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B8ZM55

- SYI_STRPJ

UniProt

B8ZM55 - SYI_STRPJ

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Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Streptococcus pneumoniae (strain ATCC 700669 / Spain 23F-1)
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 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

BioCyciSPNE561276:GJFJ-1592-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:SPN23F16600
OrganismiStreptococcus pneumoniae (strain ATCC 700669 / Spain 23F-1)
Taxonomic identifieri561276 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
ProteomesiUP000002600: 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_1000189204Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi561276.SPN23F_16600.

Structurei

3D structure databases

ProteinModelPortaliB8ZM55.
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.
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.

B8ZM55-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLKDTLNLG KTAFPMRAGL PTKEPVWQKE WEDAKLYQRR QELNEGKPHF
60 70 80 90 100
VLHDGPPYAN GNIHVGHAMN HISKDIIIRS KSMSGFNAPY IPGWDTHGLP
110 120 130 140 150
IEQVLAKQGV KRKEMDLVEY LKLCREYALS QVYKQRDDFK RLGMSGDWEN
160 170 180 190 200
LYVTLTPDYE AAQIRVFGEM ANKGYIYRGA KPVYWSWSSE SALAEAEIEY
210 220 230 240 250
HDLVSTSLYY ANKVKDGKGI LDTDTYIVVW TTTPFTITAS RGLTVGADID
260 270 280 290 300
YVLVQPASET RKFVVAAELL TSLSEKFGWA DVQVLATYRG QELNHIVTEH
310 320 330 340 350
PWDTAVDELV ILGDHVTTDS GTGIVHTAPG FGEDDYNVGI ANGLEVAVTV
360 370 380 390 400
DERGIMMANA GPEFEGQFYD KVVPTVIEKL GNLLLAQEEI SHSYPFDWRT
410 420 430 440 450
KKPIIWRAVP QWFASVSKFR QEILDAIDKV KFHTEWGKVR LYNMIRDRGD
460 470 480 490 500
WVISRQRAWG VPLPIFYAED GTAIMTAETI EHVAQLFEVH GSSIWWERDA
510 520 530 540 550
KDLLPEGFTH PGSPNGEFKK ETDIMDVWFD SGSSWNGVLV NRPNLTYPAD
560 570 580 590 600
LYLEGSDQYR GWFNSSLITS VANHGVAPYK QILSQGFTLD GKGEKMSKSL
610 620 630 640 650
GNTIAPSDVE KQFGAEILRL WVTSVDSSND VRISMDILSQ VSETYRKIRN
660 670 680 690 700
TLRFLIANTS DFNPAQDVVA YDELRSVDKY MTIRFNQLVK TIRDAYADFE
710 720 730 740 750
FLTIYKALVN FINVDLSAFY LDFAKDVVYI EGAKSLERRQ MQTVFYDILV
760 770 780 790 800
KITKLLTPIL PHTAEEIWSY LEFEAEDFVQ LSELPEAQTF ANQEEVLDTW
810 820 830 840 850
AAFMDFRGQA QKALEEARNA KVIGKSLEAH LTVYPNEVVK TLLEAVNSNV
860 870 880 890 900
AQLLIVSDLT IAEGPAPEAA LSFEDVAFTV ERAAGQVCDR CRRIDPTTAE
910 920 930
RSYQAVICDH CASIVEENFA EAVAEGFEEK
Length:930
Mass (Da):105,122
Last modified:March 3, 2009 - v1
Checksum:iB8254A0FAF2ED7BF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FM211187 Genomic DNA. Translation: CAR69433.1.
RefSeqiYP_002511550.1. NC_011900.1.

Genome annotation databases

EnsemblBacteriaiCAR69433; CAR69433; SPN23F16600.
GeneIDi7328841.
KEGGisne:SPN23F_16600.
PATRICi19674686. VBIStrPne132160_1745.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FM211187 Genomic DNA. Translation: CAR69433.1 .
RefSeqi YP_002511550.1. NC_011900.1.

3D structure databases

ProteinModelPortali B8ZM55.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 561276.SPN23F_16600.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAR69433 ; CAR69433 ; SPN23F16600 .
GeneIDi 7328841.
KEGGi sne:SPN23F_16600.
PATRICi 19674686. VBIStrPne132160_1745.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci SPNE561276:GJFJ-1592-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. "Role of conjugative elements in the evolution of the multidrug-resistant pandemic clone Streptococcus pneumoniae Spain23F ST81."
    Croucher N.J., Walker D., Romero P., Lennard N., Paterson G.K., Bason N.C., Mitchell A.M., Quail M.A., Andrew P.W., Parkhill J., Bentley S.D., Mitchell T.J.
    J. Bacteriol. 191:1480-1489(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700669 / Spain 23F-1.

Entry informationi

Entry nameiSYI_STRPJ
AccessioniPrimary (citable) accession number: B8ZM55
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: November 26, 2014
This is version 48 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