Reviewed, UniProtKB/Swiss-Prot Q81R75 (SYI2_BACAN)

Names and origin

Protein names

Recommended name:
    Isoleucyl-tRNA synthetase 2
    EC=6.1.1.5
Alternative name(s):
    Isoleucine--tRNA ligase 2
      Short name=IleRS 2

Gene names

Name:	ileS2
Ordered Locus Names:	BA_2181, GBAA_2181, BAS2027

Organism

Bacillus anthracis [Complete proteome] [HAMAP]

Taxonomic identifier

1392 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

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 MF_02003
Catalytic activity	ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP MF_02003
Cofactor	Zinc By similarity. HAMAP MF_02003
Subunit structure	Monomer By similarity. HAMAP MF_02003
Subcellular location	Cytoplasm By similarity HAMAP 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 MF_02003
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 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
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP 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	Isoleucyl-tRNA synthetase 2 HAMAP MF_02003		PRO_0000098515
Regions
	Motif	47 – 57	11	"HIGH" region HAMAP MF_02003
	Motif	590 – 594	5	"KMSKS" region HAMAP MF_02003
Sites
	Binding site	593	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q81R75-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 4E393F801CC74A8B	FASTA	1,033	118,653
	10 20 30 40 50 60 MKKVDVKESA VGREMRIRKQ WNEQNIFEQS IQNREGAQSF VFYEGPPTAN GLPHVGHALG 70 80 90 100 110 120 RTIKDVVARY KTMAGYKVLR KAGWDTHGLP VELGVEKQLG ISGKHEIEEY GIEPFIKKCK 130 140 150 160 170 180 ESVFTYEKQW REFTESIGYW VDMDDPYVTL ENPYIESVWH ILGTIHEKGL LYKGHRVSPY 190 200 210 220 230 240 CPSCQTSLSS HEVAQGYKTV KDLSATVKFK VKDSENEYFL GWTTTPWTLP ANVALAVHPN 250 260 270 280 290 300 MEYVKAKQEG HVYIVAKERV QDVLKENYEV LSVHKGEELL NISYTAPFPM KEVTNGYRVI 310 320 330 340 350 360 GADFVTADSG TGLVHIAPAY GEDDYRVVQS EGLSFLHVVD EKGEYTEAVP FLKGKFVKDC 370 380 390 400 410 420 DVDIVRYLAK EDLLYHKEKY EHSYPHCWRC DSPLLYYAGE SWLIRTTAIK DTFLQNNDTV 430 440 450 460 470 480 TWYPDHMKHG RFGKFLENMV DWNISRNRYW GTPLNVWECE RCDHQFAPKS IADLRKHSMK 490 500 510 520 530 540 ETPEDLELHK PYVDEVQVCC EKCGSTMNRT PEVIDVWFDS GSMPFAQYHY PFENKELFEE 550 560 570 580 590 600 QFPADVIAEG IDQTRGWFYS LLAVSALYTG KVPYKRVLSL GHVLDEEGQK MSKSKGNALD 610 620 630 640 650 660 PVDLVGKFGA DALRWALLVD SALWNAKRFS ERTVLEAKSK FVDTLVNVYS FYVLYANLDE 670 680 690 700 710 720 YNPNETYDVK RTKLDEWVLS RLHSTTKKVR TALDDYQFTN AAREIAALVD EVSNWYVRRS 730 740 750 760 770 780 RNRFWESGMN AEKAAAYETL HDVLVTISKL IAPFTPFVAE DVHLNLTGSS VHLEDYPVVN 790 800 810 820 830 840 ESLLQPKLEA EMDAVLQVVE LGRSNRNQHS LKVKQPLAEL VLLEHNENDM DWESYRDIVM 850 860 870 880 890 900 DELNVKAFHV ELDETKYTSY QLKLNFKKAG PKFGKNVNAV NGWLKQLSQD EVQNFVSTER 910 920 930 940 950 960 AVYEVAPGEE IVVTTEDVLV EKVAKSGFSN TTNGQYTVML DTNVTEELLQ EGVAREFIRA 970 980 990 1000 1010 1020 VQEYRKQLNL PVNLRVDVIL DTEEELQQTL TNHKELLEEN LLVKQFTFGH LTNEDDELSL 1030 GETKVRIKLS TAQ

References

[1]	"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M. Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton.
[2]	"Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor.
[3]	"Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016879 Genomic DNA. Translation: AAP26060.1. AE017334 Genomic DNA. Translation: AAT31298.1. AE017225 Genomic DNA. Translation: AAT54341.1.
RefSeq	NP_844574.1. YP_018823.1. YP_028290.1.
3D structure databases
SMR	Q81R75. Positions 10-810.
ModBase	Search...
Genome annotation databases
GeneID	1085720. 2815690. 2849029.
GenomeReviews	Gene locus BA_2181 in contig AE016879_GR. Gene locus BAS2027 in contig AE017225_GR. Gene locus GBAA_2181 in contig AE017334_GR.
KEGG	ban:BA2181. bar:GBAA2181. bat:BAS2027.
TIGR	BA_2181. GBAA_2181.
Phylogenomic databases
HOGENOM	HBG577712.
OMA	KENGAFT.
Enzyme and pathway databases
BioCyc	BANT260799:BAS2027-MONOMER. BANT261594:GBAA2181-MONOMER.
BRENDA	6.1.1.5. 267517.
Family and domain databases
HAMAP	MF_02003. Ile_tRNA_synth_type2. [Tree]
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR002300. aa-tRNA-synth_Ia. IPR002301. Ile-tRNA-synt_Ia. IPR015905. Ile-tRNA-synt_Ia_N. IPR018353. Isoleucyl-tRNA_synthetase. 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_Ia_edit. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHER	PTHR11946:SF9. Ile-tRNA-synt_Ia. 1 hit.
Pfam	PF08264. Anticodon_1. 1 hit. PF00133. tRNA-synt_1. 1 hit. [Graphical view]
PRINTS	PR00984. TRNASYNTHILE.
TIGRFAMs	TIGR00392. ileS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYI2_BACAN

Accession

Primary (citable) accession number: Q81R75
Secondary accession number(s): Q6HZE8, Q6KTD8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	June 1, 2003
Last modified:	February 9, 2010
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)