ID F0NYC7_WEEVC Unreviewed; 1135 AA.
AC F0NYC7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
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 OrderedLocusNames=Weevi_1423 {ECO:0000313|EMBL:ADX68124.1};
OS Weeksella virosa (strain ATCC 43766 / DSM 16922 / JCM 21250 / CCUG 30538 /
OS CDC 9751 / IAM 14551 / NBRC 16016 / NCTC 11634 / CL345/78).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Weeksella.
OX NCBI_TaxID=865938 {ECO:0000313|EMBL:ADX68124.1, ECO:0000313|Proteomes:UP000008641};
RN [1] {ECO:0000313|EMBL:ADX68124.1, ECO:0000313|Proteomes:UP000008641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43766 / DSM 16922 / JCM 21250 / NBRC 16016 / NCTC 11634 /
RC CL345/78 {ECO:0000313|Proteomes:UP000008641};
RX PubMed=21475590;
RA Lang E., Teshima H., Lucas S., Lapidus A., Hammon N., Deshpande S.,
RA Nolan M., Cheng J.F., Pitluck S., Liolios K., Pagani I., Mikhailova N.,
RA Ivanova N., Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brambilla E.M., Kopitz M., Rohde M., Goker M., Tindall B.J., Detter J.C.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA Kyrpides N.C.;
RT "Complete genome sequence of Weeksella virosa type strain (9751).";
RL Stand. Genomic Sci. 4:81-90(2011).
RN [2] {ECO:0000313|Proteomes:UP000008641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43766 / DSM 16922 / JCM 21250 / NBRC 16016 / NCTC 11634 /
RC CL345/78 {ECO:0000313|Proteomes:UP000008641};
RX DOI=10.4056/sigs.1603927;
RA Lang E., Teshima H., Lucas S., Lapidus A., Hammon N., Deshpande S.,
RA Nolan M., Cheng J., Pitluck S., Liolios K., Pagani I., Mikhailova N.,
RA Ivanova N., Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Brambilla E.,
RA Kopitz M., Rohde M., Goker M., Tindall B., Detter J., Woyke T., Bristow J.,
RA Eisen J., Markowitz V., Hugenholtz P., Klenk H., Kyrpides N.;
RT "Complete genome sequence of Weeksella virosa type strain (9751T).";
RL Stand. Genomic Sci. 4:81-90(2011).
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}.
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DR EMBL; CP002455; ADX68124.1; -; Genomic_DNA.
DR RefSeq; WP_013598513.1; NC_015144.1.
DR AlphaFoldDB; F0NYC7; -.
DR STRING; 865938.Weevi_1423; -.
DR KEGG; wvi:Weevi_1423; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_1_1_10; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000008641; Chromosome.
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; 3.30.720.200; -; 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; 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:UP000008641};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 20..720
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 768..911
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 50..60
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 681..685
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 684
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1135 AA; 129846 MW; 87B59EF0CD2F4453 CRC64;
MAKNFKEYKH LNLVQIADET LKEWKEQNVF EKSITSRDGK DSYVFYEGPP SANGKPGIHH
VLARSIKDIF CRFQTLKGKQ VIRKAGWDTH GLPVELGTEK ELGITKEDIG TKITIEQYNE
ACKRTVMRYT DLWNNLTEKM GYWVDMDDPY ITYKPKYMET VWWLLKQIYD KGYLYKGYTI
QPYSPKAGTG LSSHELNQPG TYQEVTDTTI VAQFKVDKNS TKLFDNQEND VYILAWTTTP
WTLPSNTALT VGPNIDYVVV ETFNQYTHEP ITVVLAKALL SKQFTKPYHL AETEEDFTDY
TAGNKTIPYR IIREIKGKDL VGIRYEQLLP WALPYENADN AFQVIPGDFV TTEDGTGIVH
TAPTFGADDA RVAKDAGVPP MLVLDDHGNA VPLVDLQGRF VASLPKGYGG KFVKNEYYDE
GQAPEKSVDV EIAILLKEQN RAFKVEKYKH SYPHCWRTDK PILYYPLDSW FIKVTEVKDR
MVELNKEINW KPKATGEGRF GNWLENVNDW NLSRSRYWGI PLPVWRTEDG EEEIIIGSVE
ELVQEIEKSI AVGIQKENPF KDFEVGNMSE ENYDLIDLHK NVVDEITLVS ASGKPMKREA
DLIDVWFDSG AMPYAQVHYP FENKELIDNH TMYPADFIAE GVDQTRGWFY TLHAIATLVF
DSKAYKNVMS NGLVLDKNGQ KMSKRLGNAI DPFDTLETYG PDATRWYMIA NAQPWENLKF
DLAGVDEVRR KFFGTLYNTY SFFALYANVD GFTYAEKEIP VEERDELDQW ILSELNTLIQ
QVDEFFSDYE PTKAARAIQE FVIDNLSNWH VRLSRRRFWK GDYSKDKIAA YQTLYTVLET
VAILSSPIAP FFMDRLYKDL NDATGKNEAT SVHLANFPQV NQALINEELQ EQTRLAQLAT
SMILSLRKLS DNRVRQPLQK VMIPVLNETM KNRLLAVSDL LKQEVNVKEI QLLTNEEASD
ILVKSIKPNF KTLGPKFGKD MKAVAAATAQ LTNEQIVELE NTGYIELEVN GEKHTIEVDD
FEIATKDIPG WTVASNAQLT VALDLTLTQA LIDEGISREL VNRIQNLRKE NGFEVTDRID
IIIEKNPAIE QAVTANMEYV RNETLADNLT FDTTIVNGIP VEINDEKLQL TILKH
//
