B9DUU7 (B9DUU7_STRU0) 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 CAR42801.1
Ordered Locus Names:	SUB1284

Organism

Streptococcus uberis (strain ATCC BAA-854 / 0140J) [Complete proteome] [HAMAP] EMBL CAR42801.1

Taxonomic identifier

218495 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus › Streptococcus uberis

Protein attributes

Sequence length	931 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 SAAS SAAS002301
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 HAMAP-Rule MF_02002 SAAS SAAS002301
Cellular component	Cytoplasm HAMAP-Rule MF_02002
Ligand	ATP-binding HAMAP-Rule MF_02002 SAAS SAAS002301 Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase HAMAP-Rule MF_02002 SAAS SAAS002301 EMBL CAR42801.1 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)
	B9DUU7 [UniParc]. Last modified March 24, 2009. Version 1. Checksum: 89969FB79AAD126D	FASTA	931	105,427
	10 20 30 40 50 60 MKLKETLNLG KTAFPMRAGL PNKEPLWQAA WDEAQIYQKR QKLNEGKPSF HLHDGPPYAN 70 80 90 100 110 120 GNIHVGHALN KISKDIIVRA KSMSGYNAPY VPGWDTHGLP IEQVLAKKGI KRKEMDLAEY 130 140 150 160 170 180 LEMCRDYALS QVDKQRQDFK RLGVSADWDN PYVTLDPAYE ADQVRVFGAM ADKGYIYRGA 190 200 210 220 230 240 KPVYWSWSSE SALAEAEIEY HDIDSTSLYY ANKVKDGKGI LDTDSYIVVW TTTPFTVTAS 250 260 270 280 290 300 RGLTVGPDMD YVLVQPASTS KKYLVAEGLL DSLAPKFAWT DFEILSHHKG SELEYIVTEH 310 320 330 340 350 360 PWDSDVDELV ILGDHVTLDS GTGIVHTAPG FGEDDYNVGT KYKLEVAVTV DERGMMMENA 370 380 390 400 410 420 GPDFQGQFYD KVLPTVIEKL GDLLLAKEVI NHSYPFDWRT KKPIIWRAVP QWFASVSDFR 430 440 450 460 470 480 QEILDEIEKT TFHPSWGKTR LYNMIRDRGD WVISRQRAWG VPLPIFYAED GTAIMTKEVT 490 500 510 520 530 540 DHVANLFEKE GSIIWWKKEA KELLPEDFSH PGSPNGEFTK ETDIMDVWFD SGSSWNGVMN 550 560 570 580 590 600 AREQLSYPAD LYLEGSDQYR GWFNSSLITS VAVNGHAPYK AVLSQGFVLD GKGEKMSKSK 610 620 630 640 650 660 GNIISPNDVA KQYGAEILRL WVTSVDTDND VRVSMDILGQ VSETYRKIRN TLRFLIANTS 670 680 690 700 710 720 DFNPNTNRVA YEELAPVDKY LTIKFNKLVE VFNNSYENYD FMAIYKAVVN FVTIDLSAFY 730 740 750 760 770 780 LDFAKDVVYI EAANSLARRR MQTVFYDILV KITKLLTPIL PHTAEEIWSY LEFEEEEFVQ 790 800 810 820 830 840 LTEMPVAEIF EGEEDILSAW DAFMTLRTQA QKALEEARNE KVIGKSLEAH LTIYASDEVK 850 860 870 880 890 900 TLLTALDSDI ALLMIVSQLT IADFADAPTN AISFENVAFT VDHAVGEVCE RSRRVDPTTR 910 920 930 MRSYGAFVCD ASAKIIEENF PEAVSQGFES N

References

[1]

"Evidence for niche adaptation in the genome of the bovine pathogen Streptococcus uberis." Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A., Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R., Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D., Parkhill J. BMC Genomics 10:54-54(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-854 / 0140J.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM946015 Genomic DNA. Translation: CAR42801.1.
RefSeq	YP_002562588.1. NC_012004.1.
3D structure databases
ProteinModelPortal	B9DUU7.
ModBase	Search...
Protein-protein interaction databases
STRING	218495.SUB1284.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAR42801; CAR42801; SUB1284.
GeneID	7391876.
KEGG	sub:SUB1284.
PATRIC	19808276. VBIStrUbe20775_1254.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0060.
HOGENOM	HOG000246402.
KO	K01870.
OMA	KQVLTHG.
ProtClustDB	PRK13804.
Enzyme and pathway databases
BioCyc	SUBE218495:GJ7D-1318-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. [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

B9DUU7_STRU0

Accession

Primary (citable) accession number: B9DUU7

Entry history

Integrated into UniProtKB/TrEMBL:	March 24, 2009
Last sequence update:	March 24, 2009
Last modified:	May 29, 2013
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)