Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Combined Automated Annotation using Multiple IEA Methods
Structural and functional features of Pseudomonas cytochrome c peroxidase.
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Heme 1 has Lys in place of the cytochrome Met sixth ligand, lowering its redox potential and enabling peroxidatic activity; heme 2 has a cytochrome role; the two distal heme faces point toward each other, allowing inter-heme communication.
"From the present results we conclude that the two distal heme surfaces in the peroxidase are oriented toward each other."
Crystal structure of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa.
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Crystal structure of P. aeruginosa CCP at 2.4 A; two cytochrome c-like domains, each with a covalent c-heme; the low-potential heme is the peroxidatic site and the high-potential heme takes electrons from cytochrome c and azurin; periplasmic location.
"PsCCP is organized into two domains, both of them containing a covalent c-haem in a structure reminiscent of class 1 cytochromes c."