{PDOC51795}
{PS51795; ZF_FLZ}
{BEGIN}
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* Zinc finger FLZ-type profile *
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Zinc fingers  are  a  ubiquitous  class  of  protein  domain with considerable
variation in  structure  and  function.  The  FCS-type zinc finger is a highly
diverged group  of  C2-C2 zinc finger which is present in animals, prokaryotes
and viruses,  but  not in plant. It is named after the conserved phenylalanine
and serine  residues  associated  with  the  third cysteine. The FCS-type zinc
finger is a structurally diverse family which accommodate both nucleic-protein
and protein-protein  interaction  zinc fingers. The FCS-Like Zinc finger (FLZ)
domain is  a  plant specific domain found in all taxa except algae. FLZ domain
containing proteins  are  bryophytic  in  origin  and  this  protein family is
expanded in higher plants. Although the molecular functions of the FLZ protein
family members  in  general  are  not well understood, many of the members are
attributed to plant growth and development, stress mitigation, sugar signaling
and senescence.  The FLZ-type zinc finger is likely to be involved in protein-
protein interaction [1,2,3].

The FLZ-type  zinc  finger  is predicted to form an alpha-beta-alpha secondary
structure composed of an N-terminal short alpha-helix, a beta hairpin followed
by a longer C-terminal alpha helix. Four highly conserved cysteine residues in
the FLZ-type   zinc  finger  are  believed  to  bind  zinc  in  a  tetrahedral
coordination [1,2].

Some proteins known to contain a FLZ-type zinc finger are listed below [4]:

 - Arabidopsis  thaliana MEDIATOR OF ABA-REGULATED DORMANCY 1 (MARD1) or FLZ9,
   involved in  absissic  acid (ABA)-mediated seed dormancy and induced during
   senescence.
 - Arabidopsis thaliana INCREASED RESISTANCE TO MYZUS PERSICAE (IRM1) or FLZ4,
   constitutive overexpression  of  IRM1  results  in mechanical barriers that
   make it  difficult  for  M.  persicae  to reach the phloem and subsequently
   reduces its population size.
 - Wheat  salt related hypothetical protein (TaSRHP), overexpression of TaSHRP
   results in enhanced resistance to salt and drought stress.

The profile we developed covers the entire FLZ-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: March 2016 / First entry.

[ 1] He Y., Gan S.
     "A novel zinc-finger protein with a proline-rich domain mediates
     ABA-regulated seed dormancy in Arabidopsis."
     Plant Mol. Biol. 54:1-9(2004).
     PubMed=15159630; DOI=10.1023/B:PLAN.0000028730.10834.e3
[ 2] K M.J., Laxmi A.
     "DUF581 is plant specific FCS-like zinc finger involved in
     protein-protein interaction."
     PLoS ONE 9:E99074-E99074(2014).
     PubMed=24901469; DOI=10.1371/journal.pone.0099074
[ 3] Jamsheer K M., Mannully C.T., Gopan N., Laxmi A.
     "Comprehensive Evolutionary and Expression Analysis of FCS-Like Zinc
     finger Gene Family Yields Insights into Their Origin, Expansion and
     Divergence."
     PLoS ONE 10:E0134328-E0134328(2015).
     PubMed=26252898; DOI=10.1371/journal.pone.0134328
[ 4] Jamsheer K M., Laxmi A.
     "Expression of Arabidopsis FCS-Like Zinc finger genes is
     differentially regulated  by sugars, cellular energy level, and
     abiotic stress."
     Front. Plant Sci. 6:746-746(2015).
     PubMed=26442059; DOI=10.3389/fpls.2015.00746

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