ID A0A093I2A4_STRCA Unreviewed; 1282 AA.
AC A0A093I2A4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 13-SEP-2023, entry version 27.
DE RecName: Full=isoleucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013165};
DE EC=6.1.1.5 {ECO:0000256|ARBA:ARBA00013165};
DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00032665};
DE Flags: Fragment;
GN ORFNames=N308_01916 {ECO:0000313|EMBL:KFV88071.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV88071.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV88071.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV88071.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
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DR EMBL; KL206989; KFV88071.1; -; Genomic_DNA.
DR STRING; 441894.ENSSCUP00000020298; -.
DR Proteomes; UP000053584; Unassembled WGS sequence.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR CDD; cd00818; IleRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR HAMAP; MF_02003; Ile_tRNA_synth_type2; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363035};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363035};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363035};
KW Reference proteome {ECO:0000313|Proteomes:UP000053584}.
FT DOMAIN 49..655
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 711..867
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV88071.1"
FT NON_TER 1282
FT /evidence="ECO:0000313|EMBL:KFV88071.1"
SQ SEQUENCE 1282 AA; 146796 MW; 25C85ED9E711627A CRC64;
WERMVHQVPE NIAFPNEEEK ILELCTQVYL SCLKTECLIV IKNVFLYLRF NFYDGPPFAT
GLPHYGHILA GTIKDIVTRF AHQSGFHVDR RFGWDCHGLP VEYEIDKTLG IKGPEDVAKM
GIAEYNAQCR GIVMRYSKEW EFNVTRLGRW IDFENDYKTL YPEFMESVWW VFKQLYDKGL
VYRGVKVMPF STACNTPLSN FESHQNYKDV QDPSVIVSFP LDEDANVSLV AWTTTPWTLP
SNLALCVNPE LQYVKLRGKY NATGKLYILM EARLIALYKS DTEYEILDRQ VHTLLFPGIA
LKGKTYKPLF EYFIKCKDNG AFTVVVDNYV KEEEGTGVVH QSPYFGADDY RVCMDFNIIQ
KDSVPVCPVD ASGCFTAEVT DFAGQYVKDA DKNIIKLLKE KGRLVSSSTF KHSYPFCWRS
DTPLIYKAVP SWFVRVEHMV EKLQENNAQC YWVPDFVREK RFGNWLKDAR DWAISRNRYW
GTPIPLWVSE DFEEVVCIGS MAELEELTGV KVTDIHRESI DHLAIPSRCG KGSLHRVPEV
FDCWFESGSM PYAQVHYPFE NKKDLEDAFP ADFIAEGIDQ TRGWFYTLLV LSTALFGRPP
FKNVIVNGLV LASDGQKMSK RKKNYPDPMT IVNSYGADAL RLYLINSPVV RAENLRFKEE
GVKDILKDVF LPWYNAYRFL VQNVQILQHK DEGREFLYNE NTVKESNNIM DKWILSFTQS
LIQFFKAEMA AYRLYTVVPR LVKFVDILTN WYVRMNRRRL KGENGTEDCI MALETLFSVL
YSMCRLMAPY TPFITELMYQ NLKTLIDPAS VQEKNTESIH YLMLPQVRED LIDKKIESAV
SCLQSVIELG RVIRDRKTIP VKYPLKEVVV IHQDPEALEN IRSLERYILE ELNVRQVTLS
TDKDKYGIRL RAEPDHMVLG KRLKGAFKLV MAAIKELKSE QLEKFQETGA IVVEGHELHG
EDLRLMYTFD QVAGGSAQFE AHSDAQVLVL LDVTPDQSMV DEGVAREVIN RIQKLRKKRN
LVPTDEITVY YRSNPEGDYL DTVIKEHMDF IFATVKASLK PYPVPTSKEV LIQERTQLKG
SELEITLVRG GLSHSVGPAC AYVNLKVCVN GTEQDGMLLL ENPKGDNTLN FTRLVDAVSC
IFDLKNSKLT FFNGKTELIN NTDLLSLSGK TLHVTSGSAP ALSNSPEALV CKYINLQLVD
AKPQECQKGT VGTLLMENPL GQNGLTYQGL LHETAKVFGL RSRRLKLFLD EAQTQEITKD
ISMKILNMKT VYVCVIPTTA EC
//
