{PDOC51340}
{PS51340; MOSC}
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* MOSC domain profile *
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The molybdenum  cofactor  (MOCO)  sulfurase  C-terminal  (MOSC)  domain  is  a
conserved region  of  about  125-170  residues present in diverse metal-sulfur
cluster biosynthesis  proteins  from  both  prokaryotes  and  eukaryotes. MOSC
domains occur either as stand-alone forms such as the bacterial YiiM proteins,
or fused  to  other  domains  such  as  a  NifS-like  catalytic domain in MOCO
sulfurase. The  MOSC  domain  is  predicted to be a sulfur-carrier domain that
receives sulfur  abstracted  by  the  pyridoxal  phosphate-dependent NifS-like
enzymes, on  its  conserved  cysteine,  and  delivers  it for the formation of
diverse sulfur-metal clusters [1].

The MOSC  domain  contains  several  patches  of  hydrophobic  residues and an
absolutely conserved cysteine residue situated closer to the C-terminal end of
the domain.   The   absolutely  conserved  cysteine  in  the  MOSC  domain  is
reminiscent of  the analogous conservation of a cysteine in the active site of
the thioredoxin    (see   <PDOC00172>)   and   rhodanese   (see   <PDOC00322>)
superfamilies. Members  of  both these superfamilies, especially of the latter
one, have   been  implicated  in  the  synthesis  of  Fe-S  clusters,  through
mobilization of  sulfur  with  their  active  cysteine.  The  MOSC  domain  is
predicted to  adopt  a  beta-strand-rich fold with a couple of isolated alpha-
helical elements [1].

The profile we developed covers the entire MOSC domain.

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

[ 1] Anantharaman V., Aravind L.
     "MOSC domains: ancient, predicted sulfur-carrier domains, present in
     diverse metal-sulfur cluster biosynthesis proteins including
     Molybdenum cofactor sulfurases."
     FEMS Microbiol. Lett. 207:55-61(2002).
     PubMed=11886751

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