SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A5IFX5

- SYI_LEGPC

UniProt

A5IFX5 - SYI_LEGPC

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Isoleucine--tRNA ligase
Gene
ileS, LPC_2353
Organism
Legionella pneumophila (strain Corby)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile).UniRule annotation

Cofactori

Binds 1 zinc ion per subunit By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei559 – 5591Aminoacyl-adenylate By similarity
Binding sitei603 – 6031ATP By similarity
Metal bindingi894 – 8941Zinc By similarity
Metal bindingi897 – 8971Zinc By similarity
Metal bindingi914 – 9141Zinc By similarity
Metal bindingi917 – 9171Zinc By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. aminoacyl-tRNA editing activity Source: InterPro
  3. isoleucine-tRNA ligase activity Source: UniProtKB-HAMAP
  4. zinc ion binding Source: UniProtKB-HAMAP
Complete GO annotation...

GO - Biological processi

  1. isoleucyl-tRNA aminoacylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciLPNE400673:GCIT-1047-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Isoleucine--tRNA ligase (EC:6.1.1.5)
Alternative name(s):
Isoleucyl-tRNA synthetase
Short name:
IleRS
Gene namesi
Name:ileS
Ordered Locus Names:LPC_2353
OrganismiLegionella pneumophila (strain Corby)
Taxonomic identifieri400673 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella
ProteomesiUP000001569: Chromosome

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 931931Isoleucine--tRNA ligaseUniRule annotation
PRO_1000022087Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi400673.LPC_2353.

Structurei

3D structure databases

ProteinModelPortaliA5IFX5.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi58 – 6811"HIGH" regionUniRule annotation
Add
BLAST
Motifi600 – 6045"KMSKS" regionUniRule annotation

Domaini

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.UniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0060.
HOGENOMiHOG000246402.
KOiK01870.
OMAiKPVHWCL.
OrthoDBiEOG644ZM1.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPiMF_02002. Ile_tRNA_synth_type1.
InterProiIPR001412. 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]
PANTHERiPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamiPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
PRINTSiPR00984. TRNASYNTHILE.
SUPFAMiSSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsiTIGR00392. ileS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A5IFX5-1 [UniParc]FASTAAdd to Basket

« Hide

MAEYKDTLNL PNTSFPMKAS LSVREPEMLA DWQAKGIYQK IRKARVGSKR    50
FILHDGPPYA NGHLHCGHAL NKILKDIIIK SKTFSGFDAP FVPGWDCHGL 100
PIELNVEKKV GKAGSKISPR EFRAKCREYA ASQIDIQRDE FQRLGVLGDW 150
YNPYVTMDYH YEANIVRALG LMIKNGHLQQ GFKPVHWCID CGSALAEAEV 200
DYEDKTSPSI DVAFSAVNPS EFLNCFETQP AVKPLILPIW TTTPWTLPAN 250
EAVCLHPEID YALIDAGNSY YIVATDLVES VMARYGISHY KTSGFAKGRV 300
FEHFKLQHPF YKRQVPVVLA EHVTTESGTG CVHTAPAHGP DDYLVGQSYQ 350
LPLINPVMAN GCFAENVELF AGISVLKANE TILAVLSERN VLLASESIRH 400
SYPHCWRHKS PMIFLATPQW FISMDKSNLR QAIINEIDKV NWVPDWGKAR 450
ISNMVENRPD WCISRQRSWG TPMPLFVHKT TRELHPDTLE LIERVAVMIE 500
KSGIDAWFDL DSSELLGDDA KHYDKITDTM DVWLDSGISH YSVLKHNNDL 550
DFPADVYFEG SDQHRGWFNS SLTTAVAMYG VAPYKTVLTH GYTVDAEGKK 600
LSKSKGNYVA LDKLVNQHGA DILRLWVAST DYRHEVSISE EIIKRNADAY 650
RRIRNTARFL LANLFDFNPA SDCIDAKELL ELDRWALKRC QLLQEEIITA 700
YENYHFHLIY QKIHNFCAVD MGSFYLDLIK DRQYTTAKDS IARRSCQTAM 750
YHMVKAFTIW LAPILSFTAE EIWQTIPGNN SESIFIEHWY NAWPTIDAVN 800
MEDWEQLHIV RDEVNKALEE TRQRGEIGSA LAAEVTVYAD AKVLPKLTRL 850
GEELRFLFIT SEAKACPISQ SPKGLAVTDC GVSIQVTASV HEKCARCWHR 900
REDVGQNQEH PELCLRCVGN ISRYHEERLY I 931
Length:931
Mass (Da):105,933
Last modified:June 26, 2007 - v1
Checksum:iE02C6D9F6C2A3DFA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000675 Genomic DNA. Translation: ABQ56275.1.
RefSeqiYP_001251621.1. NC_009494.2.

Genome annotation databases

EnsemblBacteriaiABQ56275; ABQ56275; LPC_2353.
GeneIDi5180184.
KEGGilpc:LPC_2353.
PATRICi22311275. VBILegPne45588_2450.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000675 Genomic DNA. Translation: ABQ56275.1 .
RefSeqi YP_001251621.1. NC_009494.2.

3D structure databases

ProteinModelPortali A5IFX5.
ModBasei Search...

Protein-protein interaction databases

STRINGi 400673.LPC_2353.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABQ56275 ; ABQ56275 ; LPC_2353 .
GeneIDi 5180184.
KEGGi lpc:LPC_2353.
PATRICi 22311275. VBILegPne45588_2450.

Phylogenomic databases

eggNOGi COG0060.
HOGENOMi HOG000246402.
KOi K01870.
OMAi KPVHWCL.
OrthoDBi EOG644ZM1.

Enzyme and pathway databases

BioCyci LPNE400673:GCIT-1047-MONOMER.

Family and domain databases

Gene3Di 1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPi MF_02002. Ile_tRNA_synth_type1.
InterProi 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 ]
PANTHERi PTHR11946:SF9. PTHR11946:SF9. 1 hit.
Pfami PF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view ]
PRINTSi PR00984. TRNASYNTHILE.
SUPFAMi SSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsi TIGR00392. ileS. 1 hit.
PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Identification and characterization of a new conjugation/ type IVA secretion system (trb/tra) of L. pneumophila Corby localized on a mobile genomic island."
    Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E., Steinert M., Buchrieser C., Hacker J., Heuner K.
    Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Corby.

Entry informationi

Entry nameiSYI_LEGPC
AccessioniPrimary (citable) accession number: A5IFX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 26, 2007
Last modified: May 14, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi