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pcm protein (Desulfovibrio vulgaris Hildenborough) - STRING interaction network
"pcm" - Protein-L-isoaspartate O-methyltransferase in Desulfovibrio vulgaris Hildenborough
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Predicted Interactions
gene neighborhood
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gene co-occurrence
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textmining
co-expression
protein homology
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pcmProtein-L-isoaspartate O-methyltransferase; Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins (210 aa)    
Predicted Functional Partners:
surE
5’-nucleotidase SurE; Nucleotidase that shows phosphatase activity on nucleoside 5’-monophosphates; Belongs to the SurE nucleotidase family (250 aa)
   
  0.940
DVU_1848
Uncharacterized protein; Identified by similarity to OMNI-NTL03PA05518; match to protein family HMM PF00597 (197 aa)
              0.883
gltX-1
Glutamyl-Q tRNA(Asp) synthetase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5- dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon (324 aa)
   
   
  0.766
miaA
tRNA dimethylallyltransferase; Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A); Belongs to the IPP transferase family (309 aa)
         
  0.680
polA
DNA polymerase I; Identified by similarity to SP-P00582; match to protein family HMM PF00476; match to protein family HMM PF01367; match to protein family HMM PF02739; match to protein family HMM TIGR00593 (1015 aa)
   
   
  0.666
DVU_1847
Iron-sulfur cluster carrier protein; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP (297 aa)
   
        0.664
tgt
Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1’ of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1’ of the ribose to form th [...] (375 aa)
   
   
  0.646
ispD
Bifunctional enzyme IspD/IspF; Bifunctional enzyme that catalyzes the formation of 4- diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl- D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2- phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4- cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF); In the N-terminal section; belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily (395 aa)
   
   
  0.643
DVU_1850
CBS domain protein; Identified by match to protein family HMM PF00571 (142 aa)
              0.639
hisS
Histidine--tRNA ligase; Identified by similarity to SP-P04804; match to protein family HMM PF00587; match to protein family HMM PF03129; match to protein family HMM TIGR00442 (417 aa)
   
   
  0.619
Your Current Organism:
Desulfovibrio vulgaris Hildenborough
NCBI taxonomy Id: 882
Other names: D. vulgaris str. Hildenborough, Desulfovibrio vulgaris (STRAIN HILDENBOROUGH), Desulfovibrio vulgaris ATCC 29579, Desulfovibrio vulgaris Hildenborough, Desulfovibrio vulgaris str. Hildenborough, Desulfovibrio vulgaris subsp. vulgaris (strain Hildenborough), Desulfovibrio vulgaris subsp. vulgaris ATCC 29579, Desulfovibrio vulgaris subsp. vulgaris str. Hildenborough
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