(data stored in ACNUC7421 zone)

SWISSPROT: Q2ILW2_ANADE

ID   Q2ILW2_ANADE            Unreviewed;       946 AA.
AC   Q2ILW2;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 109.
DE   RecName: Full=Isoleucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02002};
DE            EC=6.1.1.5 {ECO:0000256|HAMAP-Rule:MF_02002};
DE   AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02002};
DE            Short=IleRS {ECO:0000256|HAMAP-Rule:MF_02002};
GN   Name=ileS {ECO:0000256|HAMAP-Rule:MF_02002};
GN   OrderedLocusNames=Adeh_0012 {ECO:0000313|EMBL:ABC79790.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC79790.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As
CC       IleRS can inadvertently accommodate and process structurally
CC       similar amino acids such as valine, to avoid such errors it has
CC       two additional distinct tRNA(Ile)-dependent editing activities.
CC       One activity is designated as 'pretransfer' editing and involves
CC       the hydrolysis of activated Val-AMP. The other activity is
CC       designated 'posttransfer' editing and involves deacylation of
CC       mischarged Val-tRNA(Ile). {ECO:0000256|HAMAP-Rule:MF_02002}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-
CC         isoleucyl-tRNA(Ile); Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666,
CC         Rhea:RHEA-COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58045, ChEBI:CHEBI:78442, ChEBI:CHEBI:78528,
CC         ChEBI:CHEBI:456215; EC=6.1.1.5; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02002, ECO:0000256|SAAS:SAAS01125826};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02002};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_02002};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02002}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02002}.
CC   -!- DOMAIN: IleRS has two distinct active sites: one for
CC       aminoacylation and one for editing. The misactivated valine is
CC       translocated from the active site to the editing site, which
CC       sterically excludes the correctly activated isoleucine. The single
CC       editing site contains two valyl binding pockets, one specific for
CC       each substrate (Val-AMP or Val-tRNA(Ile)). {ECO:0000256|HAMAP-
CC       Rule:MF_02002}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. IleS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_02002}.
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DR   EMBL; CP000251; ABC79790.1; -; Genomic_DNA.
DR   RefSeq; WP_011419073.1; NC_007760.1.
DR   STRING; 290397.Adeh_0012; -.
DR   EnsemblBacteria; ABC79790; ABC79790; Adeh_0012.
DR   KEGG; ade:Adeh_0012; -.
DR   eggNOG; ENOG4105C07; Bacteria.
DR   eggNOG; COG0060; LUCA.
DR   HOGENOM; HOG000246402; -.
DR   KO; K01870; -.
DR   OMA; HLGTAWN; -.
DR   BioCyc; ADEH290397:G1G5W-13-MONOMER; -.
DR   Proteomes; UP000001935; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR   HAMAP; MF_02002; Ile_tRNA_synth_type1; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR033708; Anticodon_Ile_BEm.
DR   InterPro; IPR002301; Ile-tRNA-ligase.
DR   InterPro; IPR023585; Ile-tRNA-ligase_type1.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   InterPro; IPR010663; Znf_FPG/IleRS.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 2.
DR   Pfam; PF06827; zf-FPG_IleRS; 1.
DR   PRINTS; PR00984; TRNASYNTHILE.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q2ILW2.
DR   SWISS-2DPAGE; Q2ILW2.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02002,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00470441,
KW   ECO:0000313|EMBL:ABC79790.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02002,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00470429};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001935};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02002};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02002,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00106025,
KW   ECO:0000313|EMBL:ABC79790.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02002};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02002,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00470402};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02002,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00470368};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_02002}.
FT   DOMAIN       27    277       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      321    673       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      719    870       Anticodon_1. {ECO:0000259|Pfam:PF08264}.
FT   DOMAIN      918    943       zf-FPG_IleRS. {ECO:0000259|Pfam:PF06827}.
FT   MOTIF        60     70       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02002}.
FT   MOTIF       636    640       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02002}.
FT   METAL       919    919       Zinc. {ECO:0000256|HAMAP-Rule:MF_02002}.
FT   METAL       922    922       Zinc. {ECO:0000256|HAMAP-Rule:MF_02002}.
FT   METAL       939    939       Zinc. {ECO:0000256|HAMAP-Rule:MF_02002}.
FT   METAL       942    942       Zinc. {ECO:0000256|HAMAP-Rule:MF_02002}.
FT   BINDING     595    595       Aminoacyl-adenylate. {ECO:0000256|HAMAP-
FT                                Rule:MF_02002}.
FT   BINDING     639    639       ATP. {ECO:0000256|HAMAP-Rule:MF_02002}.
SQ   SEQUENCE   946 AA;  105571 MW;  8442A39CC629AE31 CRC64;
     MDSKYSVNLP KTDFPMKANL PQREPEILRQ WEEQAIFQRL VAQNAGRPGA KRFVLHDGPP
     YANGDIHIGH ALNKILKDVV VKYRNLNGEV ADYIPGWDCH GLPIELKVDK ELGPKKRELD
     RPAIIEACRK YAQKWIEKQR ESFKRLGVFG RWETPYATMS RGYEAEIVRT FARAAEKGFL
     YRGKKPVYWC ITDRTALAEA EVEYEQHRSP SIYVAFDLVS KLPDPKLAGR PARLVIWTTT
     PWTLPANLAV AAHPEFTYVA YDLNGQVVVV AKDLLAGFLA DVAPGELSVT DVPAPHSPPA
     HEAATGGGGT VLAPHLAHPE RVLAHLDGSA LEGLRYRHPF LDRESQVILG DHVTLEAGTG
     LVHTAPGHGQ EDYVVGLRYG LEVLNPVDGA GRFTERAGKY AGKKIFEANP EIVADLAASG
     HLLSDPKASL EHSYPHCWRC HNPVVFRATD QWFLSLEHAD LRKATLAEID RVRWIPHWGR
     ERIHNMIENR PDWCVSRQRT WGVPIPVFYC EGCNEALLSP PVMERVAAAF EAEGMEAWYR
     HPPADFTQGA ACPKCGKTEF RREQDILDVW WDSGVSWAAV IEREGLELPV DLYLEGSDQH
     RGWFHSSLLT SMALRGAAPY RAVLTHGFIL DQHGKAMSKS AGNGIEPSEI IKKYGADILR
     LWVSASDYRD DIGLGDQILA GLAEGYRKIR NTIRYALGAL DGFDPARDAV PEAELEPIDR
     WALARLAAWD EKVAKAYEDY EFHLAYHATM QFCAVELSAL YFDVIKDRLY TWKADGRQRR
     SAQTALHAIA QDLIRLLAPI LSFTASEAWS YLPGRPTESV WLAGLPRRAR PADADALEAR
     YGKLFEVRGV VQSKLEEARR AKLIGSGLEA MVTVRAEGEQ RRLLEEARAE LPALFIVSKV
     VLAAGPLSAE VARAPGVKCE RCWIYAEEVG RDAAHPTLCA KCVGNL
//

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