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PP1S52_149V6.1 protein (Physcomitrella patens) - STRING interaction network
"PP1S52_149V6.1" - Predicted protein in Physcomitrella patens
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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PP1S52_149V6.1Predicted protein; Catalytic subunit of the molybdopterin synthase complex, a complex that catalyzes the conversion of precursor Z into molybdopterin. Acts by mediating the incorporation of 2 sulfur atoms from thiocarboxylated MOCS2A into precursor Z to generate a dithiolene group (166 aa)    
Predicted Functional Partners:
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)
 
  0.996
PP1S403_17V6.1
Predicted protein; Acts as a sulfur carrier required for molybdopterin biosynthesis. Component of the molybdopterin synthase complex that catalyzes the conversion of precursor Z into molybdopterin by mediating the incorporation of 2 sulfur atoms into precursor Z to generate a dithiolene group. In the complex, serves as sulfur donor by being thiocarboxylated (-COSH) at its C-terminus by MOCS3. After interaction with MOCS2B, the sulfur is then transferred to precursor Z to form molybdopterin (97 aa)
 
  0.994
PP1S180_13V6.1
Predicted protein (443 aa)
 
  0.994
PP1S23_46V6.2
Predicted protein (445 aa)
 
  0.994
PP1S166_112V6.1
Predicted protein (323 aa)
 
 
  0.993
PP1S126_106V6.1
Predicted protein (698 aa)
 
 
  0.985
PP1S84_287V6.6
Predicted protein; Regulatory subunit of the dimeric ECR1-AXR1 E1 enzyme. E1 activates NEDD8/RUB1 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-ECR1 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of RCE1 (529 aa)
   
  0.814
PP1S79_267V6.1
Predicted protein; Regulatory subunit of the dimeric ECR1-AXR1 E1 enzyme. E1 activates NEDD8/RUB1 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-ECR1 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of RCE1 (520 aa)
   
  0.814
PP1S74_65V6.1
Predicted protein (1058 aa)
   
  0.814
PP1S73_159V6.1
Predicted protein (692 aa)
   
  0.814
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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