Reviewed, UniProtKB/Swiss-Prot Q5PAL9 (SYI_ANAMM)

Names and origin

Protein names

Recommended name:
    Isoleucyl-tRNA synthetase
    EC=6.1.1.5
Alternative name(s):
    Isoleucine--tRNA ligase
      Short name=IleRS

Gene names

Name:	ileS
Ordered Locus Names:	AM684

Organism

Anaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]

Taxonomic identifier

234826 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma

Protein attributes

Sequence length	1101 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	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.
Catalytic activity	ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP MF_02003
Cofactor	Zinc By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity.
Domain	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.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	isoleucyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP isoleucine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1101	1101	Isoleucyl-tRNA synthetase HAMAP MF_02003		PRO_0000098514
Regions
	Motif	50 – 60	11	"HIGH" region HAMAP MF_02003
	Motif	629 – 633	5	"KMSKS" region HAMAP MF_02003
Sites
	Binding site	632	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5PAL9-1 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 981A2927BF1933CD	FASTA	1,101	125,904
	10 20 30 40 50 60 MNYYPEVKGN PEFSAIEKEI LQYWNSEKIF EESVNTRSRD RSFVFYDGPP FANGLPHYGH 70 80 90 100 110 120 LLTGFIKDAV ARYKTMRGFR VERKFGWDCH GLPAEMLAEK ELGVSGKVSI ESFGIDKFND 130 140 150 160 170 180 YCRSSIMRFT QQWREYVERQ GRWVDFENGY RTMDKSFMES VMWAFHELWH KGLVYESVKV 190 200 210 220 230 240 VPYSWACQTP LSNFETKMDN AYREKVSKSV TVRFKLSEQV GFVPQGVESC SILAWTTTPW 250 260 270 280 290 300 TLVSNFALAI NTNMDYVGAV VGAEMLIFSA GYLDHFMRYC ERHSLECAKV VQIPAKELLA 310 320 330 340 350 360 VKYMPPFPYF ADSKNAFMVL DAEFVAEGAG TGIVHLAPGF GEDDFLLCKQ HGIPNLGEES 370 380 390 400 410 420 RGMLSVICPI DDAGRFTAAV GDFAGQHVFD VVDAVIRQLK EKGLWFATEQ CTHSYPHCWR 430 440 450 460 470 480 TDTPLIYRAT SSWYVEVTKL KARMVELNKE VNWVPEHVQS GQFGKWLDGA KDWSVSRHRF 490 500 510 520 530 540 WGAPVPVWRS DDPKYPRTDV YGSIKKVLPD VKALEEDFGP VEDLHRPYID NLVRPNPDDP 550 560 570 580 590 600 TGKSMMRRVP DVLDCWFESG SMPYAQMHYP FENKEFFDSH FPADFITEYI AQTRGWFYTL 610 620 630 640 650 660 FVLSTGLFDR HPFKNCICHG VVLDIKGQKL SKRLNNYPDP MEMFEKYGAD SVRFTMLSHA 670 680 690 700 710 720 VSIGGDLLLD QDGDVVRDTL KSVVKPIWNS YSFFTVYANS DQMQGRILES LEGITNIMDQ 730 740 750 760 770 780 YILYECACMV VKVLEAMESS SAGVRDPYNI RLACAAIVQF SDKLNNWYIR GCRGRFWMRD 790 800 810 820 830 840 KTADKSDAYN TLYTVLYHLA RTIAPFLPFI AESIWLGLSF QREKSVHLAD FPDASSFSAV 850 860 870 880 890 900 HQYKKNAEYM QLAMDVCSHV LSLRNAHNIR VRQPLRRMVV YPYNCESLLD MPQQYRDIIL 910 920 930 940 950 960 NEVNVKSLQI ASTIGDMASF ELKLNFALLG QRVPEKVKQI ITLARAGVWE VQSDGSLLLG 970 980 990 1000 1010 1020 APGCEQCVIQ KDEFSLNLKV HSEYACQIIS GGVPVGVLHI DHELTRELLL EGIARDVMRL 1030 1040 1050 1060 1070 1080 IQQARKDCGL EMLDHAEVII NTDAAEIIEA ISIWYDFIKQ QTFSHTLEHR PAQAVVEDCS 1090 1100 KYTKISGKDF DIFLCKSALC S

References

[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: 15618402] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000030 Genomic DNA. Translation: AAV86661.1.
RefSeq	YP_153916.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3171286.
GenomeReviews	Gene locus AM684 in contig CP000030_GR.
KEGG	ama:AM684.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q5PAL9.
OMA	Q5PAL9. SNWYVRR.
Enzyme and pathway databases
BioCyc	AMAR234826:AM684-MON.
Family and domain databases
HAMAP	MF_02003. [Tree]
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR002300. aa-tRNA-synth_Ia. IPR002301. Ile-tRNA-synt_Ia. IPR015905. Ile-tRNA-synt_Ia_N. IPR018353. Isoleucyl-tRNA_synthetase. IPR014729. Rossmann-like_a/b/a_fold. IPR013155. V/L/I-tRNA-synth_anticodon-bd. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHER	PTHR11946:SF9. Ile-tRNA-synt_Ia. 1 hit.
Pfam	PF08264. Anticodon_1. 1 hit. PF00133. tRNA-synt_1. 1 hit. [Graphical view]
PRINTS	PR00984. TRNASYNTHILE.
TIGRFAMs	TIGR00392. ileS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYI_ANAMM

Accession

Primary (citable) accession number: Q5PAL9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	January 4, 2005
Last modified:	June 16, 2009
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)