Isoleucine--tRNA ligase - Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)

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O29622 (SYI_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 89. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	AF_0633

Organism

Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) [Reference proteome] [HAMAP]

Taxonomic identifier

224325 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus ›

Protein attributes

Sequence length	1018 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 Reference 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 – 1018

1018

Isoleucine--tRNA ligase HAMAP-Rule MF_02003

PRO_0000098575

Regions

Motif

43 – 53

"HIGH" region HAMAP-Rule MF_02003

Motif

586 – 590

"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site

589

ATP By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

O29622 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 58C8BBE472FF1D0F
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FASTA

1,018

118,885

        10         20         30         40         50         60 
MLPAKYSPKD VESEIFKFWE DNDIYRKVKE KGGRKFYFVD GPPYTTGRIH LGTAWNKVLK 

        70         80         90        100        110        120 
DTILRYKRMM GFAPTDTPGW DMHGLPIEVK VEQELGFRTK RDIESFGIDK FIERCMNYAL 

       130        140        150        160        170        180 
ANKDAMTEQF KSLAVWMDWE NPYMTIKAEY MNAAWFAIKR AHERGLLERK KMVVNWCHRC 

       190        200        210        220        230        240 
ETALADAEVE YWDEEDPSIY VKFPVKGEKD TYIVIWTTTP WTLPANMAVA VHPSLEYAKF 

       250        260        270        280        290        300 
RAVKDGKVEY LILAKELADS VLGKGDYDSW EVVETYLGED LEGLEYEHPL ADEVPLQKNW 

       310        320        330        340        350        360 
KHQVFFADFV TAENTGCVHI APGHGVEDYE LGVEKGLEVF NPVDDRGVYT EEAGKYAGKH 

       370        380        390        400        410        420 
VKEANDDIID DLYRKDLLLA EERIVHRYGH CWRCKTPIIY RATEQWFIKI SELKDEMLEE 

       430        440        450        460        470        480 
IDKVMWIPEW AGSARFKDWV SNAKDWCISR QRYWGIPIPV WICEKCGEMK VVGSINEIEW 

       490        500        510        520        530        540 
ENDLDLHRPK IDAVTFSCQC GGVMRRVPDV FDVWFDSGVA SWGSIAYPLR KDKFEELWPA 

       550        560        570        580        590        600 
DFITEGHDQT RGWFYSQLGT SVVCFDKAPY KAVLMHGFTL DEQGRKMSKS LGNVVEPEEV 

       610        620        630        640        650        660 
VGQIGVDGFR LYVLYSAPWE DLRFSWEEAR NINRMLNVVW NAVRFAHTYM SLDNYSFGEK 

       670        680        690        700        710        720 
GELKIEDRWI LSRLESFIKE ANEAMEGYQV HRVVRAFFDF FVEDFSRWYI QIIRPRVWEE 

       730        740        750        760        770        780 
RDSPSKLAAY YTMFRVIDRS LRAIAPFAPL IAEWFYQHVV KEFREGEESI FMEEYSTAEV 

       790        800        810        820        830        840 
EMIDGELEAA MKVAKEIVEA AANARNKAKR KLRWPLRELV IESGSEKVRK AVEMLEETIL 

       850        860        870        880        890        900 
SQCNVKQVRV VDSFEKEIEI KPNYKYIGPL LKEKAGEFAK YVASLKEIPE KLVFDGVELD 

       910        920        930        940        950        960 
PKQAIVVDYR LPEGYEYAEF SGGVVYIYKE LDDELVREAF AREVIRRIQE MRKELDLDVE 

       970        980        990       1000       1010 
EFIETTVEMD AELVKGWEDY IKSETRSQKL VFGKAEGYVR EWNIEGKKVK IGIKRLRG

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References

[1]

"The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus."
Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G.

Venter J.C.
Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000782 Genomic DNA. Translation: AAB90608.1.
PIR	A69329.
RefSeq	NP_069467.1. NC_000917.1.
3D structure databases
ProteinModelPortal	O29622.
ModBase	Search...
Protein-protein interaction databases
STRING	224325.AF0633.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAB90608; AAB90608; AF_0633.
GeneID	1483851.
KEGG	afu:AF0633.
Phylogenomic databases
eggNOG	COG0060.
KO	K01870.
OMA	WFYSQLG.
ProtClustDB	PRK06039.
Enzyme and pathway databases
BioCyc	AFUL224325:GJBC-648-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_ARCFU

Accession

Primary (citable) accession number: O29622

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents