Q3Z7P5 (SYI_DEHE1) 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:	DET1038

Organism

Dehalococcoides ethenogenes (strain 195) [Complete proteome] [HAMAP]

Taxonomic identifier

243164 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Chloroflexi › Dehalococcoidetes › Dehalococcoidales › Dehalococcoidaceae › Dehalococcoides › Dehalococcoides mccartyi

Protein attributes

Sequence length	1014 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.
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_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 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 – 1014	1014	Isoleucine--tRNA ligase HAMAP-Rule MF_02003		PRO_0000098540
Regions
	Motif	48 – 58	11	"HIGH" region HAMAP-Rule MF_02003
	Motif	628 – 632	5	"KMSKS" region HAMAP-Rule MF_02003
Sites
	Binding site	631	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3Z7P5 [UniParc]. Last modified September 27, 2005. Version 1. Checksum: DBA88E1091CC8AE2	FASTA	1,014	116,015
	10 20 30 40 50 60 MFKAVNPRQN FPQMEEDILK LWQDKGVFKK SIENRRDGKR FTLYEGPPTA NGRPGIHHVL 70 80 90 100 110 120 SRVFKDVIPR YKVMKGYYAP RIGGWDTHGL PVELEVEKEL GFTSKNDIEK YGIAEFNARC 130 140 150 160 170 180 RSSVFKYVSE WNKLTERIAY WVDLDNAYIT MDNNYIESGW WALKQMWDKG LVYQGHRVTP 190 200 210 220 230 240 HCPRCGTSLS SHEVAQGYKD NTEDPSVFVK FEIAKESLAK AGLAKKWAYP ADKPLYLLAW 250 260 270 280 290 300 TTTPWTLPAN TALAVSAADQ YAILDMTDYY MILAKPRLSA LKLAENPVAG ECLGSDLSGL 310 320 330 340 350 360 FYKPLFDPRE FGIPVRNMQD NSETGVSEEL LYPVITTSYV SMDDGTGIVH TAPAYGELDY 370 380 390 400 410 420 ESGVKYGLKF VHHVDLQGRI TGSYPFAGKF VKEADKDISR NLKERGLMFR NERMHHTYPF 430 440 450 460 470 480 CWRCDSPLIY YAKQSWYIRT TAVRDELIKG NQQINWYPEH IKDGRFGDWL ENNIDWAFSR 490 500 510 520 530 540 ERYWGTPVPI WRCEKCGRTE CVGGIDELKA KPNFKGMQEK LDIHRPYVDE WTYDCDKCGG 550 560 570 580 590 600 NMKRVTEVMD CWYDSGAMPV AQYHYPFEPE SRSIAKDGRF PADYICEAVD QTRGWFYSLH 610 620 630 640 650 660 AISTLIFNRP CYQNVICLGH ILDERGEKMS KSRNNVIQPA TVLDKYGADA VRWYFYTAAP 670 680 690 700 710 720 PGNARRFSEK LVGEVTRQFL LMLWNVYSFF VTYANIDSFT PSEKYLEGEV PELDRWILSE 730 740 750 760 770 780 LNQLVLDVDK GLDNYDPTQA GRRIEDFVGY LSNWYVRRSR RRFWKSENDA DKLSAYQALY 790 800 810 820 830 840 TCLVTLSRLL APFTPFVAEE LYQNLVLSAD PSALESVHLT DFPVADTALI DEQLDNEIRL 850 860 870 880 890 900 VMKVSSMGRS ARSKAALKVR QPLAEVRVVL ASAGERTGLM RLAEQVLEEL NVKALAVEEP 910 920 930 940 950 960 GTVIPEKNYA ASTEGAYTVA VYTGLSPELL AEGTAREIVH RLQTMRKSAG FEIADYINTH 970 980 990 1000 1010 YQADEYLDSV IRMHSEYIKK ETLSNQLIKG NAPEGAYAES LDIDGHSLSL WVAR

References

[1]

"Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides ethenogenes." Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M., Methe B.A., Ward N.L., Nelson W.C., DeBoy R.T., Khouri H.M., Kolonay J.F., Dodson R.J., Daugherty S.C., Brinkac L.M., Sullivan S.A., Madupu R., Nelson K.E., Kang K.H. , Impraim M., Tran K., Robinson J.M., Forberger H.A., Fraser C.M., Zinder S.H., Heidelberg J.F. Science 307:105-108(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 195.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000027 Genomic DNA. Translation: AAW39707.1.
RefSeq	YP_181754.1. NC_002936.3.
3D structure databases
ProteinModelPortal	Q3Z7P5.
ModBase	Search...
Protein-protein interaction databases
STRING	243164.DET1038.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAW39707; AAW39707; DET1038.
GeneID	3229669.
KEGG	det:DET1038.
PATRIC	21609123. VBIDehEth89364_0979.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0060.
HOGENOM	HOG000246403.
KO	K01870.
OMA	IYANIDG.
ProtClustDB	PRK06039.
Enzyme and pathway databases
BioCyc	DETH243164:GJNF-1039-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	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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYI_DEHE1

Accession

Primary (citable) accession number: Q3Z7P5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	September 27, 2005
Last modified:	May 1, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program