A1AW09 (SYI_RUTMC) 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:	Rmag_0340

Organism

Ruthia magnifica subsp. Calyptogena magnifica [Complete proteome] [HAMAP]

Taxonomic identifier

413404 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › unclassified Gammaproteobacteria › sulfur-oxidizing symbionts › Candidatus Ruthia magnifica

Protein attributes

Sequence length	922 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. HAMAP-Rule MF_02002
Subunit structure	Monomer By similarity. HAMAP-Rule MF_02002
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_02002.
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 – 922	922	Isoleucine--tRNA ligase HAMAP-Rule MF_02002		PRO_1000022113
Regions
	Motif	58 – 68	11	"HIGH" region HAMAP-Rule MF_02002
	Motif	593 – 597	5	"KMSKS" region HAMAP-Rule MF_02002
Sites
	Metal binding	885	1	Zinc By similarity
	Metal binding	888	1	Zinc By similarity
	Metal binding	905	1	Zinc By similarity
	Metal binding	908	1	Zinc By similarity
	Binding site	552	1	Aminoacyl-adenylate By similarity
	Binding site	596	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1AW09 [UniParc]. Last modified January 23, 2007. Version 1. Checksum: CF5316BC7F9E8F8A	FASTA	922	105,262
	10 20 30 40 50 60 MSDYKSSLNL PATQFPMKAN LANREGGFLK KWQNDGLYDQ IRQQNQGKPK FVLHDGPPYA 70 80 90 100 110 120 NGDIHIGHTV NKVLKDMIVK SKSLSGFDAP YVPGWDCHGL PIEFNVEKKY GKVGVKIDAS 130 140 150 160 170 180 TFRSKCRKYA DQQVLKQKQD FQRLGILSDW DNPYLTKDFQ YESDIVRALG RIVKNGHVSK 190 200 210 220 230 240 GYKPVHWCTE CGSALAETEV EYKDNQSEAI DVKFRIIDDS VFNMNKPVSV VIWTTTPWTL 250 260 270 280 290 300 PANEAVALHP ELNYVLVDIG DEYLLLAQAL VETSISRYGI EATIGEQTFS GSELEGLKIK 310 320 330 340 350 360 HPFYDKQVPI ILGEYVTIDA GTGAVHTAPA HGQEDFIVGL KYNLPVECLV DIKGVFFKET 370 380 390 400 410 420 ELLGGQFIFK ANDSVIEILK QANTLVKHES LMHSYPHCWR HKTPVIFRAT PQWFISMQKN 430 440 450 460 470 480 GLIDTVNREI SKVQWMPDWG KKRIELMMDS RPDWCISRQR FWGVPITLFV HKQTGELHPN 490 500 510 520 530 540 TQALFVSIAN RIEKEGIEAW FKSDAQDFIG NDANDYDKTT DILDVWFDSG VSHFTVLKAR 550 560 570 580 590 600 KELSNVADLY LEGADQHRGW FQLSLISSVA INGKAPYKNV LTHGFVVDKN GKKMSKSLGN 610 620 630 640 650 660 VMSPQKIVNN LGADVLRLWI ASTDYTSEMT VGDEILKRSA DSYRRIRNTM RFMLANMQAF 670 680 690 700 710 720 NPVEHLLDNK QMLDLDKWIV AKTANLQTQI IKAYEQYNFH HVVQLILNFC SNDLGGFYLD 730 740 750 760 770 780 VIKDRQYTTQ ANSLARRSAQ SALHHITEAM VRWLAPILSF TAEEIWQNMP SEKNTSIFLA 790 800 810 820 830 840 SWYQDLTFGY ENKAIDITRE ISPFIRKQME GMRGEKIIGS SLESEIDIYC ETDIFSTLSQ 850 860 870 880 890 900 LDDELRFIFI TSYIRIHSLN EKNDDCIKAI EGVFIKVSKS RHEKCVRCWH HREDVGNNAK 910 920 HPELCGRCVE NVDGKGEIRK FA

References

[1]

"The Calyptogena magnifica chemoautotrophic symbiont genome." Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J., Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M., Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M. Science 315:998-1000(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000488 Genomic DNA. Translation: ABL02116.1.
RefSeq	YP_903587.1. NC_008610.1.
3D structure databases
ProteinModelPortal	A1AW09.
ModBase	Search...
Protein-protein interaction databases
STRING	413404.Rmag_0340.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABL02116; ABL02116; Rmag_0340.
GeneID	4554628.
KEGG	rma:Rmag_0340.
PATRIC	32000323. VBICanRut45856_0386.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0060.
HOGENOM	HOG000246402.
KO	K01870.
OMA	KQVLTHG.
ProtClustDB	PRK05743.
Enzyme and pathway databases
BioCyc	CRUT413404:GHM7-353-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_RUTMC

Accession

Primary (citable) accession number: A1AW09

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program