ID A0A1Y4CI14_9BACT Unreviewed; 1145 AA.
AC A0A1Y4CI14;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=B5F81_06285 {ECO:0000313|EMBL:OUO42971.1};
OS Muribaculum sp. An287.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae;
OC Muribaculum.
OX NCBI_TaxID=1965623 {ECO:0000313|EMBL:OUO42971.1, ECO:0000313|Proteomes:UP000243574};
RN [1] {ECO:0000313|Proteomes:UP000243574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An287 {ECO:0000313|Proteomes:UP000243574};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUO42971.1}.
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DR EMBL; NFIX01000006; OUO42971.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4CI14; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000243574; 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 Gene3D; 3.40.50.620; HUPs; 2.
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:UP000243574};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 18..727
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 775..922
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 688..692
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 691
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1145 AA; 129145 MW; 0BB3F36D55E494D7 CRC64;
MRFKEYKGLD PVAINNEILE KWNREKCFGQ SMKEREGAPR FIFFEGPPSA NGMPGIHHVM
ARSIKDAVCR FKTQSGYRVE RRAGWDTHGL PVELGVEKKL GITKEDIGSK ISVEEYNDTC
RKEVMKYTEE WESLTQRIGY WVDMDDPYIT YDNRYIETLW YLLKKIYEKG LLYKGYSIQP
YSPAAGTGLS THELNQPGCY RDVKDTTAVV QFEVIKNEKS QKLYGCETLP VFFIAWTTTP
WTLPSNTALC VGPDIDYVRV MSFNPYSGEP GIYVVAKALV SCHFNPKAAE IPLEDYRPGD
KLVPYKVLDG VFKGSELAGI SYHQLIPWVN PGEGAFRVIC GDYVTTDEGT TGIVHIAPTF
GADDDRVAKA SGIPPMLMTD RNGQKQAMVD RKGRFYCVED LSEDFVRSSV DDSYRQFAGR
YVKNAYDSSL PADAPTLDVD LCVMLKQQGK AFKIEKHVHT YPHCWRTDKP VLYYPLDSWF
IRTTAVRDEM IKLNNTIVWK PESTGSGRFG KWLENIQDWN LSRSRYWGTP LPVWRSEDGK
EEKCIGSVRE LYDEIEKSVA AGYMESNPLK DRGFNPDDMS LENYNRIDLH RPYVDNIFLV
SASGKKMKRE SDLIDVWFDS GAMPYAQEGL RNLGKDSFGA TADFIAEGVD QTRGWFYTLH
AIHTMVSGTP AFKCVISNGL VLDKEGNKMS KRLGNAVDPF AVLDKYGADA LRWYMLTNSQ
PWDNLKFDEA GVDEVRRKFF GTLYNTYSFF ALYANVDSFD PSVPQVPVAS RAETDRWIIS
LMNTLIKDVR AAYEDYDITA AGRMIQDFVC DHLSNWYVRL NRKRFWGGEM DDDKLAAYQT
LYSALTTVAV LAAPIAPFFM ERLYLDLKPE AKSVHFTLMP EPDASLIDTE LEERMALAQR
ASSMILALRR KVNIKVRQPL AKIVVPIIDP KMQERFEKVR DIVLGEVNVK EVEFITDTAG
LITKKIKPNF KTLGKRYGKQ MKEIAAFMAG LSQQDIAAIE SAGLSGGTYT LALASGDAVL
EPGDYEVTSE DMPGWLVASE GTLTIALDIT ITDGLRREGT ARELINRIQN LRKDSGFEVT
DKINVLIDGG KYAAEISDSL ADFSDYICAQ TLALSISAVS GLDGAAETEW GEGFIKIKVT
KVKNI
//