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Isoleucine--tRNA ligase (EC 6.1.1.5) (Isoleucyl-tRNA synthetase) (IleRS)

 A0A2E6V7Y7_9FLAO        Unreviewed;      1134 AA.
A0A2E6V7Y7;
31-JAN-2018, integrated into UniProtKB/TrEMBL.
31-JAN-2018, sequence version 1.
25-APR-2018, entry version 4.
RecName: Full=Isoleucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02003};
EC=6.1.1.5 {ECO:0000256|HAMAP-Rule:MF_02003};
AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02003};
Short=IleRS {ECO:0000256|HAMAP-Rule:MF_02003};
Name=ileS {ECO:0000256|HAMAP-Rule:MF_02003};
ORFNames=CMO82_00530 {ECO:0000313|EMBL:MBL85132.1};
Winogradskyella sp.
Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
Flavobacteriaceae; Winogradskyella.
NCBI_TaxID=1883156 {ECO:0000313|EMBL:MBL85132.1};
[1] {ECO:0000313|EMBL:MBL85132.1}
NUCLEOTIDE SEQUENCE.
STRAIN=SP247 {ECO:0000313|EMBL:MBL85132.1};
Tully B.J., Graham E.D., Heidelberg J.F.;
"The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from
the Global Oceans.";
Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As
IleRS can inadvertently accommodate and process structurally
similar amino acids such as valine, to avoid such errors it has
two additional distinct tRNA(Ile)-dependent editing activities.
One activity is designated as 'pretransfer' editing and involves
the hydrolysis of activated Val-AMP. The other activity is
designated 'posttransfer' editing and involves deacylation of
mischarged Val-tRNA(Ile). {ECO:0000256|HAMAP-Rule:MF_02003}.
-!- CATALYTIC ACTIVITY: ATP + L-isoleucine + tRNA(Ile) = AMP +
diphosphate + L-isoleucyl-tRNA(Ile). {ECO:0000256|HAMAP-
Rule:MF_02003, ECO:0000256|SAAS:SAAS00654659}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000256|HAMAP-Rule:MF_02003};
-!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02003}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02003}.
-!- DOMAIN: IleRS has two distinct active sites: one for
aminoacylation and one for editing. The misactivated valine is
translocated from the active site to the editing site, which
sterically excludes the correctly activated isoleucine. The single
editing site contains two valyl binding pockets, one specific for
each substrate (Val-AMP or Val-tRNA(Ile)). {ECO:0000256|HAMAP-
Rule:MF_02003}.
-!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
family. IleS type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_02003}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:MBL85132.1}.
-----------------------------------------------------------------------
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EMBL; PBLD01000001; MBL85132.1; -; Genomic_DNA.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
GO; GO:0000049; F:tRNA binding; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1.
Gene3D; 3.40.50.620; -; 3.
Gene3D; 3.90.740.10; -; 1.
HAMAP; MF_02003; Ile_tRNA_synth_type2; 1.
InterPro; IPR002300; aa-tRNA-synth_Ia.
InterPro; IPR033709; Anticodon_Ile_ABEc.
InterPro; IPR002301; Ile-tRNA-ligase.
InterPro; IPR023586; Ile-tRNA-ligase_type2.
InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
Pfam; PF08264; Anticodon_1; 1.
Pfam; PF00133; tRNA-synt_1; 1.
PRINTS; PR00984; TRNASYNTHILE.
SUPFAM; SSF47323; SSF47323; 2.
SUPFAM; SSF50677; SSF50677; 1.
TIGRFAMs; TIGR00392; ileS; 1.
3: Inferred from homology;
Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02003,
ECO:0000256|SAAS:SAAS00654661};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_02003,
ECO:0000256|SAAS:SAAS00654675};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02003};
Ligase {ECO:0000256|HAMAP-Rule:MF_02003,
ECO:0000256|SAAS:SAAS00654661};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_02003};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02003,
ECO:0000256|SAAS:SAAS00654675};
Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02003,
ECO:0000256|SAAS:SAAS00654687};
Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
DOMAIN 22 719 tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
DOMAIN 769 921 Anticodon_1. {ECO:0000259|Pfam:PF08264}.
MOTIF 50 60 "HIGH" region. {ECO:0000256|HAMAP-
Rule:MF_02003}.
MOTIF 682 686 "KMSKS" region. {ECO:0000256|HAMAP-
Rule:MF_02003}.
BINDING 685 685 ATP. {ECO:0000256|HAMAP-Rule:MF_02003}.
SEQUENCE 1134 AA; 129546 MW; 6D0BB9FAB3C9D874 CRC64;
MSTKFPEYKG LNLPKVAEDI NSYWEANNIF EKSVTTREGK EPYVFFEGPP SANGLPGVHH
VLARAIKDIF PRYKTMKGFQ VKRKAGWDTH GLPVELGVEK ELGITKEDIG TKITVEEYNE
ACKKAVMRYT DIWNDLTKKM GYWVDMDDPY ITYKSKYMES VWWLLKQIYD KNLLYKGYTI
QPYSPKAGTG LSSHELNQPG TYQDVTDTTV VAQFKAIAET LPDFLQDEGD IHFLAWTTTP
WTLPSNTALT VGPKIDYVLV ETYNQYTFKP INVVLAKSLV GKQFDGKYKQ VETKPELIEF
KEGDKKIPFY VVKEFKGKDL VGIKYEQLLD YALPNDNPEN AFRVISGDFV TTEDGTGIVH
TAPTFGADDA LVAKQATPEI PPMLVKDDNG NLVPLVDLQG RFRPEMGEFA GKYVKNEYYN
EGEAPEKSVD VELAIKLKIE NKAFKVEKYK HSYPNCWRTD KPILYYPLDS WFIKVTDVKG
RMHELNTTIN WKPKSTGEGR FGNWLANAND WXLSRSRFWG IPLPIWRTED GKEQLCIGSV
EELKAEIAKA VEAGVMSEDI FADFEVGNMS EENYEKIDLH KNVVDKIVLV SPSGKPMKRE
SDLIDVWFDS GSMPYAQWHY PFENKDFIDK KEAFPADFIA EGVDQTRGWF YTLHAIGTMV
FDSVAYKNVV SNGLVLDKNG QKMSKRLGNA VDPFETLANH GADATRWYMI SNANPWDNLK
FDIEGVEEVK RKFFGTLYNT YSFFSLYTNL DGFKYEEADI PLNERPELDR WILSELNTLI
KKVDEYYAEY EPTKAARAIS DFTQDYLSNW YVRLSRRRFW KGDYQADKIS AYQTLYTCME
TIAKLGAPIA PFFMDRLYLD LNAVTQKEGF ESVHLAEFPK ADESAIDKVL ERKMENAQTI
SSLVLSLRAK EKIKVRQPLE KIMIPIDNQQ QKEEIKAVED LIKHEVNIKN IELLEDASDI
LVKQIKPNFK ALGPRFGKDM KLIASAISAF SAEDIKKIEQ NGNLDVEING KNINLGLDDV
EITSQDIEGW LVANEGALTV ALDVTITEEL RKEGIARELV NRIQNLRKDS GFEVTDRIDV
QLQNDAQVAA AIASNEDYIK SETLTEELQL MDNLNDGIEI AFDEVNTRLF IQKH


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