ID A0A1E5PPY7_9ACTN Unreviewed; 1059 AA.
AC A0A1E5PPY7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=BGK67_09950 {ECO:0000313|EMBL:OEJ31618.1};
OS Streptomyces subrutilus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=36818 {ECO:0000313|EMBL:OEJ31618.1, ECO:0000313|Proteomes:UP000095705};
RN [1] {ECO:0000313|EMBL:OEJ31618.1, ECO:0000313|Proteomes:UP000095705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10-1-1 {ECO:0000313|EMBL:OEJ31618.1,
RC ECO:0000313|Proteomes:UP000095705};
RA Chen X.;
RT "The complete genome of Streptomyces subrutilus 10-1-1.";
RL Submitted (AUG-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}.
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:OEJ31618.1}.
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DR EMBL; MEHK01000001; OEJ31618.1; -; Genomic_DNA.
DR RefSeq; WP_069919911.1; NZ_MEHK01000001.1.
DR AlphaFoldDB; A0A1E5PPY7; -.
DR STRING; 36818.BGK67_09950; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000095705; 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; 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:UP000095705};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 23..640
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 699..844
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 53..63
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 612..616
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 615
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1059 AA; 117526 MW; 0E9B1E06AAF22AE8 CRC64;
MTTPPQYRPV PAQVDLPALE HAVLDFWRES KTFAKTLEQS EGRPEWVFYE GPPTANGMPG
AHHIEARVFK DVFPRFRTMR GYHVARKAGW DCHGLPVELA VEKELGFNGK QDIEAYGIAE
FNAKCRESVT RHTDAFTELT TRMGYWVDLD DAYRTMDPEY VESVWWSLKE IFNKGLLTQD
HRVAPWCPRC GTGLSDHELA QGYETVVDPS VYVRFPLTSG PLAGEAALLV WTTTPWTLVS
NTAVAAHPEV TYVVATNGTE KLVVAQPLLE KSLGEGWEAT GLTFTGKEME RWTYQRPFEL
VEFPSVSEGT DGSRPAEAHY VVNAEYVTTE DGTGLVHQSP AFGADDLAVC RAYGLPVVNP
VRPDGTFEEE VPLVGGVFFK KADEKLTADL DARGLLFKHI AYEHSYPHCW RCHTALLYYA
QPSWYIRTTA VKDAMLRENE KTNWFPDSVK QGRFGDWLNN NIDWALSRNR YWGTPLPIWR
CEENHLTCVG SRAELSELSG EDHSGLDPHR PYIDDVTFTC THEGCSLEAV RVPEVIDAWY
DSGSMPFAQW GYPYKNKEIF EKRYPAQFIS EAIDQTRGWF YTLMAVGTLV FDKSSYENVV
CLGHILAEDG RKMSKHLGNI LQPIPLMDQH GADAVRWFMA AGGSPWAARR VGHGTIQEVV
RKTLLTYWNT VAFQALYART SNWAPSASDP APADRTVLDR WLLSELHTLV AEVTDALESY
DTQRAGKLLS SFVDDLSNWY VRRSRRRFWQ GDAAALRTLH DVVETVTRLM APLTPFITER
VWQDMIVPVT PEAPESVHLS SWPVADTGAI DPALSQQMLL VRRLVELGRA TRAESGVKTR
QPLSRALVGA VGFDALSPEL QAQITEELNV SSLASLSEVG GSLVDTTAKA NFRALGKRFG
KGVQDVAKAV AAADAAALSL ALRSGGASVE VNGESVTLTP EEVIITETPR EGWSVASDSG
ATVALDLEIT PELRLAGLAR DAIRLIQEAR KNSGLDVADR IALRWTSTDP EVTTALSDHA
ALIADEVLAT DFASGEADAT YGEAFTDDSL SLAFRLRKA
//