Reviewed, UniProtKB/Swiss-Prot P27001 (SYFA_THETH)

Names and origin

Protein names

Recommended name:
    Phenylalanyl-tRNA synthetase alpha chain
    EC=6.1.1.20
Alternative name(s):
    Phenylalanine--tRNA ligase alpha chain
      Short name=PheRS

Gene names

Name:

pheS

Organism

Thermus thermophilus

Taxonomic identifier

274 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

Protein attributes

Sequence length	350 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-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe). HAMAP MF_00281
Cofactor	Binds 2 magnesium ions per tetramer. HAMAP MF_00281
Subunit structure	Tetramer of two alpha and two beta chains. HAMAP MF_00281
Subcellular location	Cytoplasm. HAMAP MF_00281
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha chain type 1 subfamily.
Caution	The sequence shown here has been extracted from PDB entry 1B70.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	phenylalanyl-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 magnesium ion binding Inferred from electronic annotation. Source: HAMAP phenylalanine-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 – 350

350

Phenylalanyl-tRNA synthetase alpha chain HAMAP MF_00281

PRO_0000126786

Sites

Metal binding

262

1

Magnesium HAMAP MF_00281

Secondary structure

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350

Helix Strand Turn

Details...

Helix

16 – 31

16

Turn

39 – 41

3

Helix

42 – 44

3

Helix

49 – 61

13

Helix

63 – 73

11

Helix

76 – 83

8

Helix

102 – 115

14

Turn

116 – 118

3

Beta strand

126 – 129

4

Helix

130 – 133

4

Turn

134 – 138

5

Beta strand

141 – 143

3

Helix

146 – 148

3

Beta strand

153 – 155

3

Beta strand

173 – 175

3

Beta strand

177 – 179

3

Helix

181 – 189

9

Beta strand

192 – 203

12

Beta strand

214 – 225

12

Helix

230 – 244

15

Beta strand

251 – 255

5

Beta strand

261 – 271

11

Turn

272 – 275

4

Beta strand

276 – 286

11

Helix

288 – 300

13

Beta strand

311 – 318

8

Helix

319 – 327

9

Helix

332 – 336

5

Helix

340 – 343

4

Helix

344 – 346

3

Sequences

	Sequence		Length	Mass (Da)
	P27001-1 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: DEE0237F7CD9A461	FASTA	350	39,259
	10 20 30 40 50 60 MLEEALAAIQ NARDLEELKA LKARYLGKKG LLTQEMKGLS ALPLEERRKR GQELNAIKAA 70 80 90 100 110 120 LEAALEAREK ALEEAALKEA LERERVDVSL PGASLFSGGL HPITLMEREL VEIFRALGYQ 130 140 150 160 170 180 AVEGPEVESE FFNFDALNIP EHHPARDMWD TFWLTGEGFR LEGPLGEEVE GRLLLRTHTS 190 200 210 220 230 240 PMQVRYMVAH TPPFRIVVPG RVFRFEQTDA THEAVFHQLE GLVVGEGIAM AHLKGAIYEL 250 260 270 280 290 300 AQALFGPDSK VRFQPVYFPF VEPGAQFAVW WPEGGKWLEL GGAGMVHPKV FQAVDAYRER 310 320 330 340 350 LGLPPAYRGV TGFAFGLGVE RLAMLRYGIP DIRYFFGGRL KFLEQFKGVL

References

[1]	"Crystal structures of phenylalanyl-tRNA synthetase complexed with phenylalanine and a phenylalanyl-adenylate analogue." Reshetnikova L., Moor N., Lavrik O., Vassylyev D.G. J. Mol. Biol. 287:555-568(1999) [PubMed: 10092459] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B70	X-ray	2.70	A	1-350	[»]
1B7Y	X-ray	2.50	A	1-350	[»]
2AKW	X-ray	2.80	A	85-350	[»]
2ALY	X-ray	2.60	A	85-350	[»]
2AMC	X-ray	2.70	A	85-350	[»]
2IY5	X-ray	3.10	A	1-350	[»]

DisProt

DP00053.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:6104N.

Enzyme and pathway databases

BRENDA

6.1.1.20. 245.

Family and domain databases

HAMAP

MF_00281.
[Tree]

InterPro

IPR006195. aa-tRNA-synth_II_cons-reg.
IPR002319. Phe-tRNA-synth_IIc-rel.
IPR004529. Phe-tRNA-synth_IIc_asu.
IPR018157. Phe-tRNA-synth_IIc_C.
IPR004188. Phe-tRNA_synth_II_N.
[Graphical view]

PANTHER

PTHR11538. tRNA-synt_2d. 1 hit.

Pfam

PF02912. Phe_tRNA-synt_N. 1 hit.
PF01409. tRNA-synt_2d. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00468. pheS. 1 hit.

PROSITE

PS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SYFA_THETH

Accession

Primary (citable) accession number: P27001

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	June 16, 2009
This is version 80 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)