SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q0I3G4

- THII_HISS1

UniProt

Q0I3G4 - THII_HISS1

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

tRNA sulfurtransferase

Gene
thiI, HS_0902
Organism
Histophilus somni (strain 129Pt) (Haemophilus somnus)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

L-cysteine + 'activated' tRNA = L-serine + tRNA containing a thionucleotide.UniRule annotation
[IscS]-SSH + [ThiS]-COAMP = [IscS]-SH + [ThiS]-COSH + AMP.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei265 – 2651ATP By similarity
Binding sitei287 – 2871ATP; via amide nitrogen By similarity
Binding sitei296 – 2961ATP By similarity
Active sitei456 – 4561Cysteine persulfide intermediate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi183 – 1842ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. sulfurtransferase activity Source: UniProtKB-HAMAP
  3. tRNA binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. thiamine biosynthetic process Source: UniProtKB-HAMAP
  2. thiamine diphosphate biosynthetic process Source: UniProtKB-UniPathway
  3. thiazole biosynthetic process Source: InterPro
  4. tRNA thio-modification Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Thiamine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciHSOM205914:GJ7V-935-MONOMER.
UniPathwayiUPA00060.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA sulfurtransferase (EC:2.8.1.4)
Alternative name(s):
Sulfur carrier protein ThiS sulfurtransferase
Thiamine biosynthesis protein ThiI
tRNA 4-thiouridine synthase
Gene namesi
Name:thiI
Ordered Locus Names:HS_0902
OrganismiHistophilus somni (strain 129Pt) (Haemophilus somnus)
Taxonomic identifieri205914 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus
ProteomesiUP000001970: Chromosome

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 484484tRNA sulfurtransferaseUniRule annotationPRO_1000074229Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi344 ↔ 456Redox-active By similarity

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi205914.HS_0902.

Structurei

3D structure databases

ProteinModelPortaliQ0I3G4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 165105THUMPAdd
BLAST
Domaini404 – 48481RhodaneseAdd
BLAST

Sequence similaritiesi

Belongs to the ThiI family.
Contains 1 rhodanese domain.
Contains 1 THUMP domain.

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG0301.
HOGENOMiHOG000227469.
KOiK03151.
OrthoDBiEOG6TBHGR.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.40.50.620. 1 hit.
HAMAPiMF_00021. ThiI.
InterProiIPR001763. Rhodanese-like_dom.
IPR014729. Rossmann-like_a/b/a_fold.
IPR026340. Thiazole_biosynth_dom.
IPR020536. ThiI_AANH.
IPR004114. THUMP.
IPR003720. tRNA_STrfase.
[Graphical view]
PfamiPF02568. ThiI. 1 hit.
PF02926. THUMP. 1 hit.
[Graphical view]
SMARTiSM00981. THUMP. 1 hit.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 1 hit.
TIGRFAMsiTIGR04271. ThiI_C_thiazole. 1 hit.
TIGR00342. TIGR00342. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
PS51165. THUMP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q0I3G4-1 [UniParc]FASTAAdd to Basket

« Hide

MKFIIKLFPE IMIKSESVRK RFVKILTGNI RNVLNKYDDT VAVVKHWDYI    50
EVRSKNIENR ILLVELLGRI PGIHHFLEVE EKPFVTLHDI FEQTLSDVAT 100
QIENKTFCVR VKRKGKHDFS SLDAERYIGG GLNQAVASAK VQLSKPDVTV 150
RIDIENDKMM LIKARHQGIG GYPIGTQEDV LSLISGGFDS GVSSYMLIRR 200
GSRVHYCFFN LGGATHEIGV KQMAYHIWKR FSGSHKVRFV AINFEQVVAE 250
ILEKVDNGQM GVVLKRMMVR AASKVAQRFG IQAIVTGEAL GQVSSQTLTN 300
LRLIDEAAES LVLRPLITHD KEQIIAKAKE IGTEDIAKSM PEFCGVISKS 350
PTVKAVKEKI EQEESYFDFS VLESAVQNAQ YLDIRQIAEQ TKKEVFEVDE 400
ITVLSANDVI LDIRSPEEVD DKPLEISGQN IILMPFYKLS SHFAELDQSK 450
NYVLYCERGV MSKLQALYLR EKGFDNVKVL NKIS 484
Length:484
Mass (Da):54,756
Last modified:October 3, 2006 - v1
Checksum:i8D24364396FA415B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000436 Genomic DNA. Translation: ABI25177.1.
RefSeqiYP_719112.1. NC_008309.1.

Genome annotation databases

EnsemblBacteriaiABI25177; ABI25177; HS_0902.
GeneIDi4240394.
KEGGihso:HS_0902.
PATRICi20281817. VBIHaeSom53361_0945.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000436 Genomic DNA. Translation: ABI25177.1 .
RefSeqi YP_719112.1. NC_008309.1.

3D structure databases

ProteinModelPortali Q0I3G4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 205914.HS_0902.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABI25177 ; ABI25177 ; HS_0902 .
GeneIDi 4240394.
KEGGi hso:HS_0902.
PATRICi 20281817. VBIHaeSom53361_0945.

Phylogenomic databases

eggNOGi COG0301.
HOGENOMi HOG000227469.
KOi K03151.
OrthoDBi EOG6TBHGR.

Enzyme and pathway databases

UniPathwayi UPA00060 .
BioCyci HSOM205914:GJ7V-935-MONOMER.

Family and domain databases

Gene3Di 3.40.250.10. 1 hit.
3.40.50.620. 1 hit.
HAMAPi MF_00021. ThiI.
InterProi IPR001763. Rhodanese-like_dom.
IPR014729. Rossmann-like_a/b/a_fold.
IPR026340. Thiazole_biosynth_dom.
IPR020536. ThiI_AANH.
IPR004114. THUMP.
IPR003720. tRNA_STrfase.
[Graphical view ]
Pfami PF02568. ThiI. 1 hit.
PF02926. THUMP. 1 hit.
[Graphical view ]
SMARTi SM00981. THUMP. 1 hit.
[Graphical view ]
SUPFAMi SSF52821. SSF52821. 1 hit.
TIGRFAMsi TIGR04271. ThiI_C_thiazole. 1 hit.
TIGR00342. TIGR00342. 1 hit.
PROSITEi PS50206. RHODANESE_3. 1 hit.
PS51165. THUMP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd."
    Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J.
    J. Bacteriol. 189:1890-1898(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 129Pt.

Entry informationi

Entry nameiTHII_HISS1
AccessioniPrimary (citable) accession number: Q0I3G4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 3, 2006
Last modified: July 9, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi