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.

Q31CU4

- SYI_PROM9

UniProt

Q31CU4 - SYI_PROM9

(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, PMT9312_0240
Organism
Prochlorococcus marinus (strain MIT 9312)
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 sitei582 – 5821Aminoacyl-adenylate By similarity
Binding sitei626 – 6261ATP By similarity
Metal bindingi936 – 9361Zinc By similarity
Metal bindingi939 – 9391Zinc By similarity
Metal bindingi956 – 9561Zinc By similarity
Metal bindingi959 – 9591Zinc 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

Enzyme and pathway databases

BioCyciPMAR74546:GHRG-246-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:PMT9312_0240
OrganismiProchlorococcus marinus (strain MIT 9312)
Taxonomic identifieri74546 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000002715: 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 – 968968Isoleucine--tRNA ligaseUniRule annotation
PRO_1000022100Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi74546.PMT9312_0240.

Structurei

3D structure databases

ProteinModelPortaliQ31CU4.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi68 – 7811"HIGH" regionUniRule annotation
Add
BLAST
Motifi623 – 6275"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.

Q31CU4-1 [UniParc]FASTAAdd to Basket

« Hide

MKSQNNKEYK SEFSYKETLN LLKTDFSMRA NSVLREPEIQ NFWAKNNIDF    50
ELGSNNSGKI FTLHDGPPYA NGALHMGHAL NKVLKDIINK YKTLRGFRVH 100
YVPGWDCHGL PIELKVLQNL KSSERKNLDT LNLRKKATDY AYVQINNQME 150
GFKRWGIWGN WDNPYLTLKK SYESAQIGVF GKMFLNGYIY RGLKPVHWSP 200
SSRTALAEAE LEYPDEHYSK SIYVSLKITK LSDEILLKFY QENPNFKKDF 250
FLSNSFITIW TTTPWTIPAN EAVAVNPKIN YVFAIDEEKR IYLLAKELSS 300
EISNKFNKDL TTLLEVKGVT LEDIEYQHPT KNKNCRIVIG GDYITIESGT 350
GIVHTAPGHG IDDFNVGRKY DLPTTCVVDE KGNLNEYSGQ FQGSNVLKDA 400
NDLIIDYLEE KDLLLLQENY KHRYPYDWRT KKPTIFRATE QWFASVNGFR 450
SSALKAIEDV EWIPATGKKR IYSMVVGRGD WCISRQRSWG LPIPVFYKKN 500
GNEILLNSEI INHIQKLFSE HGADIWWDWD VKHLLPDNYV KESDLWKKGT 550
DTMDVWFDSG SSWAAVCEQR SELKYPADLY LEGSDQHRGW FQSSLLTSVA 600
VNNKPPYKKV LTHGFALDEN GRKMSKSLGN VVDPNIIING GNNKKIEPAY 650
GADVLRLWVS SVDYSVDVPI GSNILKQLSD VYRKVRNTAR YLLGNIHDYD 700
PNIDSFEIDQ LPLLDQWMLG RLVEVTDQIS NAYENYEFSK FFQILQSFCV 750
VDLSNFYLDI AKDRLYVSSK SQFRRRSCQF VMSKVVENLA VLISPVLCHM 800
AEDIWQNVPY STKEKSVFQR GWPNFSQSWK NEILNEHIAN LRNLRVEINK 850
AIEGCRNKQI IGAALETEVN YLPKDKVVKD SLTWLKKFGN EEVDLFRDWL 900
IVSNFQVVSE LAKNSLIIDN NEIGKIQILK AHGQKCDRCW HYQEEIFSGI 950
QNTKLCKRCS HIINLEFT 968
Length:968
Mass (Da):111,880
Last modified:December 6, 2005 - v1
Checksum:i7C924A4490B4BEDA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000111 Genomic DNA. Translation: ABB49301.1.
RefSeqiWP_011375805.1. NC_007577.1.
YP_396737.1. NC_007577.1.

Genome annotation databases

EnsemblBacteriaiABB49301; ABB49301; PMT9312_0240.
GeneIDi3765026.
KEGGipmi:PMT9312_0240.
PATRICi23004102. VBIProMar70153_0245.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000111 Genomic DNA. Translation: ABB49301.1 .
RefSeqi WP_011375805.1. NC_007577.1.
YP_396737.1. NC_007577.1.

3D structure databases

ProteinModelPortali Q31CU4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 74546.PMT9312_0240.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABB49301 ; ABB49301 ; PMT9312_0240 .
GeneIDi 3765026.
KEGGi pmi:PMT9312_0240.
PATRICi 23004102. VBIProMar70153_0245.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci PMAR74546:GHRG-246-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. "Complete sequence of Prochlorococcus marinus str. MIT 9312."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MIT 9312.

Entry informationi

Entry nameiSYI_PROM9
AccessioniPrimary (citable) accession number: Q31CU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 6, 2005
Last modified: September 3, 2014
This is version 64 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

Similar proteinsi