ID A0A2U2JBR1_9FLAO Unreviewed; 1134 AA.
AC A0A2U2JBR1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=DIS07_04500 {ECO:0000313|EMBL:PWG05711.1};
OS Polaribacter aquimarinus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=2100726 {ECO:0000313|EMBL:PWG05711.1, ECO:0000313|Proteomes:UP000245670};
RN [1] {ECO:0000313|EMBL:PWG05711.1, ECO:0000313|Proteomes:UP000245670}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZY113 {ECO:0000313|EMBL:PWG05711.1,
RC ECO:0000313|Proteomes:UP000245670};
RA Lu D.;
RT "Polaribacter aquimarinus sp. nov., isolated from sediment in a sediment of
RT sea.";
RL Submitted (MAY-2018) 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:PWG05711.1}.
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DR EMBL; QFFG01000002; PWG05711.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2JBR1; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000245670; 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; 3.30.720.200; -; 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:UP000245670};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 20..720
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 769..921
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 50..60
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 682..686
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 685
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1134 AA; 129893 MW; C42D94EE816DBADF CRC64;
MKAKFPEYKG LDLPKVAEEI LNYWQENDIF EKSVTSREGA KPFVFFEGPP SANGLPGVHH
VLARAIKDIF PRYKTMKGYQ VKRKAGWDTH GLPIELGVEK ELGITKEDIG VKISVEEYNA
ACRKAVMRYT DIWNDLTQKM GYWVDMDDPY ITYEPKYMES VWWLLKQIYN KELIYKGYTI
QPYSPKAGTG LSSHELNQPG TYQDVTDTTI VAQFKVIANS LPEFLKKYDN LNFIAWTTTP
WTLPSNTALT VGPKIDYAVV ATYNQYTFEP VHVILAKNLI GKQFSGKYAV TEDLEVLKNY
SRDDKKIPYF ICDECKGADL VGIKYEQLLD YVLPNDNPKD AFRVIAGDFV TTEDGTGIVH
TAPTFGADDA LVAKQAIPEI PPLLVKDEND NLVPLVDLQG RFRPEVTDFA GKYVKNEYYA
DGEVPEKSVD VEIAIKLKIE NKAFKVEKYK HSYPNCWRTD KPILYYPLDS WFIKVTDVKD
RMHELNKTIN WKPESTGTGR FGNWLANAND WNLSRSRYWG IPLPIWRTED GKEQICIGSV
SELKEEMAKA VKAGVLKADI FADFEVGNNA DENYAKIDLH KNIVDEITLV SASGKPMKRE
SDLIDVWFDS GSMPYAQWHY PFENREKIDG NTSYPADFIA EGVDQTRGWF YTLHAISTMV
FDSVAYKNVV SNGLVLDKNG QKMSKRLGNA VDPFETLGKY GADATRWYMI SNANPWDNLK
FDLEGIEEVK RKFFGTLYNT YSFFSLYTNI DGFSYDEADI PLEERPELDR WILSELHTLI
NKVDKFYADY EPTRAARAIS DFTQEYLSNW YVRLSRRRFW KGDYQTDKIS AYQTLYTCML
TIAKLASPIA PFFMDRLYQD LNSVTSKESS ESIHLAEFPV FNESLVDKSL ERKMENAQII
SSLVLSLRAK EKIKVRQPLQ KIMIPVDSEQ QKEEILAVSN LIKHEVNIKE IQILEDASDI
LIKQIKPNFK ALGPKFGKEM RFVAGEVQKF TQEDINKIEK EGEISIEING KNIILERADV
EISSKDIEGW LVANEGLLTV ALDVTITEDL RKEGIARELV NRIQNARKDS GLEVTDRIKL
TVLNYQNLQQ SISDNKGYIM SETLTKDLVF VDELKNGIDI EFDAIKSRIL IEKM
//
