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Protein

tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS

Gene

tiaS

Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ATP-dependent agmatine transferase that catalyzes the formation of 2-agmatinylcytidine (agm2C) at the wobble position (C34) of tRNA(Ile2), converting the codon specificity from AUG to AUA.1 Publication

Catalytic activityi

ATP + agmatine + (tRNA(Ile)2)-cytidine(34) + H2O = (tRNA(Ile)2)-2-agmatinylcytidine(34) + AMP + 2 phosphate.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi268 – 329OBAdd BLAST62

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ligase activity, forming carbon-nitrogen bonds Source: UniProtKB
  • nucleic acid binding Source: InterPro

GO - Biological processi

  • tRNA wobble cytosine modification Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.3.4.22. 414.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS (EC:6.3.4.22)
Short name:
tRNA(Ile2)-agm2C synthetase
Alternative name(s):
tRNA(Ile2) agmatidine synthetase
Gene namesi
Name:tiaS
Ordered Locus Names:AF_2259
OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifieri224325 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
Proteomesi
  • UP000002199 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi140R → A: Loss of activity. 1 Publication1
Mutagenesisi141G → A: Loss of activity. 1 Publication1
Mutagenesisi163Y → A: Decrease in activity. 1 Publication1
Mutagenesisi164R → A: Decrease in activity. 1 Publication1
Mutagenesisi217R → A: Decrease in activity. 1 Publication1
Mutagenesisi218G → A: Decrease in activity. 1 Publication1
Mutagenesisi248T → A: Decrease in activity. 1 Publication1
Mutagenesisi249D → A: Decrease in activity. 1 Publication1
Mutagenesisi352C → A: Almost loss of activity. 1 Publication1
Mutagenesisi355C → A: Almost loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004072881 – 420tRNA(Ile2) 2-agmatinylcytidine synthetase TiaSAdd BLAST420

Interactioni

Protein-protein interaction databases

STRINGi224325.AF2259.

Structurei

Secondary structure

1420
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1 – 7Combined sources7
Beta strandi13 – 15Combined sources3
Helixi20 – 32Combined sources13
Beta strandi35 – 44Combined sources10
Beta strandi53 – 55Combined sources3
Beta strandi57 – 66Combined sources10
Helixi68 – 78Combined sources11
Beta strandi87 – 89Combined sources3
Beta strandi94 – 98Combined sources5
Helixi99 – 102Combined sources4
Turni103 – 105Combined sources3
Helixi106 – 114Combined sources9
Helixi119 – 128Combined sources10
Beta strandi133 – 135Combined sources3
Helixi141 – 150Combined sources10
Beta strandi157 – 163Combined sources7
Helixi166 – 168Combined sources3
Beta strandi169 – 171Combined sources3
Helixi177 – 187Combined sources11
Beta strandi190 – 196Combined sources7
Turni197 – 200Combined sources4
Beta strandi203 – 205Combined sources3
Beta strandi208 – 219Combined sources12
Helixi221 – 230Combined sources10
Beta strandi239 – 244Combined sources6
Beta strandi252 – 254Combined sources3
Helixi255 – 257Combined sources3
Beta strandi266 – 280Combined sources15
Turni281 – 283Combined sources3
Beta strandi284 – 291Combined sources8
Beta strandi294 – 300Combined sources7
Helixi302 – 306Combined sources5
Helixi307 – 311Combined sources5
Beta strandi319 – 327Combined sources9
Beta strandi330 – 340Combined sources11
Beta strandi344 – 346Combined sources3
Turni353 – 355Combined sources3
Beta strandi359 – 361Combined sources3
Beta strandi363 – 365Combined sources3
Beta strandi368 – 370Combined sources3
Turni371 – 374Combined sources4
Beta strandi375 – 377Combined sources3
Beta strandi383 – 385Combined sources3
Beta strandi391 – 395Combined sources5
Helixi398 – 400Combined sources3
Beta strandi403 – 405Combined sources3
Helixi408 – 410Combined sources3
Beta strandi414 – 416Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AMTX-ray2.90A1-420[»]
3AMUX-ray3.10A1-420[»]
3AU7X-ray2.60A1-343[»]
A386-420[»]
4RVZX-ray2.90Z1-420[»]
SMRiO28025.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO28025.

Family & Domainsi

Sequence similaritiesi

Belongs to the TiaS family.Curated
Contains 1 OB DNA-binding domain.Curated

Phylogenomic databases

eggNOGiarCOG01115. Archaea.
COG1571. LUCA.
KOiK06932.
OMAiGMCTTYL.

Family and domain databases

HAMAPiMF_01892. tRNA_Ile2_agm2C_synt. 1 hit.
InterProiIPR013696. DUF1743.
IPR004365. NA-bd_OB_tRNA.
IPR024913. tRNA_Ile2__agm2C_synt.
[Graphical view]
PfamiPF08489. DUF1743. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O28025-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVWVGIDDT DSSRGMCTTY LAVLAMERVE RELGKVIGFP RLIRLNPTIP
60 70 80 90 100
YKTRGNGAVS FLVEVDDVGE LVDVVNEVII EHAMLDDEKT NPGAVFVDEE
110 120 130 140 150
LAVKLKPFAD KAIKDVLQID EALFVIGKYF IPHLRHKKGR GLIGALAAVG
160 170 180 190 200
AELEDFTLEL IAYRYPERFG TEREYDEESF FDMDYELYPQ TFDNVDWCND
210 220 230 240 250
VVVCIPNTPC PVLYGIRGES VEALYKAMES VKTEPVDRRM IFVTNHATDM
260 270 280 290 300
HLIGEEEVHR LENYRSYRLR GRVTLEPYDI EGGHVFFEID TKFGSVKCAA
310 320 330 340 350
FEPTKQFRNV IRLLRKGDVV EVYGSMKKDT INLEKIQIVE LAEIWVEKNP
360 370 380 390 400
ICPSCGRRME SAGRGQGFRC KKCRTKADEK LREKVERELQ PGFYEVPPSA
410 420
RRHLSKPLIR MNVEGRHIFR
Length:420
Mass (Da):48,222
Last modified:January 1, 1998 - v1
Checksum:i846D3F445EEC4885
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB88990.1.
PIRiC69532.
RefSeqiWP_010879748.1. NC_000917.1.

Genome annotation databases

EnsemblBacteriaiAAB88990; AAB88990; AF_2259.
GeneIDi24796023.
KEGGiafu:AF_2259.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB88990.1.
PIRiC69532.
RefSeqiWP_010879748.1. NC_000917.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AMTX-ray2.90A1-420[»]
3AMUX-ray3.10A1-420[»]
3AU7X-ray2.60A1-343[»]
A386-420[»]
4RVZX-ray2.90Z1-420[»]
SMRiO28025.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224325.AF2259.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB88990; AAB88990; AF_2259.
GeneIDi24796023.
KEGGiafu:AF_2259.

Phylogenomic databases

eggNOGiarCOG01115. Archaea.
COG1571. LUCA.
KOiK06932.
OMAiGMCTTYL.

Enzyme and pathway databases

BRENDAi6.3.4.22. 414.

Miscellaneous databases

EvolutionaryTraceiO28025.

Family and domain databases

HAMAPiMF_01892. tRNA_Ile2_agm2C_synt. 1 hit.
InterProiIPR013696. DUF1743.
IPR004365. NA-bd_OB_tRNA.
IPR024913. tRNA_Ile2__agm2C_synt.
[Graphical view]
PfamiPF08489. DUF1743. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTIAS_ARCFU
AccessioniPrimary (citable) accession number: O28025
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 90 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.