Analysis of the proteins responsible for The DNA degradation (Dnd) system

DndA DndB DndC DndD DndE
Dnd protein DndC
Putative function Putative [4Fe-4S] ATP pyrophosphatase, an iron-sulfur protein
DndC sequence of Streptomyces lividans 1326 MSTPKAAAPFQDRPLAEIVEELTEEIRELYVADEVPWVVGYSGGKDSTAVLQLVWLALKDLPAEQRTKPVHVISTDTLVE
NPVVAAWVGQSLDTMRTAAQEQQLPIESHKLTPEIKDTFWVSLIGKGYPAPRPKFRWCTERLKIKPSNAFIRRVVRRHGE
AILVLGIRKAESQARARAMARHEKGRVRDRLSPNGNLPNSLVYSPIEAWSTEEVWAFLMQYPNPWGHKNKDLLTMYQGAS
DDSECPLVVDDTTPSCGDSRFGCWTCTLVEQDKSMTAMIRNDDEKQWMRPLLKLRNELDDVTKEAQTRDFRRMNGNVQLF
GDRPIPGPYKQSAREDWLRKLLAAQAQVRKKAPEHVRNIELISMAELQEIRRIWVFEKHEVEDSLPQIYEQATGEKFPGL
PLDEQLVLGAEEIGLLKEACEDDPIHFSMTRELLAIERQYRTMTRRAGLFEALEKAIKKGYYEDADDALRFAKRLQEMRE
SDPTQTTADEEITTDAPA
Length 498 aa
Homologues in dndDB  32 
Consensus based on Muscle-derived MSA in dndDB MMSKLKLAEDLAEYEDFINQEGFAGRPLEELIAEIQELYCADKRPWVIGYSGGKDSTAVLQLVWLALLGLPPEQRTKPVF
VISSDTLVETPVVVDWIKDSLAAIEAAAKRQGLPITAHKVTPKINDTFWVNLIGKGYPAPTRKFRWCTERLKIDPVSDFI
KDKVSQFGEVIVVLGSRSSESASRAQVIAKHKIDGSRDRLSRHSTPLPNAFVYTPIETWSVDDVWKYLRGAFLETKETPY
APEDIWIDKYDLEWPNPWGGNNRDLLTLYKDASAQGECPLVVDTSTPSCGNSRFGCWTCTVVTKDKAMEALIQNGEEKEW
MSPLLDFRNKLARDRGETTDPENKDEYRDFKRRTGKVSYQYAKDGEDPSAERKHVPGPYWLKYRKQWLKELLEAQRDLRA
EGKPEEVRNIELITLEELHAIRRIWLEDPNEPDWEDSLPKIYREVYGEDLDWRVLDDQPSFGAEDADLLKELCQEFDVEA
LPELVMKLLELERSMEGLSRRSGIFDKLEELLKQDWGSLEEIAALEQAQALLQKKAEDDIHLEEDEKYEEELQALQKEIE
AEFESSLLIDEEKER
Length of Consensus 575 aa
NCBI-BLASTP similar proteins  67 
Putative conserved domains in pfam highlighted: PF01507,PAPS_reduct, Phosphoadenosine, phosphosulfate reductase family


Pfam-A Matches:
Putative conserved domains in CCD cd01713: PAPS_reductase, This domain is found in phosphoadenosine phosphosulphate (PAPS) reductase enzymes
cl00292: AANH_like, Adenine nucleotide alpha hydrolases superfamily including N type ATP PPases
Protein structure Crystal structure of phosphoadenylyl sulphate (PAPS) reductase, PDB entry 1sur
Literature D. You, L. Wang, F. Yao, X. Zhou, and Z. Deng (2007). A novel DNA modification by sulfur: DndA is a NifS-like cysteine desulfurase capable of assembling DndC as an iron-sulfur cluster protein in Streptomyces lividans. Biochemistry, 46(20):6126-33. [Abstract] [Full Text]

Other Literature D.L. You, T.G. Xu, F. Yao, X.F. Zhou, and Z.X. Deng (2008) Direct evidence that ThiI is an ATP pyrophosphatase for the adenylation of uridine in 4-thiouridine biosynthesis. Chembiochem, 9(12):1879-82. [Abstract]

ThiI is an enzyme that plays a role in the biosynthesis of both thiamin and 4-thiouridine at position 8 in bacterial tRNA. Using kinetic assays and mass spectrometry, we have identified ThiI as ATP pyrophosphatase that catalyzes the hydrolysis of ATP to AMP and pyrophosphate. Our results provide a direct evidence for the formation of adenylation intermediate in the tRNA modification process.
Cross-references Sequence database UniProtKB search: dndC
Protein family database InterPro: IPR017598 Putative sulfurtransferase, DndC
Interesting links TMHMM v. 2.0, Prediction of transmembrane helices in proteins
SignalP v3.0, Prediction of signal peptide cleavage sites
Jpred v3.0, protein secondary structure prediction
Last update 11/10/2008
PF00266 PF02662 PF04214 PF01507 PF02349