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DATA
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PDOC00515
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1995-07-26
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*************************************************
* High potential iron-sulfur proteins signature *
*************************************************
High potential iron-sulfur proteins (HiPIP) [1] are a specific class of high-
redox potential 4Fe-4S ferredoxins that functions in anaerobic electron
transport and which occurs in photosynthetic bacteria and in Paracoccus
denitrificans.
The HiPIPs are small proteins which show significant variation in their
sequences, their sizes (from 63 to 85 amino acids), and in their oxidation-
reduction potentials. As shown in the following schematic representation the
iron-sulfur cluster is bound by four conserved cysteine residues.
[ 4Fe-4S cluster]
| | | |
xxxxxxxxxxxxxxxxxxxCxCxxxxxxxCxxxxxCxxxx
********
'C': conserved cysteine involved in the binding of the iron-sulfur cluster.
'*': position of the pattern.
-Consensus pattern: C-x(7,9)-[LIVM]-x(3)-G-[YW]-C-x(2)-[YW]
[The two C's are 4Fe-4S ligands]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in SWISS-PROT: NONE.
-Last update: December 1991 / First entry.
[ 1] Breiter D.R., Meyer T.E., Rayment I., Holden H.M.
J. Biol. Chem. 266:18660-18667(1991).