P23395 (SYM_THET8) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methionine--tRNA ligase
EC=6.1.1.10

Alternative name(s):
Methionyl-tRNA synthetase
Short name=MetRS

Gene names

Name:	metG
Synonyms:	metS
Ordered Locus Names:	TTHA1298

Organism

Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus › Thermus thermophilus

Protein attributes

Sequence length	618 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. HAMAP-Rule MF_01228
Catalytic activity	ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met). HAMAP-Rule MF_01228
Cofactor	Binds 1 zinc ion per subunit.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm HAMAP-Rule MF_01228.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2A subfamily. Contains 1 tRNA-binding domain.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding RNA-binding Zinc tRNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	methionyl-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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW methionine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP tRNA binding 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 – 618

618

Methionine--tRNA ligase HAMAP-Rule MF_01228

PRO_0000139258

Regions

Domain

518 – 618

101

tRNA-binding

Motif

12 – 22

11

"HIGH" region HAMAP-Rule MF_01228

Motif

297 – 301

5

"KMSKS" region HAMAP-Rule MF_01228

Sites

Metal binding

127

1

Zinc

Metal binding

130

1

Zinc

Metal binding

144

1

Zinc

Metal binding

147

1

Zinc

Binding site

300

1

ATP By similarity

Experimental info

Sequence conflict

615 – 618

4

AVVK → RW in AAA27510. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

618

Helix Strand Turn

Details...

Beta strand

4 – 8

5

Helix

20 – 38

19

Beta strand

42 – 50

9

Helix

54 – 63

10

Helix

67 – 84

18

Beta strand

90 – 94

5

Helix

98 – 113

16

Beta strand

117 – 127

11

Turn

128 – 131

4

Beta strand

132 – 134

3

Turn

136 – 138

3

Turn

145 – 147

3

Beta strand

152 – 161

10

Helix

163 – 166

4

Helix

167 – 175

9

Beta strand

180 – 183

4

Helix

184 – 194

11

Beta strand

204 – 206

3

Turn

207 – 209

3

Beta strand

219 – 224

6

Helix

226 – 231

6

Helix

233 – 236

4

Turn

237 – 242

6

Helix

244 – 249

6

Helix

250 – 252

3

Beta strand

253 – 258

6

Helix

259 – 261

3

Helix

262 – 266

5

Helix

268 – 276

9

Beta strand

282 – 287

6

Turn

300 – 302

3

Helix

308 – 315

8

Helix

317 – 327

11

Helix

338 – 348

11

Helix

349 – 353

5

Helix

354 – 367

14

Helix

379 – 386

8

Helix

387 – 396

10

Helix

400 – 421

22

Helix

423 – 426

4

Turn

427 – 429

3

Helix

431 – 452

22

Turn

453 – 455

3

Helix

457 – 466

10

Helix

475 – 479

5

Beta strand

480 – 482

3

Sequences

	Sequence		Length	Mass (Da)
	P23395 [UniParc]. Last modified March 29, 2005. Version 2. Checksum: 920A449052C62558	FASTA	618	70,693
	10 20 30 40 50 60 MEKVFYVTTP IYYVNAEPHL GHAYTTVVAD FLARWHRLDG YRTFFLTGTD EHGETVYRAA 70 80 90 100 110 120 QAAGEDPKAF VDRVSGRFKR AWDLLGIAYD DFIRTTEERH KKVVQLVLKK VYEAGDIYYG 130 140 150 160 170 180 EYEGLYCVSC ERFYTEKELV EGLCPIHGRP VERRKEGNYF FRMEKYRPWL QEYIQENPDL 190 200 210 220 230 240 IRPEGYRNEV LAMLAEPIGD LSISRPKSRV PWGIPLPWDE NHVTYVWFDA LLNYVSALDY 250 260 270 280 290 300 PEGEAYRTFW PHAWHLIGKD ILKPHAVFWP TMLKAAGIPM YRHLNVGGFL LGPDGRKMSK 310 320 330 340 350 360 TLGNVVDPFA LLEKYGRDAL RYYLLREIPY GQDTPVSEEA LRTRYEADLA DDLGNLVQRT 370 380 390 400 410 420 RAMLFRFAEG RIPEPVAGEE LAEGTGLAGR LRPLVRELKF HVALEEAMAY VKALNRYINE 430 440 450 460 470 480 KKPWELFKKE PEEARAVLYR VVEGLRIASI LLTPAMPDKM AELRRALGLK EEVRLEEAER 490 500 510 520 530 540 WGLAEPRPIP EEAPVLFPKK EAKVEAKPKE EAWIGIEDFA KVELRVAEVL AAEKHPNADR 550 560 570 580 590 600 LLVLRLSLGN EERTVVSGIA KWYRPEELVG KKVVLVANLK PAKLRGIESQ GMILAAQEGE 610 ALALVTVEGE VPPGAVVK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Methionyl-tRNA synthetase gene from an extreme thermophile, Thermus thermophilus HB8. Molecular cloning, primary-structure analysis, expression in Escherichia coli, and site-directed mutagenesis." Nureki O., Muramatsu T., Suzuki K., Kohda D., Matsuzawa H., Ohta T., Miyazawa T., Yokoyama S. J. Biol. Chem. 266:3268-3277(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete genome sequence of Thermus thermophilus HB8." Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S. Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HB8 / ATCC 27634 / DSM 579.
[3]	"The 2.0-A crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules." Sugiura I., Nureki O., Ugaji-Yoshikawa Y., Kuwabara S., Shimada A., Tateno M., Lorber B., Giege R., Moras D., Yokoyama S., Konno M. Structure 8:197-208(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M64273 Genomic DNA. Translation: AAA27510.1.
AP008226 Genomic DNA. Translation: BAD71121.1.

RefSeq

YP_144564.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A8H	X-ray	2.00	A	1-500	[»]
1WOY	X-ray	2.00	A	1-500	[»]
2D54	X-ray	2.00	A	1-502	[»]
2D5B	X-ray	1.80	A	1-500	[»]

ProteinModelPortal

P23395.

SMR

P23395. Positions 1-500, 512-615.

ModBase

Search...

Protein-protein interaction databases

STRING

300852.TTHA1298.

Proteomic databases

PRIDE

P23395.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAD71121; BAD71121; BAD71121.

GeneID

3169329.

KEGG

ttj:TTHA1298.

PATRIC

23957557. VBITheThe93045_1276.

Phylogenomic databases

eggNOG

COG0143.

HOGENOM

HOG000200401.

KO

K01874.

OMA

RINYDLA.

ProtClustDB

PRK12267.

Family and domain databases

Gene3D

2.40.50.140. 1 hit.
3.40.50.620. 2 hits.

HAMAP

MF_01228. Met_tRNA_synth_type2. Fused.

InterPro

IPR004495. Met-tRNA-synth_Ia_bsu_C.
IPR014758. Met-tRNA_synth.
IPR023457. Met-tRNA_synth_2.
IPR015413. Methionyl/Leucyl_tRNA_Synth.
IPR012340. NA-bd_OB-fold.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002547. tRNA-bd_dom.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]

Pfam

PF09334. tRNA-synt_1g. 1 hit.
PF01588. tRNA_bind. 1 hit.
[Graphical view]

PRINTS

PR01041. TRNASYNTHMET.

SUPFAM

SSF50249. Nucleic_acid_OB. 1 hit.
SSF47323. tRNAsyn_1a_bind. 1 hit.

TIGRFAMs

TIGR00398. metG. 1 hit.
TIGR00399. metG_C_term. 1 hit.

PROSITE

PS00178. AA_TRNA_LIGASE_I. False negative.
PS50886. TRBD. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1641341.

EvolutionaryTrace

P23395.

Entry information

Entry name

SYM_THET8

Accession

Primary (citable) accession number: P23395
Secondary accession number(s): Q5SIR6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	March 29, 2005
Last modified:	May 1, 2013
This is version 111 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program