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Database: UniProt
Entry: S5TK01_9CORY
LinkDB: S5TK01_9CORY
Original site: S5TK01_9CORY 
ID   S5TK01_9CORY            Unreviewed;      1070 AA.
AC   S5TK01;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 59.
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:AGS35221.1};
GN   ORFNames=B841_08740 {ECO:0000313|EMBL:AGS35221.1};
OS   Corynebacterium maris DSM 45190.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1224163 {ECO:0000313|EMBL:AGS35221.1, ECO:0000313|Proteomes:UP000015388};
RN   [1] {ECO:0000313|EMBL:AGS35221.1, ECO:0000313|Proteomes:UP000015388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Coryn-1 {ECO:0000313|Proteomes:UP000015388};
RA   Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT   "The complete genome sequence of Corynebacterium maris Coryn-1 (=DSM
RT   45190).";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003924; AGS35221.1; -; Genomic_DNA.
DR   RefSeq; WP_020935154.1; NC_021915.1.
DR   AlphaFoldDB; S5TK01; -.
DR   STRING; 1224163.B841_08740; -.
DR   KEGG; cmd:B841_08740; -.
DR   PATRIC; fig|1224163.3.peg.1756; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_11; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000015388; 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   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; 1.
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:UP000015388};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT   DOMAIN          34..675
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          723..864
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           64..74
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT   MOTIF           641..645
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT   BINDING         644
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1070 AA;  119501 MW;  14795F2CA1B48273 CRC64;
     MTDAQNTTGA VGSAYPKVDM TGGSSRFPQM EEQVLRYWQE DDTFQASLKN REGNEEYVFY
     DGPPFANGLP HYGHLLTGYV KDIIPRYRTM AGYHVPRVFG WDTHGLPAEL EAEKQLGITD
     KGQIEEMGLA KFNEYCATSV LKYTEEWKEY VTRQARWVDF DNGYKTMDLS YMESVIWAFK
     QLYDKGLVYQ GFRVLPYSWA EHTPLSNQET RLDDSYKMRQ DPTLTVTLPL TGAREGTAGE
     KTLADNPVLA ETAALAWTTT PWTLPSNLAL AVHPEVTYAV VKVGADSSEA EFAGSHLILA
     EPLVGAYAKE LGEEREVVAT FAGAELEGLV YEPVFDFFAD NPNSFQIIVA DYVTTEDGTG
     IVHQAPAFGE EDMESCKDYG IELVIPVDMD GQFTSLVPPY EGQLVFDANK DIIKDLKSAG
     RVLRHQTIEH SYPHSWRSGE PLIYMALPSW FVDVTKIRDR MVELNHEGIE WLPGHVRDGQ
     FGKWLENARD WNISRTRYWG SPIPAWVSDD ENYPRIDVYG SLDELEADFG VRPESLHRPY
     IDELTRPNPD DPTGKSTMRR VTDVLDVWFD SGAMPFAQFH YPFENKEFFE SHHPADFIVE
     YIGQTRGWFY LLHVLSVALF DRPAFKKVVA HGIVLGDDGQ KMSKSKGNYP NVNEVFDRDG
     SDAMRWFLMS SPILRGGNLI VTEQGIREGV RQAILPIWNA YTFLQLYASQ EAEFSFDSED
     VLDRYILAKL HDLVESVEKS LDGTDIAAAT EEVRLFADVL TNWYVRRSRD RFWAGQEEHP
     EAFNTLYTVL EVLTRTVAPL LPYVTEVIWR ALTGGRSVHL TDFPDAAKIP ADAQLVSAMD
     AVRGVCSAAS SVRKSNKLRN RLPLPGLTVA LDDSAQLEPF TAVIRDEVNV KEVTLTDDVD
     AVGTFEVVVN AKVAGPRLGR DVQTVIKAVK SGDYQREGET VVAGGIELND GEFTERLVAA
     DPASTAAIDG LGGLVVLDMT VTEELEAEGW AADVIRGLQD ARKAEDFAVS DRIATVLSVP
     ADKKDWAERH AEHIAAETLS TGFTVTVDEI TEGTAHQVVK GVQASVVKQS
//
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