Q2S9T9 (SYI_HAHCH) 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:	HCH_05933

Organism

Hahella chejuensis (strain KCTC 2396) [Complete proteome] [HAMAP]

Taxonomic identifier

349521 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Hahellaceae › Hahella › Hahella chejuensis

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_1000022075
Regions
	Motif	58 – 68	11	"HIGH" region HAMAP-Rule MF_02002
	Motif	605 – 609	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	564	1	Aminoacyl-adenylate By similarity
	Binding site	608	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2S9T9 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: 2C175D4B31DA6BFB	FASTA	941	106,642
	10 20 30 40 50 60 MSDYKHTLNL PQTDFPMRGN LPQREPDMLK RWGDIELYEK IREEFKGREK FILHDGPPYA 70 80 90 100 110 120 NGNIHLGHAV NKILKDIIVK SKTVAGYDAP YVPGWDCHGL PIEHKVETMI GRAGDKVGYK 130 140 150 160 170 180 EFRRKCREYA LEQVAKQRED FIRLGVFGDW FKPYLTLDFK TEADIIRALG KIATSGHLQK 190 200 210 220 230 240 GYKPVYWSVV GGSALAEAEV EYKDKTSNSI DVSYPAENEQ DLLSAFADAS GEGAVSIVIW 250 260 270 280 290 300 TTTPWTLPAS LAVSLGAEID YALTQCSVDG RPQRWIVAEK MLESVMARCG VEDYQVVGRC 310 320 330 340 350 360 TGQDLEGKTF LHPFYKRSIP ALLGDHVTLD AGTGVVHTAP DHGMEDFAVC NKYGIETINP 370 380 390 400 410 420 LDDRGVYRDN VELFAGEHVY KVDDHVIEVL KERGRLLSHG KITHSYAHCW RTKTPLIYRA 430 440 450 460 470 480 TPQWFISMDK QGLRDQALAE IKLVRWVPSW GQNRIEAMIE QSPDWCISRQ RTWGVPIAFF 490 500 510 520 530 540 VHKETQELHP DTARLVEEVA KQVEKTGIDA WWDINAEDLL GADAQNYEKV TDTLDVWFDS 550 560 570 580 590 600 GVTHSAVLEQ REELGQFPAD LYLEGSDQHR GWFQSSLKTA VAIKGKAPYR QVLTHGFTVD 610 620 630 640 650 660 EKGHKMSKSL GNGIEPQEVM NKLGADILRL WVAATDYSAE MVLSKNILER TADSYRRIRN 670 680 690 700 710 720 TSRFLLANIN DFDPVKDMVA MDDLLALDRW IVDRAWLLQE ELKKAYEQYN FVQVYQKVHN 730 740 750 760 770 780 FCSVELGSFY LDVIKDRQYT MKLDSLGCRS AQTAQYHVIE ALVRWIAPIL SFTAEEIWSY 790 800 810 820 830 840 IPGQRAESIF LETFYEGLQP LAEGSEMGRD YWSRLLRVRT SVNKALEEAR NAGKVKGSLT 850 860 870 880 890 900 TEVSLFATPE MQHDLNALGE ELRFVFITSG ASVFGVEDAS ESNSVATETE GLRVGIRSSE 910 920 930 940 HKKCGRCWHH REDVGAHGSH EDLCGRCIEN IDGSGEERKY A

References

[1]

"Genomic blueprint of Hahella chejuensis, a marine microbe producing an algicidal agent." Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G., Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K., Oh T.K., Kim J.F. Nucleic Acids Res. 33:7066-7073(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KCTC 2396.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000155 Genomic DNA. Translation: ABC32585.1.
RefSeq	YP_437010.1. NC_007645.1.
3D structure databases
ProteinModelPortal	Q2S9T9.
ModBase	Search...
Protein-protein interaction databases
STRING	349521.HCH_05933.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3842782.
KEGG	hch:HCH_05933.
PATRIC	22092096. VBIHahChe29232_5388.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0060.
HOGENOM	HOG000246402.
KO	K01870.
OMA	KQVLTHG.
ProtClustDB	PRK05743.
Enzyme and pathway databases
BioCyc	HCHE349521:GHAL-5743-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_HAHCH

Accession

Primary (citable) accession number: Q2S9T9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 24, 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