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
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
CAZ97463.1Radical SAM proteins catalyze diverse reactions, including unusual methylations, isomerization, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation. Evidence exists that these proteins generate a radical species by reductive cleavage of S:-adenosylmethionine (SAM) through an unusual Fe-S center. The exact function of this protein is unclear. Localized in the cytoplasm; Family membership. (650 aa)    
Predicted Functional Partners:
CAZ97125.1
The HNOB (Heme NO Binding) module, is a predominantly alpha-helical module and binds heme via a covalent linkage to histidine. The HNOB domain is predicted to function as a heme-dependent sensor for gaseous ligands, and transduce diverse downstream signals, in both bacteria and animals; Probably, acts as effector domain belonging to a two-component system; Family membership.
 
  
 0.885
ppk2
Polyphosphate kinase 2; Ppk2 was first identified in Pseudomonas aeruginosa by Zhang and cowokers (PNAS, 2006). Ppk2 belongs to a polyphosphate kinase family unrelated to that of Ppk1. Pkk2 also distinguished from PPK1 by the following: synthesis of poly P from GTP or ATP, a preference for Mn2+ over Mg2+, and a stimulation by poly P. The reverse reaction, a poly P-driven nucleoside diphosphate kinase synthesis of GTP from GDP, is 75-fold greater than the forward reaction, poly P synthesis from GTP. Localized in the cytoplasm; High confidence in function and specificity.
   
    0.690
CAZ97462.1
RNA pseudouridine synthase; Enzyme responsible for synthesis of pseudouridine from uracil in tRNA or rRNA by rotation of the C1'-N-1 glycosidic bond of uridine to a C1'-C5; Belongs to the pseudouridine synthase RluA family; localized in the cytoplasm; Specificity unclear.
  
    0.651
ccoNO
Fusion of the subunits CcoN and CcoO of the Cytochrome cbb3 oxidase. Converts the ferrocytochrome to ferricytochrome. Belongs to the ccoNOQP operon. Contains 13 transmembrane helices; Localized in the cytoplasmic membrane; High confidence in function and specificity.
   
  
 0.585
hemN
Oxygen-independent coproporphyrinogen III oxidase is involved in Porphyrin biosynthesis. It Catalysis the reaction: Coproporphyrinogen-III + 2 S-adenosyl-L-methionine = protoporphyrinogen-IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine; Binds 1 4Fe-4S cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine; Localized in the cytoplasm; High confidence in function and specificity.
  
  
 0.420
hemN-2
Oxygen-independent coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family.
  
  
 0.420
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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