Q0AAD1 (SYI_ALHEH) 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:	Mlg_0852

Organism

Alkalilimnicola ehrlichei (strain MLHE-1) [Complete proteome] [HAMAP]

Taxonomic identifier

187272 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Chromatiales › Ectothiorhodospiraceae › Alkalilimnicola › Alkalilimnicola ehrlichii

Protein attributes

Sequence length	941 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
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 – 941	941	Isoleucine--tRNA ligase HAMAP-Rule MF_02002		PRO_1000022040
Regions
	Motif	58 – 68	11	"HIGH" region HAMAP-Rule MF_02002
	Motif	603 – 607	5	"KMSKS" region HAMAP-Rule MF_02002
Sites
	Metal binding	904	1	Zinc By similarity
	Metal binding	907	1	Zinc By similarity
	Metal binding	924	1	Zinc By similarity
	Metal binding	927	1	Zinc By similarity
	Binding site	562	1	Aminoacyl-adenylate By similarity
	Binding site	606	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0AAD1 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: 2B8F9AE6731EAC86	FASTA	941	105,903
	10 20 30 40 50 60 MSDYKHTLNL PKTGFPMRGN LAKREPERLA GWYQTDLYGR LRRERAGKPR FVLHDGPPYA 70 80 90 100 110 120 NGDIHIGHAV NKILKDIIIK ARSMDGYDVP YVPGWDCHGL PIELMVEKKR GKAGAKVSPR 130 140 150 160 170 180 AFRDACREFA ASQVDGQRED FKRLGVLGDW DNPYLTMDYR TEADILRALG RIIQRGHVTR 190 200 210 220 230 240 GFKPVHWCAD CGSALAEAEV EYEEKTSPAI DVRFAVLEPE ELDRRAGLGG EAAAAGRVAI 250 260 270 280 290 300 PIWTTTPWTL PANQAVALHP ELEYVVVAFD DELLVLAAEL VESAMARYEV DDYRVVGRCD 310 320 330 340 350 360 GAVLEGLRLA HPFLEREVPV ILGGHVTTDG GTGAVHTAPG HGQDDYVVGQ QYDLPTDNPV 370 380 390 400 410 420 DGNGVFLPDT PFFAGQHVFK ANPKVVDLLA ERGALLHHEP YRHSYPHCWR HKTPILFRAT 430 440 450 460 470 480 PQWFISLDKA GMREHAMAAI KGVSWHPEWG QARIESMVNG RPDWCISRQR NWGVPIALFV 490 500 510 520 530 540 DKRSGEPHPE SERLIEAVAR RVEEAGVDAW FELDPAELLG ADAERYEKVT DILDVWFDSG 550 560 570 580 590 600 VTHATVLERR DELQVPADLY LEGSDQHRGW FQSSLLTSVG VRETAPYKGV LTHGFTVDEK 610 620 630 640 650 660 GHKMSKSRGN VVAPQKVMDT LGADILRLWV ASSDYSAEMA VSDGILKRTA DAYRRMRNTA 670 680 690 700 710 720 RFLLANLNGF EPAEHAVAPP DMLPLDRWAV DRAYLLQQQV REAYERYEFH RIYQMVHNFC 730 740 750 760 770 780 VVDLGGFYLD VIKDRQYTTK PDSLARRSCQ TALWHVAEGL VRWLAPIISF TAEEIWEHLP 790 800 810 820 830 840 GERSDSVLLE TWYEGLFPLD DSDPFGRAFW DDVLAVRAGV NRELEQLRND KVIGASLQAE 850 860 870 880 890 900 VQLFCPPELK AKLDRLGDEL RFVLITSEAR VEDLERAPVE SVEVPGENGQ GFRLFAAASQ 910 920 930 940 HPKCTRCWHH RPDVGHHADH PELCGRCVSN VDGEGETRHY A

References

[1]

"Complete sequence of Alkalilimnicola ehrilichei MLHE-1." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MLHE-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000453 Genomic DNA. Translation: ABI56206.1.
RefSeq	YP_741696.1. NC_008340.1.
3D structure databases
ProteinModelPortal	Q0AAD1.
ModBase	Search...
Protein-protein interaction databases
STRING	187272.Mlg_0852.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABI56206; ABI56206; Mlg_0852.
GeneID	4270789.
KEGG	aeh:Mlg_0852.
PATRIC	20860933. VBIAlkEhr114327_0851.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0060.
HOGENOM	HOG000246402.
KO	K01870.
OMA	KQVLTHG.
ProtClustDB	PRK05743.
Enzyme and pathway databases
BioCyc	AEHR187272:GHAX-908-MONOMER.
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_ALHEH

Accession

Primary (citable) accession number: Q0AAD1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program