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Q9HJT4

- SYI_THEAC

UniProt

Q9HJT4 - SYI_THEAC

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Protein
Isoleucine--tRNA ligase
Gene
ileS, Ta0879
Organism
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
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

Zinc By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei594 – 5941ATP 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

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

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:Ta0879
OrganismiThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Taxonomic identifieri273075 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma
ProteomesiUP000001024: 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 – 10261026Isoleucine--tRNA ligaseUniRule annotation
PRO_0000098595Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi273075.Ta0879.

Structurei

3D structure databases

ProteinModelPortaliQ9HJT4.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi51 – 6111"HIGH" regionUniRule annotation
Add
BLAST
Motifi591 – 5955"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.
HOGENOMiHOG000246403.
KOiK01870.
OMAiRVEHMVE.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPiMF_02003. Ile_tRNA_synth_type2.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023586. Ile-tRNA-ligase_type2.
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]
PfamiPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
[Graphical view]
PRINTSiPR00984. TRNASYNTHILE.
SUPFAMiSSF47323. SSF47323. 2 hits.
SSF50677. SSF50677. 1 hit.
TIGRFAMsiTIGR00392. ileS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9HJT4-1 [UniParc]FASTAAdd to Basket

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MQSLRFRQID PGMTLREIDS EILKYWKDKN ILEKILSKGG SKKFVFLEGP     50
PTANGRPHIG HAMTRTIKDI VLRYNTMTDH KIYRRVGGWD CHGLPVELEA 100
EKHFGFHTKS EIVNFGVEKF NQYCRESIFR YIDEWKQVDD LIGFSIDHNG 150
DYITLRNDYM ESEWFALKTM YNSGLLYKDY TVVPYCPRCE TSLSSHEVAQ 200
GYKDVKDPSV YVRFKSADEE NTYFVAWTTT PWTLPSNEFL VVNPDMEYSL 250
VEAQGSRYYV ASSRAGYIFK EYREIRRMHG RDLVGKRYLQ LMPFLDPPSG 300
SLKVVAGSFV TSEDGSGIVH AAPAFGADDY QIGKEEGVEI LNPVDKNGRF 350
ADPRIPWNGK FVRDANEDII VYLKKNQMLL KSEKYEHSYP FCYRCDTPLL 400
YYPLDAWFIA VSRIRDKLVE YNERINWKPD YLKHGRFGNF LGEAKDWNLS 450
RDRFWGTPLP AWRCKNGHLV FVGSRKEIED LGGKVPEDLH RPYIDEVRFK 500
CPTCGEEMSR EPYVIDTWFD SGSATYAASH YPFEKNFDPE TDVPVSFITE 550
AIDQTRGWFY VLHVIATIMF NKNAYESALS INFILDAQGR KMSKSKGNSV 600
YALDFLNEVP PDSLRLFFLY GAPWKSKNLD KKVIDEVSRK TLMTVLNVYS 650
FFAYNANIDN FQWNGLQLSG NALDRYMVSK VNSFVRSSRD AYESLDFHEV 700
VRASMEFVDD LSNFYLRLSR RRFWAEGFDD DKLSAYSTLY YALKAFSEVM 750
APITPFFSDF IYLNLGGDKE SVHLEAFPEF DSTLMDEKLE SEMDRAYSVI 800
ETVRRLRQEN SIKGRQPLRE ILIAGDMEES IIDVVKSELN AKDIKLIERD 850
QEPIRLSADL RMDRAAPVLR SRVNAVRHKI RSMDGLEVQR QISEKGFVEI 900
DGVRLDPDMV EISRVPDPNY AYSQTEKYGI DVFINKNIDR DGYLEGLARE 950
LVRRIQVMRK EMNLNYTDRI ITHLDLSDDF LEALNKHAEY IKNETQSDSI 1000
ITDKVEGMKL WEINGEPVRI KIDLAR 1026
Length:1,026
Mass (Da):119,169
Last modified:December 20, 2005 - v2
Checksum:i0FE6AA2C39E9B50F
GO

Sequence cautioni

The sequence CAC12008.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL445065 Genomic DNA. Translation: CAC12008.1. Different initiation.
RefSeqiNP_394338.1. NC_002578.1.

Genome annotation databases

EnsemblBacteriaiCAC12008; CAC12008; CAC12008.
GeneIDi1456418.
KEGGitac:Ta0879.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL445065 Genomic DNA. Translation: CAC12008.1 . Different initiation.
RefSeqi NP_394338.1. NC_002578.1.

3D structure databases

ProteinModelPortali Q9HJT4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 273075.Ta0879.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAC12008 ; CAC12008 ; CAC12008 .
GeneIDi 1456418.
KEGGi tac:Ta0879.

Phylogenomic databases

eggNOGi COG0060.
HOGENOMi HOG000246403.
KOi K01870.
OMAi RVEHMVE.

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_02003. Ile_tRNA_synth_type2.
InterProi IPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023586. Ile-tRNA-ligase_type2.
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 ]
Pfami PF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
[Graphical view ]
PRINTSi PR00984. TRNASYNTHILE.
SUPFAMi SSF47323. SSF47323. 2 hits.
SSF50677. SSF50677. 1 hit.
TIGRFAMsi TIGR00392. ileS. 1 hit.
PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
    Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
    Nature 407:508-513(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.

Entry informationi

Entry nameiSYI_THEAC
AccessioniPrimary (citable) accession number: Q9HJT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: May 14, 2014
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference 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

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