Isoleucine--tRNA ligase - Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)

Preferred order of sections

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:	lpg0937

Organism

Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) [Complete proteome] [HAMAP]

Taxonomic identifier

272624 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Legionellaceae › Legionella ›

Protein attributes

Sequence length	931 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 – 931

931

Isoleucine--tRNA ligase HAMAP-Rule MF_02002

PRO_0000098407

Regions

Motif

58 – 68

11

"HIGH" region HAMAP-Rule MF_02002

Motif

600 – 604

5

"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding

894

1

Zinc By similarity

Metal binding

897

1

Zinc By similarity

Metal binding

914

1

Zinc By similarity

Metal binding

917

1

Zinc By similarity

Binding site

559

1

Aminoacyl-adenylate By similarity

Binding site

603

1

ATP By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q5ZWZ6 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: CF03AFB63E240166
Show »

FASTA

931

105,636

        10         20         30         40         50         60 
MAEYKDTLNL PNTSFPMKAS LSVREPEMLA DWQAKGIYQK IRKARVGSKR FILHDGPPYA 

        70         80         90        100        110        120 
NGHLHCGHAL NKILKDIIIK SKTFSGFDAP FVPGWDCHGL PIELNVEKKV GKAGSKISPR 

       130        140        150        160        170        180 
EFRAKCREYA ASQIDIQRDE FQRLGVLGDW YNPYVTMDYH YEANIVRALG LMIKNGHLQQ 

       190        200        210        220        230        240 
GFKPVHWCID CGSALAEAEV DYEDKTSPSI DVAFSAVNPS EFLNCFGTQP AVKPLILPIW 

       250        260        270        280        290        300 
TTTPWTLPAN EAVCLHPEID YALIDAGNSY YIVATDLVES VMARYGISHY KTSGSAKGRV 

       310        320        330        340        350        360 
FEHFKLQHPF YKRQVPVVLA EHVTTESGTG CVHTAPAHGP DDYLVGQSYQ LPLINPVMAN 

       370        380        390        400        410        420 
GCFAENVELF AGISVLKANE TILTVLSERN VLLASESIRH SYPHCWRHKS PMIFLATPQW 

       430        440        450        460        470        480 
FVSMDKSNLR QAIINEIDKV NWVPDWGKAR ISNMVENRPD WCISRQRSWG TPMPLFVHKT 

       490        500        510        520        530        540 
TRELHPDTLE LIEKVAVMIE KSGIDAWFDL DSSELLGDDA KHYDKITDTM DVWLDSGISH 

       550        560        570        580        590        600 
YSVLKHNNDL DFPADVYFEG SDQHRGWFNS SLTTAVAMYG VAAYKTVLTH GYTVDAEGKK 

       610        620        630        640        650        660 
LSKSKGNYVA LDKLVNQHGA DILRLWVAST DYRHEVSISE EIIKRNADAY RRIRNTARFL 

       670        680        690        700        710        720 
LANLFDFNPA SDCIDAKELL ELDRWALKRC QLLQEEIITA YENYHFHLIY QKIHNFCAVD 

       730        740        750        760        770        780 
MGSFYLDLIK DRQYTTAKDS IARRSCQTAM YHMVKAFTIW LAPILSFTAE EIWQTIPGNN 

       790        800        810        820        830        840 
SESIFIEHWY DAWPTIDAVN MEDWEQLHIV RDEVNKALEE TRQRGEIGSA LAAEVTVYAD 

       850        860        870        880        890        900 
AKALPKLTRL GEELRFLFIT SEAKACPISQ SPKGLAVTDC GVSIQVTASV HEKCARCWHR 

       910        920        930 
REDVGQNQEH PELCLRCVGN ISGYHEERLY I

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References

[1]

"The genomic sequence of the accidental pathogen Legionella pneumophila."
Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G., Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V., Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S.

Russo J.J.
Science 305:1966-1968(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Philadelphia 1 / ATCC 33152 / DSM 7513.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017354 Genomic DNA. Translation: AAU27024.1.
RefSeq	YP_094971.1. NC_002942.5.
3D structure databases
ProteinModelPortal	Q5ZWZ6.
ModBase	Search...
Protein-protein interaction databases
STRING	272624.lpg0937.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAU27024; AAU27024; lpg0937.
GeneID	3078903.
KEGG	lpn:lpg0937.
PATRIC	22328882. VBILegPne29832_0969.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0060.
HOGENOM	HOG000246402.
KO	K01870.
OMA	KQVLTHG.
ProtClustDB	PRK05743.
Enzyme and pathway databases
BioCyc	LPNE272624:GHDI-977-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_LEGPH

Accession

Primary (citable) accession number: Q5ZWZ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	November 23, 2004
Last modified:	May 1, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents