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.

Q2RK59

- SYI_MOOTA

UniProt

Q2RK59 - SYI_MOOTA

(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, Moth_0863
Organism
Moorella thermoacetica (strain ATCC 39073)
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 sitei555 – 5551Aminoacyl-adenylate By similarity
Binding sitei599 – 5991ATP By similarity
Metal bindingi896 – 8961Zinc By similarity
Metal bindingi899 – 8991Zinc By similarity
Metal bindingi916 – 9161Zinc By similarity
Metal bindingi919 – 9191Zinc 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

BioCyciMTHE264732:GH0A-899-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:Moth_0863
OrganismiMoorella thermoacetica (strain ATCC 39073)
Taxonomic identifieri264732 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeMoorella groupMoorella
ProteomesiUP000007053: 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 – 930930Isoleucine--tRNA ligaseUniRule annotationPRO_1000022092Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi264732.Moth_0863.

Structurei

3D structure databases

ProteinModelPortaliQ2RK59.
SMRiQ2RK59. Positions 1-926.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi57 – 6711"HIGH" regionUniRule annotationAdd
BLAST
Motifi596 – 6005"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.

Q2RK59-1 [UniParc]FASTAAdd to Basket

« Hide

MDYSKTLNLP RTDFPMRANL PQREPEILKF WEENDIYGKV QEANRGKPKF    50
ILHDGPPYAN GHLHLGHTLN KILKDIIIKY HSMNGYDAPY VPGWDTHGLP 100
IEQQAIKNLG LNRHAVDVVE FRNRCRDYAL KYVNIQREEF KRLGVRGDWE 150
HPYLTLEPEY EAIQIGIFGE MAKKGYIYKG LKPVYWCTDC ETALAEAEVE 200
YGEERSPSIY VKFPVADARG LFEPRGSSIV IWTTTPWTLP ANVAIALHPE 250
FKYVLIQVGE ERLLMAAELV RPVLELLGVK DYQVVATFTG SELEGVVCRN 300
PLMDRDSVVI LGEHVTLEQG TGCVHTAPGH GLEDYEVGMR YHLPVLSPLD 350
DRGRFTEEGG QFAGLFIDEA NKAVVKELEA RGALLHFGFI KHQYPHCWRC 400
KHPIIFRATE QWFASIEGFR QEALEAIKKV KWIPSWGEDR IYNMVADRSD 450
WCISRQRTWG VPIPIFYCAN CGREIINDAT ISHLQELFRK HGSNVWFARE 500
AGELVPPGLK CPECGSKEFR KETDIMDVWF DSGSSHAAVL ATRPELAWPA 550
DLYLEGSDQH RGWFNSSLST AVATRGRAPY RQVLTHGFLV DEEGRKMSKS 600
LGNGIDPADV IRQRGADVLR LWVASADYRR DVAASENIMR QITEAYRKIR 650
NTCRFLLANL ADFDPGKDQV PREEMLELDR WAMNRLQRLI ARVTMAYDDY 700
EFHVVYHTIH NFCAVDLSAV YLDIIKDRLY TWPAASKGRR SAQTVLYETI 750
NVLVRLLTPI LAFTTEEIWR YLPGEDDRPI SVQLAGWPQV KTEFLDDELE 800
EKWKRILQVR DVVARALERA RQEQDLGNSL NAAVHLYPDA DMYQFLKPLG 850
DELATIMIVS RVDLHQPGEE APAGSLEAPE LPGLRVYVTG APGQKCERCW 900
MVSETVGQDT DHPTLCRRCA TVVKEMYMNG 930
Length:930
Mass (Da):106,238
Last modified:January 24, 2006 - v1
Checksum:iF09E475EDD3423AE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000232 Genomic DNA. Translation: ABC19180.1.
RefSeqiYP_429723.1. NC_007644.1.

Genome annotation databases

EnsemblBacteriaiABC19180; ABC19180; Moth_0863.
GeneIDi3831750.
KEGGimta:Moth_0863.
PATRICi22638876. VBIMooThe6753_0926.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000232 Genomic DNA. Translation: ABC19180.1 .
RefSeqi YP_429723.1. NC_007644.1.

3D structure databases

ProteinModelPortali Q2RK59.
SMRi Q2RK59. Positions 1-926.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 264732.Moth_0863.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABC19180 ; ABC19180 ; Moth_0863 .
GeneIDi 3831750.
KEGGi mta:Moth_0863.
PATRICi 22638876. VBIMooThe6753_0926.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci MTHE264732:GH0A-899-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 39073.

Entry informationi

Entry nameiSYI_MOOTA
AccessioniPrimary (citable) accession number: Q2RK59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 24, 2006
Last modified: May 14, 2014
This is version 68 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, 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

Similar proteinsi