{PDOC52013}
{PS52013; ZF_C6H2}
{BEGIN}
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* Zinc finger C6H2-type profile *
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Methionine Aminopeptidases (MetAPs) are "metalloenzymes" primarily responsible
for the  co-translational  cleavage of the initial methionine residue from the
nascent polypeptides.  MetAPs are classified into two isoforms: namely, MetAP1
and MetAP2. Only one type of MetAP, either type 1 or type 2, can be found in a
prokaryotic cell. Archaea contain type 2 MetAPs, and eubacteria contain type 1
MetAPs. However,  all  eukaryotic  genomes  studied  to date encode at least a
cytosolic type  1  MetAP  and  a cytosolic type 2 MetAP. All MetAPs C-terminal
catalytic domains are conserved in both prokaryotes and eukaryotes. Extensions
at the  N-terminus  of  the  catalytic  domain  of eukaryotic cytosolic MetAPs
distinguish them  from  their prokaryotic counterparts. Within this N-terminal
region, MetAP1  has  a  C6H2-type  zinc  finger,  with four pairs of conserved
cysteine and histidine residues and conserved aromatic residues. The C6H2-type
zinc finger  is essential for the normal processing function of MetAP1 and may
be important  for  the proper functional alignment of MetAP1 on the ribosomes.
It is a protein-protein interaction domain [1,2,3,4].

The structure  of  the  C6H2-type  zinc  finger shows a BetaBetaAlphaBetaAlpha
cross-brace fold with a 1,3,2 antiparallel beta-sheet (see <PDB:7SEK>). Zn1 is
coordinated by C1, C2, C5, and C6, and Zn2 by C3, C4, H7, and H8 [4].

The profile we developed covers the entire C6H2-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: December 2022 / First entry.

[ 1] Weako J., Uba A.I., Keskin O., Guersoy A., Yelekci K.
     "Identification of potential inhibitors of human methionine
     aminopeptidase (type  II) for cancer therapy: Structure-based virtual
     screening, ADMET prediction and  molecular dynamics studies."
     Comput. Biol. Chem. 86:107244-107244(2020).
     PubMed=32252002; DOI=10.1016/j.compbiolchem.2020.107244
[ 2] Zhang F., Bhat S., Gabelli S.B., Chen X., Miller M.S., Nacev B.A.,
     Cheng Y.L., Meyers D.J., Tenney K., Shim J.S., Crews P., Amzel L.M.,
     Ma D., Liu J.O.
     "Pyridinylquinazolines selectively inhibit human methionine
     aminopeptidase-1 in  cells."
     J. Med. Chem. 56:3996-4016(2013).
     PubMed=23634668; DOI=10.1021/jm400227z
[ 3] Vetro J.A., Chang Y.-H.
     "Yeast methionine aminopeptidase type 1 is ribosome-associated and
     requires its  N-terminal zinc finger domain for normal function in
     vivo."
     J. Cell. Biochem. 85:678-688(2002).
     PubMed=11968008; DOI=10.1002/jcb.10161
[ 4] Weiss A., Murdoch C.C., Edmonds K.A., Jordan M.R., Monteith A.J.,
     Perera Y.R., Rodriguez Nassif A.M., Petoletti A.M., Beavers W.N.,
     Munneke M.J., Drury S.L., Krystofiak E.S., Thalluri K., Wu H.,
     Kruse A.R.S., DiMarchi R.D., Caprioli R.M., Spraggins J.M.,
     Chazin W.J., Giedroc D.P., Skaar E.P.
     "Zn-regulated GTPase metalloprotein activator 1 modulates vertebrate
     zinc  homeostasis."
     Cell 185:2148-2163.e27(2022).
     PubMed=35584702; DOI=10.1016/j.cell.2022.04.011

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