ID   SYI2_OCEIH              Reviewed;        1022 AA.
AC   Q8ET99;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Isoleucine--tRNA ligase 2 {ECO:0000255|HAMAP-Rule:MF_02003};
DE            EC=6.1.1.5 {ECO:0000255|HAMAP-Rule:MF_02003};
DE   AltName: Full=Isoleucyl-tRNA synthetase 2 {ECO:0000255|HAMAP-Rule:MF_02003};
DE            Short=IleRS 2 {ECO:0000255|HAMAP-Rule:MF_02003};
GN   Name=ileS2 {ECO:0000255|HAMAP-Rule:MF_02003}; OrderedLocusNames=OB0362;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
CC   -!- FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS
CC       can inadvertently accommodate and process structurally similar amino
CC       acids such as valine, to avoid such errors it has two additional
CC       distinct tRNA(Ile)-dependent editing activities. One activity is
CC       designated as 'pretransfer' editing and involves the hydrolysis of
CC       activated Val-AMP. The other activity is designated 'posttransfer'
CC       editing and involves deacylation of mischarged Val-tRNA(Ile).
CC       {ECO:0000255|HAMAP-Rule:MF_02003}.
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:0000255|HAMAP-
CC         Rule:MF_02003};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02003};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02003}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02003}.
CC   -!- DOMAIN: IleRS has two distinct active sites: one for aminoacylation and
CC       one for editing. The misactivated valine is translocated from the
CC       active site to the editing site, which sterically excludes the
CC       correctly activated isoleucine. The single editing site contains two
CC       valyl binding pockets, one specific for each substrate (Val-AMP or Val-
CC       tRNA(Ile)). {ECO:0000255|HAMAP-Rule:MF_02003}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       IleS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02003}.
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DR   EMBL; BA000028; BAC12318.1; -; Genomic_DNA.
DR   RefSeq; WP_011064767.1; NC_004193.1.
DR   AlphaFoldDB; Q8ET99; -.
DR   SMR; Q8ET99; -.
DR   STRING; 221109.22776041; -.
DR   PRIDE; Q8ET99; -.
DR   EnsemblBacteria; BAC12318; BAC12318; BAC12318.
DR   KEGG; oih:OB0362; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_9; -.
DR   OMA; KMMAPFT; -.
DR   OrthoDB; 32262at2; -.
DR   PhylomeDB; Q8ET99; -.
DR   Proteomes; UP000000822; 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   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   PANTHER; PTHR42780; PTHR42780; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00984; TRNASYNTHILE.
DR   SUPFAM; SSF47323; SSF47323; 2.
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; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..1022
FT                   /note="Isoleucine--tRNA ligase 2"
FT                   /id="PRO_0000098552"
FT   MOTIF           40..50
FT                   /note="'HIGH' region"
FT   MOTIF           582..586
FT                   /note="'KMSKS' region"
FT   BINDING         585
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1022 AA;  116800 MW;  4BCF597F1774244B CRC64;
     MDHAQRERSM RAHWKENRTF QRSIENREGQ QTYVFYEGPP TANGMPHAGH ALGRTIKDFV
     ARYKTMSGYQ VLRKAGWDTH GLPVELEVEK QLNIRGKDDI EKFGVERFIE KCKESVFVYE
     NEWKEFTDKL GYWVDMEDPY KTLNNPYIES VWNILATIHD EDLLYKGHRV VPYCPNCETS
     LSSHEVAQGY KDVTDLSVTA KFRIKNKENE YILGWTTTPW TLPGNVALAV NPEMTYVKAK
     QGEEIYVVAK SLANTVLGEA YEVVEEVSGE DLVGINYEAP FDFISLDNGH YVIGADFVTD
     TSGTGIVHLN PAHGEDDYNA IQAKGMDFVN VVDSKGRYED VIAPLAGQFV KDSDVDIIKM
     LAKDGTLYEK QKYEHSYPHC WRCDTPLLYY AMEGWFIKTT AVKERMQENN QSVEWFPNHM
     RDGRFGNFLD NMVDWNIGRN RYWGTPLNVW VCDDCDKQKS PHSIQELRAF ADSDVPEDIE
     LHKPYVDKIT FDCECGGKMH RTKEVIDVWF DSGSMPFAQY HHPFENDELF NKQFPADVVI
     EGVDQTRGWF YSLLAVSTLF TGKTPYKRVL SLGHILDEHG RKMSKSKGNA LSPVELIEEF
     GADALRWALL ADSSPWNNKR FSKKTVSQAK SKVIDTILNV YSFYSMYADI DKFNVAEHAT
     DAKTTLDSWI LSRLNSVIKE VTTSLDQYDI TKGARSIALF VDELSNWYVR RSRQRFWSSG
     MNEDKKAAFT TLHEVLSKLT QLMAPYIPFV ADDIYTNLQG DSVHVSDFPK VDEAAIDEKL
     EADMQGVLEV IEGARSLRNE VNIKTKQPLA ELVVVPNDEQ LQSGLQAYTS IIEEEINVKQ
     VSFKKDTADF LDTEMKLNFP VAGPKLGKQV GQAKGKVENF TEQEKEAFLV NGTINVELQD
     GSEVTLEKED IIVEKKGQEG YQLFEGNRFV LLLDTNLTEK LKEEGFVREF IRAVQTYRKE
     LDLPVEQRVD IYVNSDENAE RILSEFDALI HDGLIINSVQ FAEKEDMKQV TVNDTEMGLS
     IV