Ibergirhynchia contraria (F. A. Roemer, 1850), an Early Carboniferous seep-related rhynchonellide brachiopod from the Harz Mountains, Germany - A possible successor to Dzieduszyckia?

A new genus Ibergirhynchia, a member of the rhynchonellide superfamily Dimerelloidea, is described for the species Terebratula contraria Roemer, 1850, from Early Carboniferous deposits of the Harz Mountains, Germany. Ibergirhynchia contraria is from a monospecific brachiopod limestone that formed on top of the drowned Devonian Iberg Reef which persisted as a seamount during Famennian and Early Carboniferous times. Ibergirhynchia contraria is considered a cold seep-related brachiopod based on this locality. Such seep associations have been observed for Mesozoic representatives of the rhynchonellide superfamily Dimerelloidea. Ibergirhynchia is considered the first Paleozoic representative of the family Rhynchonellinidae. Ibergirhynchia resembles Dzieduszyckia externally and may be derived from this dimerelloid.

Sequence analysis of the cupin gene family in Synechocystis PCC6803

The recently described cupin superfamily of proteins includes the germin and germinlike proteins, of which the cereal oxalate oxidase is the best characterized. This superfamily also includes seed storage proteins, in addition to several microbial enzymes and proteins with unknown function. All these proteins are characterized by the conservation of two central motifs, usually containing two or three histidine residues presumed to be involved with metal binding in the catalytic active site. The present study on the coding regions of Synechocystis PCC6803 identifies a previously unknown group of 12 related cupins, each containing the characteristic two-motif signature. This group comprises 11 single-domain proteins, ranging in length from 104 to 289 residues, and includes two phosphomannose isomerases and two epimerases involved in cell wall synthesis, a member of the pirin group of nuclear proteins, a possible transcriptional regulator, and a close relative-of a cytochrome c551 from Rhodococcus. Additionally, there is a duplicated, two-domain protein that has close similarity to an oxalate decarboxylase from the fungus Collybia velutipes and that is a putative progenitor of the storage proteins of land plants.