C0QP76 (SYI_PERMH) 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:	PERMA_0684

Organism

Persephonella marina (strain DSM 14350 / EX-H1) [Complete proteome] [HAMAP]

Taxonomic identifier

123214 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Aquificae › Aquificae › Aquificales › Hydrogenothermaceae › Persephonella › Persephonella marina

Protein attributes

Sequence length	947 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 – 947	947	Isoleucine--tRNA ligase HAMAP-Rule MF_02002		PRO_1000216243
Regions
	Motif	57 – 67	11	"HIGH" region HAMAP-Rule MF_02002
	Motif	609 – 613	5	"KMSKS" region HAMAP-Rule MF_02002
Sites
	Metal binding	908	1	Zinc By similarity
	Metal binding	911	1	Zinc By similarity
	Metal binding	926	1	Zinc By similarity
	Metal binding	929	1	Zinc By similarity
	Binding site	568	1	Aminoacyl-adenylate By similarity
	Binding site	612	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	C0QP76 [UniParc]. Last modified May 5, 2009. Version 1. Checksum: DE47D4F7B6D5933A	FASTA	947	110,771
	10 20 30 40 50 60 MEWKDTLNLP KTAFPMKGNL PNKEPEIIKK WEEIDLYKRL REERKGKEKY ILHDGPPYAN 70 80 90 100 110 120 GNIHLGHALN KILKDILVKY ESMKGKDAPF VPGWDCHGLP IEQQVEKLLK KEKKRKEDLS 130 140 150 160 170 180 KSEFRKLCRE YALKYVNIQR EEFKRLGIIG NWEKPYLTMR PSYQAQEIRE LGKIFRKGIA 190 200 210 220 230 240 YRGKKPVYWC IYDKTAEAEA EVEYKEKKDP SIYVAFELVE SPFDIKEKVY AVIWTTTPWT 250 260 270 280 290 300 LPANLGIMVN PDFDYLFLRS EDKVYIVAKD LLESFSEKTG IEGEVIKEVK GRELEFLEYR 310 320 330 340 350 360 HPFIDRVSKI YLSEFVELGT GTGLVHMAPG HGQEDYIIGQ RYGVEAFAPV DDEGRFTDEA 370 380 390 400 410 420 PEFIQGLRVF EANERIVEKL RENGVLLHHE TVKHSYPHCW RCKNPVIFRA TPQWFISMDG 430 440 450 460 470 480 ITEKGETLRG EALKEIERVK WIPHWGENRI KSMIENRPDW CISRQRSWGV PIAVFYCKRC 490 500 510 520 530 540 GNIIDDEKVF EHIADLVEKD EFGADIWFER EAEELLPEGY RCPKCDGEEF KKEEDILDVW 550 560 570 580 590 600 FDSGVSHASV LKSGFWDELK WPADMYLEGS DQHRGWFQSS LLEGVASYGR APYDAVLTHG 610 620 630 640 650 660 FILDEKGNKM SKSLGNVIPP EKIIKMYGAD ILRLWVVSED YTEDIKIGMN LLKSIADDYR 670 680 690 700 710 720 KIRNTFRYFL GNLYDFDANK DRVPYENLLE IDRWMLSKLQ RLIDRSHSAY SNYRFHKIYH 730 740 750 760 770 780 EIKRFVIVDL SAVYLDILKD RLYVYAPDSL ERRSAQTVLY ELLDSLTKLL APILSFTTEE 790 800 810 820 830 840 IWGYVREINP SVKESIHLEE MPVVNQDYID PELEETYEKL MKVRDDILKA LEEARRSDII 850 860 870 880 890 900 RHPYEAKVVL SLPDEYRSVV EKRIDWIKFF FTVSQVELSD QAEGDVIIGG EKVEGGKIAV 910 920 930 940 KKASGEKCPR CWIYDESVGK DGQPVCDRCM EQLERMEIKI SDIEEAK

References

[1]

"Complete and draft genome sequences of six members of the Aquificales." Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S., Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A. J. Bacteriol. 191:1992-1993(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 14350 / EX-H1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001230 Genomic DNA. Translation: ACO03207.1.
RefSeq	YP_002730472.1. NC_012440.1.
3D structure databases
ProteinModelPortal	C0QP76.
ModBase	Search...
Protein-protein interaction databases
STRING	123214.PERMA_0684.
Proteomic databases
PRIDE	C0QP76.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACO03207; ACO03207; PERMA_0684.
GeneID	7674544.
KEGG	pmx:PERMA_0684.
PATRIC	22914835. VBIPerMar119911_0726.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0060.
HOGENOM	HOG000246402.
KO	K01870.
OMA	KQVLTHG.
ProtClustDB	PRK05743.
Enzyme and pathway databases
BioCyc	PMAR123214:GIZP-683-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_PERMH

Accession

Primary (citable) accession number: C0QP76

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 22, 2009
Last sequence update:	May 5, 2009
Last modified:	May 1, 2013
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program