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.

B9KD44

- SYI_CAMLR

UniProt

B9KD44 - SYI_CAMLR

(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, Cla_1161
Organism
Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060)
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 bindingi894 – 8941Zinc By similarity
Metal bindingi897 – 8971Zinc By similarity
Metal bindingi909 – 9091Zinc By similarity
Metal bindingi912 – 9121Zinc 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

BioCyciCLAR306263:GH7X-1159-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:Cla_1161
OrganismiCampylobacter lari (strain RM2100 / D67 / ATCC BAA-1060)
Taxonomic identifieri306263 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
ProteomesiUP000007727: 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 annotation
PRO_1000189141Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi306263.Cla_1161.

Structurei

3D structure databases

ProteinModelPortaliB9KD44.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi59 – 6911"HIGH" regionUniRule annotation
Add
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.
OMAiERLMLHQ.
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.
[Graphical view]
PANTHERiPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamiPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 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.

B9KD44-1 [UniParc]FASTAAdd to Basket

« Hide

MDYKDTLLLP NTTFAMRANL AELEPKRFDK WFENNYAYEK MKQKRQGVSE    50
SFTLHDGPPY ANGHLHIGHA LNKILKDIII KMHYFQGKKV RFTPGWDCHG 100
LPIEQQVEVK LKDKKQNLSK KQIRELCREH AREFVNIQRD EFKSLGVIAD 150
WDEPYLTMKN AFEADIYKAL CKIAKKGLLL ERSKPVFWSW AAKSALAEAE 200
VEYEEKEDYS IYVAFNLDEA SCKKLGVENA KAVIWTTTPW TLPANQAISL 250
NPNEKYIITK EGYIFAKALL ENMINKNFTQ GEIQKELLGS EFENLSAINP 300
LNQRKSTLIL GEHVLMDGGT GLVHTAPGHG EDDYYACLKY NIEVIMPVDD 350
GGYYDETLRA KGLLPEHLLA EFIGLHIFKA NERILELLGE ALLESSKFTH 400
SYPFCWRTHK PVIYRATKQW FILMDEKKLD GKSLRELALE QLNSVKFYPE 450
SGVKRLSSMI ENRPDWCISR QRDWGVPIAF FRDKKSQEVI FDDDVLDHLV 500
GIFEKNGADA WWDLEIKDLL PPNSKYNPNN LEKVYDILDV WFDSGSTWEA 550
VLNSARYDAG EYQASMYLEG SDQHRGWFQS SLLISTAINH KTPYKNILTH 600
GFTVDEKGQK MSKSKGNVVL PQNVAKNYGV EILRLWIMLS DYSTDLKISD 650
NILKQVSEQY RKIRNTIRFL LANTNDIEFV ETKNFTLLDK WILMRAKIAF 700
EICENAFEKY EFSKGFSVLL NFLSADLSGI YLDICKDRLY CNAKDDSKRV 750
SAQSAMVLIA RKLFALLAPS LTYTIDEALE HANVAIKENA KDVFDLLNKQ 800
GFEYEYKIED ELFIKSREKF FEIIDGLKKD KIIKSTLELS LQTSANELLS 850
EDLEEIADWF MVSVVESIDE QKALAEFKID NIGFKIVKSS LNKCPRCWKF 900
LAKEDGCLCP RCNGVEKAKN V 921
Length:921
Mass (Da):106,124
Last modified:March 24, 2009 - v1
Checksum:i16261B95FDBB0591
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000932 Genomic DNA. Translation: ACM64483.1.
RefSeqiYP_002575734.1. NC_012039.1.

Genome annotation databases

EnsemblBacteriaiACM64483; ACM64483; Cla_1161.
GeneIDi7410325.
KEGGicla:Cla_1161.
PATRICi20062809. VBICamLar15090_1149.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000932 Genomic DNA. Translation: ACM64483.1 .
RefSeqi YP_002575734.1. NC_012039.1.

3D structure databases

ProteinModelPortali B9KD44.
ModBasei Search...

Protein-protein interaction databases

STRINGi 306263.Cla_1161.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACM64483 ; ACM64483 ; Cla_1161 .
GeneIDi 7410325.
KEGGi cla:Cla_1161.
PATRICi 20062809. VBICamLar15090_1149.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci CLAR306263:GH7X-1159-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.
[Graphical view ]
PANTHERi PTHR11946:SF9. PTHR11946:SF9. 1 hit.
Pfami PF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 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. "The complete genome sequence and analysis of the human pathogen Campylobacter lari."
    Miller W.G., Wang G., Binnewies T.T., Parker C.T.
    Foodborne Pathog. Dis. 5:371-386(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RM2100 / D67 / ATCC BAA-1060.

Entry informationi

Entry nameiSYI_CAMLR
AccessioniPrimary (citable) accession number: B9KD44
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 40 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