STRINGSTRING
hsp20-1 hsp20-1 hsp60-4 hsp60-4 pfdB pfdB RCIX2297 RCIX2297 hsp60-3 hsp60-3 hsp60-2 hsp60-2 hsp20-3 hsp20-3 RCIX1138 RCIX1138 RCIX1090 RCIX1090 pfdA pfdA dnaK dnaK dnaJ dnaJ LRC445 LRC445 hsp60-1 hsp60-1 hsp20-2 hsp20-2 RCIX2503 RCIX2503
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:
hsp20-1Chaperonin Hsp20; Belongs to the small heat shock protein (HSP20) family. (147 aa)
hsp60-4Chaperonin Hsp60 (GroEL-like); Belongs to the TCP-1 chaperonin family. (549 aa)
pfdBChaperonin cofactor prefoldin, beta subunit; Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding. (126 aa)
RCIX2297Predicted phosphoesterase (RecJ-like). (702 aa)
hsp60-3Chaperonin Hsp60 (GroEL-like); Belongs to the TCP-1 chaperonin family. (560 aa)
hsp60-2Chaperonin Hsp60 (GroEL-like); Belongs to the TCP-1 chaperonin family. (548 aa)
hsp20-3Chaperonin Hsp20; Belongs to the small heat shock protein (HSP20) family. (144 aa)
RCIX1138Predicted protein interacting with DnaK (DnaJ-like). (242 aa)
RCIX1090Predicted Zn-finger protein interacting with DnaK (DnaJ-like). (494 aa)
pfdAPutative chaperonin cofactor prefoldin, alpha subunit; Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding. (138 aa)
dnaKChaperonin Hsp70; Acts as a chaperone. (623 aa)
dnaJChaperonin Hsp40; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK an [...] (380 aa)
LRC445Putative chaperonin (DnaJ family), N-terminal fragment. (175 aa)
hsp60-1Chaperonin Hsp60 (GroEL-like); Belongs to the TCP-1 chaperonin family. (536 aa)
hsp20-2Chaperonin Hsp20; Belongs to the small heat shock protein (HSP20) family. (165 aa)
RCIX2503Hypothetical protein. (234 aa)
Your Current Organism:
Methanocella arvoryzae
NCBI taxonomy Id: 351160
Other names: M. arvoryzae MRE50, Methanocella arvoryzae MRE50, Methanocella arvoryzae str. MRE50, Methanocella arvoryzae strain MRE50, uncultured methanogenic archaeon RC-I, uncultured methanogenic archaeon Rice Cluster I
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