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Protein

Tyrosine--tRNA ligase

Gene

tyrS

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).UniRule annotation

Catalytic activityi

ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr).UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei37 – 371TyrosineUniRule annotation1 Publication
Binding sitei168 – 1681TyrosineUniRule annotation1 Publication
Binding sitei172 – 1721TyrosineUniRule annotation1 Publication
Binding sitei175 – 1751TyrosineUniRule annotation1 Publication
Binding sitei190 – 1901TyrosineUniRule annotation1 Publication
Binding sitei254 – 2541ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-1003-MONOMER.
BRENDAi6.1.1.1. 5244.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine--tRNA ligaseUniRule annotation (EC:6.1.1.1UniRule annotation)
Alternative name(s):
Tyrosyl-tRNA synthetaseUniRule annotation
Short name:
TyrRSUniRule annotation
Gene namesi
Name:tyrSUniRule annotation
Ordered Locus Names:PH1011
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000752 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 375375Tyrosine--tRNA ligasePRO_0000240269Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi70601.PH1011.

Structurei

Secondary structure

1
375
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 119Combined sources
Beta strandi15 – 195Combined sources
Helixi21 – 3010Combined sources
Beta strandi35 – 406Combined sources
Helixi48 – 6316Combined sources
Beta strandi69 – 724Combined sources
Helixi74 – 796Combined sources
Helixi82 – 854Combined sources
Helixi87 – 9610Combined sources
Helixi98 – 10811Combined sources
Helixi113 – 1153Combined sources
Beta strandi116 – 1205Combined sources
Helixi122 – 1254Combined sources
Helixi128 – 13811Combined sources
Helixi143 – 1486Combined sources
Helixi149 – 1535Combined sources
Helixi164 – 17815Combined sources
Beta strandi182 – 1876Combined sources
Helixi188 – 1903Combined sources
Helixi191 – 20010Combined sources
Helixi201 – 2033Combined sources
Beta strandi205 – 2073Combined sources
Beta strandi209 – 2113Combined sources
Beta strandi214 – 2163Combined sources
Beta strandi219 – 2235Combined sources
Beta strandi233 – 2364Combined sources
Helixi240 – 25011Combined sources
Helixi252 – 2543Combined sources
Helixi257 – 2593Combined sources
Helixi267 – 27610Combined sources
Helixi288 – 2958Combined sources
Turni296 – 2983Combined sources
Beta strandi299 – 3024Combined sources
Beta strandi305 – 3073Combined sources
Helixi311 – 3133Combined sources
Beta strandi317 – 3215Combined sources
Helixi322 – 3309Combined sources
Helixi336 – 35015Combined sources
Helixi352 – 3609Combined sources
Helixi363 – 3708Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CYCX-ray2.20A/B1-375[»]
ProteinModelPortaliO58739.
SMRiO58739. Positions 1-371.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO58739.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi251 – 2555"KMSKS" region

Sequence similaritiesi

Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 4 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiarCOG01886. Archaea.
COG0162. LUCA.
HOGENOMiHOG000228238.
KOiK01866.
OMAiHVIAIEV.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_02009. Tyr_tRNA_synth_type4.
InterProiIPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR023678. Tyr-tRNA-ligase_4.
IPR023617. Tyr-tRNA-ligase_arc/euk-type.
[Graphical view]
PfamiPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PIRSFiPIRSF006588. TyrRS_arch_euk. 1 hit.

Sequencei

Sequence statusi: Complete.

O58739-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDIEERINLV LKKPTEEVLT VENLRHLFEI GAPLQHYIGF EISGYIHLGT
60 70 80 90 100
GLMAGAKIAD FQKAGIKTRV FLADWHSWIN DKLGGDLEVI QEVALKYFKV
110 120 130 140 150
GMEKSIEVMG GDPKKVEFVL ASEILEKGDY WQTVIDISKN VTLSRVMRSI
160 170 180 190 200
TIMGRQMGEA IDFAKLIYPM MQVADIFYQG VTIAHAGMDQ RKAHVIAIEV
210 220 230 240 250
AQKLRYHPIV HEGEKLKPVA VHHHLLLGLQ EPPKWPIESE EEFKEIKAQM
260 270 280 290 300
KMSKSKPYSA VFIHDSPEEI RQKLRKAFCP AREVRYNPVL DWVEYIIFRE
310 320 330 340 350
EPTEFTVHRP AKFGGDVTYT TFEELKRDFA EGKLHPLDLK NAVAEYLINL
360 370
LEPIRRYFEK HPEPLELMRS VKITR
Length:375
Mass (Da):43,276
Last modified:August 1, 1998 - v1
Checksum:i8A4BC945037A9F1B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA30108.1.
PIRiF71093.
RefSeqiWP_010885097.1. NC_000961.1.

Genome annotation databases

EnsemblBacteriaiBAA30108; BAA30108; BAA30108.
GeneIDi1443332.
KEGGipho:PH1011.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA30108.1.
PIRiF71093.
RefSeqiWP_010885097.1. NC_000961.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CYCX-ray2.20A/B1-375[»]
ProteinModelPortaliO58739.
SMRiO58739. Positions 1-371.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi70601.PH1011.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA30108; BAA30108; BAA30108.
GeneIDi1443332.
KEGGipho:PH1011.

Phylogenomic databases

eggNOGiarCOG01886. Archaea.
COG0162. LUCA.
HOGENOMiHOG000228238.
KOiK01866.
OMAiHVIAIEV.

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-1003-MONOMER.
BRENDAi6.1.1.1. 5244.

Miscellaneous databases

EvolutionaryTraceiO58739.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_02009. Tyr_tRNA_synth_type4.
InterProiIPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR023678. Tyr-tRNA-ligase_4.
IPR023617. Tyr-tRNA-ligase_arc/euk-type.
[Graphical view]
PfamiPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PIRSFiPIRSF006588. TyrRS_arch_euk. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH TYROSINE, SUBUNIT.

Entry informationi

Entry nameiSYY_PYRHO
AccessioniPrimary (citable) accession number: O58739
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: August 1, 1998
Last modified: November 11, 2015
This is version 97 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

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.