Reviewed, UniProtKB/Swiss-Prot Q1LSS9 (SYI_BAUCH)

Names and origin

Protein names

Recommended name:
    Isoleucyl-tRNA synthetase
    EC=6.1.1.5
Alternative name(s):
    Isoleucine--tRNA ligase
      Short name=IleRS

Gene names

Name:	ileS
Ordered Locus Names:	BCI_0556

Organism

Baumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]

Taxonomic identifier

374463 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Candidatus Baumannia

Protein attributes

Sequence length	938 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP 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.
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
Gene Ontology (GO)
Biological process	isoleucyl-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 isoleucine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 938	938	Isoleucyl-tRNA synthetase HAMAP MF_02002		PRO_1000022042
Regions
	Motif	58 – 68	11	"HIGH" region HAMAP MF_02002
	Motif	602 – 606	5	"KMSKS" region HAMAP MF_02002
Sites
	Metal binding	901	1	Zinc By similarity
	Metal binding	904	1	Zinc By similarity
	Metal binding	921	1	Zinc By similarity
	Metal binding	924	1	Zinc By similarity
	Binding site	561	1	Aminoacyl-adenylate By similarity
	Binding site	605	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1LSS9-1 [UniParc]. Last modified May 30, 2006. Version 1. Checksum: 697B57DCEEB6DAAA	FASTA	938	107,240
	10 20 30 40 50 60 MIDYKNTLNL PKTQFAMRGN LAIREPIMLK RWHQQDLYQL ICQATQGKKT FFLHDGPPYA 70 80 90 100 110 120 NGSIHIGHSV NKILKDIIIK SKRLMGYCSP YIPGWDCHGL PIELKVEQLI GKPGKKVSAS 130 140 150 160 170 180 EFIIACRNYA SEQVTWQKKD FIRLGVLGDW DNIYRTMDFH TEANIIRTLS KIIENGHVYQ 190 200 210 220 230 240 GNKPVHWCID CRSALAEAEV EYYDYTSPSI YVIFAATNTH DVAARFGIPN VLSSISFLVW 250 260 270 280 290 300 TTTPWTIPAN RAISIHPNLN YQLVKVNQQG FILAADLVTS VLTYLGIQNW TVVKNIKGYV 310 320 330 340 350 360 LELLRFSHPF MKFDVPVVLS NHVTINVGTG VVHTSPSHGP DDYLIGREYN LEIVNIVGPD 370 380 390 400 410 420 GCYLPGTFSL LDGTSVYQSN QTVISLLKDR GALLHTGTIQ HSYPHCWRHK TPLIFRATPQ 430 440 450 460 470 480 WFISMDKKKL RQQSLKEIKK IQWIPSNSQA SITNMVNNRQ DWCISRQRIW GVPMSLFVHN 490 500 510 520 530 540 HTKKLHPQTS EIMEYVAKQV EKKGIQAWWD LDPIKILGDD IVNYSKINDI LDVWFDSGST 550 560 570 580 590 600 HSSVINAQTE FANHEIDMYL EGADQHRGWF MSSLISSTAI KGKAPYKTVI THGFAVDSNG 610 620 630 640 650 660 RKMSKSIGNV VSPQQVVDKL GADILRLWVA STNYTDDMTI SDEILKRSVD TYRRIRNTAR 670 680 690 700 710 720 FLLANLNGFE PKQHSVSIDK MIILDQWAID RAQVAQDEII AAYNSYEFHS VVQRIMQFCS 730 740 750 760 770 780 VEMGSFYLDI IKDRQYTTQY NSIARRSCQT ALFHIIEAMV RWIAPIISFT ADEIWGFIPG 790 800 810 820 830 840 KRSPSVFIEE WYKNLSRLDA EQHMNDTYWN TLLQVRSDVN YLIEQARIKK NIGSSLETQV 850 860 870 880 890 900 TLYSEPILAM QLRQLGNELH FVLLTSAVQI ADYQEADNNA LQSTRIKGLK ITLNHATGRK 910 920 930 CQRCWHYEQD IGNNTQYPEI CGRCVINIAG NGEERKFV

References

[1]

"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters." Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A. PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000238 Genomic DNA. Translation: ABF14142.1.
RefSeq	YP_588985.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q1LSS9.
Genome annotation databases
GeneID	4056571.
GenomeReviews	Gene locus BCI_0556 in contig CP000238_GR.
KEGG	bci:BCI_0556.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1LSS9.
OMA	FPMRGNL.
Family and domain databases
HAMAP	MF_02002. [Tree]
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR002300. aa-tRNA-synth_Ia. IPR010663. DNA_glyclase/IsotRNA_synth_Znf. IPR002301. Ile-tRNA-synt_Ia. IPR015905. Ile-tRNA-synt_Ia_N. IPR018353. Isoleucyl-tRNA_synthetase. IPR014729. Rossmann-like_a/b/a_fold. IPR013155. V/L/I-tRNA-synth_anticodon-bd. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHER	PTHR11946:SF9. Ile-tRNA-synt_Ia. 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.
TIGRFAMs	TIGR00392. ileS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYI_BAUCH

Accession

Primary (citable) accession number: Q1LSS9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	May 30, 2006
Last modified:	November 3, 2009
This is version 29 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)