O58792 (SYI_PYRHO) 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:	PH1065

Organism

Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]

Taxonomic identifier

70601 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus › Pyrococcus horikoshii

Protein attributes

Sequence length	1066 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_02003
Catalytic activity	ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule 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. HAMAP-Rule MF_02003
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 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 – 1066	1066	Isoleucine--tRNA ligase HAMAP-Rule MF_02003		PRO_0000098590
Regions
	Motif	49 – 59	11	"HIGH" region HAMAP-Rule MF_02003
	Motif	625 – 629	5	"KMSKS" region HAMAP-Rule MF_02003
Sites
	Binding site	628	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	O58792 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 4C9444C82BB14018	FASTA	1,066	125,941
	10 20 30 40 50 60 MIKEPEFRDY TPGKLEEKIE EFWKENNIYQ KIKELRKNGP KYYFLDGPPY VSGAIHLGTA 70 80 90 100 110 120 WNKIIKDMII RFRTMQGYNV WRQPGFDMHG LPIEVKVEQA LGLKTKKEIE EKIGVENFIK 130 140 150 160 170 180 KCKEFALNNL KIMTEQFKML GIWMDWDDPY MTIKNEYIES AWFTLKKAWE KGLLEKDKRV 190 200 210 220 230 240 LHWCPRCETA LAEHEVRGEY KLRKDPSIYV KFPIEGKENE YLLIWTTTPW TLPANLAVSA 250 260 270 280 290 300 HPEYDYVKVK VEFNGKEEYW ILAKALVDKV LGEIGVKGEV IEEFKGRELE GLRYIHVLMD 310 320 330 340 350 360 EYPRQKEFRE KYEWAHRIIL ADFVTLEEGT GLVHTAPGHG EEDFEVGKKY GLPIYSPVDD 370 380 390 400 410 420 QGRYVEGKWK GIYVKEADPQ IIEHLKEKGY LVKAGEIEHK YPHCWRCKTP LIFRATDQWF 430 440 450 460 470 480 LKVSKVKDRI IKENDEKVTW YPDWVKIRFD NGVRDSGDWV ISRQRYWGIP LPIWQSEDGE 490 500 510 520 530 540 IYVVGSWREL VELAVAIEVN GERIDLPESY EEKLKVIEEK LGPEDLHRPY VDAFIIKVNG 550 560 570 580 590 600 KEMRRVKDVV DVWFDSGIAS WASLGYPRNK ELFEKLWPAD FIVEGEDQVT KWFYSQQAAS 610 620 630 640 650 660 VIAFDTVPYR RVAMHGYVLD EKGDKMSKSL GNIIRPEEVV EKAGRDTFRF YMLWATNPWE 670 680 690 700 710 720 NLKFSWKGVE QVRRMLNILW NVYVLSATYM SLDNFDPRNV KVEELAFREE DKWILSRVNS 730 740 750 760 770 780 LIREVENGIE TFYLTKATRA LYNFVVEDLS RWYVRLIRKR LWVEGDDPDK LAAYYTLWKV 790 800 810 820 830 840 FDVLLRLMAP FTPYITEEIY QNLMRPFIGI ESVHMLDWPK VDESAVDEDL EKEMEFIRRI 850 860 870 880 890 900 VEAGSAARQK ARIKLRYPVR KIIIETQDET VKKAVERLNY ILRDQLNAKE VVIGKVEREL 910 920 930 940 950 960 TVKPNFAKVG PEFKGDSRLV AKWINEHGLE LYEKGEVDVE IEGKKFHLTR EHIIVEEKLP 970 980 990 1000 1010 1020 DFLVAEDFEG GRVYVDKTLT RELLAEGLAR EFVRRIQEMR KRLDLDVNDR IVVTIETTDD 1030 1040 1050 1060 NRELLQENLD YIMRETRAIE VRFEEAKGYV VEWPEVQAKI GIEKVE

References

[1]

"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3." Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H. DNA Res. 5:55-76(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000001 Genomic DNA. Translation: BAA30164.1.
PIR	F71100.
RefSeq	NP_142976.1. NC_000961.1.
3D structure databases
ProteinModelPortal	O58792.
ModBase	Search...
Protein-protein interaction databases
STRING	70601.PH1065.
Proteomic databases
PRIDE	O58792.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAA30164; BAA30164; BAA30164.
GeneID	1443389.
KEGG	pho:PH1065.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0060.
HOGENOM	HOG000246403.
KO	K01870.
OMA	WFYSQLG.
ProtClustDB	PRK06039.
Enzyme and pathway databases
BioCyc	PHOR70601:GJWR-1060-MONOMER.
Family and domain databases
Gene3D	3.40.50.620. 2 hits. 3.90.740.10. 1 hit.
HAMAP	MF_02003. Ile_tRNA_synth_type2.
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR002300. aa-tRNA-synth_Ia. IPR002301. Ile-tRNA-ligase. IPR023585. Ile-tRNA-ligase_type1. 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]
PANTHER	PTHR11946:SF9. PTHR11946:SF9. 1 hit.
Pfam	PF08264. Anticodon_1. 1 hit. PF00133. tRNA-synt_1. 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_PYRHO

Accession

Primary (citable) accession number: O58792

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 1, 1998
Last modified:	May 1, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program