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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
MJ_1598Conserved hypothetical protein; Similar to GP:1652098 percent identity: 35.67; identified by sequence similarity; putative; Belongs to the UPF0284 family. (350 aa)    
Predicted Functional Partners:
cobS
Cobalamin (5'-phosphate) synthase (cobS); Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'- phosphate; Belongs to the CobS family.
 
  
 0.942
cobY
Conserved hypothetical protein; Guanylyltransferase that catalyzes the synthesis of adenosylcobinamide-GDP (AdoCbi-GDP) from adenosylcobinamide-phosphate (AdoCbi-P) and GTP. Is involved in adenosylcobalamin biosynthesis. Binds one GTP per dimer. Cannot use other NTPs or GDP. Does not display AdoCbi kinase activity. Is also able to catalyze the condensation of 2- phospho-L-lactate (LP) with GTP in vitro to form PPi and (2S)-lactyl-2- diphospho-5'-guanosine (LPPG), but is much less efficient than CofC, the presumed enzyme catalyzing this reaction in vivo.
 
     0.864
cobQ
Cobyric acid synthase (cbiP); Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation (By similarity); Belongs to the CobB/CobQ family. CobQ subfamily.
  
  
 0.829
hisC
Histidinol-phosphate aminotransferase (hisC); Similar to SP:P06986 GB:U02071 GB:X03416 PID:41695 PID:41710 percent identity: 29.00; identified by sequence similarity; putative.
  
  
 0.808
cbiA
Cobyrinic acid a,c-diamide synthase (cbiA); Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP- dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source.
  
  
 0.806
MJ_1599
Hypothetical protein; Identified by GeneMark; putative; M. jannaschii predicted coding region MJ1599.
       0.748
cobD
Cobalamin biosynthesis protein B (cbiB); Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
 
  
 0.738
MJ_1130
O-sialoglycoprotein endopeptidase (gcp); Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. The Kae1 domain likely plays a direct catalytic role in this reaction (By similarity). The Bud32 domain probably displays kinase activity that regulates Kae1 function. In vitro, exhibits low ATPase activity, but does not bind DNA and does [...]
     
 0.734
proS
prolyl-tRNA synthetase (proS); Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). Can inadvertently accommodate and process non-cognate amino acids such as cysteine and alanine.
     
 0.688
cbiG
Cobalamin biosynthesis protein (cbiG); Catalyzes the hydrolysis of the ring A acetate delta-lactone of cobalt-precorrin-5A resulting in the loss of the C-20 carbon and its attached methyl group in the form of acetaldehyde.
  
  
 0.663
Your Current Organism:
Methanocaldococcus jannaschii
NCBI taxonomy Id: 243232
Other names: M. jannaschii DSM 2661, Methanocaldococcus jannaschii DSM 2661, Methanocaldococcus jannaschii str. DSM 2661, Methanococcus jannaschii DSM 2661
Server load: high (86%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.