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Q5PAL9

- SYI_ANAMM

UniProt

Q5PAL9 - SYI_ANAMM

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Protein
Isoleucine--tRNA ligase
Gene
ileS, AM684
Organism
Anaplasma marginale (strain St. Maries)
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

Zinc By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei632 – 6321ATP 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
Complete GO annotation...

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

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:AM684
OrganismiAnaplasma marginale (strain St. Maries)
Taxonomic identifieri234826 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeAnaplasma
ProteomesiUP000006557: 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 – 11011101Isoleucine--tRNA ligaseUniRule annotation
PRO_0000098514Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi234826.AM684.

Structurei

3D structure databases

ProteinModelPortaliQ5PAL9.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi50 – 6011"HIGH" regionUniRule annotation
Add
BLAST
Motifi629 – 6335"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.
HOGENOMiHOG000246403.
KOiK01870.
OMAiENRDWFE.
OrthoDBiEOG644ZM1.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPiMF_02003. Ile_tRNA_synth_type2.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023586. Ile-tRNA-ligase_type2.
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]
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.

Q5PAL9-1 [UniParc]FASTAAdd to Basket

« Hide

MNYYPEVKGN PEFSAIEKEI LQYWNSEKIF EESVNTRSRD RSFVFYDGPP     50
FANGLPHYGH LLTGFIKDAV ARYKTMRGFR VERKFGWDCH GLPAEMLAEK 100
ELGVSGKVSI ESFGIDKFND YCRSSIMRFT QQWREYVERQ GRWVDFENGY 150
RTMDKSFMES VMWAFHELWH KGLVYESVKV VPYSWACQTP LSNFETKMDN 200
AYREKVSKSV TVRFKLSEQV GFVPQGVESC SILAWTTTPW TLVSNFALAI 250
NTNMDYVGAV VGAEMLIFSA GYLDHFMRYC ERHSLECAKV VQIPAKELLA 300
VKYMPPFPYF ADSKNAFMVL DAEFVAEGAG TGIVHLAPGF GEDDFLLCKQ 350
HGIPNLGEES RGMLSVICPI DDAGRFTAAV GDFAGQHVFD VVDAVIRQLK 400
EKGLWFATEQ CTHSYPHCWR TDTPLIYRAT SSWYVEVTKL KARMVELNKE 450
VNWVPEHVQS GQFGKWLDGA KDWSVSRHRF WGAPVPVWRS DDPKYPRTDV 500
YGSIKKVLPD VKALEEDFGP VEDLHRPYID NLVRPNPDDP TGKSMMRRVP 550
DVLDCWFESG SMPYAQMHYP FENKEFFDSH FPADFITEYI AQTRGWFYTL 600
FVLSTGLFDR HPFKNCICHG VVLDIKGQKL SKRLNNYPDP MEMFEKYGAD 650
SVRFTMLSHA VSIGGDLLLD QDGDVVRDTL KSVVKPIWNS YSFFTVYANS 700
DQMQGRILES LEGITNIMDQ YILYECACMV VKVLEAMESS SAGVRDPYNI 750
RLACAAIVQF SDKLNNWYIR GCRGRFWMRD KTADKSDAYN TLYTVLYHLA 800
RTIAPFLPFI AESIWLGLSF QREKSVHLAD FPDASSFSAV HQYKKNAEYM 850
QLAMDVCSHV LSLRNAHNIR VRQPLRRMVV YPYNCESLLD MPQQYRDIIL 900
NEVNVKSLQI ASTIGDMASF ELKLNFALLG QRVPEKVKQI ITLARAGVWE 950
VQSDGSLLLG APGCEQCVIQ KDEFSLNLKV HSEYACQIIS GGVPVGVLHI 1000
DHELTRELLL EGIARDVMRL IQQARKDCGL EMLDHAEVII NTDAAEIIEA 1050
ISIWYDFIKQ QTFSHTLEHR PAQAVVEDCS KYTKISGKDF DIFLCKSALC 1100
S 1101
Length:1,101
Mass (Da):125,904
Last modified:January 4, 2005 - v1
Checksum:i981A2927BF1933CD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000030 Genomic DNA. Translation: AAV86661.1.
RefSeqiYP_153916.1. NC_004842.2.

Genome annotation databases

EnsemblBacteriaiAAV86661; AAV86661; AM684.
GeneIDi3171286.
KEGGiama:AM684.
PATRICi20947361. VBIAnaMar46146_0597.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000030 Genomic DNA. Translation: AAV86661.1 .
RefSeqi YP_153916.1. NC_004842.2.

3D structure databases

ProteinModelPortali Q5PAL9.
ModBasei Search...

Protein-protein interaction databases

STRINGi 234826.AM684.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAV86661 ; AAV86661 ; AM684 .
GeneIDi 3171286.
KEGGi ama:AM684.
PATRICi 20947361. VBIAnaMar46146_0597.

Phylogenomic databases

eggNOGi COG0060.
HOGENOMi HOG000246403.
KOi K01870.
OMAi ENRDWFE.
OrthoDBi EOG644ZM1.

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_02003. Ile_tRNA_synth_type2.
InterProi IPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023586. Ile-tRNA-ligase_type2.
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 ]
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 genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins."
    Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr.
    Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: St. Maries.

Entry informationi

Entry nameiSYI_ANAMM
AccessioniPrimary (citable) accession number: Q5PAL9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 4, 2005
Last modified: May 14, 2014
This is version 67 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

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