Reviewed, UniProtKB/Swiss-Prot P46207 (SYI_AQUPY)

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

Organism

Aquifex pyrophilus

Taxonomic identifier

2714 [NCBI]

Taxonomic lineage

Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length	529 AA.
Sequence status	Fragment.
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_02002
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 1 subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
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: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – ›529	›529	Isoleucyl-tRNA synthetase HAMAP MF_02002		PRO_0000098342
Regions
	Motif	523 – 527	5	"KMSKS" region HAMAP MF_02002
Sites
	Binding site	482	1	Aminoacyl-adenylate By similarity
	Binding site	526	1	ATP By similarity
Experimental info
	Non-terminal residue	1	1
	Non-terminal residue	529	1

Sequences

	Sequence		Length	Mass (Da)
	P46207-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: FB6C40D69E26DDD8	FASTA	529	61,379
	10 20 30 40 50 60 DTHGLPIERA VEKELSKKKI RKESLPKTEF RKLCREYANR YVNIQKEEFI RLGVLGDWEN 70 80 90 100 110 120 PYLTMSPEYE ATEIRELGKF FEKGLAYRSK KPVYWCIYDK TAEGQAEVEY YEKEDPSIYV 130 140 150 160 170 180 KFPLKKEIEG KKAYAVIWTT TPWTLPANLG IMVKEDADYS LVEVEGEVWI VAKELLENFF 190 200 210 220 230 240 KNIGKTYTRV LKDVKGRDLV GLEYEHPFVD RDELKGYLSE ETLKNMWRIY PSEFVSLDTG 250 260 270 280 290 300 TGLVHMAPGH GQEDYTVGKR YNLEPYAPLD DSGRFVEPAP EFIRGVRVFD ANKLIIALLK 310 320 330 340 350 360 EKGYLVHEAR IRHSYPHCWR CKNPVIFRAT PQWFIGMDIE YEGKTLSGES LEEIEKVKWI 370 380 390 400 410 420 PEYGKNRIKS MVENRPDWCI SRQRFWGVPI TVFYCENCGE VIKDKEVFER IASLVEKHPG 430 440 450 460 470 480 GTDVWFEKSP EEILPEGYKC PKCGGTSFRK EEDILDVWFD SGCSHASVIR PLGFEKADLY 490 500 510 520 LEGSDQHRGW FQASLLESVG SYGEAPYRSV LTHGFIVDEQ GRKMSKSLV

References

[1]	"Root of the universal tree of life based on ancient aminoacyl-tRNA synthetase gene duplications." Brown J.R., Doolittle W.F. Proc. Natl. Acad. Sci. U.S.A. 92:2441-2445(1995) [PubMed: 7708661] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	L37096 Genomic DNA. Translation: AAA87287.1.
PIR	I39658.
3D structure databases
HSSP	HSSP built from PDB template 1FFY based on UniProtKB P41972.
ModBase	Search...
Enzyme and pathway databases
BRENDA	6.1.1.5. 271525.
Family and domain databases
HAMAP	MF_02002. [Tree]
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR002300. aa-tRNA-synth_Ia. IPR015905. Ile-tRNA-synt_Ia_N. IPR018353. Isoleucyl-tRNA_synthetase. IPR014729. Rossmann-like_a/b/a_fold. [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	PF00133. tRNA-synt_1. 1 hit. [Graphical view]
PRINTS	PR00984. TRNASYNTHILE.
PROSITE	PS00178. AA_TRNA_LIGASE_I. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYI_AQUPY

Accession

Primary (citable) accession number: P46207

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 56 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)