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.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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rtcBProtein of unknown function UPF0027; GTP-dependent RNA ligase that is involved in tRNA splicing and RNA repair. Joins RNA with 2',3'-cyclic-phosphate or 3'-phosphate ends to RNA with 5'-hydroxy ends; Belongs to the RtcB family. (480 aa)    
Predicted Functional Partners:
MMP0647
ATP/GTP-binding site motif A (P-loop):Protein of unknown function DUF101; Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently.
 
 0.995
rtcA
RNA 3'-terminal phosphate cyclase; Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.
 
  
 0.945
rnz
Conserved hypothetical protein; Zinc phosphodiesterase, which displays some tRNA 3'- processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA; Belongs to the RNase Z family.
 
   
 0.938
endA
tRNA-intron endonuclease; Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a stem of 4 bp.
     
 0.932
lysC
Aspartate kinase; Citation: Tang G, Zhu-Shimoni JX, Amir R, Zchori IB, Galili G. (1997) Plant Mol Biol 34:287-93; Belongs to the aspartokinase family.
  
  
 0.872
MMP1201
Staphylococcus nuclease (SNase-like):Thermonuclease; Citation: Mol. Cell. Biochem. (1978) 22: 67-77.
     
 0.863
MMP0457
Probable ATP dependent RNA helicase; Citation: Mol. Cell 2001; 8:251-62. Nucleic Acids Res. 1999; 27:3811-20. Prog. Nucleic Acid Res. Biol. 2002; 72:307-31, PNAS (2001) 98:; Belongs to the DEAD box helicase family.
   
 0.775
flpA-2
Fibrillarin; Involved in pre-rRNA and tRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine to catalyze the site-specific 2'-hydroxyl methylation of ribose moieties in rRNA and tRNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA; Belongs to the methyltransferase superfamily. Fibrillarin family.
   
 0.775
asd
Aspartate-semialdehyde dehydrogenase; Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate; Belongs to the aspartate-semialdehyde dehydrogenase family.
  
    0.703
aIF-1A
Translation initiation factor 1A (aIF-1A); Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits.
     
 0.701
Your Current Organism:
Methanococcus maripaludis S2
NCBI taxonomy Id: 267377
Other names: M. maripaludis S2, Methanococcus maripaludis LL, Methanococcus maripaludis str. S2, Methanococcus maripaludis strain S2
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