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Q1LSS9

- SYI_BAUCH

UniProt

Q1LSS9 - SYI_BAUCH

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Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Baumannia cicadellinicola subsp. Homalodisca coagulata
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).UniRule annotation

Catalytic activityi

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile).UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei561 – 5611Aminoacyl-adenylateUniRule annotation
Binding sitei605 – 6051ATPUniRule annotation
Metal bindingi901 – 9011ZincUniRule annotation
Metal bindingi904 – 9041ZincUniRule annotation
Metal bindingi921 – 9211ZincUniRule annotation
Metal bindingi924 – 9241ZincUniRule annotation

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

BioCyciBCIC374463:GI6Q-556-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Isoleucine--tRNA ligaseUniRule annotation (EC:6.1.1.5UniRule annotation)
Alternative name(s):
Isoleucyl-tRNA synthetaseUniRule annotation
Short name:
IleRSUniRule annotation
Gene namesi
Name:ileSUniRule annotation
Ordered Locus Names:BCI_0556
OrganismiBaumannia cicadellinicola subsp. Homalodisca coagulata
Taxonomic identifieri374463 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaCandidatus Baumannia
ProteomesiUP000002427: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 938938Isoleucine--tRNA ligasePRO_1000022042Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi374463.BCI_0556.

Structurei

3D structure databases

ProteinModelPortaliQ1LSS9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi58 – 6811"HIGH" regionAdd
BLAST
Motifi602 – 6065"KMSKS" region

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)).UniRule annotation

Sequence similaritiesi

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.UniRule annotation

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.

Q1LSS9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIDYKNTLNL PKTQFAMRGN LAIREPIMLK RWHQQDLYQL ICQATQGKKT
60 70 80 90 100
FFLHDGPPYA NGSIHIGHSV NKILKDIIIK SKRLMGYCSP YIPGWDCHGL
110 120 130 140 150
PIELKVEQLI GKPGKKVSAS EFIIACRNYA SEQVTWQKKD FIRLGVLGDW
160 170 180 190 200
DNIYRTMDFH TEANIIRTLS KIIENGHVYQ GNKPVHWCID CRSALAEAEV
210 220 230 240 250
EYYDYTSPSI YVIFAATNTH DVAARFGIPN VLSSISFLVW TTTPWTIPAN
260 270 280 290 300
RAISIHPNLN YQLVKVNQQG FILAADLVTS VLTYLGIQNW TVVKNIKGYV
310 320 330 340 350
LELLRFSHPF MKFDVPVVLS NHVTINVGTG VVHTSPSHGP DDYLIGREYN
360 370 380 390 400
LEIVNIVGPD GCYLPGTFSL LDGTSVYQSN QTVISLLKDR GALLHTGTIQ
410 420 430 440 450
HSYPHCWRHK TPLIFRATPQ WFISMDKKKL RQQSLKEIKK IQWIPSNSQA
460 470 480 490 500
SITNMVNNRQ DWCISRQRIW GVPMSLFVHN HTKKLHPQTS EIMEYVAKQV
510 520 530 540 550
EKKGIQAWWD LDPIKILGDD IVNYSKINDI LDVWFDSGST HSSVINAQTE
560 570 580 590 600
FANHEIDMYL EGADQHRGWF MSSLISSTAI KGKAPYKTVI THGFAVDSNG
610 620 630 640 650
RKMSKSIGNV VSPQQVVDKL GADILRLWVA STNYTDDMTI SDEILKRSVD
660 670 680 690 700
TYRRIRNTAR FLLANLNGFE PKQHSVSIDK MIILDQWAID RAQVAQDEII
710 720 730 740 750
AAYNSYEFHS VVQRIMQFCS VEMGSFYLDI IKDRQYTTQY NSIARRSCQT
760 770 780 790 800
ALFHIIEAMV RWIAPIISFT ADEIWGFIPG KRSPSVFIEE WYKNLSRLDA
810 820 830 840 850
EQHMNDTYWN TLLQVRSDVN YLIEQARIKK NIGSSLETQV TLYSEPILAM
860 870 880 890 900
QLRQLGNELH FVLLTSAVQI ADYQEADNNA LQSTRIKGLK ITLNHATGRK
910 920 930
CQRCWHYEQD IGNNTQYPEI CGRCVINIAG NGEERKFV
Length:938
Mass (Da):107,240
Last modified:May 30, 2006 - v1
Checksum:i697B57DCEEB6DAAA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000238 Genomic DNA. Translation: ABF14142.1.
RefSeqiYP_588985.1. NC_007984.1.

Genome annotation databases

EnsemblBacteriaiABF14142; ABF14142; BCI_0556.
GeneIDi4056571.
KEGGibci:BCI_0556.
PATRICi21074621. VBIBauCic75062_0527.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000238 Genomic DNA. Translation: ABF14142.1 .
RefSeqi YP_588985.1. NC_007984.1.

3D structure databases

ProteinModelPortali Q1LSS9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 374463.BCI_0556.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABF14142 ; ABF14142 ; BCI_0556 .
GeneIDi 4056571.
KEGGi bci:BCI_0556.
PATRICi 21074621. VBIBauCic75062_0527.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci BCIC374463:GI6Q-556-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. "Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
    Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
    PLoS Biol. 4:1079-1092(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiSYI_BAUCH
AccessioniPrimary (citable) accession number: Q1LSS9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 30, 2006
Last modified: November 26, 2014
This is version 65 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