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Database: UniProt
Entry: A0A1G3MU13_9SPIR
LinkDB: A0A1G3MU13_9SPIR
Original site: A0A1G3MU13_9SPIR 
ID   A0A1G3MU13_9SPIR        Unreviewed;      1054 AA.
AC   A0A1G3MU13;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 31.
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   ORFNames=A2004_04155 {ECO:0000313|EMBL:OHD33499.1};
OS   Spirochaetes bacterium GWC1_61_12.
OC   Bacteria; Spirochaetota.
OX   NCBI_TaxID=1802180 {ECO:0000313|EMBL:OHD33499.1, ECO:0000313|Proteomes:UP000178922};
RN   [1] {ECO:0000313|EMBL:OHD33499.1, ECO:0000313|Proteomes:UP000178922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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|HAMAP-Rule:MF_02003}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OHD33499.1}.
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DR   EMBL; MIAU01000039; OHD33499.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G3MU13; -.
DR   Proteomes; UP000178922; Unassembled WGS sequence.
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; 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.
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}; Cytoplasm {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}; Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT   DOMAIN          18..645
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          694..842
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   MOTIF           48..58
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT   MOTIF           608..612
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT   BINDING         611
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1054 AA;  119752 MW;  652643060E5F680B CRC64;
     MFKPVDTKVS FPKLEEDVLA FWQAHKVFEQ SLEQRKDAPE YVFFDGPPFA TGLPHFGHFI
     PGTIKDIIPR YKTMKGFRVE RRFGWDCHGL PVEYEMEKEL GISGKKAIED FGVANFNEAC
     RSIVLRYTKE WRTIMTRAGR WVDFDHDYKT MDPDYMESIW AVVKKLWDLG LIYEGHYILP
     YCPRCSTVLS NHELQMGGYQ NVHDPAITVK FRVTGQPTAA PEGSPLRGLA EGNTFFLAWT
     TTPWTLPSNL ALAVGPEVDY VLVRDGTERY VLAEARLSAY YKDIASVQVL ARCKGSDLLG
     AQYEPLFPYF ADQAAKGAFR LFKADYVTTE DGTGIVHTAP GFGEDDYQTL KGTGIDTICP
     VDGECKFTSE VTDYAGQFVK NTDKPIIERL KLEGKLVKRE QYLHAYPHCW RCSSPLIYRA
     ISSWFVKIDP IKPKMLRANQ QIHWVPAHIQ GGRFGKWLEN ARDWAISRNR YWGNPLPIWK
     CDACAKTECV GSRDELKQRS GTKPDDLHKH FVDQISWKCG CGGTMRRIPE VLDCWFESGS
     MPYAQVHYPF ENKQHFEDHF PADFIAEGQD QTRGWFYTLT ILAAAMFDKP AFKACVVNGM
     ILAADGKKMS KSLRNYTDPM LVMQEFGADA LRLVLMRSPA TRAEDLCYSD ESVKEVIKSL
     ILPLWSAYSF LVTYARLDAV DPVEAKADTG NPLDRWILSV AETMVKAVSD GLEAYDMPRA
     IDPIYDFVDA LNNWYIRRSR RRFWRSENDG DKVEAYAALY RVLKRLMLCL SPFAPFIAET
     MWQNLRRDSE ATSIHLADWP EHEAAFVDAD LEWKMASVRQ AVSMGRALRY QHNLKIRQPL
     SEVQLVTRDA RQRAVLLEME DIIREELNVK AVVFKDNEED LVEYKAKANF RVLGKELGKD
     MKEGAAIIEQ LSGREIAHLL DGAELVIEVA GKSLSLTKDK LDIQRLEKAS LRVINEGTLT
     MALNAEITLE LQAEGYVRDL IRGIQTLRKD SGLAVSDRIE LATAGSAILQ AAFNNYTELI
     GSETLAVKVE WAEGADMTTI EADAESWRIA IRKA
//
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