Reviewed, UniProtKB/Swiss-Prot P56926 (SYQ_DEIRA)

Names and origin

Protein names

Recommended name:
    Glutaminyl-tRNA synthetase
    EC=6.1.1.18
Alternative name(s):
    Glutamine--tRNA ligase
      Short name=GlnRS

Gene names

Name:	glnS
Ordered Locus Names:	DR_2611

Organism

Deinococcus radiodurans [Complete proteome] [HAMAP]

Taxonomic identifier

1299 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	852 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln). HAMAP MF_00126
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm. HAMAP MF_00126
Sequence similarities	In the N-terminal section; belongs to the class-I aminoacyl-tRNA synthetase family. In the C-terminal section; belongs to the gatB/gatE family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	glutaminyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro glutamyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP carbon-nitrogen ligase activity, with glutamine as amido-N-donor Inferred from electronic annotation. Source: InterPro glutamine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 852

852

Glutaminyl-tRNA synthetase HAMAP MF_00126

PRO_0000195832

Regions

Region

1 – 635

635

Glutaminyl-tRNA synthetase HAMAP MF_00126

Region

636 – 852

217

GatB-like HAMAP MF_00126

Motif

74 – 84

11

"HIGH" region HAMAP MF_00126

Motif

308 – 312

5

"KMSKS" region HAMAP MF_00126

Sites

Binding site

311

1

ATP By similarity

Secondary structure

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852

Helix Strand Turn

Details...

Helix

51 – 61

11

Beta strand

69 – 72

4

Beta strand

76 – 78

3

Helix

82 – 84

3

Helix

85 – 97

13

Beta strand

101 – 106

6

Turn

111 – 113

3

Helix

116 – 129

14

Beta strand

137 – 139

3

Helix

140 – 143

4

Helix

144 – 156

13

Beta strand

159 – 163

5

Helix

167 – 174

8

Turn

185 – 188

4

Helix

191 – 202

12

Beta strand

212 – 215

4

Helix

224 – 226

3

Beta strand

230 – 234

5

Turn

240 – 242

3

Beta strand

247 – 250

4

Helix

252 – 263

12

Beta strand

266 – 271

6

Helix

272 – 274

3

Turn

275 – 277

3

Helix

278 – 287

10

Beta strand

295 – 299

5

Beta strand

302 – 304

3

Helix

311 – 319

9

Beta strand

322 – 325

4

Beta strand

331 – 333

3

Helix

334 – 340

7

Helix

344 – 353

10

Beta strand

361 – 363

3

Helix

365 – 377

13

Beta strand

385 – 394

10

Beta strand

401 – 408

8

Helix

410 – 414

5

Beta strand

424 – 426

3

Helix

431 – 433

3

Beta strand

435 – 440

6

Beta strand

442 – 447

6

Helix

448 – 450

3

Beta strand

467 – 470

4

Turn

471 – 473

3

Beta strand

474 – 483

10

Beta strand

489 – 496

8

Turn

512 – 514

3

Beta strand

516 – 523

8

Beta strand

526 – 530

5

Helix

566 – 569

4

Beta strand

574 – 582

9

Helix

584 – 588

5

Beta strand

594 – 597

4

Turn

598 – 600

3

Beta strand

601 – 605

5

Helix

607 – 611

5

Beta strand

621 – 626

6

Sequences

	Sequence		Length	Mass (Da)
	P56926-1 [UniParc]. Last modified May 30, 2000. Version 1. Checksum: 82911AA229D25F79	FASTA	852	93,471
	10 20 30 40 50 60 MGAFGWEQDR GAPFSGRSPR ILTRMTDAPR PTAGADAPAR PPAAPLVAPN FITEIIERDL 70 80 90 100 110 120 EAGKYPRVVT RFPPDPSGYA HLGHVFASLL DFNTARQYGG QFNLRMDDTN PELARQEYVD 130 140 150 160 170 180 SIADDLKWLG LDWGEHFYYA SDYFDRYYAY AEQLIRQGDA YVESVSPEEL SRLRGNATTP 190 200 210 220 230 240 GTPSPYRDRS VEENLDLLRR MKAGEFADGE HVLRAKIDLT APNMKLRDPV LYRIVNKPHF 250 260 270 280 290 300 RTSDEWHIYP AYDFEHPLQD AIEGVTHSMC SLEFVDNRAI YDWLMEKLNF DPRPHQYEFG 310 320 330 340 350 360 RRGLEYTITS KRKLRELVQA GRVSGWDDPR MPTLRAQRRL GVTPEAVRAF AAQIGVSRTN 370 380 390 400 410 420 RTVDIAVYEN AVRDDLNHRA PRVMAVLDPV KVTLTNLDGE KTLSLPYWPH DVVRDSPDGL 430 440 450 460 470 480 VGMPGGGRVA PEEAVRDVPL TRELYIERDD FSPAPPKGFK RLTPGGTVRL RGAGIIRADD 490 500 510 520 530 540 FGTDEAGQVT HIRATLLGED AKAAGVIHWV SAERALPAEF RLYDRLFRVP HPEGENADVE 550 560 570 580 590 600 DDSAGPAEHE AEPGAGQETA PVSQGFMRYL TPDSLRVLRG YVEPSVAGDP ADTRYQFERQ 610 620 630 640 650 660 GYFWRDPVEL ERVDSREDAL VFGRIITLKD TWGKQGGGTQ QKAEGKKRPS TKGRGPDEVR 670 680 690 700 710 720 GEGSSSPAKA HAPKAQPLTP EQDAEFTRLL GLGASEGDAR TIARDPALLA FVGGAAPGDT 730 740 750 760 770 780 FAQVASWTVN ELVAGLRAGE VKVRAADLAP LAEGVASGQL SARIAREALA RAAASGDAPL 790 800 810 820 830 840 TIIEREGLNA GLSAEALQQV VAQVIAANPD KAEAYRGGKT ALLGFFTGQV MRATAGKADP 850 QALAAALKDA LA

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 / IFO 15346 / LMG 4051 / NCIB 9279 / R1.

+

Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AE000513 Genomic DNA. Translation: AAF12148.1.

PIR

A75253.

RefSeq

NP_296330.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HZ7	X-ray	2.30	A	2-852	[»]

ModBase

Search...

Genome annotation databases

GeneID

1798434.

GenomeReviews

Gene locus DR_2611 in contig AE000513_GR.

KEGG

dra:DR_2611.

NMPDR

fig|243230.1.peg.2789.

TIGR

DR_2611.

Phylogenomic databases

HOGENOM

P56926.

Enzyme and pathway databases

BioCyc

DRAD243230:DR_2611-MON.
MetaCyc:MON-14055.

BRENDA

6.1.1.18. 96172.

Family and domain databases

HAMAP

MF_00126. Fused.
[Tree]

InterPro

IPR001412. aa-tRNA-synth_I_CS.
IPR018027. Asn/Gln_amidotransferase.
IPR004514. Gln-tRNA-synth_Ic.
IPR000924. Glu/Gln-tRNA-synth_Ic.
IPR020061. Glu/Gln-tRNA-synth_Ic_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ic_cat-dom.
IPR020059. Glu/Gln-tRNA-synth_Ic_codon-bd.
IPR020060. Glu/Gln-tRNA-synth_Ic_N.
IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
[Graphical view]

Gene3D

G3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:2.40.240.10. Rbsml_L25/Gln-tRNA_synth_b-brl. 1 hit.

PANTHER

PTHR10119:SF3. GlnS. 1 hit.
PTHR10119. Glu_tRNA-synt_1c. 1 hit.

Pfam

PF02637. GatB_Yqey. 1 hit.
PF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
[Graphical view]

PRINTS

PR00987. TRNASYNTHGLU.

TIGRFAMs

TIGR00440. glnS. 1 hit.

PROSITE

PS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SYQ_DEIRA

Accession

Primary (citable) accession number: P56926

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 30, 2000
Last modified:	July 28, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)