Reviewed, UniProtKB/Swiss-Prot Q0SM18 (SYI_BORAP)

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:	BAPKO_0886

Organism

Borrelia afzelii (strain PKo) [Complete proteome] [HAMAP]

Taxonomic identifier

390236 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group

Protein attributes

Sequence length	1042 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_02003
Cofactor	Zinc 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 2 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: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1042	1042	Isoleucyl-tRNA synthetase HAMAP MF_02003		PRO_1000022148
Regions
	Motif	48 – 58	11	"HIGH" region HAMAP MF_02003
	Motif	594 – 598	5	"KMSKS" region HAMAP MF_02003
Sites
	Binding site	597	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0SM18-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 51B78BF0D7E1C44F	FASTA	1,042	122,522
	10 20 30 40 50 60 MFKKVENKAN FPKIEEKILK FWNDNKIFEK SMKQREGCEE FTFYDGPPFA TGLPHFGHFV 70 80 90 100 110 120 PNTIKDIIPR YQTMRGKYVK RNFGWDTHGL PVEYEVEKKL GISGKYEIEN YGIENFNKEC 130 140 150 160 170 180 KKIVLRYTEE WKNIILRLGR WVDFEKGYKT MDINFMESVW WVFKSLYNKG LIYESYYVLP 190 200 210 220 230 240 YSPKLATPLS NFEVNLGEYK EVNDPSLTIK FKIKDKNEYL LAWTTTPWTL PSNLGIAVGQ 250 260 270 280 290 300 EIEYSKIFDK KKEEILILGS KKLDSYYDDE NSYTIIEKFK GSKLEGIEYE PIFNYFLEQK 310 320 330 340 350 360 DKGAFKVHMA DYVTTDDGTG IVHIAPFGEE DYRILKKHTN VDIIDPLDAE CKFTNRVKDF 370 380 390 400 410 420 QGLFVKDADK KIIENLKLRN FLFKRENYLH RYPFCYRTNY PIIYRPISSW FVNVEKIKTK 430 440 450 460 470 480 LLEVNEKINW MPAHLKKGRF GKWLENAKDW AISRNRFWGN PIPIWICSKT GKKICVGSKK 490 500 510 520 530 540 ELESLSGQKI EDLHKDKVDK ITWPSKDGGT FIRTSEVLDC WFESGAMPYA SNHYPFTNES 550 560 570 580 590 600 NFKNIFPADF IAEGLDQTRG WFYTLTILGV SLFESTAFKN VIVNGLVLSS DGRKMSKSFK 610 620 630 640 650 660 NYTDPMEVIN TFGADALRLY LIMSPVVKAD DLKYSDNGVR DVLKNIIIPI WNAYSFFTTY 670 680 690 700 710 720 AIIDKFQPPK NLNLVKNNNL DKWIISELES LKKILNNEID KYNLTKSIES LLEFIDKLNN 730 740 750 760 770 780 WYIRRSRRRF WKSENDKDKN DAYETLYYAI KTLMILLAPF IPFITEEIYQ NLKTDEDKQS 790 800 810 820 830 840 IHLNDYPKAN ENLINKTIEE KINLARKITS MARSLRSLHN IKIRMPISMI YIVTKNQNEQ 850 860 870 880 890 900 NMLIEMQEII LDEINAKEMK IKSNEEDLIT YKAKANFKEL GKKLGKDMKT VSIEISKLKN 910 920 930 940 950 960 EDIIKIINGI SYEIKVGNTK YYLSLNDIIL EREEKDNLKV INEESITIGI DSLITKELYL 970 980 990 1000 1010 1020 EGLTREFVRQ IQNLRKEKNF DVSDRINLYI ENNETLQEIL NKFEKYIKTE TLALNIIFNK 1030 1040 SKLEKKINLD DNIFTIIGIE KC

References

[1]

"Comparative genome analysis: selection pressure on the Borrelia vls cassettes is essential for infectivity." Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J., Wilske B., Platzer M. BMC Genomics 7:211-211(2006) [PubMed: 16914037] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000395 Genomic DNA. Translation: ABH02110.1.
RefSeq	YP_710286.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4227163.
GenomeReviews	Gene locus BAPKO_0886 in contig CP000395_GR.
KEGG	baf:BAPKO_0886.
NMPDR	fig|390236.5.peg.888.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0SM18.
OMA	Q0SM18. SNWYVRR.
Enzyme and pathway databases
BioCyc	BAFZ390236:BAPKO_0886-MON.
Family and domain databases
HAMAP	MF_02003. [Tree]
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR002300. aa-tRNA-synth_Ia. 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. [Graphical view]
PRINTS	PR00984. TRNASYNTHILE.
TIGRFAMs	TIGR00392. ileS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYI_BORAP

Accession

Primary (citable) accession number: Q0SM18

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	September 5, 2006
Last modified:	June 16, 2009
This is version 22 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)