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Database: UniProt
Entry: B2HQ62_MYCMM
LinkDB: B2HQ62_MYCMM
Original site: B2HQ62_MYCMM 
ID   B2HQ62_MYCMM            Unreviewed;      1066 AA.
AC   B2HQ62;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   24-JAN-2024, entry version 103.
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:ACC40805.1};
GN   OrderedLocusNames=MMAR_2356 {ECO:0000313|EMBL:ACC40805.1};
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC40805.1, ECO:0000313|Proteomes:UP000001190};
RN   [1] {ECO:0000313|EMBL:ACC40805.1, ECO:0000313|Proteomes:UP000001190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
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:0000256|ARBA:ARBA00025217, ECO:0000256|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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000114, ECO:0000256|HAMAP-
CC         Rule:MF_02003};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-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 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:0000256|HAMAP-Rule:MF_02003}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       IleS type 2 subfamily. {ECO:0000256|ARBA:ARBA00007078,
CC       ECO:0000256|HAMAP-Rule:MF_02003}.
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DR   EMBL; CP000854; ACC40805.1; -; Genomic_DNA.
DR   RefSeq; WP_012394105.1; NC_010612.1.
DR   AlphaFoldDB; B2HQ62; -.
DR   STRING; 216594.MMAR_2356; -.
DR   KEGG; mmi:MMAR_2356; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_11; -.
DR   OMA; EIIVIHK; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000001190; 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   CDD; cd00818; IleRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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   NCBIfam; TIGR00392; ileS; 1.
DR   PANTHER; PTHR42780:SF1; ISOLEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR42780; SOLEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF19302; DUF5915; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00984; TRNASYNTHILE.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 2.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_02003};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_02003};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02003};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02003};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02003};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_02003};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_02003}; Reference proteome {ECO:0000313|Proteomes:UP000001190};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT   DOMAIN          28..667
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          715..854
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           59..69
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT   MOTIF           633..637
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT   BINDING         636
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1066 AA;  119311 MW;  25FF282FAC4EE0C4 CRC64;
     MTDSTYPRSN LGADHRGGSP DFPELETQVL DYWARDETFR ASIERRDGAP EYVFYDGPPF
     ANGLPHYGHL LTGYVKDIVP RYRTMRGFKV ERRFGWDTHG LPAELEVERQ LGITDKSQID
     AMGIAAFNDA CRASVLRYTD EWQQYVTRQA RWVDFDNDYK TLDLGYMESV IWAFRQLWDK
     GLAYEGYRVL PYCWRDETPL SNHELRMDDD VYQSRQDPAL TVGFKVVDGE PQGELAGAYL
     LVWTTTPWTL PSNLAVAVHP DVTYVQVRVG DRRLVLAEAR LAAYTRELGE EPEVIGSYRG
     ADLLGMRYLP PFAYFMDSPN AFAVLAGEFV TTEDGTGIVH MAPAYGEDDM AVTSPVGIEP
     VTPVDAKGRF DSSVPDYQGQ HVFDANAQII RDLKNQSGPA AANGAVLIRH ETYEHPYPHC
     WRCRNPLIYR AVSSWFVTVT KFRERMVELN QQITWYPEHV KDGQFGKWLQ GARDWSISRN
     RYWGTPIPVW KSDDPAYPRI DVYGSLDELE RDFGVRPTNL HRPYIDELTR PNPDDPTGQS
     TMRRIPDVLD VWFDSGSMPY AQVHYPFENG DWFLGGAAGD AGAHYPGDFI VEYIGQTRGW
     FYTLHVLATA LFDRPAFKTC VAHGIVLGSD GQKMSKSLRN YPDVAEVFHR DGSDAMRWFL
     MASPILRGGN LIVTEQGIRE GVRQVLLPFW NAYSFLALYA PKVGTWRTDS DHVLDRYILA
     KLAVLRDDLT QAMEVCDISG ACEQLRQFTE ALTNWYVRRS RSRFWQEDVD AIDTLHTVLE
     ITARLAAPLL PLVTEVIWRG LTGERSVHLT DWPQAGEVPA DAELVAAMDQ VREVCSAASS
     LRKAKKLRVR LPLPKLTVAV ENPQALKPFT DLIADELNVK QVELTDAIGT YGRFELTVNA
     RVAGPRLGKD VQAAIKAVKA GEGVVNSDGT LTAGPAVLQP EEYSSRLVAA DPEFTAALPG
     GAGLVVLDGT VTPELEAEGW AKDRIRELQE LRKSTGLDVS DRIQVLISVP GERAEWARTH
     RDLIAGEILA TTFEFGEPDD GVEIGDGVRV AIAKSGGAGV SGREQA
//
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