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Database: UniProt
Entry: A0A1H3RM26_9ACTN
LinkDB: A0A1H3RM26_9ACTN
Original site: A0A1H3RM26_9ACTN 
ID   A0A1H3RM26_9ACTN        Unreviewed;      1069 AA.
AC   A0A1H3RM26;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=SAMN05444365_108151 {ECO:0000313|EMBL:SDZ26700.1};
OS   Micromonospora pattaloongensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=405436 {ECO:0000313|EMBL:SDZ26700.1, ECO:0000313|Proteomes:UP000242415};
RN   [1] {ECO:0000313|Proteomes:UP000242415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45245 {ECO:0000313|Proteomes:UP000242415};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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}.
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DR   EMBL; FNPH01000008; SDZ26700.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3RM26; -.
DR   STRING; 405436.SAMN05444365_108151; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000242415; 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; 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:UP000242415};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT   DOMAIN          63..675
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          726..865
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          40..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           74..84
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   1069 AA;  119441 MW;  3287B941EB9051FD CRC64;
     MAYPKNAPDG TGVPASPDLP GVERRVLDYW TADKTFEASV EARPASGRQS EAPGSAAGGE
     RAADNEYVFY DGPPFANGLP HYGHLFTGYV KDVVPRYQTM RGRRVERRFG WDCHGLPAEV
     EAERQLNIST KAEILDLGVD RFNDVCRTSV LTYTSEWERY VTRQARWVDF ANDYKTLDLD
     YMESVMWAFK TLHDKGLVYE GFRVLAYCWR CETPLSNTET RMDDVYRDRQ DPTVSVWFEL
     TADDTVAERS PEVAELLQGP VKIGVWTTTP WTLPSNLALA VGPDIDYAVL ERDGERFIVG
     AARVAAYAKE LEGYRQLGTV RGSLLVGRRY TPLYDFLVDQ AGPNAYQVLG AEFVTTEDGT
     GVVHMAPAFG EDDQNACNAA GIPTIVTVDD HTRFTALVPP YEGQQVFDVN KSVIRDLKDR
     GLVLRQDTYT HSYPHCWRCD TPLVYKAVSS WFVAVSQFRD RMVELNQQIT WTPAHVKDGS
     FGKWLAGARD WSISRNRFWG SPIPVWKSDD PNYPRVDVYG SLDELERDFG VRVNDLHRPT
     IDELTRPNPD DPTGRSTMRR VAEVLDCWFE SGSMPFAQVH YPFENREWFE NHYPGDFIVE
     YIGQTRGWFY TMHVLATALF DRPAFRNCVS HGILLGADGR KMSKSLRNYP DVYEVFDTHG
     SDAMRWMLMS SPVLRGGDMA VTEAGIRDAV RQVLLPLWNV WYFFSLYANA DGYEAVRRTD
     SAHLLDRYVL AKTGELVEQV SQQLDEYDIS GACASVRGYL DALTNWYVRR SRDRFWSGDR
     DAFDTLYTVL ETLCRVVAPL APLTAEEIWR GLTGERSVHL TDWPAAAEFP ADHELVAAMD
     AIRDVCSAGL SLRKAKGLRV RLPLSALTVA TPAAERLRPF AELVADEVNV KSVEFTAEVS
     RYCEQVLTVV PRALGPRVGG QVQSVIRAVK AGEWSLVDGA PVAAGVTLQE GEYELRMVAA
     DAENSAPLPG GEGVVVLDTT VTPELAAEGL ARDVVRVVQQ ARRDADLNIS DRITVTVAAS
     AEVEAAVRAH ADFVAREVLA EQVTFDPSAT GFAGEVGEAE RVQVTVTRV
//
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