Q4AAS1 (SYI_MYCHJ) 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:	MHJ_0028

Organism

Mycoplasma hyopneumoniae (strain J / ATCC 25934 / NCTC 10110) [Complete proteome] [HAMAP]

Taxonomic identifier

262719 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Tenericutes › Mollicutes › Mycoplasmatales › Mycoplasmataceae › Mycoplasma › Mycoplasma hyopneumoniae

Protein attributes

Sequence length	886 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.
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. 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 – 886	886	Isoleucine--tRNA ligase HAMAP-Rule MF_02002		PRO_0000098420
Regions
	Motif	60 – 70	11	"HIGH" region HAMAP-Rule MF_02002
	Motif	587 – 591	5	"KMSKS" region HAMAP-Rule MF_02002
Sites
	Metal binding	856	1	Zinc By similarity
	Metal binding	859	1	Zinc By similarity
	Metal binding	870	1	Zinc By similarity
	Metal binding	873	1	Zinc By similarity
	Binding site	546	1	Aminoacyl-adenylate By similarity
	Binding site	590	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4AAS1 [UniParc]. Last modified May 29, 2007. Version 2. Checksum: CDCBAD01DD5853F7	FASTA	886	104,050
	10 20 30 40 50 60 MDKNFYKNSL NIFNSNFSMK ANLSEKDKFY ADFWEKNQIY QQILRKRRGN PRFILHDGPP 70 80 90 100 110 120 YANGDIHIGH ALNKILKDII VRYKTMAGFY SPFVPGWDTH GLPIENKIIN QIGSKSTLEI 130 140 150 160 170 180 RRKSNDFANS QILAQMKQFK KLNLLTDFKQ IYQTNTPNYE AKQLKLFKKM VSRGLVYRAL 190 200 210 220 230 240 KPVYWSPSSQ SALAEAEIEY LEYRSPSLFT SFDIKKGNNF VAENDKLIIW TTTPWTLIAN 250 260 270 280 290 300 SGVAVGENFD YVRIKNGENF YVLAANLLEK LAVIFDWKHY EIIDNFPGRA ILGIKYLHPI 310 320 330 340 350 360 FEKICPIVSG NHVSLDVGSG LVHLAPLFGE DDYWIGRENN LEMVMHVNDD GKFNENAGQF 370 380 390 400 410 420 SGQFYADSNK LITEFLEKKS KILHLSFIDH SFPHDWRTLK PVIYRGTPQW FVSIEKIKKD 430 440 450 460 470 480 LEKAIEEIEF PENWLKKRLT KMVVERKDWL ISRQRSWGIP LIIFYDQNKD PVLDKPEIFD 490 500 510 520 530 540 YIISLVEKFG SRIWYEKTTD ELLPEKYQNL GWTKENDILD VWFDSGVSFF AANISDEKPP 550 560 570 580 590 600 FDIYFEGSDQ YRGWFNSSLI NSVIYFGFSP YKKLLSHGFV VDAKGNKMSK SRGNGVDPLL 610 620 630 640 650 660 ILSKYGCDIF RLWVANSEYY NDIVYSEAIF EQNVEIYRKI RNTVRFLITN LADFKPTKYE 670 680 690 700 710 720 LTEVDLYIFN KIQKLKNEII QNYDQNRFVR VVKIINNFII EFSNFYLSIV KDILYADKKE 730 740 750 760 770 780 SLKRRQVQYN LYELLQVLNI AIAPIMPTTA EEIYSFIQKN NKQISVHMEE FFKESHFDEE 790 800 810 820 830 840 LDAKWNEFFQ IKDSVYQLIE QKIKSKEIKR PNEVGVLLKT DSDFIKSIDL KKLLMVAKVE 850 860 870 880 FSNGKTEILQ LNWEKCPRCW NHFEKINKVC ARCFEVLSEI VPEKNS

References

[1]

"Swine and poultry pathogens: the complete genome sequences of two strains of Mycoplasma hyopneumoniae and a strain of Mycoplasma synoviae." Vasconcelos A.T.R., Ferreira H.B., Bizarro C.V., Bonatto S.L., Carvalho M.O., Pinto P.M., Almeida D.F., Almeida L.G.P., Almeida R., Alves-Junior L., Assuncao E.N., Azevedo V.A.C., Bogo M.R., Brigido M.M., Brocchi M., Burity H.A., Camargo A.A., Camargo S.S. , Carepo M.S., Carraro D.M., de Mattos Cascardo J.C., Castro L.A., Cavalcanti G., Chemale G., Collevatti R.G., Cunha C.W., Dallagiovanna B., Dambros B.P., Dellagostin O.A., Falcao C., Fantinatti-Garboggini F., Felipe M.S.S., Fiorentin L., Franco G.R., Freitas N.S.A., Frias D., Grangeiro T.B., Grisard E.C., Guimaraes C.T., Hungria M., Jardim S.N., Krieger M.A., Laurino J.P., Lima L.F.A., Lopes M.I., Loreto E.L.S., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martinkovics C.T., Medeiros S.R.B., Moreira M.A.M., Neiva M., Ramalho-Neto C.E., Nicolas M.F., Oliveira S.C., Paixao R.F.C., Pedrosa F.O., Pena S.D.J., Pereira M., Pereira-Ferrari L., Piffer I., Pinto L.S., Potrich D.P., Salim A.C.M., Santos F.R., Schmitt R., Schneider M.P.C., Schrank A., Schrank I.S., Schuck A.F., Seuanez H.N., Silva D.W., Silva R., Silva S.C., Soares C.M.A., Souza K.R.L., Souza R.C., Staats C.C., Steffens M.B.R., Teixeira S.M.R., Urmenyi T.P., Vainstein M.H., Zuccherato L.W., Simpson A.J.G., Zaha A. J. Bacteriol. 187:5568-5577(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: J / ATCC 25934 / NCTC 10110.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017243 Genomic DNA. Translation: AAZ44122.2.
RefSeq	YP_278833.1. NC_007295.1.
3D structure databases
ProteinModelPortal	Q4AAS1.
ModBase	Search...
Protein-protein interaction databases
STRING	262719.MHJ_0028.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAZ44122; AAZ44122; MHJ_0028.
GeneID	3563614.
KEGG	mhj:MHJ_0028.
PATRIC	20013758. VBIMycHyo90918_0029.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0060.
HOGENOM	HOG000246402.
KO	K01870.
OMA	KQVLTHG.
ProtClustDB	PRK05743.
Enzyme and pathway databases
BioCyc	MHYO262719:GJ59-28-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_MYCHJ

Accession

Primary (citable) accession number: Q4AAS1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	May 29, 2007
Last modified:	May 1, 2013
This is version 64 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program