A8G2P6 (SYI_PROM2) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Isoleucine--tRNA ligase
EC=6.1.1.5

Alternative name(s):
Isoleucyl-tRNA synthetase
Short name=IleRS

Gene names

Name:	ileS
Ordered Locus Names:	P9215_02601

Organism

Prochlorococcus marinus (strain MIT 9215) [Complete proteome] [HAMAP]

Taxonomic identifier

93060 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Cyanobacteria › Prochlorales › Prochlorococcaceae › Prochlorococcus › Prochlorococcus marinus

Protein attributes

Sequence length	965 AA.
Sequence status	Complete.
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. HAMAP-Rule MF_02002
Catalytic activity	ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02002
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_02002
Subunit structure	Monomer By similarity. HAMAP-Rule MF_02002
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_02002.
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. HAMAP-Rule MF_02002
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 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 regulation of translational fidelity Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP aminoacyl-tRNA editing activity Inferred from electronic annotation. Source: InterPro 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 – 965	965	Isoleucine--tRNA ligase HAMAP-Rule MF_02002		PRO_1000070890
Regions
	Motif	68 – 78	11	"HIGH" region HAMAP-Rule MF_02002
	Motif	623 – 627	5	"KMSKS" region HAMAP-Rule MF_02002
Sites
	Metal binding	936	1	Zinc By similarity
	Metal binding	939	1	Zinc By similarity
	Metal binding	956	1	Zinc By similarity
	Metal binding	959	1	Zinc By similarity
	Binding site	582	1	Aminoacyl-adenylate By similarity
	Binding site	626	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	A8G2P6 [UniParc]. Last modified November 13, 2007. Version 1. Checksum: 0AC02A57042FD2E0	FASTA	965	111,282
	10 20 30 40 50 60 MKSQNSKEQK SEFSYKETLN LLKTDFSMRA NSVLREPEIQ DFWAKNNIDF ELGLNNSGKT 70 80 90 100 110 120 FTLHDGPPYA NGSLHMGHAL NKVLKDIINK YKTLKGFKVH YVPGWDCHGL PIELKVLQNL 130 140 150 160 170 180 KSHERKNLNS LSLRKKATDY AHKQINNQME GFKRWGIWGD WDNPYLTLKK SYESAQIGVF 190 200 210 220 230 240 GKMFLNGYIY RGLKPVHWSP SSRTALAEAE LEYPDDHYSK SIYVSLKITK VPDKVLLKGC 250 260 270 280 290 300 QENPNIKKES FLGNSFITIW TTTPWTIPAN EAVAVNPKIS YVFVIDEDKR IFLFAKNLFS 310 320 330 340 350 360 EISEKFNKIF KILFEVKGSS LENIEYQHPT KNKNCRIVIG GDYITTESGT GIVHTAPGHG 370 380 390 400 410 420 IDDFNVGQKY DLPITCVVDE KGNLNEYSGQ FKGSNVLKDS NDLIIEYLKG KNLLLLQENY 430 440 450 460 470 480 KHRYPYDWRT KKPTIFRATE QWFASVDGFR SSALKAIEDV EWMPATGKKR IYSMVVGRGD 490 500 510 520 530 540 WCISRQRSWG VPIPVFYKKN GNEILLNSEI INHIQELFSE YGADIWWDWE VKNLLPENYL 550 560 570 580 590 600 KESDLWEKGT DTMDVWFDSG SSWAAVCEQR SELKYPADLY LEGSDQHRGW FQSSLLTSVA 610 620 630 640 650 660 VNNKPPYKRV LTHGFALDEN GRKMSKSLGN VVDPNIIING GNNKKSEPAY GADVLRLWVS 670 680 690 700 710 720 SVDYSVDVPI GSNILKQLSD VYRKVRNTAR YLLGNIHDYD PNIDSFEIDQ LPLLDQWMLG 730 740 750 760 770 780 RLVEVSSQIS HAYESYEFSR FFQILQSFCV VDLSNFYLDI AKDRLYVSAK SQFRRRSCQF 790 800 810 820 830 840 VMSKVVENLA VLISPVLCHM AEDIWQNIPY LTKEKSVFQR GWPIFSQSWK NESLNQHITN 850 860 870 880 890 900 LRNLRVEINK AIEGCRNKQI IGAALETEVN YLPKDKFVKD SLNWLRKFGN EDVDLFRDWL 910 920 930 940 950 960 IVSNFQVVSY LAENSLIIDS NELGEIQILK ARGLKCDRCW HYQKEIVSGI QNTKLCKRCA KIINL

References

[1]

"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus." Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W. PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MIT 9215.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000825 Genomic DNA. Translation: ABV49877.1.
RefSeq	YP_001483463.1. NC_009840.1.
3D structure databases
ProteinModelPortal	A8G2P6.
ModBase	Search...
Protein-protein interaction databases
STRING	93060.P9215_02601.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABV49877; ABV49877; P9215_02601.
GeneID	5616291.
KEGG	pmh:P9215_02601.
PATRIC	22989932. VBIProMar119824_0257.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0060.
HOGENOM	HOG000246402.
KO	K01870.
OMA	KQVLTHG.
ProtClustDB	PRK05743.
Enzyme and pathway databases
BioCyc	PMAR93060:GI08-265-MONOMER.
Family and domain databases
Gene3D	3.40.50.620. 2 hits. 3.90.740.10. 1 hit.
HAMAP	MF_02002. Ile_tRNA_synth_type1.
InterPro	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]
PANTHER	PTHR11946:SF9. PTHR11946:SF9. 1 hit.
Pfam	PF08264. Anticodon_1. 1 hit. PF00133. tRNA-synt_1. 1 hit. PF06827. zf-FPG_IleRS. 1 hit. [Graphical view]
PRINTS	PR00984. TRNASYNTHILE.
SUPFAM	SSF47323. tRNAsyn_1a_bind. 1 hit. SSF50677. ValRS_IleRS_edit. 1 hit.
TIGRFAMs	TIGR00392. ileS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYI_PROM2

Accession

Primary (citable) accession number: A8G2P6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	November 13, 2007
Last modified:	May 29, 2013
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program