Q6F175 (SYI_MESFL) 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:	Mfl389

Organism

Mesoplasma florum (strain ATCC 33453 / NBRC 100688 / NCTC 11704 / L1) (Acholeplasma florum) [Reference proteome] [HAMAP]

Taxonomic identifier

265311 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Tenericutes › Mollicutes › Entomoplasmatales › Entomoplasmataceae › Mesoplasma › Mesoplasma florum

Protein attributes

Sequence length	908 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 Reference 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 – 908	908	Isoleucine--tRNA ligase HAMAP-Rule MF_02002		PRO_0000098414
Regions
	Motif	59 – 69	11	"HIGH" region HAMAP-Rule MF_02002
	Motif	595 – 599	5	"KMSKS" region HAMAP-Rule MF_02002
Sites
	Metal binding	882	1	Zinc By similarity
	Metal binding	885	1	Zinc By similarity
	Metal binding	898	1	Zinc By similarity
	Metal binding	901	1	Zinc By similarity
	Binding site	554	1	Aminoacyl-adenylate By similarity
	Binding site	598	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6F175 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 8DC53125D359C17A	FASTA	908	104,380
	10 20 30 40 50 60 MKNIYKDTLL IGQTDFDMRA GLKDKEPVIQ EMWDAKKIYD QKQKLNEGKP LFMLHDGPPY 70 80 90 100 110 120 ANGDLHIGHA LNKTLKDMII RWKNANGYLA PFIMGWDTHG LPIETAVTKM GIDRKQTPAV 130 140 150 160 170 180 EFRDMCKDYA LKQVANQANQ FKRLGIFSNS DVKYVTLTHD FEVSELRLFQ KMYEKEMVYK 190 200 210 220 230 240 ALKPIYWSPS SESALAESEI EYKDVKSPTI FVAMKVVEGN AKIDTDTEIV IWTTTPWTIP 250 260 270 280 290 300 SNQMAAVGEN IEYNIVKAND RKFILASSLV NKVAEQIGWE TFEILDTLKG PEIVGVKYAH 310 320 330 340 350 360 PLYEQKINPV VIGHHVTDEA GTGIVHTAGG FGEDDYIIVK QHGIEPFAPI DDQGKFTNEI 370 380 390 400 410 420 AEFDEKLVGV FYEDANKIVG MDLEAKQRLL KLKFVSHSYP HDWRTKKPVI YRCTSQWFIG 430 440 450 460 470 480 LDKAKNQILA NVDQITTKPE WAKKRLYQVL EDRTDWTISR QRLWGVPIVA FYDQNDKLVL 490 500 510 520 530 540 NNEILAFAID KIAELGTNAW FDKPADTFLP EAYRNKNLKK EKDILDVWFD SGSSAIALSE 550 560 570 580 590 600 RFKNLPLPYD LYLEGNDQYR GWFNASMINS TIYSGKSPYK KLISHGMTVD EKGNKMSKSL 610 620 630 640 650 660 GNGIDPIEFA NTQGADILRL WVASTDYTDD QKIGPEIIKQ IGESYRKIRN TMRFILANLF 670 680 690 700 710 720 DFDPSKDYQT NLTEVDRYAL NNLSVVKNKA SEAYDNLSYN QVYNLVVNYV TKDLSSFYLD 730 740 750 760 770 780 FIKDILYIEK NDSIRRRQVQ TVLYEQLWML IDLLRPILIH TIEEVYQAMV NLNKTDSVHL 790 800 810 820 830 840 LDNKKQDFIE SNEFVTKWNN IMVLRDDVNK ALEIAREQKI INKGFEATVK VCLKDEFKNI 850 860 870 880 890 900 ESTTELEKIF IVNSLSFTND CSGLSEQKIA FVGVELKNGT KCERCWGIFD TLINNEICER CNSVVESL

References

[1]

Birren B.W., Stange-Thomann N., Hafez N., DeCaprio D., Fisher S., Butler J., Elkins T., Kodira C.D., Major J., Wang S., Nicol R., Nusbaum C. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33453 / NBRC 100688 / NCTC 11704 / L1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017263 Genomic DNA. Translation: AAT75748.1.
RefSeq	YP_053632.1. NC_006055.1.
3D structure databases
ProteinModelPortal	Q6F175.
ModBase	Search...
Protein-protein interaction databases
STRING	265311.Mfl389.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAT75748; AAT75748; Mfl389.
GeneID	2898000.
KEGG	mfl:Mfl389.
PATRIC	22473517. VBIMesFlo3168_0389.
Phylogenomic databases
eggNOG	COG0060.
HOGENOM	HOG000246402.
KO	K01870.
OMA	KQVLTHG.
ProtClustDB	PRK05743.
Enzyme and pathway databases
BioCyc	MFLO265311:GHIB-410-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

SYI_MESFL

Accession

Primary (citable) accession number: Q6F175

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	August 16, 2004
Last modified:	May 1, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program