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.

A6Q4I1

- SYI_NITSB

UniProt

A6Q4I1 - SYI_NITSB

(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, NIS_1282
Organism
Nitratiruptor sp. (strain SB155-2)
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 sitei564 – 5641Aminoacyl-adenylate By similarity
Binding sitei608 – 6081ATP By similarity
Metal bindingi888 – 8881Zinc By similarity
Metal bindingi891 – 8911Zinc By similarity
Metal bindingi903 – 9031Zinc By similarity
Metal bindingi906 – 9061Zinc 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

BioCyciNSP387092:GHA5-1322-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:NIS_1282
OrganismiNitratiruptor sp. (strain SB155-2)
Taxonomic identifieri387092 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaNitratiruptor
ProteomesiUP000001118: 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 – 918918Isoleucine--tRNA ligaseUniRule annotation
PRO_1000022095Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi387092.NIS_1282.

Structurei

3D structure databases

ProteinModelPortaliA6Q4I1.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi57 – 6711"HIGH" regionUniRule annotation
Add
BLAST
Motifi605 – 6095"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.

A6Q4I1-1 [UniParc]FASTAAdd to Basket

« Hide

MDYKETLLLP KTTFPMRGNL PQNEPKRFAK WFEKDVYEKM KKSREGKELF    50
TLHDGPPYAN GHIHIGHALN KILKDIIVKF NYFEGKAVRF TPGWDCHGLP 100
IEQQVEKKLG TAKKEQLPKT KIRELCREHA AKFVGIQKEE FKNLGVIADW 150
EKPYLTMDYA FEADIYRALC EIAKEGLLVE RSKPVYWSWA AKTALAEAEV 200
EYEDKVSPSI YVAFKLDKEA VQKIGKEASI IIWTTTPWTL PANTGIALNP 250
DIEYVLTSDG YVVAADLLDE LKEKGIVKGD VEKSISPKDL ENLHAINPLN 300
GRRSRIVLGE HVTTESGTGA VHTAPGHGED DYRVGLKYDL EVLMPVDDAG 350
RYDETIVREK LLPEEFVGMN VFEANDKICE LLGDALLKKE DIKHSYPHCW 400
RTHKPIIFRA TKQWFIAVDK APKDLQKTLR QIALEEVEKT TFYPEWGRNR 450
LKSMIENRPD WCISRQRDWG VPIAFFRNKK TGEVIYDEKV LNYIAMIFER 500
MGTDAWYSLS VEELLYPGSG YDPNDLEKVM DILDVWFDSG STWYAVLKSR 550
RYDAGNYPAD LYLEGSDQHR GWFQSSLLVS GAIEKRAPFK AILTHGFTVD 600
EKGEKMSKSK GNVVAPMDVA KKYGVEILRL WVAMSDYQSD LKISDNILKQ 650
IAEQYRKLRN TFRFMLANIN DLETIQSDFG VLDRWILAKA KSVFEEVEKQ 700
FKNYQFAKGF SALNNFIVNE FSGIYLDVCK DRLYCDALND SHRRASQSAM 750
ALIAKSMLGL IAPVLTYTAD EIVEHAPSVL RNDAEDIFDF AIEPLPEIQS 800
DFDEVYMIEA RSKFNEIVDQ LKKKKIIKSS LELVIETTSS KVLALDATER 850
EDWFIVSGVE EEIGSKELGD FKVEGDQFII KEAILHKCPR CWKYKAKEEG 900
ALCERCQKVV DGLEQAGS 918
Length:918
Mass (Da):105,037
Last modified:August 21, 2007 - v1
Checksum:iD813A33F9C6F77E5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP009178 Genomic DNA. Translation: BAF70390.1.
RefSeqiWP_012082653.1. NC_009662.1.
YP_001356747.1. NC_009662.1.

Genome annotation databases

EnsemblBacteriaiBAF70390; BAF70390; NIS_1282.
GeneIDi5361228.
KEGGinis:NIS_1282.
PATRICi22684680. VBINitSp82229_1342.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP009178 Genomic DNA. Translation: BAF70390.1 .
RefSeqi WP_012082653.1. NC_009662.1.
YP_001356747.1. NC_009662.1.

3D structure databases

ProteinModelPortali A6Q4I1.
ModBasei Search...

Protein-protein interaction databases

STRINGi 387092.NIS_1282.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAF70390 ; BAF70390 ; NIS_1282 .
GeneIDi 5361228.
KEGGi nis:NIS_1282.
PATRICi 22684680. VBINitSp82229_1342.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci NSP387092:GHA5-1322-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. "Deep-sea vent epsilon-proteobacterial genomes provide insights into emergence of pathogens."
    Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K., Horikoshi K.
    Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SB155-2.

Entry informationi

Entry nameiSYI_NITSB
AccessioniPrimary (citable) accession number: A6Q4I1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: September 3, 2014
This is version 54 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