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.

B8J3R3

- SYI_DESDA

UniProt

B8J3R3 - SYI_DESDA

(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, Ddes_0385
Organism
Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
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 sitei566 – 5661Aminoacyl-adenylate By similarity
Binding sitei610 – 6101ATP By similarity
Metal bindingi906 – 9061Zinc By similarity
Metal bindingi909 – 9091Zinc By similarity
Metal bindingi926 – 9261Zinc By similarity
Metal bindingi929 – 9291Zinc 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

BioCyciDDES525146:GIWF-397-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:Ddes_0385
OrganismiDesulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
Taxonomic identifieri525146 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio
ProteomesiUP000002598: 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 – 938938Isoleucine--tRNA ligaseUniRule annotation
PRO_1000189150Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi525146.Ddes_0385.

Structurei

3D structure databases

ProteinModelPortaliB8J3R3.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi58 – 6811"HIGH" regionUniRule annotation
Add
BLAST
Motifi607 – 6115"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.
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.

B8J3R3-1 [UniParc]FASTAAdd to Basket

« Hide

MSDYKKTLNL PQTAFPMKAN LAQREPEAIK KWEAANACAA MVEASGSEGT    50
YILHDGPPYA NGHLHMGHAL NKILKDIIVK SRNMAGYASW YVPGWDCHGL 100
PIEHKVEQDL KEKKKSLPAH VVRKLCREYA NKWLDVQRKE FKRLGVLGDW 150
DHPYISMDPA YEAVTAGELA KFVAAGGVAR AKKPIYWCCS CHTALAEAEV 200
EYNDHTSPSV YVRFALPDEG LKKVFAAADP ARAHVVIWTT TPWTLPDNMA 250
VCLHPEFTYA LVEAEGSQYI LAEELVASCA ETFGWSEYTI LDRATGERLE 300
GLKARHPFYD RQSSLVLGLH VTLDAGTGCV HTAPGHGRED YDVALKYGLE 350
IYSPMDDAGR FLPAVEFFAG LNVFEANPKV VEKLEEVGAL LQKGKIRHSY 400
PHCWRCKEPV IFRATTQWFI SMEKNDLRTR ALKAIDEEVR WIPAWGRERI 450
HNMVEFRPDW CISRQRQWGV PILALLCEDC GEAWNDPAWM QEIAARFAKH 500
PTGCDYWYEA ELKDVVPEGL ACPHCGGNHW KRETDILDVW FDSGTSFAAV 550
LEKRPELGFP ADLYLEGSDQ HRGWFHSSLL VSEGTRGCAP YRAVLTHGYV 600
VDGDGRKMSK SVGNVIAPQE LIEKFGAEIV RLWVSSVEYR EDIRLSDEIL 650
GRLVDAYRRI RNTCRFIMGN LSDITAHDLL SLDRLQPLDR FALDVAGRVH 700
ERVQQAYMDF DFHKVYHTLH NYCVTDLSSV YLDILKDRLY ASAPHSDERR 750
SAQTALWHIL CLLLRDMAPV LSFTAEEIFS HLPESLRGPE TTVFALPPLA 800
AAPYLLDEGT RDDWNVLLAV RGAVTKAIEP MRREGIIGHS LDTRITLFVA 850
DELRQRLEGL HTDLRAVCIV SQLHLEALDR APQAAYRDEE VAGLAIGVEK 900
ARGEKCERCW IYSTELGSDA SHPALCPRCT AVIKGMES 938
Length:938
Mass (Da):105,767
Last modified:March 3, 2009 - v1
Checksum:i9B0797693ACB46A0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001358 Genomic DNA. Translation: ACL48298.1.
RefSeqiWP_012624028.1. NC_011883.1.
YP_002478976.1. NC_011883.1.

Genome annotation databases

EnsemblBacteriaiACL48298; ACL48298; Ddes_0385.
GeneIDi7284048.
KEGGidds:Ddes_0385.
PATRICi21734148. VBIDesDes50650_0452.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001358 Genomic DNA. Translation: ACL48298.1 .
RefSeqi WP_012624028.1. NC_011883.1.
YP_002478976.1. NC_011883.1.

3D structure databases

ProteinModelPortali B8J3R3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 525146.Ddes_0385.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACL48298 ; ACL48298 ; Ddes_0385 .
GeneIDi 7284048.
KEGGi dds:Ddes_0385.
PATRICi 21734148. VBIDesDes50650_0452.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci DDES525146:GIWF-397-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 Desulfovibrio desulfuricans subsp. desulfuricans str. ATCC 27774."
    US DOE Joint Genome Institute
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L.
    , Kyrpides N., Ovchinnikova G., Hazen T.C.
    Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 27774 / DSM 6949.

Entry informationi

Entry nameiSYI_DESDA
AccessioniPrimary (citable) accession number: B8J3R3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: September 3, 2014
This is version 40 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