UniProtKB - A1AUS1 (TTCA_PELPD)
Protein
tRNA-cytidine(32) 2-sulfurtransferase
Gene
ttcA
Organism
Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1)
Status
Functioni
Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s2C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system.UniRule annotation
Miscellaneous
The thiolation reaction likely consists of two steps: a first activation step by ATP to form an adenylated intermediate of the target base of tRNA, and a second nucleophilic substitution step of the sulfur (S) atom supplied by the hydrosulfide attached to the Fe-S cluster.UniRule annotation
Cofactori
Protein has several cofactor binding sites:- Mg2+UniRule annotation
- [4Fe-4S] clusterUniRule annotationNote: Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by three Cys residues, the fourth Fe has a free coordination site that may bind a sulfur atom transferred from the persulfide of IscS.UniRule annotation
: tRNA modification Pathwayi
This protein is involved in tRNA modification.UniRule annotationView all proteins of this organism that are known to be involved in tRNA modification.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 128 | Iron-sulfur (4Fe-4S)UniRule annotation | 1 | |
Metal bindingi | 131 | Iron-sulfur (4Fe-4S)UniRule annotation | 1 | |
Metal bindingi | 218 | Iron-sulfur (4Fe-4S)UniRule annotation | 1 |
GO - Molecular functioni
- 4 iron, 4 sulfur cluster binding Source: UniProtKB-UniRule
- ATP binding Source: UniProtKB-UniRule
- magnesium ion binding Source: UniProtKB-UniRule
- sulfurtransferase activity Source: UniProtKB-UniRule
- tRNA binding Source: UniProtKB-KW
GO - Biological processi
- tRNA thio-modification Source: UniProtKB-UniRule
Keywordsi
Molecular function | RNA-binding, Transferase, tRNA-binding |
Biological process | tRNA processing |
Ligand | 4Fe-4S, ATP-binding, Iron, Iron-sulfur, Magnesium, Metal-binding, Nucleotide-binding |
Names & Taxonomyi
Protein namesi | Recommended name: tRNA-cytidine(32) 2-sulfurtransferaseUniRule annotation (EC:2.8.1.-UniRule annotation)Alternative name(s): Two-thiocytidine biosynthesis protein AUniRule annotation tRNA 2-thiocytidine biosynthesis protein TtcAUniRule annotation |
Gene namesi | Name:ttcAUniRule annotation Ordered Locus Names:Ppro_3499 |
Organismi | Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1) |
Taxonomic identifieri | 338966 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Deltaproteobacteria › Desulfuromonadales › Desulfuromonadaceae › Pelobacter › |
Proteomesi |
|
Subcellular locationi
- Cytoplasm UniRule annotation
GO - Cellular componenti
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000348783 | 1 – 269 | tRNA-cytidine(32) 2-sulfurtransferaseAdd BLAST | 269 |
Proteomic databases
PRIDEi | A1AUS1 |
Interactioni
Subunit structurei
Homodimer.
UniRule annotationProtein-protein interaction databases
STRINGi | 338966.Ppro_3499 |
Family & Domainsi
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 53 – 58 | PP-loop motifUniRule annotation | 6 |
Sequence similaritiesi
Belongs to the TtcA family.UniRule annotation
Phylogenomic databases
eggNOGi | ENOG4105CB3 Bacteria COG0037 LUCA |
HOGENOMi | HOG000013322 |
KOi | K14058 |
OMAi | PCKACVL |
Family and domain databases
Gene3Di | 3.40.50.620, 1 hit |
HAMAPi | MF_01850 TtcA, 1 hit |
InterProi | View protein in InterPro IPR014729 Rossmann-like_a/b/a_fold IPR011063 TilS/TtcA_N IPR012089 tRNA_Cyd_32_2_STrfase IPR035107 tRNA_thiolation_TtcA_Ctu1 |
Pfami | View protein in Pfam PF01171 ATP_bind_3, 1 hit |
PIRSFi | PIRSF004976 ATPase_YdaO, 1 hit |
i Sequence
Sequence statusi: Complete.
A1AUS1-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MLRTPKAASD PMTLTQQEMR ELPLFRRLRH AVGKAVADFA MIREGDRIAV
60 70 80 90 100
GVSGGKDSYT LLLLLEELRR RAPIDFQLVA VIIDSGYPGY RGDIVRDYVT
110 120 130 140 150
SLGIPCHLET TTHYEIITEK RRPGSSYCSI CARLKRGALY GLADSLGCNK
160 170 180 190 200
LALGHHGDDF IETLLLNQFF VGSLKAMSAN MLADNGRTTV IRPLVYASEE
210 220 230 240 250
EIVDFMGQVG LPVVSCNCPV SDSTDLKRRR MKELLKELEQ EIPHIRSSML
260
KALSNVHPRH LLDQQLQGL
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP000482 Genomic DNA Translation: ABL01092.1 |
Genome annotation databases
EnsemblBacteriai | ABL01092; ABL01092; Ppro_3499 |
KEGGi | ppd:Ppro_3499 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP000482 Genomic DNA Translation: ABL01092.1 |
3D structure databases
SMRi | A1AUS1 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 338966.Ppro_3499 |
Proteomic databases
PRIDEi | A1AUS1 |
Genome annotation databases
EnsemblBacteriai | ABL01092; ABL01092; Ppro_3499 |
KEGGi | ppd:Ppro_3499 |
Phylogenomic databases
eggNOGi | ENOG4105CB3 Bacteria COG0037 LUCA |
HOGENOMi | HOG000013322 |
KOi | K14058 |
OMAi | PCKACVL |
Family and domain databases
Gene3Di | 3.40.50.620, 1 hit |
HAMAPi | MF_01850 TtcA, 1 hit |
InterProi | View protein in InterPro IPR014729 Rossmann-like_a/b/a_fold IPR011063 TilS/TtcA_N IPR012089 tRNA_Cyd_32_2_STrfase IPR035107 tRNA_thiolation_TtcA_Ctu1 |
Pfami | View protein in Pfam PF01171 ATP_bind_3, 1 hit |
PIRSFi | PIRSF004976 ATPase_YdaO, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | TTCA_PELPD | |
Accessioni | A1AUS1Primary (citable) accession number: A1AUS1 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | September 2, 2008 |
Last sequence update: | January 23, 2007 | |
Last modified: | May 8, 2019 | |
This is version 63 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Complete proteome, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families - PATHWAY comments
Index of metabolic and biosynthesis pathways