B9MRZ5 (SYI_CALBD) 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:	Athe_1349

Organism

Caldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / Z-1320) (Anaerocellum thermophilum) [Complete proteome] [HAMAP]

Taxonomic identifier

521460 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacterales Family III. Incertae Sedis › Caldicellulosiruptor › Caldicellulosiruptor bescii

Protein attributes

Sequence length	920 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 – 920	920	Isoleucine--tRNA ligase HAMAP-Rule MF_02002		PRO_1000189120
Regions
	Motif	57 – 67	11	"HIGH" region HAMAP-Rule MF_02002
	Motif	601 – 605	5	"KMSKS" region HAMAP-Rule MF_02002
Sites
	Metal binding	890	1	Zinc By similarity
	Metal binding	893	1	Zinc By similarity
	Metal binding	910	1	Zinc By similarity
	Metal binding	913	1	Zinc By similarity
	Binding site	560	1	Aminoacyl-adenylate By similarity
	Binding site	604	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	B9MRZ5 [UniParc]. Last modified March 24, 2009. Version 1. Checksum: 64EB550849406D86	FASTA	920	107,205
	10 20 30 40 50 60 MDWSQTLNLP KTDFPMRANL AQREPQFLKF WQENDIFKKM LEKNKNNKKF ILHDGPPYAN 70 80 90 100 110 120 GDIHLGHALN KVLKDIVNKY KSLQGYYTPY IPGWDTHGLP IEQQVIKKLE VNRHEVDPVE 130 140 150 160 170 180 FRKKCKEFAL SYIDIQRQQF KRLGVFGEWE NPYMTLDPKF EARQIRVFGE MAKKGYIYKG 190 200 210 220 230 240 LKPVYWCPSC ETALAEAEIE YQEDRTYSIY VKFEVIDDKG LFSNLPIGDK KVYIVIWTTT 250 260 270 280 290 300 TWTLPGNLAI ALNADFDYSL IDIGNEILVV ASELVERVMK TNKIEQYKEI ARFKGKDLEY 310 320 330 340 350 360 VKCKHPFLDR TSLVILGEHV TLEAGTGCVH TAPGHGEEDF EVCQRYNIHV IVPVDNKGYL 370 380 390 400 410 420 TKEAGKFAGL FYEDSNKEIA KELEASGHLL GVEKITHQYP HCWRCKNPVI FRATEQWFAS 430 440 450 460 470 480 VKGFRDQALK AVDDVKWVPE WGRDRIYNMI VDRQDWCISR QRIWGVPIPI FYCKNCRKEL 490 500 510 520 530 540 ITDETIDYIA KIFEKEGSDA WFSKDVKELL PEGVKCPVCG CSEFEKETDI MDVWFDSGSS 550 560 570 580 590 600 HAYVLESRED LEWPCDMYLE GNDQYRGWFQ SSLLTAVATK GRAPYRIVLT HGFVVDGEGK 610 620 630 640 650 660 KMSKSEGNVI SPFDIINEFG ADILRLWCVS ADYTTDMRIS KDIIKQLTEI YRKIRNTARF 670 680 690 700 710 720 LLGNLYDFNP KTDKVGYENL KEIDKWALQR LYKLIEKVTK AYEEYDYNQV YHLVHNFCVI 730 740 750 760 770 780 DMSNLYLDIN KDRLYASKSE SLDRRSAQTV MYEILIALTI LIAPILSFTA EEIWQNIIFK 790 800 810 820 830 840 EEDAESVFLT RWPSINEDIL RDEALREKWD KIIEIKDIVS KQLEIARNEK LIGSSLDSKV 850 860 870 880 890 900 KIFAKCDIKR FIEENKDIIQ EVLIVSQLDV EESDSDQIKV EVYKADGSKC ERCWKFDTMV 910 920 GKNEESLNVC PRCYEVVKSK

References

[1]

"Complete sequence of chromosome of Anaerocellum thermophilum DSM 6725." Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Kataeva I., Adams M.W.W. Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-1888 / DSM 6725 / Z-1320.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001393 Genomic DNA. Translation: ACM60449.1.
RefSeq	YP_002573222.1. NC_012034.1.
3D structure databases
ProteinModelPortal	B9MRZ5.
ModBase	Search...
Protein-protein interaction databases
STRING	521460.Athe_1349.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACM60449; ACM60449; Athe_1349.
GeneID	7408930.
KEGG	ate:Athe_1349.
PATRIC	20899814. VBIAnaThe135187_1420.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0060.
HOGENOM	HOG000246402.
KO	K01870.
OMA	KQVLTHG.
ProtClustDB	CLSK2473335.
Enzyme and pathway databases
BioCyc	CBES521460:GH8H-1380-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_CALBD

Accession

Primary (citable) accession number: B9MRZ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	March 24, 2009
Last modified:	May 1, 2013
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program