P57249 (SYI_BUCAI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Isoleucine--tRNA ligase
EC=6.1.1.5

Alternative name(s):
Isoleucyl-tRNA synthetase
Short name=IleRS

Gene names

Name:	ileS
Ordered Locus Names:	BU149

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium) [Reference proteome] [HAMAP]

Taxonomic identifier

107806 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Acyrthosiphon pisum)

Protein attributes

Sequence length	940 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile) By similarity. HAMAP-Rule MF_02002
Catalytic activity	ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02002
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity.
Domain	IleRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated valine is translocated from the active site to the editing site, which sterically excludes the correctly activated isoleucine. The single editing site contains two valyl binding pockets, one specific for each substrate (Val-AMP or Val-tRNA(Ile)) By similarity. HAMAP-Rule MF_02002
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	isoleucyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP regulation of translational fidelity Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP aminoacyl-tRNA editing activity Inferred from electronic annotation. Source: InterPro isoleucine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP zinc ion 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 – 940	940	Isoleucine--tRNA ligase HAMAP-Rule MF_02002		PRO_0000098365
Regions
	Motif	58 – 68	11	"HIGH" region HAMAP-Rule MF_02002
	Motif	604 – 608	5	"KMSKS" region HAMAP-Rule MF_02002
Sites
	Metal binding	903	1	Zinc By similarity
	Metal binding	906	1	Zinc By similarity
	Metal binding	923	1	Zinc By similarity
	Metal binding	926	1	Zinc By similarity
	Binding site	563	1	Aminoacyl-adenylate By similarity
	Binding site	607	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	P57249 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: 769F5DC1504F6496	FASTA	940	110,457
	10 20 30 40 50 60 MDDYKDTLNL PKTLFSMRGN LSKKEPNILK SWNENNLYKL IRKKNQEKKI FFLHDGPPYA 70 80 90 100 110 120 NGNIHIGHAV NKILKDIIIK SKNMSGFDAP YIPSWDCHGL PIEQKVEEKI KSNQGEISTT 130 140 150 160 170 180 EFQEKCRKYA QDQVEKQKKD FIRLGVIGDW DNPHLTMNFK NEANIIKTLS KIVQKKHLYQ 190 200 210 220 230 240 DFKPIHWCLK CASSLSEAEI EYSKKKSDSI IVGFKFKYKS IIEKLFDFQI SNKKEIHLLI 250 260 270 280 290 300 WTTTPWTLPS SKAISIHPDF QYQLIETERC YLIIAKELVE KTLNTLKIKK SIIRNYVKGR 310 320 330 340 350 360 FLEKMICLHP FLKNIDLPVI LGKHVTLESG TGAVHTAPDH GLEDYIISQK YNIKTSNIVN 370 380 390 400 410 420 FKGEYISNTH DKLDGVNVLE ANSIIIELLI KNNTFFHHES LIHSYPHCWR HKSPVIYRAT 430 440 450 460 470 480 PQWFIDIDQK QLRIKLLQEI KKVRWIPEWG ESRIGEMIKK RPDWCISRQR KWGVPMSIFI 490 500 510 520 530 540 HKNTRKIHPN TFVFMKKIAK KVELEGLQVW WNIDSKEILG EEYQSYEKIL DILDVWFESG 550 560 570 580 590 600 NTHTTINYKN KNYTKKNADM FLEGSDQHRG WFMSSLIIST LISEKKPYSE VLTHGFVVDG 610 620 630 640 650 660 KGQKMSKSIG NTISPNEIVD TLGADILRLW VASSNYSNDI SISNEILKSS SDIYRRIRNT 670 680 690 700 710 720 ARFMLANISD FDPKKNIISK ENMVLLDKWA IGQTKIVQEE IIQHYNNYNF HAVIQRLMYF 730 740 750 760 770 780 CSIEMGSFYL DIIKDRQYTL KKHSQERRSS QTAIYYIINS LVRWIAPILS FTADEIWSYL 790 800 810 820 830 840 PENNSQYVFM EEWFDKLFYL DQDDLFNYQF WNEIITIKHE INKFLEEAIQ NKTINNSLET 850 860 870 880 890 900 SIILYVSHEL SNKLKILEQE TKFIFLTSDI QIKLYDTAPK NAKKSKIVPY LKVSLEKIKG 910 920 930 940 KKCPRCWHYF NFTKKNIKNS DICNRCILNT IGNGEKRIFI

References

[1]	"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: APS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000003 Genomic DNA. Translation: BAB12867.1.
RefSeq	NP_239981.1. NC_002528.1.
3D structure databases
ProteinModelPortal	P57249.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB12867; BAB12867; BAB12867.
GeneID	1109593.
KEGG	buc:BU149.
PATRIC	21243812. VBIBucAph127364_0158.
Phylogenomic databases
eggNOG	COG0060.
HOGENOM	HOG000246402.
KO	K01870.
OMA	KQVLTHG.
ProtClustDB	PRK05743.
Family and domain databases
Gene3D	3.40.50.620. 2 hits. 3.90.740.10. 1 hit.
HAMAP	MF_02002. Ile_tRNA_synth_type1.
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR002300. aa-tRNA-synth_Ia. IPR002301. Ile-tRNA-ligase. IPR023585. Ile-tRNA-ligase_type1. IPR014729. Rossmann-like_a/b/a_fold. IPR009080. tRNAsynth_1a_anticodon-bd. IPR013155. V/L/I-tRNA-synth_anticodon-bd. IPR009008. Val/Leu/Ile-tRNA-synth_edit. IPR010663. Znf_DNA_glyclase/IsotRNA_synth. [Graphical view]
PANTHER	PTHR11946:SF9. PTHR11946:SF9. 1 hit.
Pfam	PF08264. Anticodon_1. 1 hit. PF00133. tRNA-synt_1. 1 hit. PF06827. zf-FPG_IleRS. 1 hit. [Graphical view]
PRINTS	PR00984. TRNASYNTHILE.
SUPFAM	SSF47323. tRNAsyn_1a_bind. 1 hit. SSF50677. ValRS_IleRS_edit. 1 hit.
TIGRFAMs	TIGR00392. ileS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYI_BUCAI

Accession

Primary (citable) accession number: P57249

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program