Skip Header

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

tRNA sulfurtransferase

Gene

thiI

Organism
Yersinia pestis bv. Antiqua (strain Angola)
Status
Reviewed-Annotation score: 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.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 sitei266 – 2661ATPUniRule annotation
Binding sitei288 – 2881ATP; via amide nitrogenUniRule annotation
Binding sitei297 – 2971ATPUniRule annotation
Active sitei457 – 4571Cysteine persulfide intermediateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi184 – 1852ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. sulfurtransferase activity Source: UniProtKB-HAMAP
  3. tRNA adenylyltransferase activity Source: InterPro
  4. 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

BioCyciYPES349746:GHPB-3077-MONOMER.
UniPathwayiUPA00060.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA sulfurtransferaseUniRule annotation (EC:2.8.1.4UniRule annotation)
Alternative name(s):
Sulfur carrier protein ThiS sulfurtransferaseUniRule annotation
Thiamine biosynthesis protein ThiIUniRule annotation
tRNA 4-thiouridine synthaseUniRule annotation
Gene namesi
Name:thiIUniRule annotation
Ordered Locus Names:YpAngola_A3070
OrganismiYersinia pestis bv. Antiqua (strain Angola)
Taxonomic identifieri349746 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
ProteomesiUP000001204: Chromosome

Subcellular locationi

Cytoplasm 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 – 483483tRNA sulfurtransferasePRO_1000090047Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi345 ↔ 457Redox-activeUniRule annotation

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi349746.YpAngola_A3070.

Structurei

3D structure databases

ProteinModelPortaliA9QZR9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini62 – 166105THUMPUniRule annotationAdd
BLAST
Domaini405 – 48379RhodaneseUniRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG0301.
HOGENOMiHOG000227469.
KOiK03151.
OMAiKRMFMRA.
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.

A9QZR9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFIIKLFPE ITIKSQSVRL RFIKILTTNI RNVLKHLEDD TLAIVRHWDH
60 70 80 90 100
IELRTKDDNL GPEICDALTR IPGIHHILEV EDRSYSDMHN IFEQTLEAYR
110 120 130 140 150
ETLVGKTFCV RVKRRGKHEF SSGDVERYVG GGLNQHIESA KVNLTRPQVT
160 170 180 190 200
VNLEVDQDKL ILVKARHEGL GGFPIGTQED VLSLISGGFD SGVSSYMLMR
210 220 230 240 250
RGCRVHYCFF NLGGSAHEIG VKQVAHYLWN RFGSSHRVRF IAIDFEPVVG
260 270 280 290 300
EILEKVEDGQ MGVVLKRMMV RAASQVAERY GVQALVTGEA LGQVSSQTLT
310 320 330 340 350
NLRLIDNASD TLILRPLISH DKEHIINLAR QIGTEDFAKT MPEYCGVISK
360 370 380 390 400
SPTVKAVKAK IEEEESHFDF SILDRVVSEA KNVDIREIAQ QSREQVVEVE
410 420 430 440 450
TVAELADTDV LLDIRAPDEQ EEKPLKLDQV EVRSLPFYKL SSQFADLDQS
460 470 480
KTYLLYCDRG VMSRLQALYL REQGYTNVKV YRP
Length:483
Mass (Da):54,894
Last modified:February 5, 2008 - v1
Checksum:iB773AAF42D9895BD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000901 Genomic DNA. Translation: ABX88049.1.
RefSeqiYP_001607436.1. NC_010159.1.

Genome annotation databases

EnsemblBacteriaiABX88049; ABX88049; YpAngola_A3070.
GeneIDi5801543.
KEGGiypg:YpAngola_A3070.
PATRICi18575696. VBIYerPes97331_3611.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000901 Genomic DNA. Translation: ABX88049.1.
RefSeqiYP_001607436.1. NC_010159.1.

3D structure databases

ProteinModelPortaliA9QZR9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi349746.YpAngola_A3070.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABX88049; ABX88049; YpAngola_A3070.
GeneIDi5801543.
KEGGiypg:YpAngola_A3070.
PATRICi18575696. VBIYerPes97331_3611.

Phylogenomic databases

eggNOGiCOG0301.
HOGENOMiHOG000227469.
KOiK03151.
OMAiKRMFMRA.
OrthoDBiEOG6TBHGR.

Enzyme and pathway databases

UniPathwayiUPA00060.
BioCyciYPES349746:GHPB-3077-MONOMER.

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]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals new insights into the evolution and pangenome of the plague bacterium."
    Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S., Achtman M., Lindler L.E., Ravel J.
    J. Bacteriol. 192:1685-1699(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Angola.

Entry informationi

Entry nameiTHII_YERPG
AccessioniPrimary (citable) accession number: A9QZR9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 5, 2008
Last modified: January 7, 2015
This is version 56 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.