Q1JKZ4 (Q1JKZ4_STRPC) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Isoleucine--tRNA ligase HAMAP-Rule MF_02002
EC=6.1.1.5 HAMAP-Rule MF_02002

Alternative name(s):
Isoleucyl-tRNA synthetase HAMAP-Rule MF_02002

Gene names

Name:	ileS HAMAP-Rule MF_02002 EMBL ABF32425.1
Ordered Locus Names:	MGAS9429_Spy1238

Organism

Streptococcus pyogenes serotype M12 (strain MGAS9429) [Complete proteome] [HAMAP] EMBL ABF32425.1

Taxonomic identifier

370551 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus › Streptococcus pyogenes › Streptococcus pyogenes serotype M12

Protein attributes

Sequence length	933 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). SAAS SAAS023585 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. HAMAP-Rule MF_02002

Ontologies

Keywords
Biological process	Protein biosynthesis SAAS SAAS023585 HAMAP-Rule MF_02002
Cellular component	Cytoplasm HAMAP-Rule MF_02002
Ligand	ATP-binding SAAS SAAS023585 HAMAP-Rule MF_02002 Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase SAAS SAAS023585 HAMAP-Rule MF_02002 EMBL ABF32425.1 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Motif	57 – 67	11	"HIGH" region By similarity HAMAP-Rule MF_02002
	Motif	595 – 599	5	"KMSKS" region By similarity HAMAP-Rule MF_02002
Sites
	Binding site	554	1	Aminoacyl-adenylate By similarity HAMAP-Rule MF_02002
	Binding site	598	1	ATP By similarity HAMAP-Rule MF_02002

Sequences

	Sequence		Length	Mass (Da)
	Q1JKZ4 [UniParc]. Last modified June 13, 2006. Version 1. Checksum: 22001A131679F834	FASTA	933	105,065
	10 20 30 40 50 60 MKLKETLNLG KTAFPMRAGL PNKEPQWQAA WEQAELYKKR QELNAGKPAF HLHDGPPYAN 70 80 90 100 110 120 GNIHVGHALN KISKDIIVRS KSMSGFQAPY VPGWDTHGLP IEQVLAKQGI KRKEMDLAEY 130 140 150 160 170 180 LEMCRQYALS QVDKQRDDFK RLGVSADWEN PYVTLDPQFE ADQIRVFGAM AEKGYIYRGA 190 200 210 220 230 240 KPVYWSWSSE SALAEAEIEY HDIDSTSLYY ANKVKDGKGI LDTNTYIVVW TTTPFTVTAS 250 260 270 280 290 300 RGLTVGPDMD YLVVKPAGSD RQYVVAEGLL DSLAGKFGWE SFETLASHKG ADLEYIVTEH 310 320 330 340 350 360 PWDTDVEELV ILGDHVTLES GTGIVHTAPG FGEDDYNVGT KYKLEVAVTV DERGLMMENA 370 380 390 400 410 420 GPDFHGQFYN KVTPIVIDKL GDLLLAQEVI NHSYPFDWRT KKPIIWRAVP QWFASVSDFR 430 440 450 460 470 480 QDILDEIEKT TFHPSWGETR LYNMIRDRGD WVISRQRAWG VPLPIFYAED GTAIMTKEVT 490 500 510 520 530 540 DHVADLFQEN GSIIWWQKEA KDLLPEGFTH PGSPNGEFTK ETDIMDVWFD SGSSWNGVMN 550 560 570 580 590 600 ARENLSYPAD LYLEGSDQYR GWFNSSLITS VAVNGHAPYK AILSQGFVLD GKGEKMSKSK 610 620 630 640 650 660 GNIISPNDVA KQYGADILRL WVASVDTDND IRVSMEILGQ VSETYRKIRN TLRFLIANTS 670 680 690 700 710 720 DFNPATDTVA YADLGAVDKY MTIVFNQLVA TITDAYERYD FMAIYKAVVN FVTVDLSAFY 730 740 750 760 770 780 LDFAKDVVYI EAANSLERRR MQTVFYDILV KITKLLTPIL PHTTEEIWSY LEYESEAFVQ 790 800 810 820 830 840 LAEMPVAETF SAQEDILEAW SAFMTLRTQA QKALEEARNA KIIGKSLEAH LTIYASEEVK 850 860 870 880 890 900 TLLTALDSDI ALLLIVSQLT IADLADAPAD AVAFEGVAFM VEHAIGEVCE RSRRIDPTTR 910 920 930 MRSYNAFVCD HSAKIIEENF PEAVAEGFEE SGK

References

[1]

"Molecular genetic anatomy of inter- and intraserotype variation in the human bacterial pathogen group A Streptococcus." Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R., Musser J.M. Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MGAS9429.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000259 Genomic DNA. Translation: ABF32425.1.
RefSeq	YP_596969.1. NC_008021.1.
3D structure databases
ProteinModelPortal	Q1JKZ4.
SMR	Q1JKZ4. Positions 1-918.
ModBase	Search...
Protein-protein interaction databases
STRING	370551.MGAS9429_Spy1238.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABF32425; ABF32425; MGAS9429_Spy1238.
GeneID	4061215.
KEGG	spk:MGAS9429_Spy1238.
PATRIC	19753527. VBIStrPyo37061_1253.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0060.
HOGENOM	HOG000246402.
KO	K01870.
OMA	KQVLTHG.
ProtClustDB	PRK13804.
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. [Graphical view]
PANTHER	PTHR11946:SF9. PTHR11946:SF9. 1 hit.
Pfam	PF08264. Anticodon_1. 1 hit. PF00133. tRNA-synt_1. 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

Q1JKZ4_STRPC

Accession

Primary (citable) accession number: Q1JKZ4

Entry history

Integrated into UniProtKB/TrEMBL:	June 13, 2006
Last sequence update:	June 13, 2006
Last modified:	May 1, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)