{PDOC51501}
{PS51501; ZF_DNL}
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* Zinc finger DNL-type profile *
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Mitochondrial functions  rely  on  the  correct transport of resident proteins
synthesized in  the  cytosol to mitochondria. Protein import into mitochondria
is mediated by membrane protein complexes, protein translocators, in the outer
and inner   mitochondrial  membranes,  in  cooperation  with  their  assistant
proteins in  the cytosol, intermembrane space and matrix. Proteins destined to
the mitochondrial  matrix  cross  the outer membrane with the aid of the outer
membrane translocator, the tOM40 complex, and then the inner membrane with the
aid of  the  inner  membrane  translocator,  the  TIM23  complex,  and finally
mitochondrial motor and chaperone (MMC) proteins including mitochondrial heat-
shock protein  70  (mtHsp70),  and  translocase  in  the  inner  mitochondrial
membrane (Tim)15,  which is also known as zinc finger motif (Zim)17 or mtHsp70
escort protein  (Hep)1 in the matrix. Tim15 contains a zinc-finger motif (CXXC
and CXXC)  of ~100 residues, which has been named DNL after a short C-terminal
motif of D(N/H)L [1,2,3].

The DNL-type  zinc  finger  is  an L-shaped molecule (see <PDB:2E2Z>). The two
CXXC motifs  are  located  at  the  end  of  the L, and are sandwiched by two-
stranded antiparallel  beta-sheets. Two short alpha-helices constitute another
leg of  the  L.  The  outer  (convex) face of the L has a large acidic groove,
which is  lined with five acidic residues, whereas the inner (concave) face of
the L has two positively charged residues, next to the CXXC motifs [3].

The profile we developed covers the entire DNL-type zinc finger.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: July 2007 / First entry.

[ 1] Burri L., Vascotto K., Fredersdorf S., Tiedt R., Hall M.N.,
     Lithgow T.
     "Zim17, a novel zinc finger protein essential for protein import into
     mitochondria."
     J. Biol. Chem. 279:50243-50249(2004).
     PubMed=15383543; DOI=10.1074/jbc.M409194200
[ 2] Yamamoto H., Momose T., Yatsukawa Y., Ohshima C., Ishikawa D.,
     Sato T., Tamura Y., Ohwa Y., Endo T.
     "Identification of a novel member of yeast mitochondrial
     Hsp70-associated motor and chaperone proteins that facilitates protein
     translocation across the inner membrane."
     FEBS Lett. 579:507-511(2005).
     PubMed=15642367; DOI=10.1016/j.febslet.2004.12.018
[ 3] Momose T., Ohshima C., Maeda M., Endo T.
     "Structural basis of functional cooperation of Tim15/Zim17 with yeast
     mitochondrial Hsp70."
     EMBO. Rep. 8:664-670(2007).
     PubMed=17571076; DOI=10.1038/sj.embor.7400990

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