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A0A2L2U2E3 A0A2L2U2E3 A0A2L2TH48 A0A2L2TH48 A0A2L2TH91 A0A2L2TH91 A0A2L2TMP3 A0A2L2TMP3 A0A2L2TNN1 A0A2L2TNN1 A0A2L2TP43 A0A2L2TP43 A0A2L2TWM0 A0A2L2TWM0 A0A2L2TY08 A0A2L2TY08 A0A2L2U364 A0A2L2U364 A0A2L2SR25 A0A2L2SR25 A0A2L2ST63 A0A2L2ST63 A0A2L2SUZ4 A0A2L2SUZ4 A0A2L2SZZ5 A0A2L2SZZ5 A0A2L2T141 A0A2L2T141 A0A2L2T2I4 A0A2L2T2I4 A0A2L2T636 A0A2L2T636 A0A2L2T876 A0A2L2T876 A0A2L2TBP9 A0A2L2TBP9 A0A2L2TF50 A0A2L2TF50 A0A2L2TG61 A0A2L2TG61 A0A2L2TGL1 A0A2L2TGL1
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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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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Predicted Interactions
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A0A2L2U2E3Queuine tRNA-ribosyltransferase catalytic subunit 1; Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2- cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). 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, formi [...] (418 aa)
A0A2L2TH48Poly [ADP-ribose] polymerase. (760 aa)
A0A2L2TH91VIT domain-containing protein. (1054 aa)
A0A2L2TMP3Imidazole glycerol phosphate synthase hisHF; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The glutaminase domain produces the ammonia necessary for the cyclase domain to produce IGP and AICAR from PRFAR. The ammonia is channeled to the active site of the cyclase domain. Belongs to the HisA/HisF family. (549 aa)
A0A2L2TNN1Thiamine thiazole synthase; Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5- (2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron- dependent sulfide transfer from a conserved cysteine residue of the protein to a thiazole intermediate. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. May have additional roles in adaptation to various stress conditions and in DNA damage tolerance; Belongs to the T [...] (322 aa)
A0A2L2TP43Uncharacterized protein. (325 aa)
A0A2L2TWM0Amidophosphoribosyltransferase. (552 aa)
A0A2L2TY08Pribosyltran domain-containing protein. (233 aa)
A0A2L2U364Uncharacterized protein. (453 aa)
A0A2L2SR25Queuine tRNA-ribosyltransferase accessory subunit 2; Non-catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2- cyclopenten-1-yl)amino)methyl)-7-deazaguanosine); Belongs to the queuine tRNA-ribosyltransferase family. QTRT2 subfamily. (468 aa)
A0A2L2ST63Nicotinate-nucleotide pyrophosphorylase [carboxylating]; Involved in the catabolism of quinolinic acid (QA). Belongs to the NadC/ModD family. (294 aa)
A0A2L2SUZ4CAP10 domain-containing protein. (821 aa)
A0A2L2SZZ5S-methyl-5'-thioadenosine phosphorylase; Catalyzes the reversible phosphorylation of S-methyl-5'- thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates. (307 aa)
A0A2L2T141Uncharacterized protein. (411 aa)
A0A2L2T2I4CAP10 domain-containing protein. (827 aa)
A0A2L2T636CAP10 domain-containing protein. (627 aa)
A0A2L2T876Pribosyltran domain-containing protein. (275 aa)
A0A2L2TBP9Uncharacterized protein. (224 aa)
A0A2L2TF50BRCT domain-containing protein. (452 aa)
A0A2L2TG61Pribosyltran domain-containing protein. (215 aa)
A0A2L2TGL1FAD-binding PCMH-type domain-containing protein. (1138 aa)
Your Current Organism:
Fusarium venenatum
NCBI taxonomy Id: 56646
Other names: CBS 458.93, F. venenatum, Fusarium venetum
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