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pnp_3 pnp_3 deaD_2 deaD_2 xseA xseA rnhA_2 rnhA_2 xseB xseB AKA12197.1 AKA12197.1 AKA12261.1 AKA12261.1 rph rph AKA12294.1 AKA12294.1 rppH rppH pemK pemK mltC mltC yafQ yafQ mltF mltF rne rne rnhB rnhB yafQ_2 yafQ_2 rhlB_1 rhlB_1 AKA11127.1 AKA11127.1 AKA11225.1 AKA11225.1 AKA11284.1 AKA11284.1 rnb_2 rnb_2 csrA csrA
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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
pnp_3Polynucleotide phosphorylase/polyadenylase; Derived by automated computational analysis using gene prediction method: Protein Homology. (716 aa)
deaD_2DEAD/DEAH box helicase; Participates in the assembly of the large subunit of the ribosome; plays a key role in optimal cell growth at low temperature and is required for normal cell division; Derived by automated computational analysis using gene prediction method: Protein Homology. (602 aa)
xseAExodeoxyribonuclease VII large subunit; Bidirectionally degrades single-stranded DNA into large acid- insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides; Belongs to the XseA family. (511 aa)
rnhA_2Ribonuclease H; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. (153 aa)
xseBExodeoxyribonuclease VII small subunit; Bidirectionally degrades single-stranded DNA into large acid- insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides; Belongs to the XseB family. (76 aa)
AKA12197.1Cytotoxic translational repressor of toxin-antitoxin stability system; Derived by automated computational analysis using gene prediction method: Protein Homology. (83 aa)
AKA12261.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (287 aa)
rphRibonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. (238 aa)
AKA12294.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (328 aa)
rppHRNA pyrophosphohydrolase; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. RppH subfamily. (214 aa)
pemKPemk protein; Toxic component of a type II toxin-antitoxin (TA) system. (110 aa)
mltCMurein transglycosylase; Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. (363 aa)
yafQAddiction module antitoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (89 aa)
mltFMurein transglycosylase; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. (497 aa)
rneRibonuclease E; Endoribonuclease that plays a central role in RNA processing and decay. Required for the maturation of 5S and 16S rRNAs and the majority of tRNAs. Also involved in the degradation of most mRNAs. Belongs to the RNase E/G family. RNase E subfamily. (977 aa)
rnhBRibonuclease HII; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. (198 aa)
yafQ_2Toxin RelE; Derived by automated computational analysis using gene prediction method: Protein Homology. (89 aa)
rhlB_1RNA helicase; Derived by automated computational analysis using gene prediction method: Protein Homology. (411 aa)
AKA11127.1Lysozyme; Derived by automated computational analysis using gene prediction method: Protein Homology. (189 aa)
AKA11225.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (198 aa)
AKA11284.1Lysozyme; Derived by automated computational analysis using gene prediction method: Protein Homology. (188 aa)
rnb_2Exoribonuclease II; Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3' to 5' direction. (658 aa)
csrACarbon storage regulator; A key translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Mediates global changes in gene expression, shifting from rapid growth to stress survival by linking envelope stress, the stringent response and the catabolite repression systems. Usually binds in the 5'-UTR; binding at or near the Shine-Dalgarno sequence prevents ribosome-binding, repressing translation, binding elsewhere in the 5'-UTR can activate translation and/or stabilize the mRNA. Its function is antagonized by small RNA(s). (61 aa)
Your Current Organism:
Mannheimia haemolytica
NCBI taxonomy Id: 75985
Other names: ATCC 33396, CCUG 12392, CCUG 408, CIP 103426, DSM 10531, M. haemolytica, NCTC 9380, Pasteurella haemolytica, strain J.A. Watt 1266AB
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