STRINGSTRING
STRING protein interaction network
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
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
CAZ95328.1Glycoside hydrolase, family GH114; Glycoside hydrolases hydrolyse the glycosidic bond between two or more carbohydrates or between a carbohydrate and a non-carbohydrate moiety. Belongs to the family 114 of the glycoside hydrolases. Family GH114 contains endo-alpha-1,4-polygalactosaminidases, but the specificity of this protein is unclear. Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 29 and 30. Localized in the outer membrane; Specificity unclear. (292 aa)    
Predicted Functional Partners:
cysS
Cysteinyl-tRNA synthetase catalyzes the attachment of cysteine to its cognate transfer RNA molecule in a highly specific two-step reaction. It is a monomer and belongs to the class I of the aminoacyl-tRNA synthetases. It binds one zinc ion as cofactor. Localized in the cytoplasm; High confidence in function and specificity.
     
 0.911
CAZ96815.1
Modular protein containing a N-terminal domain adopting a parallel beta-helix fold and a C-terminal carbohydrate binding module of the family 13 (CBM13). The N-terminal domain is distantly related to the polysaccharide lyases of the family 9 (PL9). Features a signal peptide cleaved between residues 26 and 27. Localized in the periplasm; Specificity unclear.
  
     0.770
CAZ97788.1
Conserved hypothetical protein; Contains a N-terminal DUF 11 domain. Protein that would bind calcium ions by several EF-hand calcium-binding domains or/and by trombospondin type III domains; Signal peptide cleaved between the residues 27 and 28; Putatively localized in the outer membrane.
  
     0.769
CAZ95076.1
Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 22 and 23; Localized in the outer membrane; Hypothetical protein.
  
     0.767
CAZ96814.1
Beta-helix fold protein; This protein likely adopts a right handed parallel beta-helix fold. Displays also a C-terminal PKD domain; Signal peptide cleaved between the residues 28 and 29; Localized in the periplasmic space; Function unclear.
  
     0.766
pcaC
Modular protein displaying a N-terminal 4-carboxymuconolactone decarboxylase (CMD) domain and a C-terminal conserved domain of unknown function. CMD is involved in protocatechuate catabolism. It converts the 2-carboxy-2,5-dihydro-5-oxofuran-2-acetate to 4,5-dihydro-5-oxofuran-2-acetate; Localized in the cytoplasm:; High confidence in function and specificity.
  
     0.744
CAZ98552.1
Conserved hypothetical protein; Localized in the cytoplasm.
  
     0.736
CAZ98344.1
Conserved hypothetical protein; Putatively contains a C-terminal Globin-like domain; Probably localized in the cytoplasm.
  
     0.729
alsD
Alpha-acetolactate decarboxylase converts acetolactate into acetoin, which can be secreted by the cells. This may be a mechanism for controlling the internal pH of cells in the stationary stage; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 15 and 16; Localized in cytoplasmic and/or the outer membrane; High confidence in function and specificity.
  
     0.636
agaD
Beta-agarase D, family GH16; Cleaves the beta-1,4-linkages between beta-D-galactose and alpha-L-3,6-anhydro-galactose residues in agarose. Cleaves agarose in a random manner with retention of the anomeric-bond configuration, producing beta-anomers that give rise progressively to alpha-anomers when mutarotation takes place. Requires at least 4 consecutive agarose units and is highly intolerant to modifications.
  
     0.635
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
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