STRINGSTRING
Btus_0027 Btus_0027 Btus_0028 Btus_0028 Btus_0425 Btus_0425 Btus_0426 Btus_0426 Btus_0432 Btus_0432 Btus_0433 Btus_0433 Btus_0434 Btus_0434 Btus_0435 Btus_0435 Btus_1703 Btus_1703 Btus_1704 Btus_1704 Btus_1705 Btus_1705
Nodes:
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.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
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 to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Btus_0027PFAM: cytochrome c oxidase subunit I; KEGG: afl:Aflv_1359 cytochrome c oxidase (b(o/a)3- type) chain I; Belongs to the heme-copper respiratory oxidase family. (562 aa)
Btus_0028PFAM: cytochrome c oxidase subunit II; KEGG: bbe:BBR47_04020 probable bo3-type cytochrome c oxidase. (158 aa)
Btus_0425PFAM: cytochrome c oxidase subunit II; KEGG: bbe:BBR47_04020 probable bo3-type cytochrome c oxidase. (155 aa)
Btus_0426PFAM: cytochrome c oxidase subunit I; KEGG: bbe:BBR47_04030 probable bo3-type cytochrome c oxidase; Belongs to the heme-copper respiratory oxidase family. (556 aa)
Btus_0432Cytochrome c oxidase, subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). (334 aa)
Btus_0433Cytochrome c oxidase, subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (626 aa)
Btus_0434KEGG: gym:GYMC10_0738 cytochrome-c oxidase; PFAM: cytochrome c oxidase subunit III. (213 aa)
Btus_0435PFAM: cytochrome C oxidase subunit IV; KEGG: mcl:MCCL_0735 hypothetical protein. (104 aa)
Btus_1703PFAM: cytochrome c class I; KEGG: bbe:BBR47_24910 menaquinol-cytochrome c reductase cytochrome b/c subunit. (259 aa)
Btus_1704PFAM: Cytochrome b/b6 domain; KEGG: bbe:BBR47_24900 menaquinol-cytochrome c reductase cytochrome b subunit. (223 aa)
Btus_1705Rieske (2Fe-2S) iron-sulfur domain protein; PFAM: Rieske [2Fe-2S] iron-sulphur domain; KEGG: bay:RBAM_020720 QcrA. (181 aa)
Your Current Organism:
Kyrpidia tusciae
NCBI taxonomy Id: 562970
Other names: Bacillus tusciae DSM 2912, K. tusciae DSM 2912, Kyrpidia tusciae DSM 2912, Kyrpidia tusciae NBRC 15312, Kyrpidia tusciae str. DSM 2912, Kyrpidia tusciae strain DSM 2912
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