{PDOC00174}
{PS00196; COPPER_BLUE}
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* Type-1 copper (blue) proteins signature *
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Blue or 'type-1'  copper  proteins  are   small proteins which  bind  a single
copper atom and which are characterized  by  an intense  electronic absorption
band near 600 nm [1,2]. The most well known members of  this class of proteins
are the  plant   chloroplastic   plastocyanins, which exchange  electrons with
cytochrome  c6, and the  distantly  related bacterial  azurins, which exchange
electrons with cytochrome  c551. This family of proteins also includes all the
proteins listed below  (references  are  only provided for recently determined
sequences).

 - Amicyanin from bacteria such as Methylobacterium extorquens or Thiobacillus
   versutus that can grow on methylamine.  Amicyanin appears to be an electron
   receptor for methylamine dehydrogenase.
 - Auracyanins A and B  from Chloroflexus aurantiacus [3].  These proteins can
   donate electrons to cytochrome c-554.
 - Blue copper protein from Alcaligenes faecalis.
 - Cupredoxin (CPC) from cucumber peelings [4].
 - Cusacyanin (basic blue protein; plantacyanin, CBP) from cucumber.
 - Halocyanin from Natrobacterium pharaonis [5], a membrane associated copper-
   binding protein.
 - Pseudoazurin from Pseudomonas.
 - Rusticyanin  from  Thiobacillus ferrooxidans.  Rusticyanin is  an  electron
   carrier from cytochrome c-552 to the a-type oxidase [6].
 - Stellacyanin from the Japanese lacquer tree.
 - Umecyanin from horseradish roots.

 - Allergen Ra3 from ragweed.  This pollen protein  is evolutionary related to
   the above proteins, but seems to have lost the ability to bind copper.

Although there is an appreciable amount of divergence  in the  sequence of all
these proteins, the copper ligand sites are  conserved and we have developed a
pattern which includes two of the ligands: a cysteine and a histidine.

-Consensus pattern: [GA]-x(0,2)-[YSA]-x(0,1)-[VFY]-{SEDT}-C-x(1,2)-[PG]-
                    x(0,1)-H-x(2,4)-[MQ]
                    [C and H are copper ligands]
-Sequences known to belong to this class detected by the pattern: ALL,  except
 for allergen Ra3 and three other sequences.
-Other sequence(s) detected in Swiss-Prot: 32.

-Note: In position 5 of the pattern, only the Alcaligenes  protein  has a Val;
 all other proteins have either Phe or Tyr. In  position 9  only  CPC has Gly,
 all others have Pro.

-Last update: December 2004 / Pattern and text revised.

[ 1] Garret T.P.J., Clingeleffer D.J., Guss J.M., Rogers S.J., Freeman H.C.
     J. Biol. Chem. 259:2822-2825(1984).
[ 2] Ryden L.G., Hunt L.T.
     "Evolution of protein complexity: the blue copper-containing oxidases
     and related proteins."
     J. Mol. Evol. 36:41-66(1993).
     PubMed=8433378
[ 3] McManus J.D., Brune D.C., Han J., Sanders-Loehr J., Meyer T.E.,
     Cusanovich M.A., Tollin G., Blankenship R.E.
     "Isolation, characterization, and amino acid sequences of auracyanins,
     blue copper proteins from the green photosynthetic bacterium
     Chloroflexus aurantiacus."
     J. Biol. Chem. 267:6531-6540(1992).
     PubMed=1313011
[ 4] Mann K., Schafer W., Thoenes U., Messerschmidt A., Mehrabian Z.,
     Nalbandyan R.
     "The amino acid sequence of a type I copper protein with an unusual
     serine-and hydroxyproline-rich C-terminal domain isolated from
     cucumber peelings."
     FEBS Lett. 314:220-223(1992).
     PubMed=1468551
[ 5] Mattar S., Scharf B., Kent S.B.H., Rodewald K., Oesterhelt D.,
     Engelhard M.
     "The primary structure of halocyanin, an archaeal blue copper protein,
     predicts a lipid anchor for membrane fixation."
     J. Biol. Chem. 269:14939-14945(1994).
     PubMed=8195126
[ 6] Yano T., Fukumori Y., Yamanaka T.
     "The amino acid sequence of rusticyanin isolated from Thiobacillus
     ferrooxidans."
     FEBS Lett. 288:159-162(1991).
     PubMed=1879547

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