Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q931P5 (THII_STAAM) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable tRNA sulfurtransferase

EC=2.8.1.4
Alternative name(s):
Sulfur carrier protein ThiS sulfurtransferase
Thiamine biosynthesis protein ThiI
tRNA 4-thiouridine synthase
Gene names
Name:thiI
Ordered Locus Names:SAV1715
OrganismStaphylococcus aureus (strain Mu50 / ATCC 700699) [Complete proteome] [HAMAP]
Taxonomic identifier158878 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length407 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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

Catalytic activity

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

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

Pathway

Cofactor biosynthesis; thiamine diphosphate biosynthesis. HAMAP-Rule MF_00021

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00021.

Sequence similarities

Belongs to the ThiI family.

Contains 1 THUMP domain.

Ontologies

Keywords
   Biological processThiamine biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
RNA-binding
tRNA-binding
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processtRNA thio-modification

Inferred from electronic annotation. Source: UniProtKB-HAMAP

thiamine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

thiamine diphosphate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

sulfurtransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 407407Probable tRNA sulfurtransferase HAMAP-Rule MF_00021
PRO_0000154864

Regions

Domain61 – 165105THUMP
Nucleotide binding183 – 1842ATP By similarity
Nucleotide binding208 – 2092ATP By similarity

Sites

Binding site2651ATP By similarity
Binding site2871ATP; via amide nitrogen By similarity
Binding site2961ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q931P5 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 2BD404728AA854B7

FASTA40746,228
        10         20         30         40         50         60 
MKYDHLLVRY GELTLKGSNR KKFVNQLRNN VNKSLKGLDG FVVKGKRDRM YIELEDHADI 

        70         80         90        100        110        120 
NEITYRLSKI FGIKSISPVL KVEKTIEAMS AAAIKFAQQF EENSTFKIDV KRADKNFPMD 

       130        140        150        160        170        180 
TYELQRELGG TVLKQIENVS VNVKRPDHEI RVEVRLDAIY MYEEVVPGSG GLPVGTGGKT 

       190        200        210        220        230        240 
LLMLSGGIDS PVAGMEVMRR GVTIEAIHFH SPPFTSDQAK EKVIELTRIL AERVGPIKLH 

       250        260        270        280        290        300 
IVPFTELQKQ VNKVVHPRYT MTSTRRMMMR VADKLVHQIG ALAIVNGENL GQVASQTLHS 

       310        320        330        340        350        360 
MYAINNVTST PVLRPLLTYD KEEIIIKSKE IGTFETSIQP FEDCCTIFTP KNPVTEPNFE 

       370        380        390        400 
KVVQYESVFD FEEMINRAVE NIETLEITSD YKTIKEQQTN QLINDFL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000017 Genomic DNA. Translation: BAB57877.1.
RefSeqNP_372239.1. NC_002758.2.

3D structure databases

ProteinModelPortalQ931P5.
SMRQ931P5. Positions 3-385.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING158878.SAV1715.

2D gel databases

World-2DPAGE0002:Q931P5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB57877; BAB57877; SAV1715.
GeneID1121690.
KEGGsav:SAV1715.
PATRIC19564182. VBIStaAur52173_1769.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0301.
KOK03151.
OMAAQMKGPD.
OrthoDBEOG6TBHGR.
PhylomeDBQ931P5.

Enzyme and pathway databases

BioCycSAUR158878:GJJ5-1731-MONOMER.
UniPathwayUPA00060.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_00021. ThiI.
InterProIPR014729. Rossmann-like_a/b/a_fold.
IPR020536. ThiI_AANH.
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 nameTHII_STAAM
AccessionPrimary (citable) accession number: Q931P5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways