Q189P4 (Q189P4_CLOD6) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Phenylalanine--tRNA ligase alpha subunit HAMAP-Rule MF_00281
EC=6.1.1.20 HAMAP-Rule MF_00281

Alternative name(s):
Phenylalanyl-tRNA synthetase alpha subunit HAMAP-Rule MF_00281

Gene names

Name:	pheS HAMAP-Rule MF_00281 EMBL CAJ67532.2
Ordered Locus Names:	CD630_06990 EMBL CAJ67532.2

Organism

Clostridium difficile (strain 630) [Complete proteome] [HAMAP] EMBL CAJ67532.2

Taxonomic identifier

272563 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Clostridiales › Peptostreptococcaceae › Clostridium difficile

Protein attributes

Sequence length	339 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe). HAMAP-Rule MF_00281 SAAS SAAS004529
Cofactor	Binds 2 magnesium ions per tetramer By similarity. HAMAP-Rule MF_00281 SAAS SAAS004529
Subunit structure	Tetramer of two alpha and two beta subunits By similarity. HAMAP-Rule MF_00281 SAAS SAAS004529
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00281 SAAS SAAS004529.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. HAMAP-Rule MF_00281

Ontologies

Keywords
Biological process	Protein biosynthesis HAMAP-Rule MF_00281 SAAS SAAS004529
Cellular component	Cytoplasm HAMAP-Rule MF_00281 SAAS SAAS004529
Ligand	ATP-binding HAMAP-Rule MF_00281 SAAS SAAS004529 Magnesium HAMAP-Rule MF_00281 SAAS SAAS004529 Metal-binding HAMAP-Rule MF_00281 SAAS SAAS004529 Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase HAMAP-Rule MF_00281 SAAS SAAS004529 EMBL CAJ67532.2 Ligase
Technical term	Complete proteome
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 tRNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Sites
	Metal binding	254	1	Magnesium By similarity HAMAP-Rule MF_00281

Sequences

	Sequence		Length	Mass (Da)
	Q189P4 [UniParc]. Last modified June 28, 2011. Version 2. Checksum: 16B501BEA3EE3C32	FASTA	339	38,004
	10 20 30 40 50 60 MQEKLLALRE AALAEIKEAQ SIESVESLRV KYLGKKGEIT AILKEMGKLS AEERPVVGKV 70 80 90 100 110 120 ANEVRENIEL SINSKKEEIN AIEKERKLKE EVIDVTQPGK VLKVGKKHPI TQIIDEVTDI 130 140 150 160 170 180 FIGMGFSIAE GPEVETVENN FDALNAPKDH PSRDMSDTFY INDGVLLRTQ TSPVQVRTMR 190 200 210 220 230 240 SQELPIKVIA PGRCFRSDSP DATHSPMFHQ IEGLVVGKDV TMAEFKGTMD IFVEKLFGSD 250 260 270 280 290 300 IKTKFRPHNF PFTEPSAEVD VTCFKCGGKG CPMCKYEGWI EILGSGMVHP NVLRNCGIDP 310 320 330 EVYSGFAFGV GVERLAMLKY EIDDIRLLFE NDMRFLNQF

References

[1]

"The multidrug-resistant human pathogen Clostridium difficile has a highly mobile, mosaic genome." Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N., Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H., Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N., Brooks K., Chillingworth T. , Cronin A., Davis P., Dowd L., Fraser A., Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K., Price C., Rabbinowitsch R., Sharp S., Simmonds M., Steven K., Unwin L., Whithead S., Dupuy B., Dougan G., Barrell B.and.Parkhill.J. Nat. Genet. 38:779-786(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 630 EMBL CAJ67532.2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM180355 Genomic DNA. Translation: CAJ67532.2.
RefSeq	YP_001087175.2. NC_009089.1.
3D structure databases
ProteinModelPortal	Q189P4.
ModBase	Search...
Protein-protein interaction databases
STRING	272563.CD0699.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAJ67532; CAJ67532; CD630_06990.
GeneID	4916807.
KEGG	cdf:CD630_06990.
PATRIC	19439681. VBICloDif38397_0734.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0016.
HOGENOM	HOG000242675.
ProtClustDB	PRK00488.
Enzyme and pathway databases
BioCyc	CDIF272563:GJFE-835-MONOMER.
Family and domain databases
HAMAP	MF_00281. Phe_tRNA_synth_alpha1.
InterPro	IPR006195. aa-tRNA-synth_II. IPR004529. Phe-tRNA-synth_IIc_asu. IPR004188. Phe-tRNA_ligase_II_N. IPR022911. Phe_tRNA_ligase_alpha1_bac. IPR002319. Phenylalanyl-tRNA_Synthase. IPR010978. tRNA-bd_arm. [Graphical view]
Pfam	PF02912. Phe_tRNA-synt_N. 1 hit. PF01409. tRNA-synt_2d. 1 hit. [Graphical view]
SUPFAM	SSF46589. tRNA_binding_arm. 1 hit.
TIGRFAMs	TIGR00468. pheS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Q189P4_CLOD6

Accession

Primary (citable) accession number: Q189P4

Entry history

Integrated into UniProtKB/TrEMBL:	July 25, 2006
Last sequence update:	June 28, 2011
Last modified:	May 1, 2013
This is version 64 of the entry and version 2 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)