ID A0A0B7IDP0_9FLAO Unreviewed; 1160 AA.
AC A0A0B7IDP0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 44.
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 ECO:0000313|EMBL:CEN49870.1};
GN ORFNames=CCAND38_970006 {ECO:0000313|EMBL:CEN49870.1};
OS Capnocytophaga canis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=1848903 {ECO:0000313|EMBL:CEN49870.1, ECO:0000313|Proteomes:UP000045051};
RN [1] {ECO:0000313|EMBL:CEN49870.1, ECO:0000313|Proteomes:UP000045051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CcD38 {ECO:0000313|EMBL:CEN49870.1,
RC ECO:0000313|Proteomes:UP000045051};
RA Xiang T., Song Y., Huang L., Wang B., Wu P.;
RL Submitted (JAN-2015) 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}.
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DR EMBL; CDOI01000214; CEN49870.1; -; Genomic_DNA.
DR RefSeq; WP_042345556.1; NZ_CDOI01000214.1.
DR AlphaFoldDB; A0A0B7IDP0; -.
DR Proteomes; UP000045051; 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; 3.30.720.200; -; 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; 2.
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:UP000045051};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 18..747
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 796..948
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 709..713
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 712
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1160 AA; 132838 MW; 9A3B9A3E275A4727 CRC64;
MKFTEHKNLD LSVVAKEILT YWQENNIFEK SIETREGKEP FVFFEGPPSA NGLPGIHHVM
ARTIKDIFCR YKTQKGFQVK RKAGWDTHGL PVELGVEKEL GITKEDIGKK ISVEDYNKAC
KEAVMRYTNI WNDLTEKMGY WVDMENPYIT YKSKYMESVW WLLKQIYNKG LLYKGYTIQP
YSPKAGTGLS SHELNQPGTY RDVSDTTIVA QFRVKKLSNK FKEKLSNPFD SCDIAGASCG
GALHWADYDE ADYSKLPISI LAWTTTPWTL PSNTALAVGK DIDYVLIKTF NQYTFEPINI
VLAKVLVSKQ FGKKFFETSK EEDFKTPPSG AGGNIPYQIL AEFKGSDLEG TTYEQLIPWF
SPAENADQAF RVITGDFVTT EDGTGIVHIA PTFGADDARV AKENGIPPML IKDENDNLVP
LVDLQGRFVK GKNVPELFSG KYIKNEYYDQ DAPEKSWDVE LAILLKTENK AFKVEKYVHS
YPHCWRTDKP VLYYPLDSWF IKITDVKDRL FDLNKEINWK PKATGEGRFG NWLQNANDWN
LSRSRYWGIP LPIWRTEDKK EEIIIGSVEE LKAEIQKSIA AGLMKEDIFA DFREGNMSDE
NYEKIDLHKN VVDKIVLVST SGKPMKRESD LIDVWFDSGA MPYAQWHYPF ENKEMVEKTW
KTADFIAEGV DQTRGWFYTL HAIAGLVFDG ISYKNVVSNG LVLDKNGQKM SKRLGNAIDP
FTTLEEYGAD ATRWYMISNA NPWDNLKFDL EGVAEVRRKF FGTLYNTYSF FALYANIDGF
TYKEEEIPLE KRPEIDRWIL SELHTLIQKV DEAFADYEPT RATRLISDFV QENLSNWYVR
LCRRRFWKGE YEEDKISAYQ TLYTCLLNVA KLMAPVAPFY AEVLYRDLVS GTQKETAESV
HLTIFPTTDK SFIDKSLESK MEKAQNISSL VLSLRKKEMI KVRQPLQKIM IPISNEAEKR
EIEAVADLIK SEVNVKEIEL LEDASGILVK QIKPNFKTLG PRFGKDMKLV VAAVQQFTQE
DIQYIEKEGQ IIVKLAEKDV TLSIEDVEIT TQDIEGWLVA SSGNLLVALD IHITDELRKE
GIARELVNRI QNIRKDSGFD VTDKINICIQ KQKAVEEAVS DNLEYIKSET LTSELTFAGN
VLGEPIEFDD IVTKISVEKV
//
