WORKLIST ENTRIES (1):

CYTCHROMECII View alignment View Structure    Class II cytochrome C signature
 Type of fingerprint: COMPOUND with 2  elements
Links:
   PRINTS; PR00603 CYTOCHROMEC1; PR00604 CYTCHRMECIAB; PR00605 CYTCHROMECIC
   PRINTS; PR00606 CYTCHROMECID; PR00607 CYTCHROMECIE; PR00609 CYTOCHROMEC3
   PRINTS; PR00610 CYTOCHROMEF
   INTERPRO; IPR002321
   PROSITE; PS00190 CYTOCHROME_C
   PFAM; PF01322 Cytochrome_C_2
   PDB; 1BBH 3Dinfo; 1CGN 3Dinfo; 2CCY 3Dinfo
   SCOP; 1BBH; 1CGN; 2CCY
   CATH; 1BBH; 2CCY

 Creation date 03-JUL-1996; UPDATE 14-JUN-1999

   1. PETTIGREW, G.W. AND MOORE, G.R. 
   Cytochromes c. Biological Aspects.
   SPRINGER-VERLAG, BERLIN-HEIDELBERG-NEW YORK (1987). 

   2. AMBLER, R.P.
   Sequence variability in bacterial cytochromes c.
   BIOCHIM.BIOPHYS.ACTA 1058 42-47 (1991). 

   3. KASSNER, R.J.
   Ligand binding properties of cytochromes c'.
   BIOCHIM.BIOPHYS.ACTA 1058 8-12 (1991).

   4. MOORE, G.R.
   Bacterial 4-alpha-helical bundle cytochromes. 
   BIOCHIM.BIOPHYS.ACTA 1058 38-41 (1991).

   5. REN, Z., MEYER, T.E. AND MCREE, D.E.
   Atomic structure of a cytochrome c' with an unusual ligand-controlled dimer
   dissociation at 1.8A resolution. 
   J.MOL.BIOL. 234 433-445 (1993).

   Cytochromes c (cyt c) can be defined as electron-transfer proteins having 
   one or several haem c groups, bound to the protein by one or, more 
   generally, two thioether bonds involving sulphydryl groups of cysteine 
   residues. The fifth haem iron ligand is always provided by a histidine 
   residue. Cyt c possess a wide range of properties and function in a large 
   number of different redox processes [1]. 
   
   Ambler [2] recognised four classes of cyt c. Class II includes the 
   high-spin cyt c' and a number of low-spin cytochromes, e.g. cyt c-556. 
   The haem-attachment site is close to the C-terminus. The cyt c' are capable
   of binding such ligands as CO, NO or CN(-), albeit with rate and equilibrium
   constants 100 to 1,000,000-fold smaller than other high-spin haemoproteins
   [3]; this, coupled with its relatively low redox potential, makes it
   unlikely that cyt c' is a terminal oxidase. Thus cyt c' probably functions
   as an electron transfer protein [4]. 
  
   The 3D structures of a number of cyt c' have been determined. The molecule 
   usually exists as a dimer, each monomer folding as a four-alpha-helix bundle
   incorporating a covalently-bound haem group at the core [4]. The Chromatium
   vinosum cyt c' exhibits dimer dissociation upon ligand binding [5]. 
  
   CYTCHROMECII is a 2-element fingerprint that provides a signature for the 
   class II cyt c. The fingerprint was derived from an initial alignment of
   17 sequences: the motifs were drawn from adjacent conserved regions in
   the C-terminal part of the molecule - motif 2 includes two invariant Cys
   residues, which covalently bind the haem group, and a His residue, which
   provides the haem iron axial ligand (cf. PROSITE pattern CYTOCHROME_C).
   Two iterations on OWL28.0 were required to reach convergence, at which
   point a true set comprising 19 sequences was identified. 
  
   An update on SPTR37_9f identified a true set of 17 sequences.

  SUMMARY INFORMATION
     17 codes involving  2 elements

   COMPOSITE FINGERPRINT INDEX
  
    2|  17   17  
   --+-----------
     |   1    2  

True positives..
 CYCP_RHOCA     CYCP_RHOTE     CYCP_RHOSP     CYCP_RHOPH     
 CYCP_RHORU     CYCP_ALCSP     CYCP_CHRVI     C556_AGRTC     
 C554_RHOSH     CYCP_RHOGE     CYCP_RHOFU     CYCP_RHOMO     
 C556_AGRTA     CYCP_RHOSH     C556_AGRTB     CYCP_RHOPA     
 C556_RHOPA     


  PROTEIN TITLES
   CYCP_RHOCA       CYTOCHROME C' - RHODOBACTER CAPSULATUS (RHODOPSEUDOMONAS CAP
   CYCP_RHOTE       CYTOCHROME C' - RHODOCYCLUS TENUIS (RHODOSPIRILLUM TENUE).
   CYCP_RHOSP       CYTOCHROME C' - RHODOPSEUDOMONAS SP.
   CYCP_RHOPH       CYTOCHROME C' - RHODOSPIRILLUM PHOTOMETRICUM.
   CYCP_RHORU       CYTOCHROME C' - RHODOSPIRILLUM RUBRUM.
   CYCP_ALCSP       CYTOCHROME C' - ALCALIGENES SP. (STRAIN NCIB 11015).
   CYCP_CHRVI       CYTOCHROME C' PRECURSOR - CHROMATIUM VINOSUM.
   C556_AGRTC       CYTOCHROME C-556 (C556) - AGROBACTERIUM TUMEFACIENS (STRAIN 
   C554_RHOSH       CYTOCHROME C-554 PRECURSOR (C554) (HIGH POTENTIAL CYTOCHROME
   CYCP_RHOGE       CYTOCHROME C' - RHODOCYCLUS GELATINOSUS (RHODOPSEUDOMONAS GE
   CYCP_RHOFU       CYTOCHROME C' - RHODOSPIRILLUM FULVUM.
   CYCP_RHOMO       CYTOCHROME C' - RHODOSPIRILLUM MOLISCHIANUM.
   C556_AGRTA       CYTOCHROME C-556 (C556) - AGROBACTERIUM TUMEFACIENS (STRAIN 
   CYCP_RHOSH       CYTOCHROME C' - RHODOBACTER SPHAEROIDES (RHODOPSEUDOMONAS SP
   C556_AGRTB       CYTOCHROME C-556 (C556) - AGROBACTERIUM TUMEFACIENS (STRAIN 
   CYCP_RHOPA       CYTOCHROME C' - RHODOPSEUDOMONAS PALUSTRIS.
   C556_RHOPA       CYTOCHROME C-556 (C556) - RHODOPSEUDOMONAS PALUSTRIS.

SCAN HISTORY OWL28_0 2 150 NSINGLE SPTR37_9f 2 200 NSINGLE INITIAL MOTIF SETS CYTCHROMECII1 Length of motif = 24 Motif number = 1 Class II cytochrome c motif I - 1 PCODE ST INT ANELAKVAATGDAAAVKAQFGKVG CYCP_RHOTE 96 96 GAEVIAAANAGDATAFGAALQKLG CYCP_RHOCA 92 92 ALELASAAETGDKAAIGAKLQALG CYCP_RHORU 90 90 IVKLSAAADAGDLDKLRAAFGDVG CYCP_ALCSP 90 90 AKALAQAATAGDTAQMGKALAALG CYCP_RHOPH 90 90 ANTLAEVAATGEAEAVKTAFGDVG CYCP_CHRVI 95 95 VDKLDAAGKTGDFAQIKAAVGETG CYCP_RHOGE 93 93 GMELIAAANTGEASAFGPALKKLG CYCP_RHOSP 91 91 ESTKLAAAAKAGPDALKAQAAATG CYCP_RHOFU 92 92 ESTKLAAAAKAGPDALKAQAAATG CYCP_RHOMO 92 92 DADKVLASLPADQAGVTAAMQTLG C556_AGRTC 85 85 DADIVLANLPGDQAGVATAMKTLG C556_AGRTB 85 85 DAETALAQLPADQAGVGNTLKTLG C556_AGRTA 87 87 AVAALEPAAGAGQKELAAAVGKVG CYCP_RHOSH 93 93 KAVDGAKGKIKDVDTLKAAMQPIG C556_RHOPA 91 91 AAATAAQGTIKDEASLKANIGGVL CYCP_RHOPA 87 87 ATLAQMVDDGEEFSALRRQVGAVG CYCP_PARSP 96 96 CYTCHROMECII2 Length of motif = 12 Motif number = 2 Class II cytochrome c motif II - 1 PCODE ST INT GQTCKACHDDFR CYCP_RHOTE 119 -1 GGTCKACHDDYR CYCP_RHOCA 115 -1 GGTCKACHKEFK CYCP_RHORU 113 -1 GASCKACHDAYR CYCP_ALCSP 113 -1 GGTCKGCHETFR CYCP_RHOPH 113 -1 GAACKSCHEKYR CYCP_CHRVI 118 -1 GGACKGCHDKFK CYCP_RHOGE 116 -1 GGTCKACHDDYR CYCP_RHOSP 114 -1 GKVCKACHEEFK CYCP_RHOFU 115 -1 GKVCKACHEEFK CYCP_RHOMO 115 -1 GADCGACHQTYR C556_AGRTC 108 -1 GADCGTCHQTYR C556_AGRTB 108 -1 GGNCGACHQAYR C556_AGRTA 110 -1 GTGCKSCHDDFR CYCP_RHOSH 116 -1 GKACGNCHENFR C556_RHOPA 114 -1 LGNCKSCHDDFR CYCP_RHOPA 110 -1 GKSCKGCHDDFR CYCP_PARSP 119 -1 FINAL MOTIF SETS CYTCHROMECII1 Length of motif = 24 Motif number = 1 Class II cytochrome c motif I - 2 PCODE ST INT GAEVIAAANAGDATAFGAALQKLG CYCP_RHOCA 92 92 ANELAKVAATGDAAAVKAQFGKVG CYCP_RHOTE 96 96 GMELIAAANTGEASAFGPALKKLG CYCP_RHOSP 91 91 AKALAQAATAGDTAQMGKALAALG CYCP_RHOPH 90 90 ALELASAAETGDKAAIGAKLQALG CYCP_RHORU 90 90 IVKLSAAADAGDLDKLRAAFGDVG CYCP_ALCSP 90 90 ANTLAEVAATGEAEAVKTAFGDVG CYCP_CHRVI 118 118 DADKVLASLPADQAGVTAAMQTLG C556_AGRTC 85 85 AAAKMQAAAGTDLASLQGAMRDLG C554_RHOSH 116 116 VDKLDAAGKTGDFAQIKAAVGETG CYCP_RHOGE 93 93 ESTKLAAAAKAGPDALKAQAAATG CYCP_RHOFU 92 92 ESTKLAAAAKAGPDALKAQAAATG CYCP_RHOMO 92 92 DAETALAQLPADQAGVGNTLKTLG C556_AGRTA 87 87 AVAALEPAAGAGQKELAAAVGKVG CYCP_RHOSH 93 93 DADIVLANLPGDQAGVATAMKTLG C556_AGRTB 85 85 AAATAAQGTIKDEASLKANIGGVL CYCP_RHOPA 87 87 KAVDGAKGKIKDVDTLKAAMQPIG C556_RHOPA 91 91 CYTCHROMECII2 Length of motif = 12 Motif number = 2 Class II cytochrome c motif II - 2 PCODE ST INT GGTCKACHDDYR CYCP_RHOCA 115 -1 GQTCKACHDDFR CYCP_RHOTE 119 -1 GGTCKACHDDYR CYCP_RHOSP 114 -1 GGTCKGCHETFR CYCP_RHOPH 113 -1 GGTCKACHKEFK CYCP_RHORU 113 -1 GASCKACHDAYR CYCP_ALCSP 113 -1 GAACKSCHEKYR CYCP_CHRVI 141 -1 GADCGACHQTYR C556_AGRTC 108 -1 GAACGSCHETYR C554_RHOSH 139 -1 GGACKGCHDKFK CYCP_RHOGE 116 -1 GKVCKACHEEFK CYCP_RHOFU 115 -1 GKVCKACHEEFK CYCP_RHOMO 115 -1 GGNCGACHQAYR C556_AGRTA 110 -1 GTGCKSCHDDFR CYCP_RHOSH 116 -1 GADCGTCHQTYR C556_AGRTB 108 -1 LGNCKSCHDDFR CYCP_RHOPA 110 -1 GKACGNCHENFR C556_RHOPA 114 -1

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