STRINGSTRING
Dde_0536 Dde_0536 rlmN rlmN Dde_2837 Dde_2837 Dde_0504 Dde_0504 Dde_3237 Dde_3237 Dde_2722 Dde_2722 miaB miaB Dde_3159 Dde_3159 queH queH Dde_3241 Dde_3241 pnp pnp
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
Dde_0536Oxygen-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. (394 aa)    
Predicted Functional Partners:
rlmN
Radical SAM enzyme, Cfr family; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family.
 
   
 0.683
Dde_2837
TIGRFAM: Uroporphyrin-III C-methyltransferase, C-terminal; KEGG: dvl:Dvul_2236 uroporphyrin-III C-methyltransferase; PFAM: Tetrapyrrole methylase; Tetrapyrrole biosynthesis, uroporphyrinogen III synthase.
  
  
 0.678
Dde_0504
Non-canonical purine NTP pyrophosphatase, rdgB/HAM1 family; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family.
  
 0.660
Dde_3237
SMART: Pyruvate-flavodoxin oxidoreductase, EKR domain; TIGRFAM: Pyruvate-flavodoxin oxidoreductase; KEGG: dvl:Dvul_0348 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; PFAM: Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal; Pyruvate-flavodoxin oxidoreductase, EKR domain; 4Fe-4S ferredoxin, iron-sulphur binding, subgroup; Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Pyruvate/ketoisovalerate oxidoreductase; Belongs to the pyruvate:ferredoxin/flavodoxin oxidoreductase family.
  
  
 0.646
Dde_2722
RNA modification enzyme, MiaB family; TIGRFAM: Methylthiotransferase; PFAM: Methylthiotransferase, N-terminal; Radical SAM; KEGG: dvl:Dvul_2087 RNA modification protein; SMART: Elongator protein 3/MiaB/NifB.
 
   
 0.645
miaB
RNA modification enzyme, MiaB family; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
 
   
 0.641
Dde_3159
KEGG: dvl:Dvul_2429 hypothetical protein; TIGRFAM: Flagellar basal-body rod FlgF; Fagellar hook-basal body protein, FlgE/F/G; PFAM: Flagellar basal body rod protein, N-terminal; Protein of unknown function DUF1078, C-terminal.
    
   0.623
queH
Protein of unknown function DUF208; Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
 
     0.611
Dde_3241
Phosphate acetyltransferase; Involved in acetate metabolism. In the N-terminal section; belongs to the CobB/CobQ family.
  
  
 0.608
pnp
Polyribonucleotide nucleotidyltransferase; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction.
 
    0.596
Your Current Organism:
Desulfovibrio alaskensis
NCBI taxonomy Id: 207559
Other names: D. alaskensis G20, Desulfovibrio alaskensis G20, Desulfovibrio alaskensis str. G20, Desulfovibrio alaskensis strain G20, Desulfovibrio desulfuricans subsp. desulfuricans str. G20
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.