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Database: UniProt
Entry: A0A1Y4CI14_9BACT
LinkDB: A0A1Y4CI14_9BACT
Original site: A0A1Y4CI14_9BACT 
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
//
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