ID A0A1Q5Q1C6_9ACTO Unreviewed; 1071 AA.
AC A0A1Q5Q1C6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-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=BSZ39_09675 {ECO:0000313|EMBL:OKL53410.1};
OS Bowdeniella nasicola.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Bowdeniella.
OX NCBI_TaxID=208480 {ECO:0000313|EMBL:OKL53410.1, ECO:0000313|Proteomes:UP000185628};
RN [1] {ECO:0000313|Proteomes:UP000185628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19116 {ECO:0000313|Proteomes:UP000185628};
RA Meng X.;
RL Submitted (DEC-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|ARBA:ARBA00007078,
CC 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:OKL53410.1}.
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DR EMBL; MQVR01000063; OKL53410.1; -; Genomic_DNA.
DR RefSeq; WP_073717131.1; NZ_MQVR01000063.1.
DR AlphaFoldDB; A0A1Q5Q1C6; -.
DR STRING; 208480.SAMN02910418_01903; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000185628; 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 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:UP000185628};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 30..676
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 730..868
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
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 1071 AA; 119181 MW; BEDF3C13CBDE2E06 CRC64;
MSEDKHGVYP RHREHAVVPS PTFPAIEEDI LRYWRANDTF TKSVEMREAG ERGANEFIFY
DGPPFANGLP HYGHLLTGYV KDAIGRYQTQ LGHRVERRFG WDTHGLPAEL EAERILGIED
KSEIEGEDGM GIGAFNDACR SSVLRYTKEW EDYVTRQARW VDFDNDYKTL DLTFMESVIW
AFKSLYDKGL AYEGYRVLPY CWNDQTPLSN HELKMDDDVY QDRQDRTVTV GVRLETGELA
LIWTTTPWTL PSNLAIAVGP EIDYVVVAPT EGVLAGERVI LAEALVSAYA KELGEDVPVS
ERLKGADLVG RRYHPIFDYF ASRDADDAPG PNAFTILAGD FVTTEDGTGL VHMAPAFGED
DMIACTEAGI RPVVPVDDAG KFTADVPDYV GQQVFDANRA IITDLRDATG PIGARPEAQR
PVLVRDASYV HPYPHCWRCR EPLIYRAVSS WFVAVTKFRD RMVELNQEIA WVPEHIKDGQ
FGKWLEGARD WSISRNRYWG SPIPVWVSDN PAYPRTDVYG SIAELEADFG VEVTDLHRPF
IDTLVRPNPD DPTGTSMMRR IPDVLDCWFE SGSMPYAQVH YPFENADWFD SHFPGDFIVE
YIGQTRGWFY TLHVLSTALF DRPAFTSAIS HGIVLGSDGR KMSKSLRNYP DVSEVFDRDG
ADAMRWFLLS SPVVRGGNLV VTEEGIRAAV REALLPAWSA WYFFALYAGA YHGQHGYEAS
FRTDSPEVLD RYLMAKTGDL VREVRAALDA YDIPGATEAI RTYVDTLTNW YIRESRGRFW
NDDDAAFDTL YTALKTLCEV AAPLLPMVTE EIWRGLTGGE SVHLQDYPDA ALFPVDEDLV
AATDEARAVI SGAHALRKAE KIRVRQPLGT LRVVSTNPER LAPFADLIAS EINVKHVDLQ
DVATCGLQVR ESVAVQPREL APEMRRLTSQ LFAAAKSGAF ELAGDTLRLT LADGSTVDLA
AGQYTLSQSV ETEAGEAASV LSGGTVVVLD TMITDELAAE GIARDVIRAV QQARKDAGLH
VSDRISARLA LPADQLAAIE AYRDLVCAET LATELTLAEG EADIQVAKAD A
//
