Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

B1I721

- SYI_STRPI

UniProt

B1I721 - SYI_STRPI

(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

Organism
Streptococcus pneumoniae (strain Hungary19A-6)
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

Binds 1 zinc ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei554 – 5541Aminoacyl-adenylateUniRule annotation
Binding sitei598 – 5981ATPUniRule annotation
Metal bindingi888 – 8881ZincUniRule annotation
Metal bindingi891 – 8911ZincUniRule annotation
Metal bindingi908 – 9081ZincUniRule annotation
Metal bindingi911 – 9111ZincUniRule 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

BioCyciSPNE487214:GHY0-1736-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:SPH_1767
OrganismiStreptococcus pneumoniae (strain Hungary19A-6)
Taxonomic identifieri487214 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
ProteomesiUP000002163: 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 – 930930Isoleucine--tRNA ligasePRO_1000189203Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi487214.SPH_1767.

Structurei

3D structure databases

ProteinModelPortaliB1I721.
SMRiB1I721. Positions 1-917.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi57 – 6711"HIGH" regionAdd
BLAST
Motifi595 – 5995"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.
OMAiLGHRVHY.
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.

B1I721-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLKDTLNLG KTEFPMRAGL PTKEPVWQKE WEDAKLYQRR QELNQGKPHF
60 70 80 90 100
TLHDGPPYAN GNIHVGHAMN KISKDIIVRS KSMSGFYAPF IPGWDTHGLP
110 120 130 140 150
IEQVLSKQGV KRKEMDLVEY LKLCREYALS QVDKQREDFK RLGVSGDWEN
160 170 180 190 200
PYVTLTPDYE AAQIRVFGEM ANKGYIYRGA KPVYWSWSSE SALAEAEIEY
210 220 230 240 250
HDLVSTSLYY ANKVKDGKGV LDTDTYIVVW TTTPFTITAS RGLTVGADID
260 270 280 290 300
YVLVQPAGEA RKFVVAAELL TSLSEKFGWA DVQVLETYRG QELNHIVTEH
310 320 330 340 350
PWDTAVEELV ILGDHVTTDS GTGIVHTAPG FGEDDYNVGI ANNLEVAVTV
360 370 380 390 400
DERGIMMKNA GPEFEGQFYE KVVPTVIEKL GNLLLAQEEI SHSYPFDWRT
410 420 430 440 450
KKPIIWRAVP QWFASVSKFR QEILDEIEKV KFHSEWGKVR LYNMIRDRGD
460 470 480 490 500
WVISRQRAWG VPLPIFYAED GTAIMVAETI EHVAQLFEEH GSSIWWERDA
510 520 530 540 550
KDLLPEEFTH PGSPNGEFKK ETDIMDVWFD SGSSWNGVVV NRPELTYPAD
560 570 580 590 600
LYLEGSDQYR GWFNSSLITS VANHGVAPYK QILSQGFALD GKGEKMSKSL
610 620 630 640 650
GNTIAPSDVE KQFGAEILRL WVTSVDSSND VRISMDILSQ VSETYRKIRN
660 670 680 690 700
TLRFLIANTS DFNPAQDTVA YDELRSVDKY MTIRFNQLVK TIRDAYADFE
710 720 730 740 750
FLTIYKALVN FINVDLSAFY LDFAKDVVYI EGAKSLERRQ MQTVFYDILV
760 770 780 790 800
KITKLLTPIL PHTAEEIWSY LEFEAEDFVQ LSELPEAQTS ANQEEILDTW
810 820 830 840 850
AAFMDFRGQA QKALEEARNA KVIGKSLEAH LTVYPNEVVK TLLEAVNSNV
860 870 880 890 900
AQLLIVSDLT IAEGPAPEAA LSFEDVAFTV ERAAGEVCDR CRRIDPTTAE
910 920 930
RSYQAVICDH CASIVEENFA EAVAEGFEEK
Length:930
Mass (Da):105,337
Last modified:April 29, 2008 - v1
Checksum:i5CDE237F79892013
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000936 Genomic DNA. Translation: ACA35572.1.
RefSeqiYP_001695040.1. NC_010380.1.

Genome annotation databases

EnsemblBacteriaiACA35572; ACA35572; SPH_1767.
GeneIDi6027767.
KEGGispv:SPH_1767.
PATRICi19693648. VBIStrPne34925_1775.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000936 Genomic DNA. Translation: ACA35572.1 .
RefSeqi YP_001695040.1. NC_010380.1.

3D structure databases

ProteinModelPortali B1I721.
SMRi B1I721. Positions 1-917.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 487214.SPH_1767.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACA35572 ; ACA35572 ; SPH_1767 .
GeneIDi 6027767.
KEGGi spv:SPH_1767.
PATRICi 19693648. VBIStrPne34925_1775.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci SPNE487214:GHY0-1736-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. "Complete sequence of Streptococcus pneumoniae strain Hungary 19A-6."
    Hotopp J.D., Censini S., Masignani V., Covacci A., Tettelin H.
    Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Hungary19A-6.

Entry informationi

Entry nameiSYI_STRPI
AccessioniPrimary (citable) accession number: B1I721
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: April 29, 2008
Last modified: October 29, 2014
This is version 52 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