STRINGSTRING
PP1S402_42V6.2 protein (Physcomitrella patens) - STRING interaction network
"PP1S402_42V6.2" - Predicted protein in Physcomitrella patens
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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some 3D structure is known or predicted
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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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Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
PP1S402_42V6.2Predicted protein (664 aa)    
Predicted Functional Partners:
PP1S163_26V6.2
Predicted protein (583 aa)
 
  0.999
PP1S135_25V6.1
Aminoimidazole ribonucleotide carboxylase (598 aa)
       
  0.900
PP1S29_338V6.1
Predicted protein (278 aa)
   
 
  0.879
PP1S140_62V6.1
Annotation not available (903 aa)
   
 
  0.878
CNX5
Predicted protein; Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A. Its N-terminus first activates URM1 and MOCS2A as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and MOCS2A to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the pers [...] (467 aa)
   
   
  0.863
PP1S5151_1V6.1
Predicted protein (324 aa)
   
 
  0.854
PP1S72_262V6.1
Phosphoribosylformylglycinamidine cyclo-ligase (386 aa)
       
  0.818
PP1S53_111V6.1
Phosphoribosylformylglycinamidine cyclo-ligase (388 aa)
       
  0.818
PP1S88_47V6.1
Predicted protein (666 aa)
   
   
 
0.801
THI1-2
Predicted protein; Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron-dependent sulfide transfer from a conserved cysteine residue of the protein to a thiazole intermediate. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. May have additional roles in adaptation to various stress conditions and in DNA damage tolerance (362 aa)
   
   
  0.780
Your Current Organism:
Physcomitrella patens
NCBI taxonomy Id: 3218
Other names: Bryophyta, Bryophytina, Bryopsida, Funariaceae, Funariales, Funariidae, Moss Superclass V, Musci, P. patens, Physcomitrella, Physcomitrella Bruch & Schimp, Physcomitrella patens, Physcomitrella patens (Hedw.) Bruch & Schimp., Physcomitrium patens, Physcomitrium patens (Hedw.) Mitt., bryophytes, mosses
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