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

Q2RM06 (THII_MOOTA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. 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:Moth_0198
OrganismMoorella thermoacetica (strain ATCC 39073) [Reference proteome] [HAMAP]
Taxonomic identifier264732 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeMoorella groupMoorella

Protein attributes

Sequence length390 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

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
Reference 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 – 390390Probable tRNA sulfurtransferase HAMAP-Rule MF_00021
PRO_1000074245

Regions

Domain58 – 161104THUMP
Nucleotide binding179 – 1802ATP By similarity
Nucleotide binding204 – 2052ATP By similarity

Sites

Binding site2611ATP By similarity
Binding site2831ATP; via amide nitrogen By similarity
Binding site2921ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2RM06 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 035FB245B58B5538

FASTA39043,237
        10         20         30         40         50         60 
MYTSLLVRYG EISLKGNNRP YFEDKLLANM RRALAGLPPR RMRKTFGRVF VELHDDLEAV 

        70         80         90        100        110        120 
ARRLQRVFGI VSMSPVATAP LELEAIKKAA LAVLKDSPGS TFKVQAQRPN KRFPLTSPEV 

       130        140        150        160        170        180 
NQELGAYLLT HSQGQRVDVH HPDRVIHVEI RDEGAYIYSR IIPGPGGLPV GVTGRGLLLI 

       190        200        210        220        230        240 
SGGIDSPVAG YMGMKRGLEL TALHFHSFPF TSERSKEKVI DLCRVLAGYS GPLRLVVAPF 

       250        260        270        280        290        300 
TNIQKAIRQN CPQEFYVTIM RRMMFRIARA VAAKEEAPAI LTGESLGQVA SQTLQSMAVI 

       310        320        330        340        350        360 
NKVVDLPVLR PLVAWDKSEI IEVARRIGTY DISIRPYEDC CTLFVPKHPA TKPPLARVEA 

       370        380        390 
AEKNLAVVEL VAECLENLEI LTVEPEADVV 

« Hide

References

[1]"The complete genome sequence of Moorella thermoacetica (f. Clostridium thermoaceticum)."
Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C., Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.
Environ. Microbiol. 10:2550-2573(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39073.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000232 Genomic DNA. Translation: ABC18533.1.
RefSeqYP_429076.1. NC_007644.1.

3D structure databases

ProteinModelPortalQ2RM06.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264732.Moth_0198.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC18533; ABC18533; Moth_0198.
GeneID3832271.
KEGGmta:Moth_0198.
PATRIC22637419. VBIMooThe6753_0210.

Phylogenomic databases

eggNOGCOG0301.
HOGENOMHOG000227470.
KOK03151.
OMAAQKIDTF.
OrthoDBEOG6TBHGR.
ProtClustDBPRK01565.

Enzyme and pathway databases

BioCycMTHE264732:GH0A-215-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 nameTHII_MOOTA
AccessionPrimary (citable) accession number: Q2RM06
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: January 24, 2006
Last modified: February 19, 2014
This is version 61 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