Volume: |
98 |
| Issue: |
2 |
| Pages: |
641-5 |
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•
•
•
•
•
|
| Publication |
| First Author: |
Stoll J |
| Year: |
1990 |
| Journal: |
Genomics |
| Title: |
Characterization and chromosomal mapping of a cDNA encoding tryptophan hydroxylase from a mouse mastocytoma cell line. |
| Volume: |
7 |
| Issue: |
1 |
| Pages: |
88-96 |
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•
•
•
•
|
| Publication |
| First Author: |
Potter MD |
| Year: |
1993 |
| Journal: |
Mamm Genome |
| Title: |
Deletion mapping of the chocolate (cht) locus within the Fes-Hbb region of mouse chromosome 7. |
| Volume: |
4 |
| Issue: |
1 |
| Pages: |
46-8 |
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•
•
•
•
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| First Author: |
Potter MD |
| Year: |
1995 |
| Journal: |
Mamm Genome |
| Title: |
Genetic and physical mapping of the fitness 1 (fit1) locus within the Fes-Hbb region of mouse chromosome 7. |
| Volume: |
6 |
| Issue: |
2 |
| Pages: |
70-5 |
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•
•
•
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| Publication |
| First Author: |
Couldrey C |
| Year: |
2005 |
| Journal: |
Blood |
| Title: |
A STAT5 modifier locus on murine chromosome 7 modulates engraftment of hematopoietic stem cells during steady-state hematopoiesis. |
| Volume: |
105 |
| Issue: |
4 |
| Pages: |
1476-83 |
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•
•
•
|
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| First Author: |
Huynh H |
| Year: |
2004 |
| Journal: |
Nat Cell Biol |
| Title: |
Control of vesicle fusion by a tyrosine phosphatase. |
| Volume: |
6 |
| Issue: |
9 |
| Pages: |
831-9 |
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•
•
•
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| First Author: |
Brouillette JA |
| Year: |
2000 |
| Journal: |
Mamm Genome |
| Title: |
Estimate of nucleotide diversity in dogs with a pool-and-sequence method. |
| Volume: |
11 |
| Issue: |
12 |
| Pages: |
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•
•
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| First Author: |
Blatt C |
| Year: |
1984 |
| Journal: |
Mol Cell Biol |
| Title: |
Chromosomal mapping of murine c-fes and c-src genes. |
| Volume: |
4 |
| Issue: |
5 |
| Pages: |
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•
•
•
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| First Author: |
Udell CM |
| Year: |
2006 |
| Journal: |
J Biol Chem |
| Title: |
Fer and Fps/Fes participate in a Lyn-dependent pathway from FcepsilonRI to platelet-endothelial cell adhesion molecule 1 to limit mast cell activation. |
| Volume: |
281 |
| Issue: |
30 |
| Pages: |
20949-57 |
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•
•
•
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| First Author: |
Saga Y |
| Year: |
1996 |
| Journal: |
Development |
| Title: |
MesP1: a novel basic helix-loop-helix protein expressed in the nascent mesodermal cells during mouse gastrulation. |
| Volume: |
122 |
| Issue: |
9 |
| Pages: |
2769-78 |
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•
•
•
•
|
| Publication |
| First Author: |
Watanabe H |
| Year: |
1994 |
| Journal: |
Nat Genet |
| Title: |
Mouse cartilage matrix deficiency (cmd) caused by a 7 bp deletion in the aggrecan gene. |
| Volume: |
7 |
| Issue: |
2 |
| Pages: |
154-7 |
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•
•
•
•
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| First Author: |
Xu S |
| Year: |
2012 |
| Journal: |
Nat Immunol |
| Title: |
Constitutive MHC class I molecules negatively regulate TLR-triggered inflammatory responses via the Fps-SHP-2 pathway. |
| Volume: |
13 |
| Issue: |
6 |
| Pages: |
551-9 |
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•
•
•
•
|
| Publication |
| First Author: |
Craig AW |
| Year: |
2002 |
| Journal: |
Mol Cell Biol |
| Title: |
Fer kinase is required for sustained p38 kinase activation and maximal chemotaxis of activated mast cells. |
| Volume: |
22 |
| Issue: |
18 |
| Pages: |
6363-74 |
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•
•
•
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| Publication |
| First Author: |
Wilks AF |
| Year: |
1989 |
| Journal: |
Gene |
| Title: |
The application of the polymerase chain reaction to cloning members of the protein tyrosine kinase family. |
| Volume: |
85 |
| Issue: |
1 |
| Pages: |
67-74 |
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•
•
•
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| First Author: |
Leff SE |
| Year: |
1992 |
| Journal: |
Nat Genet |
| Title: |
Maternal imprinting of the mouse Snrpn gene and conserved linkage homology with the human Prader-Willi syndrome region. |
| Volume: |
2 |
| Issue: |
4 |
| Pages: |
259-64 |
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| First Author: |
Rohm B |
| Year: |
2000 |
| Journal: |
FEBS Lett |
| Title: |
The semaphorin 3A receptor may directly regulate the activity of small GTPases. |
| Volume: |
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| Issue: |
1 |
| Pages: |
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•
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| First Author: |
Tessarollo L |
| Year: |
1993 |
| Journal: |
Development |
| Title: |
trkC, a receptor for neurotrophin-3, is widely expressed in the developing nervous system and in non-neuronal tissues. |
| Volume: |
118 |
| Issue: |
2 |
| Pages: |
463-75 |
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| First Author: |
Copeland NG |
| Year: |
1992 |
| Journal: |
Genomics |
| Title: |
Regional localization of three convertases, PC1 (Nec-1), PC2 (Nec-2), and furin (Fur), on mouse chromosomes. |
| Volume: |
13 |
| Issue: |
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| First Author: |
Foroni L |
| Year: |
1992 |
| Journal: |
J Mol Biol |
| Title: |
The rhombotin gene family encode related LIM-domain proteins whose differing expression suggests multiple roles in mouse development. |
| Volume: |
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3 |
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Cheah YC |
| Year: |
1994 |
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Mamm Genome |
| Title: |
New murine polymorphisms detected by random amplified polymorphic DNA (RAPD) PCR and mapped by use of recombinant inbred strains. |
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Rinke de Wit TF |
| Year: |
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| Journal: |
Int Immunol |
| Title: |
Expression of tyrosine kinase gene in mouse thymic stromal cells. |
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11 |
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Slamon DJ |
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Proc Natl Acad Sci U S A |
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Expression of cellular oncogenes during embryonic and fetal development of the mouse. |
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Martin JF |
| Year: |
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Mol Cell Biol |
| Title: |
A Mef2 gene that generates a muscle-specific isoform via alternative mRNA splicing. |
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Masuhara M |
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2000 |
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Biochem Biophys Res Commun |
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Molecular cloning of murine STAP-1, the stem-cell-specific adaptor protein containing PH and SH2 domains. |
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Saunders AM |
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1990 |
| Journal: |
Genomics |
| Title: |
The syntenic relationship of proximal mouse chromosome 7 and the myotonic dystrophy gene region on human chromosome 19q. |
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Colombo MP |
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Mamm Genome |
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Localization of growth arrest-specific genes on mouse chromosomes 1, 7, 8, 11, 13, and 16. |
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Jak2 is essential for signaling through a variety of cytokine receptors. |
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Identification of tyrosine kinases expressed in the male mouse gubernaculum during development. |
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Saunders AM |
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Genomics |
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A molecular genetic linkage map of mouse chromosome 7. |
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Mouse chromosomal locations of nine genes encoding homologs of human paraneoplastic neurologic disorder antigens. |
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The protein tyrosine kinase family of the human genome. |
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International Knockout Mouse Consortium |
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MGI download of modified allele data from IKMC and creation of new knockout alleles |
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International Mouse Strain Resource |
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MGI download of germline transmission data for alleles from IMSR strain data |
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| UniProt Feature |
| Begin: |
247 |
| Description: |
Phosphotyrosine; by FES |
| Type: |
modified residue |
| End: |
247 |
|
•
•
•
•
•
|
| GO Term |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
388 |
| Description: |
Phosphotyrosine; by SYK and FES |
| Type: |
modified residue |
| End: |
388 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
405 |
| Description: |
Phosphotyrosine; by SYK and FES |
| Type: |
modified residue |
| End: |
405 |
|
•
•
•
•
•
|
| Gene |
| Type: |
gene |
| Organism: |
frog, African clawed |
|
•
•
•
•
•
|
| Gene |
| Type: |
gene |
| Organism: |
frog, African clawed |
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•
•
•
•
•
|
| Publication |
| First Author: |
Wolski SC |
| Year: |
2008 |
| Journal: |
PLoS Biol |
| Title: |
Crystal structure of the FeS cluster-containing nucleotide excision repair helicase XPD. |
| Volume: |
6 |
| Issue: |
6 |
| Pages: |
e149 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S]and [4Fe-4S][]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S]form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S]clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.The ISC system is conserved in eubacteria and eukaryotes (mitochondria), and has broad specificity, targeting general FeS proteins [, ]. It is encoded by the isc operon (iscRSUA-hscBA-fdx-iscX). IscS is a cysteine desulphurase, which obtains S from cysteine (converting it to alanine) and serves as a S donor for FeS cluster assembly. IscU and IscA act as scaffolds to accept S and Fe atoms, assembling clusters and transfering them to recipient apoproteins. HscA is a molecular chaperone and HscB is a co-chaperone. Fdx is a [2Fe-2S]-type ferredoxin. IscR is a transcription factor that regulates expression of the isc operon. IscX (also known as YfhJ) appears to interact with IscS and may function as an Fe donor during cluster assembly [].The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA []. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA [], acting as a scaffold protein in which Fe and S atoms are assembled into [FeS]cluster forms, which can then easily be transferred to apoproteins targets.In the NIF system, NifS and NifU are required for the formation of metalloclusters of nitrogenase in Azotobacter vinelandii, and other organisms, as well as in the maturation of other FeS proteins. Nitrogenase catalyses the fixation of nitrogen. It contains a complex cluster, the FeMo cofactor, which contains molybdenum, Fe and S. NifS is a cysteine desulphurase. NifU binds one Fe atom at its N-terminal, assembling an FeS cluster that is transferred to nitrogenase apoproteins []. Nif proteins involved in the formation of FeS clusters can also be found in organisms that do not fix nitrogen [].This entry represents the SufA protein of the SUF system of iron-sulphur cluster biosynthesis. SufA acts as a scaffold in which Fe and S are assembled into FeS clusters []. This system performs FeS biosynthesis even during oxidative stress and tends to be absent in obligate anaerobic and microaerophilic bacteria. |
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•
•
•
•
•
|
| Publication |
| First Author: |
Jücker M |
| Year: |
1997 |
| Journal: |
J Biol Chem |
| Title: |
The Fes protein-tyrosine kinase phosphorylates a subset of macrophage proteins that are involved in cell adhesion and cell-cell signaling. |
| Volume: |
272 |
| Issue: |
4 |
| Pages: |
2104-9 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Lill R |
| Year: |
2006 |
| Journal: |
Annu Rev Cell Dev Biol |
| Title: |
Iron-sulfur protein biogenesis in eukaryotes: components and mechanisms. |
| Volume: |
22 |
|
| Pages: |
457-86 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Proteins in this entry include HesB, IscA, SufA and ErpA, and appear to be scaffold proteins upon which 2Fe-2S clusters are assembled and subsequently transferred to acceptor proteins. Several multiprotein complexes, referred to as ISC, SUF, and NIF, are known to be necessary for building and inserting Fe-S clusters into cellular targets []. The HesB proteins are associated with the nif gene cluster. The Escherichia coli SufA protein is associated with SufS, a NifS homologue, and SufD which are involved in the FeS cluster assembly of the FhnF protein []. The Azotobacter protein IscA (homologues of which are also found in E. coli) is associated which IscS, another NifS homologue, and IscU, a NifU homologue, as well as other factors consistent with a role in FeS cluster chemistry []. ErpA is required, together with IscA, for the delivery of iron-sulphur clusters to the hydrogen-oxidizing [NiFe]-hydrogenases in Escherichia coli [, ]. |
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•
•
•
•
•
|
| Publication |
| First Author: |
Moreira MA |
| Year: |
1997 |
| Journal: |
Cytogenet Cell Genet |
| Title: |
Assignment of TCF1, TGM1, CALM1, CKB, THBS1, B2M, and FES in Ateles paniscus chamek (Platyrrhini, Primates). |
| Volume: |
79 |
| Issue: |
1-2 |
| Pages: |
92-6 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
McPherson VA |
| Year: |
2009 |
| Journal: |
Mol Cell Biol |
| Title: |
Contributions of F-BAR and SH2 domains of Fes protein tyrosine kinase for coupling to the FcepsilonRI pathway in mast cells. |
| Volume: |
29 |
| Issue: |
2 |
| Pages: |
389-401 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Huang TC |
| Year: |
1999 |
| Journal: |
Microbiology |
| Title: |
Organization and expression of nitrogen-fixation genes in the aerobic nitrogen-fixing unicellular cyanobacterium Synechococcus sp. strain RF-1. |
| Volume: |
145 ( Pt 3) |
|
| Pages: |
743-53 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
The proteins in this entry are variously annotated as iron-sulphur cluster insertion protein or Fe/S biogenesis protein. They appear to be involved in Fe-S cluster biogenesis. This family includes IscA, HesB, YadR and YfhF-like proteins. The hesB gene is expressed only under nitrogen fixation conditions []. IscA, an 11kDa member of the hesB family of proteins, binds iron and [2Fe-2S]clusters, and participates in the biosynthesis of iron-sulphur proteins. IscA is able to bind at least 2 iron ions per dimer []. Other members of this family include various hypothetical proteins that also contain the NifU-like domain () suggesting that they too are able to bind iron and are involved in Fe-S cluster biogenesis. The HesB family are found in species as divergent as Homo sapiens (Human) and Haemophilus influenzae suggesting that these proteins are involved in basic cellular functions []. |
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•
•
•
•
•
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| Protein Domain |
| Type: |
Family |
| Description: |
Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S]and [4Fe-4S][]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S]form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S]clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.The ISC system is conserved in eubacteria and eukaryotes (mitochondria), and has broad specificity, targeting general FeS proteins [, ]. It is encoded by the isc operon (iscRSUA-hscBA-fdx-iscX). IscS is a cysteine desulphurase, which obtains S from cysteine (converting it to alanine) and serves as a S donor for FeS cluster assembly. IscU and IscA act as scaffolds to accept S and Fe atoms, assembling clusters and transfering them to recipient apoproteins. HscA is a molecular chaperone and HscB is a co-chaperone. Fdx is a [2Fe-2S]-type ferredoxin. IscR is a transcription factor that regulates expression of the isc operon. IscX (also known as YfhJ) appears to interact with IscS and may function as an Fe donor during cluster assembly [].This entry represents IscX proteins (also known as hypothetical protein YfhJ) that are part of the ISC system. IscX is active as a monomer. The structure of YfhJ is an orthogonal α-bundle []. YfhJ is a small acidic protein that binds IscS, and contains a modified winged helix motif that is usually found in DNA-binding proteins []. YfhJ/IscX can bind Fe, and may function as an Fe donor in the assembly of FeS clusters |
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•
•
•
•
•
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| Publication |
| First Author: |
Cupp-Vickery JR |
| Year: |
2004 |
| Journal: |
J Mol Biol |
| Title: |
Crystal structure of IscA, an iron-sulfur cluster assembly protein from Escherichia coli. |
| Volume: |
338 |
| Issue: |
1 |
| Pages: |
127-37 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S]and [4Fe-4S][]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S]form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S]clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.The ISC system is conserved in eubacteria and eukaryotes (mitochondria), and has broad specificity, targeting general FeS proteins [, ]. It is encoded by the isc operon (iscRSUA-hscBA-fdx-iscX). IscS is a cysteine desulphurase, which obtains S from cysteine (converting it to alanine) and serves as a S donor for FeS cluster assembly. IscU and IscA act as scaffolds to accept S and Fe atoms, assembling clusters and transfering them to recipient apoproteins. HscA is a molecular chaperone and HscB is a co-chaperone. Fdx is a [2Fe-2S]-type ferredoxin. IscR is a transcription factor that regulates expression of the isc operon. IscX (also known as YfhJ) appears to interact with IscS and may function as an Fe donor during cluster assembly [].The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA []. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA [], acting as a scaffold protein in which Fe and S atoms are assembled into [FeS]cluster forms, which can then easily be transferred to apoproteins targets.In the NIF system, NifS and NifU are required for the formation of metalloclusters of nitrogenase in Azotobacter vinelandii, and other organisms, as well as in the maturation of other FeS proteins. Nitrogenase catalyses the fixation of nitrogen. It contains a complex cluster, the FeMo cofactor, which contains molybdenum, Fe and S. NifS is a cysteine desulphurase. NifU binds one Fe atom at its N-terminal, assembling an FeS cluster that is transferred to nitrogenase apoproteins []. Nif proteins involved in the formation of FeS clusters can also be found in organisms that do not fix nitrogen [].This entry is a subset of the larger family. Many members of are candidate ring hydroxylating complex subunits. However, members of the narrower family defined here are all found as part of the FeS assembly SUF system locus, in a subset of SUF-positive proteobacteria. |
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•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
209
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
124
|
| Fragment?: |
false |
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•
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•
•
|
| Publication |
| First Author: |
Rangachari K |
| Year: |
2002 |
| Journal: |
FEBS Lett |
| Title: |
SufC hydrolyzes ATP and interacts with SufB from Thermotoga maritima. |
| Volume: |
514 |
| Issue: |
2-3 |
| Pages: |
225-8 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Tapley TL |
| Year: |
2004 |
| Journal: |
J Biol Chem |
| Title: |
Preferential substrate binding orientation by the molecular chaperone HscA. |
| Volume: |
279 |
| Issue: |
27 |
| Pages: |
28435-42 |
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•
•
•
•
•
|
| Publication |
| First Author: |
Abdel-Ghany SE |
| Year: |
2005 |
| Journal: |
Plant Physiol |
| Title: |
Iron-sulfur cluster biogenesis in chloroplasts. Involvement of the scaffold protein CpIscA. |
| Volume: |
138 |
| Issue: |
1 |
| Pages: |
161-72 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
This entry represents a group of iron-sulfur assembly proteins mainly from plants and cyanobacteria, including AtCPISCA (AT1G10500, ) from Arabidopsis. AtCPISCA has homology to bacterial IscA and SufA proteins that have a scaffold function during Fe-S cluster formation. It may serve as a scaffold in chloroplast Fe-S cluster assembly [].This clade is distinctive from the proteobacteria clade shown in . Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S]and [4Fe-4S][]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S]form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S]clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.The ISC system is conserved in eubacteria and eukaryotes (mitochondria), and has broad specificity, targeting general FeS proteins [, ]. It is encoded by the isc operon (iscRSUA-hscBA-fdx-iscX). IscS is a cysteine desulphurase, which obtains S from cysteine (converting it to alanine) and serves as a S donor for FeS cluster assembly. IscU and IscA act as scaffolds to accept S and Fe atoms, assembling clusters and transfering them to recipient apoproteins. HscA is a molecular chaperone and HscB is a co-chaperone. Fdx is a [2Fe-2S]-type ferredoxin. IscR is a transcription factor that regulates expression of the isc operon. IscX (also known as YfhJ) appears to interact with IscS and may function as an Fe donor during cluster assembly [].The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA []. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA [], acting as a scaffold protein in which Fe and S atoms are assembled into [FeS]cluster forms, which can then easily be transferred to apoproteins targets.In the NIF system, NifS and NifU are required for the formation of metalloclusters of nitrogenase in Azotobacter vinelandii, and other organisms, as well as in the maturation of other FeS proteins. Nitrogenase catalyses the fixation of nitrogen. It contains a complex cluster, the FeMo cofactor, which contains molybdenum, Fe and S. NifS is a cysteine desulphurase. NifU binds one Fe atom at its N-terminal, assembling an FeS cluster that is transferred to nitrogenase apoproteins []. Nif proteins involved in the formation of FeS clusters can also be found in organisms that do not fix nitrogen []. |
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•
•
•
•
•
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| Protein Domain |
| Type: |
Family |
| Description: |
Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S]and [4Fe-4S][]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S]form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S]clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.The ISC system is conserved in eubacteria and eukaryotes (mitochondria), and has broad specificity, targeting general FeS proteins [, ]. It is encoded by the isc operon (iscRSUA-hscBA-fdx-iscX). IscS is a cysteine desulphurase, which obtains S from cysteine (converting it to alanine) and serves as a S donor for FeS cluster assembly. IscU and IscA act as scaffolds to accept S and Fe atoms, assembling clusters and transfering them to recipient apoproteins. HscA is a molecular chaperone and HscB is a co-chaperone. Fdx is a [2Fe-2S]-type ferredoxin. IscR is a transcription factor that regulates expression of the isc operon. IscX (also known as YfhJ) appears to interact with IscS and may function as an Fe donor during cluster assembly [].The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA []. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA [], acting as a scaffold protein in which Fe and S atoms are assembled into [FeS]cluster forms, which can then easily be transferred to apoproteins targets.In the NIF system, NifS and NifU are required for the formation of metalloclusters of nitrogenase in Azotobacter vinelandii, and other organisms, as well as in the maturation of other FeS proteins. Nitrogenase catalyses the fixation of nitrogen. It contains a complex cluster, the FeMo cofactor, which contains molybdenum, Fe and S. NifS is a cysteine desulphurase. NifU binds one Fe atom at its N-terminal, assembling an FeS cluster that is transferred to nitrogenase apoproteins []. Nif proteins involved in the formation of FeS clusters can also be found in organisms that do not fix nitrogen [].This entry represents the NifU protein from the NIF system that is involved in nitrogenase maturation. |
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•
•
•
•
•
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| Protein Domain |
| Type: |
Family |
| Description: |
Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S]and [4Fe-4S][]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S]form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S]clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.The ISC system is conserved in eubacteria and eukaryotes (mitochondria), and has broad specificity, targeting general FeS proteins [, ]. It is encoded by the isc operon (iscRSUA-hscBA-fdx-iscX). IscS is a cysteine desulphurase, which obtains S from cysteine (converting it to alanine) and serves as a S donor for FeS cluster assembly. IscU and IscA act as scaffolds to accept S and Fe atoms, assembling clusters and transfering them to recipient apoproteins. HscA is a molecular chaperone and HscB is a co-chaperone. Fdx is a [2Fe-2S]-type ferredoxin. IscR is a transcription factor that regulates expression of the isc operon. IscX (also known as YfhJ) appears to interact with IscS and may function as an Fe donor during cluster assembly [].The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA []. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA [], acting as a scaffold protein in which Fe and S atoms are assembled into [FeS]cluster forms, which can then easily be transferred to apoproteins targets.In the NIF system, NifS and NifU are required for the formation of metalloclusters of nitrogenase in Azotobacter vinelandii, and other organisms, as well as in the maturation of other FeS proteins. Nitrogenase catalyses the fixation of nitrogen. It contains a complex cluster, the FeMo cofactor, which contains molybdenum, Fe and S. NifS is a cysteine desulphurase. NifU binds one Fe atom at its N-terminal, assembling an FeS cluster that is transferred to nitrogenase apoproteins []. Nif proteins involved in the formation of FeS clusters can also be found in organisms that do not fix nitrogen [].This entry represents proteins belonging to the Rrf2 family of transcriptional regulators and are found, typically, as the first gene of the SUF operon. They are found only in a subset of the genomes that encode the SUF system, including the genus Xanthomonas. The conserved location suggests an autoregulatory role. |
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•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S]and [4Fe-4S][]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S]form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S]clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.The ISC system is conserved in eubacteria and eukaryotes (mitochondria), and has broad specificity, targeting general FeS proteins [, ]. It is encoded by the isc operon (iscRSUA-hscBA-fdx-iscX). IscS is a cysteine desulphurase, which obtains S from cysteine (converting it to alanine) and serves as a S donor for FeS cluster assembly. IscU and IscA act as scaffolds to accept S and Fe atoms, assembling clusters and transfering them to recipient apoproteins. HscA is a molecular chaperone and HscB is a co-chaperone. Fdx is a [2Fe-2S]-type ferredoxin. IscR is a transcription factor that regulates expression of the isc operon. IscX (also known as YfhJ) appears to interact with IscS and may function as an Fe donor during cluster assembly [].The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA []. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA [], acting as a scaffold protein in which Fe and S atoms are assembled into [FeS]cluster forms, which can then easily be transferred to apoproteins targets.In the NIF system, NifS and NifU are required for the formation of metalloclusters of nitrogenase in Azotobacter vinelandii, and other organisms, as well as in the maturation of other FeS proteins. Nitrogenase catalyses the fixation of nitrogen. It contains a complex cluster, the FeMo cofactor, which contains molybdenum, Fe and S. NifS is a cysteine desulphurase. NifU binds one Fe atom at its N-terminal, assembling an FeS cluster that is transferred to nitrogenase apoproteins []. Nif proteins involved in the formation of FeS clusters can also be found in organisms that do not fix nitrogen [].This entry represents the N-terminal of NifU and homologous proteins. NifU contains two domains: an N-terminal and a C-terminal domain () []. These domains exist either together or on different polypeptides, both domains being found in organismsthat do not fix nitrogen (e.g. yeast), so they have a broader significance in the cell than nitrogen fixation. |
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•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S]and [4Fe-4S][]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S]form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S]clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.The ISC system is conserved in eubacteria and eukaryotes (mitochondria), and has broad specificity, targeting general FeS proteins [, ]. It is encoded by the isc operon (iscRSUA-hscBA-fdx-iscX). IscS is a cysteine desulphurase, which obtains S from cysteine (converting it to alanine) and serves as a S donor for FeS cluster assembly. IscU and IscA act as scaffolds to accept S and Fe atoms, assembling clusters and transfering them to recipient apoproteins. HscA is a molecular chaperone and HscB is a co-chaperone. Fdx is a [2Fe-2S]-type ferredoxin. IscR is a transcription factor that regulates expression of the isc operon. IscX (also known as YfhJ) appears to interact with IscS and may function as an Fe donor during cluster assembly [].The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA []. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA [], acting as a scaffold protein in which Fe and S atoms are assembled into [FeS]cluster forms, which can then easily be transferred to apoproteins targets.In the NIF system, NifS and NifU are required for the formation of metalloclusters of nitrogenase in Azotobacter vinelandii, and other organisms, as well as in the maturation of other FeS proteins. Nitrogenase catalyses the fixation of nitrogen. It contains a complex cluster, the FeMo cofactor, which contains molybdenum, Fe and S. NifS is a cysteine desulphurase. NifU binds one Fe atom at its N-terminal, assembling an FeS cluster that is transferred to nitrogenase apoproteins []. Nif proteins involved in the formation of FeS clusters can also be found in organisms that do not fix nitrogen [].This entry represents SufB, which is part of the SUF system and forms a complex with SufBCD. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S]and [4Fe-4S][]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S]form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S]clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.The ISC system is conserved in eubacteria and eukaryotes (mitochondria), and has broad specificity, targeting general FeS proteins [, ]. It is encoded by the isc operon (iscRSUA-hscBA-fdx-iscX). IscS is a cysteine desulphurase, which obtains S from cysteine (converting it to alanine) and serves as a S donor for FeS cluster assembly. IscU and IscA act as scaffolds to accept S and Fe atoms, assembling clusters and transfering them to recipient apoproteins. HscA is a molecular chaperone and HscB is a co-chaperone. Fdx is a [2Fe-2S]-type ferredoxin. IscR is a transcription factor that regulates expression of the isc operon. IscX (also known as YfhJ) appears to interact with IscS and may function as an Fe donor during cluster assembly [].The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA []. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA [], acting as a scaffold protein in which Fe and S atoms are assembled into [FeS]cluster forms, which can then easily be transferred to apoproteins targets.In the NIF system, NifS and NifU are required for the formation of metalloclusters of nitrogenase in Azotobacter vinelandii, and other organisms, as well as in the maturation of other FeS proteins. Nitrogenase catalyses the fixation of nitrogen. It contains a complex cluster, the FeMo cofactor, which contains molybdenum, Fe and S. NifS is a cysteine desulphurase. NifU binds one Fe atom at its N-terminal, assembling an FeS cluster that is transferred to nitrogenase apoproteins []. Nif proteins involved in the formation of FeS clusters can also be found in organisms that do not fix nitrogen [].This entry represents SufD proteins that form part of the SufBCD complex in the SUF system. No specific functions have been assigned to these proteins. |
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