Q5UPJ7 (SYY_MIMIV) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine--tRNA ligase
EC=6.1.1.1

Alternative name(s):
Tyrosyl-tRNA synthetase
Short name=TyrRS

Gene names

Name:	YARS
Ordered Locus Names:	MIMI_L124

Organism

Acanthamoeba polyphaga mimivirus (APMV) [Reference proteome]

Taxonomic identifier

212035 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Mimiviridae › Mimivirus

Virus host

Acanthamoeba polyphaga (Amoeba) [TaxID: 5757]

Protein attributes

Sequence length	346 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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) By similarity. Ref.1 Ref.2
Catalytic activity	ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr). Ref.3
Subunit structure	Homodimer. Ref.3
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.
Biophysicochemical properties	Kinetic parameters: KM=0.5 µM for tRNA-Tyr Ref.3

Ontologies

Keywords
Biological process	Protein biosynthesis
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	tRNA aminoacylation for protein translation Inferred from electronic annotation. Source: InterPro
Cellular_component	host cell cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW tyrosine-tRNA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 346

346

Tyrosine--tRNA ligase

PRO_0000055677

Regions

Motif

47 – 56

10

"HIGH" region

Motif

230 – 234

5

"KMSKS" region

Sites

Binding site

233

1

ATP By similarity

Secondary structure

1

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346

Helix Strand Turn

Details...

Helix

6 – 17

12

Beta strand

21 – 24

4

Helix

26 – 35

10

Beta strand

39 – 45

7

Helix

53 – 68

16

Beta strand

71 – 77

7

Helix

79 – 84

6

Helix

87 – 90

4

Helix

92 – 108

17

Helix

113 – 115

3

Beta strand

116 – 120

5

Helix

121 – 127

7

Helix

129 – 147

19

Helix

169 – 179

11

Beta strand

186 – 188

3

Helix

192 – 194

3

Helix

195 – 207

13

Beta strand

214 – 218

5

Helix

236 – 238

3

Helix

246 – 255

10

Beta strand

260 – 262

3

Helix

266 – 273

8

Helix

275 – 279

5

Beta strand

282 – 284

3

Beta strand

287 – 291

5

Helix

292 – 299

8

Helix

304 – 325

22

Helix

329 – 331

3

Helix

332 – 340

9

Sequences

	Sequence		Length	Mass (Da)
	Q5UPJ7 [UniParc]. Last modified December 7, 2004. Version 1. Checksum: 43C8D8C3ECBC87B0	FASTA	346	39,723
	10 20 30 40 50 60 MENTDHTNNE HRLTQLLSIA EECETLDRLK QLVDSGRIFT AYNGFEPSGR IHIAQALITV 70 80 90 100 110 120 MNTNNIIECG GQMIIYIADW FAKMNLKMNG DINKIRELGR YFIEVFKACG INLDGTRFIW 130 140 150 160 170 180 ASEFIASNPS YIERMLDIAE FSTISRVKRC CQIMGRNESD CLKASQIFYP CMQAADVFEL 190 200 210 220 230 240 VPEGIDICQL GIDQRKVNML AIEYANDRGL KIPISLSHHM LMSLSGPKKK MSKSDPQGAI 250 260 270 280 290 300 FMDDTEQEVS EKISRAYCTD ETFDNPIFEY IKYLLLRWFG TLNLCGKIYT DIESIQEDFS 310 320 330 340 SMNKRELKTD VANYINTIID LVREHFKKPE LSELLSNVKS YQQPSK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The 1.2-megabase genome sequence of Mimivirus." Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H., La Scola B., Susan M., Claverie J.-M. Science 306:1344-1350(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], FUNCTION. Strain: Rowbotham-Bradford.
[2]	"Mimivirus TyrRS: preliminary structural and functional characterization of the first amino-acyl tRNA synthetase found in a virus." Abergel C., Chenivesse S., Byrne D., Suhre K., Arondel V., Claverie J.-M. Acta Crystallogr. F 61:212-215(2005) [PubMed] [Europe PMC] [Abstract] Cited for: CRYSTALLIZATION, FUNCTION.
[3]	"Virus-encoded aminoacyl-tRNA synthetases: structural and functional characterization of Mimivirus TyrRS and MetRS." Abergel C., Rudinger-Thirion J., Giege R., Claverie J.-M. J. Virol. 81:12406-12417(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), SUBUNIT, CATALYTIC ACTIVITY, KINETIC PARAMETERS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY653733 Genomic DNA. Translation: AAV50399.1.

RefSeq

YP_003986615.1. NC_014649.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2J5B	X-ray	2.20	A/B	2-346	[»]

ProteinModelPortal

Q5UPJ7.

SMR

Q5UPJ7. Positions 5-342.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

9924723.

Family and domain databases

Gene3D

3.40.50.620. 1 hit.

InterPro

IPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR023617. Tyr-tRNA-ligase_arc/euk-type.
[Graphical view]

Pfam

PF00579. tRNA-synt_1b. 1 hit.
[Graphical view]

PIRSF

PIRSF006588. TyrRS_arch_euk. 1 hit.

PROSITE

PS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q5UPJ7.

Entry information

Entry name

SYY_MIMIV

Accession

Primary (citable) accession number: Q5UPJ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	December 7, 2004
Last modified:	March 6, 2013
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program