ID A0A1M6MTH9_9CLOT Unreviewed; 1038 AA.
AC A0A1M6MTH9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=SAMN02745912_01415 {ECO:0000313|EMBL:SHJ86716.1};
OS Paramaledivibacter caminithermalis DSM 15212.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Paramaledivibacter.
OX NCBI_TaxID=1121301 {ECO:0000313|EMBL:SHJ86716.1, ECO:0000313|Proteomes:UP000184465};
RN [1] {ECO:0000313|EMBL:SHJ86716.1, ECO:0000313|Proteomes:UP000184465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15212 {ECO:0000313|EMBL:SHJ86716.1,
RC ECO:0000313|Proteomes:UP000184465};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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|HAMAP-Rule:MF_02003}.
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DR EMBL; FRAG01000012; SHJ86716.1; -; Genomic_DNA.
DR RefSeq; WP_073148352.1; NZ_FRAG01000012.1.
DR AlphaFoldDB; A0A1M6MTH9; -.
DR STRING; 1121301.SAMN02745912_01415; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000184465; 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}; Reference proteome {ECO:0000313|Proteomes:UP000184465};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 19..624
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 680..827
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 49..59
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 593..597
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 596
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1038 AA; 120691 MW; 09DBCA3B25E52DB2 CRC64;
MRKFEELLNK SVSENEKEIS KFWDEIDILK KSVETREGAK SFVFYEGPPT ANGRPGIHHV
ISRTLKDSVC RYKTMQGYQV KRKAGWDTHG LPVEIEVEKQ LNLNNKQEIE AYGIDKFNEK
CRESVFKYEG LWKEMTKRMA YAIDLENPYI TLDNNYIESV WWILDKFNKE GFIYEGHKIL
PYCSRCGTGL ASHEVAQGYQ EIKSNTVVVK FKVKDKENEY FLAWTTTPWT LASNVCLTVN
PDVDYVKIKA DNGEIYYLAK ELVSSVVEEE YEVLEEYKGK DLEYMEYEQL MPFVKTDKKA
FFVTLADYVT TEDGTGIVHS APAFGEDDYN TGMKYGLPVL QPVNEEGKYT ATPWEGMFVM
DADVEIIKWL YNEGKLYKKQ KVAHNYPHCW RCKTPLLYYA KPSWYIEMTK LKDKLIENNN
GVEWYPDYVG EKRFGNWLEN LNDWAISRSR YWGTPLNIWR CDECEHTTSI GSRKELVERA
IEDIDETIEL HRPYVDEIHI KCEKCGSTMT RVKDVIDCWF DSGSMPFAQH HYPFENSENF
FEELYPADFI CEGIDQTRGW FYSLLAISTF VTGKSSYKRV LVNDLILDKE GRKMSKSRGN
TVDPFALFDK YGADALRWYL LYVSPAWTPT RFDEEGLKEV QSKFFSTIKN VYNFFVLYAN
TDGIDPKEFF VEYKDRPQID RWILSKFNSL LKSVSEDLDV FDLTKAVRKI QEFVNEDLSN
WYIRRSRRRF WATELTEDKK AVYNTTYEIL VGISQMVAPF APYLSEEIYK KLTGELSVHI
SDYPTTNEAL IDSHLEEKMD LVRNLVKLGR ASREAVRIKV RQPIQKVLID GKYEELISDL
ISLIKEELNV KEVVFAKDLK EFMDFSLKPN FKVAGPKLGK KIKAFGKALA SLDASAVVPK
LEKGEAITID LDGEDFEVTN ELVKINISAK EGFTVEMENN LFVILDTTLS EELVNEGFAR
EFISKVQQLR KNNGYEMMDN IKIYFDGDDE ISKAVEIHKN YIMEETLAVS IERVSDDSFE
KQDLNDHETG IKLEKVNS
//