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B0C872 (SYI_ACAM1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:AM1_3907
OrganismAcaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]
Taxonomic identifier329726 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesAcaryochloris

Protein attributes

Sequence length971 AA.
Sequence statusComplete.
Protein existenceInferred 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 processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processisoleucyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

aminoacyl-tRNA editing activity

Inferred from electronic annotation. Source: InterPro

isoleucine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 971971Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000088541

Regions

Motif60 – 7011"HIGH" region HAMAP-Rule MF_02002
Motif604 – 6085"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9221Zinc By similarity
Metal binding9251Zinc By similarity
Metal binding9421Zinc By similarity
Metal binding9451Zinc By similarity
Binding site5631Aminoacyl-adenylate By similarity
Binding site6071ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B0C872 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 206CB68F80AB54D3

FASTA971109,792
        10         20         30         40         50         60 
MTEPGRYKKT VNLPKTKFDM RANAVKREPE LQKFWADHQI YENLSQNNPG DVFVLHDGPP 

        70         80         90        100        110        120 
YANGDLHIGH ALNKILKDTI NKFQLLQGRK VRYVPGWDCH GLPIELKVLQ NIQPENRAKL 

       130        140        150        160        170        180 
TPLKLRWKAR DFALKTVEKQ SKSFQRYGVW GNWENPYLTL KPEYEAAQIG VFGKMALKGY 

       190        200        210        220        230        240 
IYRGFKPVYW SPSSQTALAE AELEYPEGHT SRSIYVTFKV TGLSETAQPL LDEYLPTLKV 

       250        260        270        280        290        300 
AIWTTTPWTI PGNLAVSLNP DLTYAVVKAG EDYLIVAEDL VETLTETLES SFKVIKTLPG 

       310        320        330        340        350        360 
KALENSTYQH PLFEREGPLV LGDYVTTESG TGLVHTAPGH GQEDYQVGQQ YGLAMLSPVD 

       370        380        390        400        410        420 
GDGTFTDEAG PFAGLNVLNG GNEAVIEALQ SAGALLKEES YAHKYPYDWR TKKPVILRAT 

       430        440        450        460        470        480 
EQWFASVDGF REAVLDAIAT VNWIPAQGEN RITSMVSERS DWCISRQRNW GVPIPVFYND 

       490        500        510        520        530        540 
ATGEPLLNEA TVNHIQGIVA EKGSDAWWEL DNDELLPEPY RSDGNTYRKG TDTMDVWFDS 

       550        560        570        580        590        600 
GSSWAAVCDQ REPLKYPAEM YLEGSDQHRG WFQSSILTSV ATNGHAPYKT VLTHGFVLDE 

       610        620        630        640        650        660 
QGRKMSKSIG NVVDPAIVIA GGKNQKQDPP YGADVLRLWV SSVDYASDVP LGKNILKQMA 

       670        680        690        700        710        720 
DVYRKIRNTS RFLLGNLHDF DPAQDAVAYE DLPQLDRYML HRITEVFTDV TEAFESFQFF 

       730        740        750        760        770        780 
RFFQTVQNFC VVDLSNFYLD IAKDRLYISE PNAQRRRSCQ TVLAIALENL ARAIAPVLSH 

       790        800        810        820        830        840 
MAEDIWQSLP YETEHQSVFA SGWMRLEDQW HNPDLASHWI VLREIRQEVN KVLEQARTEK 

       850        860        870        880        890        900 
EIGSSLEAKV LLYVSDTDLR QQLDAMNPST GGGSNNVDEL RYLFLASQVE LLETPKNLDR 

       910        920        930        940        950        960 
LMYQFQSETL GVGVVTADGK KCDRCWNYST YVGRSKQHPL LCDRCEPIIE NLVTQGQISL 

       970 
TEEGRYQPNT K 

« Hide

References

[1]"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina."
Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. expand/collapse author list , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W.
Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MBIC 11017.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000828 Genomic DNA. Translation: ABW28892.1.
RefSeqYP_001518209.1. NC_009925.1.

3D structure databases

ProteinModelPortalB0C872.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING329726.AM1_3907.

Proteomic databases

PRIDEB0C872.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABW28892; ABW28892; AM1_3907.
GeneID5682711.
KEGGamr:AM1_3907.
PATRIC20621992. VBIAcaMar40141_3622.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycAMAR329726:GCZJ-3894-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02002. Ile_tRNA_synth_type1.
InterProIPR001412. 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]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
SUPFAMSSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_ACAM1
AccessionPrimary (citable) accession number: B0C872
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 26, 2008
Last modified: May 14, 2014
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries