STRINGSTRING
Saci_1747 Saci_1747 soxM soxM soxE soxE soxC-3 soxC-3 soxH soxH Saci_2096 Saci_2096 soxA soxA cbaA cbaA soxB soxB soxC-2 soxC-2 soxC soxC
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:
Saci_1747Hypothetical protein. (229 aa)
soxMQuinol oxidase polypeptide I/III; Terminal oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. SoxM forms the functional core of the enzyme complex; In the C-terminal section; belongs to the cytochrome c oxidase subunit 3 family. (788 aa)
soxESulfocyanin, blue copper protein; The 4 redox proteins SoxE, SoxF, SoxG and SoxH probably form part of a membrane respiratory complex together with SoxM, a catalytic subunit of cytochrome oxidase. (204 aa)
soxC-3Cytochrome b. (506 aa)
soxHCytochrome c oxidase subunit II. (146 aa)
Saci_2096Sulfocyanin. (134 aa)
soxAConserved quinol oxidase polypeptide II; The terminal 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. (168 aa)
cbaACytochrome c oxidase polypeptide I. (588 aa)
soxBCytochrome c and quinol oxidase polypeptide I; Catalyzes the reduction of oxygen to water. Subunit I binds heme a and the bimetallic center. (508 aa)
soxC-2Cytochrome b; Binds 2 heme groups (b586 and b606) which are not covalently bound to the protein. (562 aa)
soxCCytochrome b. (537 aa)
Your Current Organism:
Sulfolobus acidocaldarius DSM 639
NCBI taxonomy Id: 330779
Other names: S. acidocaldarius DSM 639, Sulfolobus acidocaldarius ATCC 33909, Sulfolobus acidocaldarius NCIB 11770
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