Skip Header

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

Q5PAL9

- SYI_ANAMM

UniProt

Q5PAL9 - SYI_ANAMM

(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
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).UniRule annotation

Catalytic activityi

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile).UniRule annotation

Cofactori

Zinc.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei632 – 6321ATPUniRule 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

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:AM684
OrganismiAnaplasma marginale (strain St. Maries)
Taxonomic identifieri234826 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeAnaplasma
ProteomesiUP000006557: 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 – 11011101Isoleucine--tRNA ligasePRO_0000098514Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi234826.AM684.

Structurei

3D structure databases

ProteinModelPortaliQ5PAL9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi50 – 6011"HIGH" regionAdd
BLAST
Motifi629 – 6335"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 2 subfamily.UniRule annotation

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

        10         20         30         40         50
MNYYPEVKGN PEFSAIEKEI LQYWNSEKIF EESVNTRSRD RSFVFYDGPP
60 70 80 90 100
FANGLPHYGH LLTGFIKDAV ARYKTMRGFR VERKFGWDCH GLPAEMLAEK
110 120 130 140 150
ELGVSGKVSI ESFGIDKFND YCRSSIMRFT QQWREYVERQ GRWVDFENGY
160 170 180 190 200
RTMDKSFMES VMWAFHELWH KGLVYESVKV VPYSWACQTP LSNFETKMDN
210 220 230 240 250
AYREKVSKSV TVRFKLSEQV GFVPQGVESC SILAWTTTPW TLVSNFALAI
260 270 280 290 300
NTNMDYVGAV VGAEMLIFSA GYLDHFMRYC ERHSLECAKV VQIPAKELLA
310 320 330 340 350
VKYMPPFPYF ADSKNAFMVL DAEFVAEGAG TGIVHLAPGF GEDDFLLCKQ
360 370 380 390 400
HGIPNLGEES RGMLSVICPI DDAGRFTAAV GDFAGQHVFD VVDAVIRQLK
410 420 430 440 450
EKGLWFATEQ CTHSYPHCWR TDTPLIYRAT SSWYVEVTKL KARMVELNKE
460 470 480 490 500
VNWVPEHVQS GQFGKWLDGA KDWSVSRHRF WGAPVPVWRS DDPKYPRTDV
510 520 530 540 550
YGSIKKVLPD VKALEEDFGP VEDLHRPYID NLVRPNPDDP TGKSMMRRVP
560 570 580 590 600
DVLDCWFESG SMPYAQMHYP FENKEFFDSH FPADFITEYI AQTRGWFYTL
610 620 630 640 650
FVLSTGLFDR HPFKNCICHG VVLDIKGQKL SKRLNNYPDP MEMFEKYGAD
660 670 680 690 700
SVRFTMLSHA VSIGGDLLLD QDGDVVRDTL KSVVKPIWNS YSFFTVYANS
710 720 730 740 750
DQMQGRILES LEGITNIMDQ YILYECACMV VKVLEAMESS SAGVRDPYNI
760 770 780 790 800
RLACAAIVQF SDKLNNWYIR GCRGRFWMRD KTADKSDAYN TLYTVLYHLA
810 820 830 840 850
RTIAPFLPFI AESIWLGLSF QREKSVHLAD FPDASSFSAV HQYKKNAEYM
860 870 880 890 900
QLAMDVCSHV LSLRNAHNIR VRQPLRRMVV YPYNCESLLD MPQQYRDIIL
910 920 930 940 950
NEVNVKSLQI ASTIGDMASF ELKLNFALLG QRVPEKVKQI ITLARAGVWE
960 970 980 990 1000
VQSDGSLLLG APGCEQCVIQ KDEFSLNLKV HSEYACQIIS GGVPVGVLHI
1010 1020 1030 1040 1050
DHELTRELLL EGIARDVMRL IQQARKDCGL EMLDHAEVII NTDAAEIIEA
1060 1070 1080 1090 1100
ISIWYDFIKQ QTFSHTLEHR PAQAVVEDCS KYTKISGKDF DIFLCKSALC

S
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.
RefSeqiWP_011114394.1. NC_004842.2.
YP_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 WP_011114394.1. NC_004842.2.
YP_153916.1. NC_004842.2.

3D structure databases

ProteinModelPortali Q5PAL9.
ModBasei Search...
MobiDBi 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: October 29, 2014
This is version 69 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