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
EDP11243.1Putative 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. (363 aa)    
Predicted Functional Partners:
lepA
GTP-binding protein LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner.
  
 0.892
EDP11244.1
Sporulation initiation factor Spo0A domain protein; COG: COG0784 FOG: CheY-like receiver; Psort location: Cytoplasmic, score:8.87.
     
 0.771
nifJ
KEGG: fnu:FN1170 0. pyruvate-flavodoxin oxidoreductase K03737; COG: COG1013 Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit; Psort location: Cytoplasmic, score:8.87.
  
  
 0.764
rlmN
23S rRNA m2A2503 methyltransferase; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs; Belongs to the radical SAM superfamily. RlmN family.
 
   
 0.758
rdgB
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.
 
  
 0.643
EDP11245.1
Hypothetical protein; Psort location: Cytoplasmic, score:8.87.
       0.609
EDP10820.1
Putative radical SAM protein YgiQ; KEGG: eci:UTI89_C3435 6.2e-123 hypothetical protein; COG: COG1032 Fe-S oxidoreductase; Psort location: Cytoplasmic, score:8.87.
  
  
 0.528
prkC
Serine/threonine-protein kinase PrkC; KEGG: lsa:LSA0692 1.5e-91 putative serine/threonine protein kinase K08884; COG: COG0515 Serine/threonine protein kinase; Psort location: CytoplasmicMembrane, score:9.49.
    
  0.528
EDP11242.1
Hypothetical protein; Psort location: Cytoplasmic, score:8.87.
       0.518
miaB
tRNA-i(6)A37 thiotransferase enzyme MiaB; 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.
 
  
 0.504
Your Current Organism:
Absiella dolichum
NCBI taxonomy Id: 428127
Other names: A. dolichum DSM 3991, Absiella dolichum ATCC 29143, Absiella dolichum DSM 3991, Eubacterium dolichum ATCC 29143, Eubacterium dolichum DSM 3991, Eubacterium dolichum strain DSM 3991
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