Q9RVD6 (SYW2_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tryptophan--tRNA ligase 2
EC=6.1.1.2

Alternative name(s):
Tryptophanyl-tRNA synthetase 2
Short name=TrpRS 2
Tryptophanyl-tRNA synthetase II
Short name=TrpRS II

Gene names

Name:	trpS2
Synonyms:	trpSII
Ordered Locus Names:	DR_1093

Organism

Deinococcus radiodurans

Taxonomic identifier

1299 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus

Protein attributes

Sequence length	351 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the formation of 5'adenyl-Trp and tRNA(Trp) but with 5-fold less activity than trpRS. Increases the solubility of the nitric oxide synthase oxygenase (nos), as well as its affinity for substrate L-arginine and its nitric-oxide synthase activity. The complex between trpS2 and nos catalyzes the regioselective nitration of tryptophan at the 4-position. Ref.2
Catalytic activity	ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp). HAMAP MF_00140_B
Subunit structure	Homodimer. Forms a complex with nos; one homodimer of trpS2 binds one homodimer of nos.
Induction	The level of expression increases 2.2-fold, 5 hours after exposure to radiation, and returns to near a base line 5 hours later. HAMAP MF_00140_B
Miscellaneous	This protein may not be involved in protein biosynthesis. HAMAP MF_00140_B
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.

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	tryptophanyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW tryptophan-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 – 351

351

Tryptophan--tRNA ligase 2 HAMAP MF_00140_B

PRO_0000136717

Regions

Motif

31 – 39

9

"HIGH" region HAMAP MF_00140_B

Motif

215 – 219

5

"KMSKS" region HAMAP MF_00140_B

Sites

Binding site

218

1

ATP By similarity

Secondary structure

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351

Helix Strand Turn

Details...

Beta strand

24 – 28

5

Helix

37 – 41

5

Helix

43 – 53

11

Beta strand

54 – 60

7

Turn

62 – 65

4

Helix

66 – 69

4

Helix

73 – 89

17

Turn

94 – 96

3

Beta strand

97 – 101

5

Helix

102 – 104

3

Helix

107 – 115

9

Beta strand

118 – 120

3

Helix

121 – 125

5

Helix

128 – 135

8

Turn

136 – 138

3

Helix

145 – 148

4

Helix

150 – 160

11

Beta strand

165 – 168

4

Helix

170 – 172

3

Helix

173 – 189

17

Beta strand

198 – 201

4

Beta strand

212 – 214

3

Helix

218 – 220

3

Helix

230 – 237

8

Turn

255 – 257

3

Helix

259 – 267

9

Helix

271 – 281

11

Helix

288 – 314

27

Helix

317 – 345

29

Sequences

	Sequence		Length	Mass (Da)
	Q9RVD6 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 7CBE69160F6CB9C5	FASTA	351	38,180
	10 20 30 40 50 60 MPFVDLEVPT MTTPTPAATP ARPRVLTGDR PTGALHLGHL AGSLQNRVRL QDEAELFVLL 70 80 90 100 110 120 ADVQALTDHF DRPEQVRENV LAVALDYLAA GLDPQKTTCV VQSAVPELAE LTVYFLNLVT 130 140 150 160 170 180 VSHLRQNPTV KAEIAQKGYG ERVPAGFFVY PVSQAADIAA FGATLVPVGD DQLPMLEQTR 190 200 210 220 230 240 EIVRRFNALY APVLAEPQAQ LSRVPRLPGL DGQAKMSKSL GNAIALGDSA DEVARKVMGM 250 260 270 280 290 300 YTDPGHLRAS DPGRVEGNPV FTFLDAFDPD PARVQALKDQ YRAGGLGDVK VKKHLIDVLN 310 320 330 340 350 GVLAPIRTRR AEYERDPDAV LRFVTEGTAR GREVAAQTLG QVRRAMRLFG H

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1." White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., Vamathevan J.J., Lam P. , McDonald L.A., Utterback T.R., Zalewski C., Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D., Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Science 286:1571-1577(1999) [PubMed: 10567266] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
[2]	"An unusual tryptophanyl tRNA synthetase interacts with nitric oxide synthase in Deinococcus radiodurans." Buddha M.R., Keery K.M., Crane B.R. Proc. Natl. Acad. Sci. U.S.A. 101:15881-15886(2004) [PubMed: 15520379] [Abstract] Cited for: FUNCTION, INTERACTION WITH NOS. Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
[3]	"Regioselective nitration of tryptophan by a complex between bacterial nitric-oxide synthase and tryptophanyl-tRNA synthetase." Buddha M.R., Tao T., Parry R.J., Crane B.R. J. Biol. Chem. 279:49567-49570(2004) [PubMed: 15466862] [Abstract] Cited for: ACTIVITY OF THE COMPLEX WITH NOS. Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000513 Genomic DNA. Translation: AAF10665.1.

PIR

E75438.

RefSeq

NP_294817.2. NC_001263.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YI8	X-ray	2.10	A/B/C	1-351	[»]
1YIA	X-ray	3.70	A/B/C	1-351	[»]
1YID	X-ray	2.40	A/B/C	1-351	[»]
2A4M	X-ray	2.30	A/B/C	21-351	[»]

ProteinModelPortal

Q9RVD6.

SMR

Q9RVD6. Positions 21-351.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1797478.

GenomeReviews

Gene locus DR_1093 in contig AE000513_GR.

KEGG

dra:DR_1093.

NMPDR

fig|243230.1.peg.1276.

PATRIC

21629774. VBIDeiRad64572_1289.

TIGR

DR_1093.

Phylogenomic databases

HOGENOM

HBG293263.

OMA

TYLDAFH.

PhylomeDB

Q9RVD6.

ProtClustDB

PRK12282.

Enzyme and pathway databases

BioCyc

DRAD243230:DR_1093-MONOMER.

Family and domain databases

HAMAP

MF_00140_B. Trp_tRNA_synth_B. Divergent sequence.
[Tree]

InterPro

IPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002306. Trp-tRNA-synth.
[Graphical view]

Gene3D

G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.

KO

K01867.

PANTHER

PTHR10055. Trp_tRNA-synt_1b. 1 hit.

Pfam

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

PRINTS

PR01039. TRNASYNTHTRP.

TIGRFAMs

TIGR00233. TrpS. 1 hit.

PROSITE

PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SYW2_DEIRA

Accession

Primary (citable) accession number: Q9RVD6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program