PPGR - Gene Detail

Basic Information

Gene ID	Lchi04922.g View in Genome Browser
Position	Scaffold530:2480400-2494927 (+) 14527bp
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	Liriodendron chinense
Also AS	AT3G61113

upstream:

Domain

Database	EntryID	E-Value	Start	end	InterPro ID	Description

Regulation&Interaction

Protein-protein interaction (PPI)

Lchi07131.g 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

Lchi08800.g elongator complex protein

Lchi21668.g Catalytic histone acetyltransferase subunit of the RNA polymerase II elongator complex, which is a component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation

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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)

Select Expression

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.