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{PDOC00039}
{PS00039; DEAD_ATP_HELICASE}
{PS00690; DEAH_ATP_HELICASE}
{BEGIN}
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* DEAD and DEAH box families ATP-dependent helicases signatures *
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A number of eukaryotic and  prokaryotic proteins have been characterized [1,2,
3] on  the  basis of their structural similarity. They all seem to be involved
in ATP-dependent,  nucleic-acid  unwinding. Proteins currently known to belong
to this family are:

 - Initiation factor eIF-4A. Found in eukaryotes, this protein is a subunit of
   a high  molecular  weight  complex  involved  in  5'cap recognition and the
   binding of mRNA to ribosomes. It is an ATP-dependent RNA-helicase.
 - PRP5  and PRP28. These yeast proteins are involved in various ATP-requiring
   steps of the pre-mRNA splicing process.
 - Pl10, a mouse protein expressed specifically during spermatogenesis.
 - An3, a Xenopus putative RNA helicase, closely related to Pl10.
 - SPP81/DED1 and DBP1, two  yeast  proteins  probably  involved  in  pre-mRNA
   splicing and related to Pl10.
 - Caenorhabditis elegans helicase glh-1.
 - MSS116, a yeast protein required for mitochondrial splicing.
 - SPB4, a yeast protein involved in the maturation of 25S ribosomal RNA.
 - p68, a human nuclear antigen. p68 has ATPase and DNA-helicase activities in
   vitro. It is involved in cell growth and division.
 - Rm62 (p62), a Drosophila putative RNA helicase related to p68.
 - DBP2, a yeast protein related to p68.
 - DHH1, a yeast protein.
 - DRS1, a yeast protein involved in ribosome assembly.
 - MAK5, a yeast protein involved in maintenance of dsRNA killer plasmid.
 - ROK1, a yeast protein.
 - ste13, a fission yeast protein.
 - Vasa, a Drosophila protein important for oocyte formation and specification
   of of embryonic posterior structures.
 - Me31B, a Drosophila maternally expressed protein of unknown function.
 - dbpA, an Escherichia coli putative RNA helicase.
 - deaD, an Escherichia coli  putative  RNA  helicase  which  can  suppress  a
   mutation in the rpsB gene for ribosomal protein S2.
 - rhlB, an Escherichia coli putative RNA helicase.
 - rhlE, an Escherichia coli putative RNA helicase.
 - srmB, an Escherichia coli protein that shows RNA-dependent ATPase activity.
   It probably interacts with 23S ribosomal RNA.

 - Caenorhabditis elegans hypothetical proteins T26G10.1, ZK512.2 and ZK686.2.
 - Yeast hypothetical protein YHR065c.
 - Yeast hypothetical protein YHR169w.
 - Fission yeast hypothetical protein SpAC31A2.07c.
 - Bacillus subtilis hypothetical protein yxiN.

All these proteins  share a number of conserved sequence motifs.  Some of them
are specific  to  this  family  while  others  are shared by other ATP-binding
proteins or  by   proteins belonging to the helicases `superfamily' [4].   One
of these motifs, called the 'D-E-A-D-box', represents a special version of the
B motif of ATP-binding proteins.

Some other proteins belong to a subfamily which have His instead of the second
Asp  and  are  thus  said  to  be  'D-E-A-H-box'  proteins [3,5,6].   Proteins
currently known to belong to this subfamily are:

 - PRP2,  PRP16,  PRP22  and  PRP43.  These yeast proteins are all involved in
   various ATP-requiring steps of the pre-mRNA splicing process.
 - Fission yeast prh1, which my be involved in pre-mRNA splicing.
 - Male-less (mle),  a   Drosophila  protein  required in  males,  for  dosage
   compensation of X chromosome linked genes.
 - RAD3 from yeast. RAD3 is a DNA  helicase involved in excision repair of DNA
   damaged by   UV light,  bulky adducts  or  cross-linking  agents.   Fission
   yeast rad15 (rhp3)  and mammalian  DNA excision repair protein XPD (ERCC-2)
   are the homologs of RAD3.
 - Yeast CHL1 (or CTF1), which  is important  for  chromosome transmission and
   normal cell cycle progression in G(2)/M.
 - Yeast TPS1.
 - Yeast hypothetical protein YKL078w.
 - Caenorhabditis elegans hypothetical proteins C06E1.10 and K03H1.2.
 - Poxviruses' early transcription  factor 70 Kd subunit  which  acts with RNA
   polymerase to initiate transcription from early gene promoters.
 - I8, a putative vaccinia virus helicase.
 - hrpA, an Escherichia coli putative RNA helicase.

We have developed signature patterns for both subfamilies.

-Consensus pattern: [LIVMF](2)-D-E-A-D-[RKEN]-x-[LIVMFYGSTN]
-Sequences known to belong to this class detected by the pattern: ALL,  except
 for YHR169w.
-Other sequence(s) detected in Swiss-Prot: 14.

-Consensus pattern: [GSAH]-x-[LIVMF](3)-D-E-[ALIV]-H-[NECR]
-Sequences known to belong to this class detected by the pattern: ALL,  except
 for hrpA.
-Other sequence(s) detected in Swiss-Prot: 6.

-Note: Proteins belonging to this family  also contain a copy  of the ATP/GTP-
 binding motif 'A' (P-loop) (see the relevant entry <PDOC00017>).

-Expert(s) to contact by email:
           Linder P.; 
linder@medecine.unige.ch -Last update: July 1999 / Text revised. [ 1] Schmid S.R., Linder P. "D-E-A-D protein family of putative RNA helicases." Mol. Microbiol. 6:283-291(1992). PubMed=1552844 [ 2] Linder P., Lasko P.F., Ashburner M., Leroy P., Nielsen P.J., Nishi K., Schnier J., Slonimski P.P. "Birth of the D-E-A-D box." Nature 337:121-122(1989). PubMed=2563148; DOI=10.1038/337121a0 [ 3] Wassarman D.A., Steitz J.A. "RNA splicing. Alive with DEAD proteins." Nature 349:463-464(1991). PubMed=1825133; DOI=10.1038/349463a0 [ 4] Hodgman T.C. "A new superfamily of replicative proteins." Nature 333:22-23(1988) and Nature 333:578-578(1988) (Errata). PubMed=3362205; DOI=10.1038/333022b0 [ 5] Harosh I., Deschavanne P. "The RAD3 gene is a member of the DEAH family RNA helicase-like protein." Nucleic Acids Res. 19:6331-6331(1991). PubMed=1956796 [ 6] Koonin E.V., Senkevich T.G. "Vaccinia virus encodes four putative DNA and/or RNA helicases distantly related to each other." J. Gen. Virol. 73:989-993(1992). PubMed=1321883 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}