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.

A7I1S7

- SYI_CAMHC

UniProt

A7I1S7 - SYI_CAMHC

(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, CHAB381_0906
Organism
Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A)
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 sitei569 – 5691Aminoacyl-adenylate By similarity
Binding sitei613 – 6131ATP By similarity
Metal bindingi896 – 8961Zinc By similarity
Metal bindingi899 – 8991Zinc By similarity
Metal bindingi911 – 9111Zinc By similarity
Metal bindingi914 – 9141Zinc By similarity

GO - Molecular functioni

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

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

BioCyciCHOM360107:GHCX-910-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:CHAB381_0906
OrganismiCampylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A)
Taxonomic identifieri360107 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
ProteomesiUP000002407: 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 – 921921Isoleucine--tRNA ligaseUniRule annotationPRO_1000022055Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi360107.CHAB381_0906.

Structurei

3D structure databases

ProteinModelPortaliA7I1S7.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi59 – 6911"HIGH" regionUniRule annotationAdd
BLAST
Motifi610 – 6145"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.

A7I1S7-1 [UniParc]FASTAAdd to Basket

« Hide

MDYKDTLFLP TTDFAMRGNL PQNEPKRFKA WYNERKVYEK MKAKRQSAGV    50
SFNLHDGPPY ANGHLHIGHA LNKILKDIIV KTHYFAGENV RYVPGWDCHG 100
LPIEQQIEIK LGGKKNETSK TKIREMCRAH AREFINIQRD EFKDMGIIGD 150
WDDPYITMKF KFEAEIYKGL CEIAKKGLLI ERSKPVFWSW AAGSALAEAE 200
VEYKDKEDYS IYIAFDLSDE ANKKIGAKGA KAVIWTTTPW TIPANQAICL 250
NPDEIYVLTS ENFIFAKHLL ENLVQKGISK GKIVKEFASG ELENLYAKNP 300
LNDRPSKFIL GEHVLMDGGT GLVHTAPGHG EDDYYVSLKY GIETIMPVDD 350
AGKYDETIKT KKLFRDNVVD EFVGMHIFKA NEKIVELLGD AVVSVGKFTH 400
SYPYCWRTHK PVIYRATKQW FIAMDKPFKD GKTLREVALN ALKEVKFYPE 450
VGRNRITSMI ENRPDWCISR QRDWGVPIAF FRDKATKEPI FDDEILNNIY 500
EIFKEKGADA WWELDIGELL PKNCKYEAKN LEKVVDILDV WFDSGSTWRA 550
VLKSGDYDAG EFRADMYLEG SDQHRGWFQS SLLVSSAINE TAPYKSILTH 600
GFTVDEKGQK MSKSVGNVIA PQEVAKKYGV EIMRLWVGLS DYSSDLKISD 650
NILKQVSEQY RKIRNTIRFL LANVSDLKEI ETNNFTMLDK WILSKANIAF 700
EETNRAFRNY DFSKGFSVLL NFLSADLSGI YLDVCKDRLY CDELDSSRRR 750
SAQSTMVLIT RTLLPLIAPT LTYTVDEVME FAPEIVKNGK KDAFDLVYEP 800
LEFEDFKKNE TGELFIESRA KFFEIIDTLK KEKKIKSTLE LVLETSSNEI 850
LSHDLDEICD WYMVSHMRSI ESRDFLAEFK VEDETFRLVL SDHHKCPRCW 900
KFDAKNEDEL CPRCQKVLNV K 921
Length:921
Mass (Da):106,166
Last modified:September 11, 2007 - v1
Checksum:iFEB0BE766577CAF5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000776 Genomic DNA. Translation: ABS51595.1.
RefSeqiYP_001406468.1. NC_009714.1.

Genome annotation databases

EnsemblBacteriaiABS51595; ABS51595; CHAB381_0906.
GeneIDi5409280.
KEGGicha:CHAB381_0906.
PATRICi20039946. VBICamHom81367_0869.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000776 Genomic DNA. Translation: ABS51595.1 .
RefSeqi YP_001406468.1. NC_009714.1.

3D structure databases

ProteinModelPortali A7I1S7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 360107.CHAB381_0906.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABS51595 ; ABS51595 ; CHAB381_0906 .
GeneIDi 5409280.
KEGGi cha:CHAB381_0906.
PATRICi 20039946. VBICamHom81367_0869.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci CHOM360107:GHCX-910-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. "Complete genome sequence of Campylobacter hominis ATCC BAA-381, a commensal isolated from the human gastrointestinal tract."
    Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Nelson K.E.
    Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A.

Entry informationi

Entry nameiSYI_CAMHC
AccessioniPrimary (citable) accession number: A7I1S7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 11, 2007
Last modified: May 14, 2014
This is version 51 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