X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
DOI=10.1006/jmbi.1999.2617; PubMed=10092459 [NCBI, ExPASy, EBI, Israel, Japan]
Reshetnikova L., Moor N., Lavrik O., Vassylyev D.G.;
"Crystal structures of phenylalanyl-tRNA synthetase complexed with phenylalanine and a phenylalanyl-adenylate analogue.";
J. Mol. Biol. 287:555-568(1999).

Comments

CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe).
COFACTOR: Binds 2 magnesium ions per tetramer.
SUBUNIT: Tetramer of two alpha and two beta chains.
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha chain type 1 subfamily [view classification].
CAUTION: The sequence shown here has been extracted from PDB entry 1B70.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

3D structure databases

PDB

1B70; X-ray; 2.70 A; A=1-350.	[ExPASy / RCSB / EBI]
1B7Y; X-ray; 2.50 A; A=1-350.	[ExPASy / RCSB / EBI]
2AKW; X-ray; 2.80 A; A=85-350.	[ExPASy / RCSB / EBI]
2ALY; X-ray; 2.60 A; A=85-350.	[ExPASy / RCSB / EBI]
2AMC; X-ray; 2.70 A; A=85-350.	[ExPASy / RCSB / EBI]
2IY5; X-ray; 3.10 A; A=1-350.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1B70; -.
1B7Y; -.
2AKW; -.
2ALY; -.
2AMC; -.
2IY5; -.

DisProt

DP00053; -.

ModBase

P27001.

Protein-protein interaction databases

DIP

DIP:6104N; -.

Enzyme and pathway databases

BRENDA

6.1.1.20; 245.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from HAMAP).
GO:0004826;	Molecular function: phenylalanine-tRNA ligase activity (inferred from electronic annotation from HAMAP).
GO:0006432;	Biological process: phenylalanyl-tRNA aminoacylation (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00281; -; 1.
PBIL [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 of domain structure.

PANTHER

PTHR11538; tRNA-synt_2d; 1.

Pfam

PF02912; Phe_tRNA-synt_N; 1.
PF01409; tRNA-synt_2d; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00468; pheS; 1.

PROSITE

PS50862; AA_TRNA_LIGASE_II; 1.
PROSITE graphical view of domain structure (profiles).

Other

ProtoNet

P27001.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium; Metal-binding; Nucleotide-binding; Protein biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 350`	`350`	`Phenylalanyl-tRNA synthetase alpha chain.`	`PRO_0000126786`
`METAL`	`262 262`		`Magnesium.`
`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`
`STRAND`	`126 129`	`4`
`HELIX`	`130 133`	`4`
`TURN`	`134 138`	`5`
`STRAND`	`141 143`	`3`
`HELIX`	`146 148`	`3`
`STRAND`	`153 155`	`3`
`STRAND`	`173 175`	`3`
`STRAND`	`177 179`	`3`
`HELIX`	`181 189`	`9`
`STRAND`	`192 203`	`12`
`STRAND`	`214 225`	`12`
`HELIX`	`230 244`	`15`
`STRAND`	`251 255`	`5`
`STRAND`	`261 271`	`11`
`TURN`	`272 275`	`4`
`STRAND`	`276 286`	`11`
`HELIX`	`288 300`	`13`
`STRAND`	`311 318`	`8`
`HELIX`	`319 327`	`9`
`HELIX`	`332 336`	`5`
`HELIX`	`340 343`	`4`
`HELIX`	`344 346`	`3`

Sequence information

Length: 350 AA [This is the length of the unprocessed precursor]

Molecular weight: 39259 Da [This is the MW of the unprocessed precursor]

CRC64: DEE0237F7CD9A461 [This is a checksum on the sequence]

        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

P27001 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools