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D3UNH6 (D3UNH6_LISSS) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Probable tRNA sulfurtransferase HAMAP-Rule MF_00021

EC=2.8.1.4 HAMAP-Rule MF_00021
Alternative name(s):
Sulfur carrier protein ThiS sulfurtransferase HAMAP-Rule MF_00021
Thiamine biosynthesis protein ThiI HAMAP-Rule MF_00021
tRNA 4-thiouridine synthase HAMAP-Rule MF_00021
Gene names
Name:thiI HAMAP-Rule MF_00021 EMBL CBH27659.1
Ordered Locus Names:lse_1508 EMBL CBH27659.1
OrganismListeria seeligeri serovar 1/2b (strain ATCC 35967 / DSM 20751 / CIP 100100 / SLCC 3954) [Complete proteome] [HAMAP] EMBL CBH27659.1
Taxonomic identifier683837 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

Protein attributes

Sequence length403 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS By similarity. HAMAP-Rule MF_00021 SAAS SAAS003720

Catalytic activity

L-cysteine + 'activated' tRNA = L-serine + tRNA containing a thionucleotide. HAMAP-Rule MF_00021 SAAS SAAS003720

[IscS]-SSH + [ThiS]-COAMP = [IscS]-SH + [ThiS]-COSH + AMP. HAMAP-Rule MF_00021 SAAS SAAS003720

Pathway

Cofactor biosynthesis; thiamine diphosphate biosynthesis. HAMAP-Rule MF_00021 SAAS SAAS003720

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00021 SAAS SAAS003720.

Sequence similarities

Belongs to the ThiI family. HAMAP-Rule MF_00021

Contains 1 THUMP domain. HAMAP-Rule MF_00021

Contains THUMP domain. SAAS SAAS003720

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain60 – 165106THUMP By similarity HAMAP-Rule MF_00021
Nucleotide binding183 – 1842ATP By similarity HAMAP-Rule MF_00021
Nucleotide binding208 – 2092ATP By similarity HAMAP-Rule MF_00021

Sites

Binding site2651ATP By similarity HAMAP-Rule MF_00021
Binding site2871ATP; via amide nitrogen By similarity HAMAP-Rule MF_00021
Binding site2961ATP By similarity HAMAP-Rule MF_00021

Sequences

Sequence LengthMass (Da)Tools
D3UNH6 [UniParc].

Last modified April 20, 2010. Version 1.
Checksum: D1D9BCF7E2F1738F

FASTA40345,068
        10         20         30         40         50         60 
MEFDRMLIRY GELSTKGKNR KQFVTKLAQN VKRAMQDLPE VRIHGERDRM YIILNGADYH 

        70         80         90        100        110        120 
LAEERLKPIF GIQSFSPAVR VDLDLDEVKN AALALVQDAH EENGTFKVAA RRSHREFPLD 

       130        140        150        160        170        180 
SNEINQEIGA HVLQNIADLT VNVKNPDVKL TIDVRKEGVF LSCRTILGAA GLPVGSSGRA 

       190        200        210        220        230        240 
MLMLSGGIDS PVAGYLAQKR GVEIEAVHFH SPPYTSEQAK QKAIDLAAKL AKYSGQVQMH 

       250        260        270        280        290        300 
IVPFTEIQEV IKQQIPESVI MTVTRRMMLR ITDELRRKRN GLAIVNGESL GQVASQTLES 

       310        320        330        340        350        360 
MLAINAVTAT PIIRPVVSMD KNEIITIAQK IDTYNLSVQP FEDCCTIFTP PSPKTKPKLD 

       370        380        390        400 
KIEHYESFTD FEALIKKAID NIETISVNIA ETEQVKDEFA DLF 

« Hide

References

[1]"Complete genome sequence of Listeria seeligeri, a nonpathogenic member of the genus Listeria."
Steinweg C., Kuenne C.T., Billion A., Mraheil M.A., Domann E., Ghai R., Barbuddhe S.B., Karst U., Goesmann A., Puhler A., Weisshaar B., Wehland J., Lampidis R., Kreft J., Goebel W., Chakraborty T., Hain T.
J. Bacteriol. 192:1473-1474(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35967 / DSM 20751 / CIP 100100 / SLCC 3954.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FN557490 Genomic DNA. Translation: CBH27659.1.
RefSeqYP_003464745.1. NC_013891.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCBH27659; CBH27659; lse_1508.
GeneID9082934.
KEGGlsg:lse_1508.
PATRIC32262913. VBILisSee138575_1503.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000227470.
KOK03151.

Enzyme and pathway databases

BioCycLSEE683837:GI10-1531-MONOMER.
UniPathwayUPA00060.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_00021. ThiI.
InterProIPR014729. Rossmann-like_a/b/a_fold.
IPR020536. ThiI_C_dom.
IPR004114. THUMP.
IPR003720. tRNA_STrfase.
[Graphical view]
PfamPF02568. ThiI. 1 hit.
PF02926. THUMP. 1 hit.
[Graphical view]
SMARTSM00981. THUMP. 1 hit.
[Graphical view]
TIGRFAMsTIGR00342. TIGR00342. 1 hit.
PROSITEPS51165. THUMP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameD3UNH6_LISSS
AccessionPrimary (citable) accession number: D3UNH6
Entry history
Integrated into UniProtKB/TrEMBL: April 20, 2010
Last sequence update: April 20, 2010
Last modified: February 19, 2014
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)