STRINGSTRING
ACLA_057310 ACLA_057310 ACLA_058800 ACLA_058800 cfd1 cfd1 ACLA_072520 ACLA_072520 nbp35 nbp35 TAH18 TAH18 ACLA_066050 ACLA_066050 nar1 nar1 cia1 cia1 dre2 dre2 ACLA_085750 ACLA_085750
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:
ACLA_057310Cytoplasmic protein required for cell viability, putative. (200 aa)
ACLA_058800DNA repair/transcription protein, putative. (1057 aa)
cfd1Cytosolic Fe-S cluster assembly factor cfd1; Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The nbp35-cfd1 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins; Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP2/CFD1 subfamily. (315 aa)
ACLA_072520Thioredoxin, putative. (270 aa)
nbp35Cytosolic Fe-S cluster assembly factor nbp35; Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The nbp35-cfd1 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins; Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP1/NBP35 subfamily. (344 aa)
TAH18NADPH-dependent diflavin oxidoreductase 1; Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis. Transfers electrons from NADPH to the Fe-S cluster of DRE2. Positively controls H(2)O(2)-induced cell death; In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. (646 aa)
ACLA_066050BolA domain protein; Belongs to the BolA/IbaG family. (134 aa)
nar1Cytosolic Fe-S cluster assembly factor nar1; Component of the cytosolic Fe/S protein assembly machinery. Required for maturation of extramitochondrial Fe/S proteins. May play a role in the transfer of pre-assembled Fe/S clusters to target apoproteins (By similarity). (597 aa)
cia1Probable cytosolic iron-sulfur protein assembly protein 1; Essential component of the cytosolic iron-sulfur (Fe/S) protein assembly machinery. Required for the maturation of extramitochondrial Fe/S proteins. (453 aa)
dre2Fe-S cluster assembly protein dre2; Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex cfd1-nbp35. Electrons are transferred to dre2 from NADPH via the FAD- and FMN-containing protein tah18. Tah18-dre2 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by [...] (310 aa)
ACLA_085750BolA domain protein; Belongs to the BolA/IbaG family. (92 aa)
Your Current Organism:
Aspergillus clavatus
NCBI taxonomy Id: 344612
Other names: A. clavatus NRRL 1, Aspergillus clavatus NRRL 1
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.