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Database: UniProt
Entry: U7DAL4_9BACT
LinkDB: U7DAL4_9BACT
Original site: U7DAL4_9BACT 
ID   U7DAL4_9BACT            Unreviewed;      1091 AA.
AC   U7DAL4;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 52.
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=CALK_0237 {ECO:0000313|EMBL:ERP39072.1};
OS   Chitinivibrio alkaliphilus ACht1.
OC   Bacteria; Fibrobacterota; Chitinivibrionia; Chitinivibrionales;
OC   Chitinivibrionaceae; Chitinivibrio.
OX   NCBI_TaxID=1313304 {ECO:0000313|EMBL:ERP39072.1, ECO:0000313|Proteomes:UP000017148};
RN   [1] {ECO:0000313|EMBL:ERP39072.1, ECO:0000313|Proteomes:UP000017148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACht1 {ECO:0000313|EMBL:ERP39072.1,
RC   ECO:0000313|Proteomes:UP000017148};
RX   PubMed=24112708;
RA   Sorokin D.Y., Gumerov V.M., Rakitin A.L., Beletsky A.V., Damste J.S.,
RA   Muyzer G., Mardanov A.V., Ravin N.V.;
RT   "Genome analysis of Chitinivibrio alkaliphilus gen. nov., sp. nov., a novel
RT   extremely haloalkaliphilic anaerobic chitinolytic bacterium from the
RT   candidate phylum Termite Group 3.";
RL   Environ. Microbiol. 0:0-0(2013).
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:ERP39072.1}.
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DR   EMBL; ASJR01000002; ERP39072.1; -; Genomic_DNA.
DR   RefSeq; WP_022635785.1; NZ_ASJR01000002.1.
DR   AlphaFoldDB; U7DAL4; -.
DR   STRING; 1313304.CALK_0237; -.
DR   PATRIC; fig|1313304.3.peg.219; -.
DR   eggNOG; COG0060; Bacteria.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000017148; 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; 2.
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:UP000017148};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT   DOMAIN          22..512
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          530..682
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          731..881
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   MOTIF           54..64
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT   MOTIF           644..648
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT   BINDING         647
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1091 AA;  125256 MW;  B2D0C589E7D39D99 CRC64;
     MAQGYFKAVD TKVNFPRVEE KILATWKKNK TFQKSLEKTR QNETEDFVFY DGPPFATGLP
     HYGHLLAGTI KDIVPRYWTM RGHHVDRRFG WDTHGLPVEN EMEKEFQVSG KKEIDDMGLH
     LFNEACRSIV LRYTSQWQEV VERMGRWVDF DNQYRTMDAP YMESIWWVFK EIWGKGLIYE
     GFRVQPYCPR CTTPLSNFEV NEGYQDKKDI SITVKMPVKG QENTSILVWT TTPWTLPSNV
     ALAVGPDIPY VKVQDGDEFF ILAEARLSAY YKNESDYTVV ETYTGRDLTG LSYTPMFPYF
     AERSEKFFQV HTADFVSTED GTGIVHIAPA FGEDDFLVGK ELGLPIVCPV DEEGRYTEEV
     CDYAGQFVHD ANVQIVADIK ETGRLVHKQT ITHRYPFCYR CDTPLIYKAI NTWFMQIEPL
     KPNMHENNSR IHWVPGHLQK GRFGKGIEGA PDWNIARNRY WGTPIPLWRC ECGHIECVGS
     LKDLHVRAGK GNEEAGKTAH KEVVSRIKKA LRDKAQSQLE KFNIDPAWAE AVGSTEISEN
     DLHSHIVNAL TLSCPECENA MERTPEVLDC WFESGSMPYA QNHYPFENKE YFEKNFPANF
     IAEGIDQTRG WFYTLTVLSS ALFGREAFQN VIVNGIILAE DGNKMSKRLK NYAPPQEIMD
     KVGADAIRLF LINSPAVKAE NLRFSEEGVR EMARSILIPF WNAYSFFVTY ANIDSWKPTS
     TEAPASDNEL DRWVISLLAY VIRDVNREME EYNLYKVVPL MVDFIDNLTN WYIRRSRRRF
     WKSQNDGDKE NAYQTLYHVL VEFSKVMAPF LPFLTDAVYE NLVCGTTPDA PESVHLCDFP
     RTQEKQVDED IITQMALVRN AVGIGRLLRS RYGIKNRQPL SDITVIIRDA HKRHLVADMK
     HLIMDELNVK DVRLEEREES VLHISAKPNF KKLGPIFGKE MKKVGPEITA FTPEDITDLE
     AGATRSVLGR DITFEDILLV RNKKEGVEVE TDGEVTLALN TEITESLARE GLVRELINRI
     QNHRKESGYE VSDRITLTLS CPAPLRDAMG DFMEIIQSET LTEKLTFDDA REARETCTVE
     EYSVGITSQK A
//
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