Q81E30 (SYI2_BACCR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Isoleucine--tRNA ligase 2
EC=6.1.1.5

Alternative name(s):
Isoleucyl-tRNA synthetase 2
Short name=IleRS 2

Gene names

Name:	ileS2
Ordered Locus Names:	BC_2164

Organism

Bacillus cereus (strain ATCC 14579 / DSM 31) [Reference proteome] [HAMAP]

Taxonomic identifier

226900 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group › Bacillus cereus

Protein attributes

Sequence length	1033 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_02003
Catalytic activity	ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02003
Cofactor	Zinc By similarity. HAMAP-Rule MF_02003
Subunit structure	Monomer By similarity. HAMAP-Rule MF_02003
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_02003.
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_02003
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily.
Sequence caution	The sequence AAP09130.1 differs from that shown. Reason: Erroneous initiation.

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 – 1033	1033	Isoleucine--tRNA ligase 2 HAMAP-Rule MF_02003		PRO_0000098517
Regions
	Motif	47 – 57	11	"HIGH" region HAMAP-Rule MF_02003
	Motif	590 – 594	5	"KMSKS" region HAMAP-Rule MF_02003
Sites
	Binding site	593	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q81E30 [UniParc]. Last modified December 20, 2005. Version 2. Checksum: 3BDB95615706F6A2	FASTA	1,033	118,308
	10 20 30 40 50 60 MEKVDVKESA VGREMRIRKQ WNEQNIFEQS IQNREGAQSF VFYEGPPTAN GLPHVGHALG 70 80 90 100 110 120 RTIKDLVARY KTMAGYKVLR KAGWDTHGLP VELGVEKQLG ISGKHEIEEY GIEPFIQKCK 130 140 150 160 170 180 ESVFTYEKQW REFTESIGYW VDMDDPYVTL KNPYIESVWH ILGTIHEKGL LYKGHRVSPY 190 200 210 220 230 240 CPSCQTSLSS HEVAQGYKTV KDLSATVKFK VKDSENEYFL GWTTTPWTLP ANVALAVHPN 250 260 270 280 290 300 MEYVKAKQES HVYIVAKERV QEVLKENYEV LSVHKGEELL NTSYTAPFPM KEVTNGYRVI 310 320 330 340 350 360 AADFVTGDSG TGLVHIAPAY GEDDYRVVQS EGLSFLHVVD EKGEYTEAVP FLKGKFVKDC 370 380 390 400 410 420 DVDIVRYLAK EGLLYHKEKY EHSYPHCWRC DSPLLYYAGE SWLIRTTAIK DTFLQNNDSV 430 440 450 460 470 480 TWYPDHMKHG RFGKFLENMV DWNISRNRYW GTPLNVWECE SCDHQFAPKS IAELRKHSTK 490 500 510 520 530 540 ETPEDLELHK PYVDEVQVCC GKCGGTMNRT PEVIDVWFDS GSMPFAQYHY PFENKELFEE 550 560 570 580 590 600 QFPADVIAEG IDQTRGWFYS LLAVSALYTG KVPYKRVLSL GHVLDEEGQK MSKSKGNALD 610 620 630 640 650 660 PVDLVDKFGA DALRWALLVD SAPWNAKRFS ERTVLEAKSK FVDTLVNVYS FYVLYANLDE 670 680 690 700 710 720 YNPKETYDVK LTKLDEWVLS RLHSTTKKVR TALDDYQFTN AAREIAALVD EVSNWYVRRS 730 740 750 760 770 780 RNRFWESGMN AEKAAAYETL HEVLVTISKL IAPFTPFVAE DIHLNLEGSS VHLADYPVVN 790 800 810 820 830 840 ESLLQPKLEA EMDAVLQVVE LGRSNRNQHS LKVKQPLAEL VLLEHNENDM DWESYRDIVM 850 860 870 880 890 900 DELNVKAFHV ELDETKYTSY QLKLNFKTAG PKFGKNVNAV NGWLKQLSQE EVQNFVSTGR 910 920 930 940 950 960 AVYEATPEGE VVVTGEDVLV EKVAKSGFSN TTNGQYTVML DTNVTEELLQ EGVAREFIRA 970 980 990 1000 1010 1020 VQEYRKQLNL PVNLRVDIIL DTEEELQRTL TNHKDLLEEN LLVKQFTFGH LTNEDDELSL 1030 GETKLRIKLS AAN

References

[1]

"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis." Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C. Nature 423:87-91(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016877 Genomic DNA. Translation: AAP09130.1. Different initiation.
RefSeq	NP_831929.1. NC_004722.1.
3D structure databases
ProteinModelPortal	Q81E30.
ModBase	Search...
Protein-protein interaction databases
STRING	226900.BC2164.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAP09130; AAP09130; BC_2164.
GeneID	1204513.
KEGG	bce:BC2164.
PATRIC	32600157. VBIBacCer54481_2186.
Phylogenomic databases
eggNOG	COG0060.
KO	K01870.
OMA	SRSRYWG.
ProtClustDB	PRK06039.
Enzyme and pathway databases
BioCyc	BCER226900:GJEU-2164-MONOMER.
Family and domain databases
Gene3D	3.40.50.620. 2 hits. 3.90.740.10. 1 hit.
HAMAP	MF_02003. Ile_tRNA_synth_type2.
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR002300. aa-tRNA-synth_Ia. IPR002301. Ile-tRNA-ligase. IPR023586. Ile-tRNA-ligase_type2. 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]
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

SYI2_BACCR

Accession

Primary (citable) accession number: Q81E30

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	December 20, 2005
Last modified:	May 1, 2013
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program