Basic Information
Gene ID
Pop_G14G023658
Position
chrG14:12430888-12431615 (+)
727bp
Gene Type
gene
Gene Description (Protein Product)
"Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys)
Organism
Also AS Potri.014G078200AT3G61113Potri.014G078200.v4.1

Gene Structure

upstream:

Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
Pop_G16G016169 Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with NCS6 CTU1 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position
Pop_UnG037361 Cysteine desulfurase 1
Pop_UnG037360 Cysteine desulfurase 1
Regulatory gene
Pop_A01G003804 Growth-regulating factor
Pop_A01G004214 Growth-regulating factor
Pop_A01G006027 LOB domain-containing protein

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Annotation

Orthologous Group
Orthologous ID Species Number All hits in PereRegDB Hits of this species Orthologous Detail

Expression Profile
DataSet Number of Samples expressed(TPM>1) Mean Min Max Standard deviation(SD) Coeffcient variation(CV)


Pathway
KEGG Term Name Description
map04122 Sulfur relay system Ubiquitin and ubiquitin-like proteins (Ubls) are signalling messengers that control many cellular functions, such as cell proliferation, apoptosis, and DNA repair. It is suggested that Ub-protein modification evolved from prokaryotic sulfurtransfer systems. Molybdenum cofactor (Moco) and thiamin are sulfur-containing cofactors whose biosynthesis includes a key sulfur transfer step that uses unique sulfur carrier proteins, MoaD and ThiS. Ubiquitin, MoaD, and ThiS are all structurally related proteins whose C-termini are activated through adenylation by homologous E1-like enzymes. s2T biosynthesis may share similar chemistry with Moco and thiamin synthesis. In Saccharomyces cerevisiae, Urm1 and Uba4 function as part of a ubl protein conjugation system, though they have sequence homology to bacterial sulfur-transfer enzymes and the ability to function in sulfur transfer.