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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colored nodes:
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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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
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[Homology]
Score
KXB74109.1KEGG: cpy:Cphy_2001 1.7e-78 DEAD/DEAH box helicase; K11927 ATP-dependent RNA helicase RhlE; Psort location: Cytoplasmic, score: 9.97. (597 aa)    
Predicted Functional Partners:
nnrD
YjeF domain protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epim [...]
   
 0.886
KXB77642.1
30S ribosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence.
   
 0.880
pnp
Polyribonucleotide nucleotidyltransferase; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction.
 
 
 0.857
rpsE
Ribosomal protein S5; Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. Belongs to the universal ribosomal protein uS5 family.
  
 0.844
rpsD
Ribosomal protein S4; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
  
 0.822
KXB74110.1
Permease, YjgP/YjgQ family; KEGG: hip:CGSHiEE_03515 3.9e-10 leucyl aminopeptidase K11720; Psort location: CytoplasmicMembrane, score: 10.00.
  
    0.820
lon
Endopeptidase La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
   
   0.790
tgt
tRNA-guanine transglycosylase; 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 the [...]
  
 
 0.786
rpsK
30S ribosomal protein S11; Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine- Dalgarno cleft in the 70S ribosome; Belongs to the universal ribosomal protein uS11 family.
   
 0.783
KXB79112.1
UvrD/REP helicase; KEGG: pmz:HMPREF0659_A6530 7.4e-291 UvrD/REP helicase K03657; Psort location: Cytoplasmic, score: 9.97.
  
 0.762
Your Current Organism:
Prevotella amnii
NCBI taxonomy Id: 419005
Other names: CCUG 53648, DSM 23384, JCM 14753, P. amnii, Prevotella amnii Lawson et al. 2008 emend. Hahnke et al. 2016
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