ID   A0A1D9F710_9MICC        Unreviewed;      1099 AA.
AC   A0A1D9F710;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   31-JAN-2018, entry version 10.
DE   RecName: Full=Isoleucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02003};
DE            EC=6.1.1.5 {ECO:0000256|HAMAP-Rule:MF_02003};
DE   AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02003};
DE            Short=IleRS {ECO:0000256|HAMAP-Rule:MF_02003};
GN   Name=ileS {ECO:0000256|HAMAP-Rule:MF_02003,
GN   ECO:0000313|EMBL:AOY71143.1};
GN   ORFNames=ARZXY2_1596 {ECO:0000313|EMBL:AOY71143.1};
OS   Arthrobacter sp. ZXY-2.
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=1806905 {ECO:0000313|EMBL:AOY71143.1, ECO:0000313|Proteomes:UP000177289};
RN   [1] {ECO:0000313|EMBL:AOY71143.1, ECO:0000313|Proteomes:UP000177289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZXY-2 {ECO:0000313|EMBL:AOY71143.1,
RC   ECO:0000313|Proteomes:UP000177289};
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL   Submitted (SEP-2016) 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_02003}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-isoleucine + tRNA(Ile) = AMP +
CC       diphosphate + L-isoleucyl-tRNA(Ile). {ECO:0000256|HAMAP-
CC       Rule:MF_02003, ECO:0000256|SAAS:SAAS00654659}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02003};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02003}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02003}.
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_02003}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. IleS type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_02003}.
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DR   EMBL; CP017421; AOY71143.1; -; Genomic_DNA.
DR   RefSeq; WP_021470691.1; NZ_CP017421.1.
DR   Proteomes; UP000177289; 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; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 1.
DR   HAMAP; MF_02003; Ile_tRNA_synth_type2; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR033709; Anticodon_Ile_ABEc.
DR   InterPro; IPR002301; Ile-tRNA-ligase.
DR   InterPro; IPR023586; Ile-tRNA-ligase_type2.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00984; TRNASYNTHILE.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00392; ileS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02003,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00654661};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02003,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00654675};
KW   Complete proteome {ECO:0000313|Proteomes:UP000177289};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02003};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02003,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00654679};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02003};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02003,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00654658};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02003,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00654687};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT   DOMAIN       30    697       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      753    891       Anticodon_1. {ECO:0000259|Pfam:PF08264}.
FT   MOTIF        68     78       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02003}.
FT   MOTIF       663    667       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02003}.
FT   BINDING     666    666       ATP. {ECO:0000256|HAMAP-Rule:MF_02003}.
SQ   SEQUENCE   1099 AA;  121430 MW;  D0A19FDF69E38D34 CRC64;
     MTHYPKASAS PSGTHGVSAS VKFPEIEERI LKYWDQDGTF QASIDQREAD LPGGTAGSNE
     FVFYDGPPFA NGLPHYGHLL TGYAKDLVGR YQTQRGKRVE RRFGWDTHGL PAELEAMKQL
     GMTDKTQIEA MGIDKFNDAC RASVMKYANE WKAYVTRQAR WVDFDNDYKT LNVEYMESVL
     WAFKQLHEKG LTYNGYRVLP YCWKDETPLS NHELRMDDDV YKNRQDQTVT VTFPIKAGES
     EVSQALAGVQ ALAWTTTPWT LPTNLALAVG PDISYAVLPA GPNGIKAAAA EAPVTGSFLL
     AADLVASYAK DLGYDDAAAA AAAVTATYTG SQLAGLEYEP LWNDFADAEK YGTQNAWRIL
     VAEYVTTTDG TGIVHQAPAY GEDDQKVCEE AGIPVVLSVD EGAKFLPLFA HGELAGIVGL
     QVFDANKPIT QVLRADGRLV RQASYEHSYP HCWRCRNPLI YRAVSSWYVE VTKFKDRMSE
     LNQDINWIPG NVKDGQFGKW LENARDWSIS RNRYWGSPIP VWQSDDPEYP RTDVYGSLAE
     LEADFGRLPV NNEGQVDLHR PFIDELTRPN PDDPTGKSTM RRVEDVLDVW FDSGSMPYGQ
     VHYPFQNEEW FNTHNPADFI VEYIGQTRGW FYMLHILSTA LFDRPAFRNV ISHGIVLGSD
     GQKMSKSLRN YPDVSEVLDR DGSDAMRWFL MSSPILRGGN LIVTEQGIRD GVRQVILPLW
     NVYSFFTLYT NAANGGSGYD AKLRYDGYSD TLDQYLLANT GDLVRNVTES LDTYDISGAC
     DELRSYLDML TNWYVRRSRQ RFFDENVDAF DALYTALEAV CRVAASLLPL VTEEIWRGLT
     GGRSVHLVDW PDAALFPANP ELVEAMDRVQ QICSTGSSLR KAANLRVRLP LQELTVVAPG
     ADALEGFAAV VADELNLRSV RLLDTASASP EEFGIQQKLV VNARAAGPRL GKNVQQAIKG
     SKSGDWSVND AGVVVAGGLE LEPQEYTLET VVAETPDGGA AAAAVLPSGG FVVLNTEVTP
     ELAAEGLARD MVRAIQQARK DAGLNVSDRI KTTVEAQQDV VEALQANAGL VKTETLTLEL
     EVLVSGADEP RVTVTKAGA
//