STRINGSTRING
A0A1V6QAQ8 A0A1V6QAQ8 A0A1V6QB42 A0A1V6QB42 A0A1V6QB73 A0A1V6QB73 A0A1V6QFK1 A0A1V6QFK1 A0A1V6QHU8 A0A1V6QHU8 A0A1V6QJJ3 A0A1V6QJJ3 A0A1V6QQH6 A0A1V6QQH6 A0A1V6QS88 A0A1V6QS88 A0A1V6QT24 A0A1V6QT24 A0A1V6QV00 A0A1V6QV00 A0A1V6QV55 A0A1V6QV55 A0A1V6QVG1 A0A1V6QVG1 A0A1V6QWV1 A0A1V6QWV1 A0A1V6QXY8 A0A1V6QXY8 A0A1V6QY15 A0A1V6QY15 A0A1V6R0X7 A0A1V6R0X7 A0A1V6R0Z0 A0A1V6R0Z0 A0A1V6R3A3 A0A1V6R3A3 A0A1V6R567 A0A1V6R567 A0A1V6R5R7 A0A1V6R5R7 A0A1V6R6C6 A0A1V6R6C6 A0A1V6R6L8 A0A1V6R6L8 A0A1V6R8B7 A0A1V6R8B7 A0A1V6R9X9 A0A1V6R9X9 A0A1V6RAK0 A0A1V6RAK0 A0A1V6RB84 A0A1V6RB84 A0A1V6RDH7 A0A1V6RDH7 A0A1V6RDY2 A0A1V6RDY2 A0A1V6RI00 A0A1V6RI00 A0A1V6RJZ5 A0A1V6RJZ5 A0A1V6RKG0 A0A1V6RKG0 A0A1V6RKW3 A0A1V6RKW3 A0A1V6RL74 A0A1V6RL74 A0A1V6RM47 A0A1V6RM47 A0A1V6RNR3 A0A1V6RNR3 A0A1V6RP64 A0A1V6RP64 A0A1V6RPB1 A0A1V6RPB1 A0A1V6RPI3 A0A1V6RPI3
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:
A0A1V6QAQ8CMP/dCMP-type deaminase domain-containing protein. (353 aa)
A0A1V6QB42Thymidylate_kin domain-containing protein. (226 aa)
A0A1V6QB73Queuine 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. (467 aa)
A0A1V6QFK1Uncharacterized protein. (334 aa)
A0A1V6QHU8Dihydrofolate synthetase; Belongs to the folylpolyglutamate synthase family. (413 aa)
A0A1V6QJJ3Adenylosuccinate synthetase; Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP. (423 aa)
A0A1V6QQH6Serine hydroxymethyltransferase; Interconversion of serine and glycine. Belongs to the SHMT family. (525 aa)
A0A1V6QS88ACT domain-containing protein. (287 aa)
A0A1V6QT24DHFR domain-containing protein; Belongs to the dihydrofolate reductase family. (278 aa)
A0A1V6QV00ADSL_C domain-containing protein. (446 aa)
A0A1V6QV55SAICAR_synt domain-containing protein. (301 aa)
A0A1V6QVG1Adenylosuccinate lyase; Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily. (483 aa)
A0A1V6QWV1Uncharacterized protein. (336 aa)
A0A1V6QXY8Queuine 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 [...] (415 aa)
A0A1V6QY15Thymidylat_synt domain-containing protein. (336 aa)
A0A1V6R0X7MGS domain-containing protein. (595 aa)
A0A1V6R0Z0Pterin-binding domain-containing protein. (465 aa)
A0A1V6R3A3Flavoprotein domain-containing protein. (235 aa)
A0A1V6R567Flavoprotein domain-containing protein. (251 aa)
A0A1V6R5R7Uncharacterized protein. (939 aa)
A0A1V6R6C6Formyl_trans_N domain-containing protein. (223 aa)
A0A1V6R6L8FSH1 domain-containing protein. (287 aa)
A0A1V6R8B7Glycine cleavage system P protein; The glycine cleavage system catalyzes the degradation of glycine. (1057 aa)
A0A1V6R9X9ATP-grasp domain-containing protein. (803 aa)
A0A1V6RAK0Uncharacterized protein. (307 aa)
A0A1V6RB84Amidophosphoribosyltransferase. (580 aa)
A0A1V6RDH7Aminomethyltransferase; The glycine cleavage system catalyzes the degradation of glycine; Belongs to the GcvT family. (483 aa)
A0A1V6RDY2FSH1 domain-containing protein. (239 aa)
A0A1V6RI00Glutamine amidotransferase type-1 domain-containing protein. (1360 aa)
A0A1V6RJZ5Uncharacterized protein. (119 aa)
A0A1V6RKG0Folylpolyglutamate synthase; Catalyzes conversion of folates to polyglutamate derivatives allowing concentration of folate compounds in the cell and the intracellular retention of these cofactors, which are important substrates for most of the folate-dependent enzymes that are involved in one-carbon transfer reactions involved in purine, pyrimidine and amino acid synthesis; Belongs to the folylpolyglutamate synthase family. (517 aa)
A0A1V6RKW3Phosphoribosylaminoimidazole carboxylase; In the C-terminal section; belongs to the AIR carboxylase family. Class I subfamily. (572 aa)
A0A1V6RL74AB hydrolase-1 domain-containing protein. (366 aa)
A0A1V6RM47FSH1 domain-containing protein. (258 aa)
A0A1V6RNR3Glycine cleavage system H protein; The H protein shuttles the methylamine group of glycine from the P protein to the T protein; Belongs to the GcvH family. (170 aa)
A0A1V6RP64Uncharacterized protein. (403 aa)
A0A1V6RPB1Serine hydroxymethyltransferase; Interconversion of serine and glycine. Belongs to the SHMT family. (469 aa)
A0A1V6RPI3dUTPase domain-containing protein. (188 aa)
Your Current Organism:
Penicillium solitum
NCBI taxonomy Id: 60172
Other names: ATCC 9923, CBS 288.36, CBS 424.89, FRR 937, IBT 3948, IFO 7765, IMI 039810, IMI 092225, LSHB P52, MUCL 28668, MUCL 29173, NRRL 937, P. solitum
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