Known metabolic pathways, protein complexes, signal transduction pathways, etc ... from curated databases.
Genes that are sometimes fused into single open reading frames.
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Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
colored nodes: query proteins and first shell of interactors
white nodes: second shell of interactors
empty nodes: proteins of unknown 3D structure
filled nodes: some 3D structure is known or predicted
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
from curated databases
annotation not available (758 aa)
Predicted Functional Partners:
Protein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently (437 aa)
Identified by similarity to SP-P39627; similar to GP-4741793 (544 aa)
Uncharacterized protein; Identified by Glimmer2; putative (279 aa)
Uncharacterized protein; Identified by Glimmer2; putative (185 aa)
Lipoprotein, putative; Identified by match to protein family HMM PF03938 (188 aa)
annotation not available (318 aa)
Uncharacterized protein; Identified by similarity to GP-21899254 (466 aa)
Uncharacterized protein; Identified by similarity to GP-21899254 (476 aa)
Uncharacterized protein; Identified by Glimmer2; putative (115 aa)
Cytochrome c3; Participates in sulfate respiration coupled with phosphorylation by transferring electrons from the enzyme dehydrogenase to ferredoxin (129 aa)
Your Current Organism:
Desulfovibrio vulgaris Hildenborough
NCBI taxonomy Id: 882 Other names: D. vulgaris str. Hildenborough, Desulfovibrio vulgaris (STRAIN HILDENBOROUGH), Desulfovibrio vulgaris ATCC 29579, Desulfovibrio vulgaris Hildenborough, Desulfovibrio vulgaris str. Hildenborough, Desulfovibrio vulgaris subsp. vulgaris (strain Hildenborough), Desulfovibrio vulgaris subsp. vulgaris ATCC 29579, Desulfovibrio vulgaris subsp. vulgaris str. Hildenborough