ID A0A7K6CRZ0_9PASS Unreviewed; 1285 AA.
AC A0A7K6CRZ0;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 08-OCT-2025, entry version 14.
DE RecName: Full=Isoleucine--tRNA ligase, cytoplasmic {ECO:0000256|ARBA:ARBA00069879};
DE EC=6.1.1.5 {ECO:0000256|ARBA:ARBA00013165};
DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00032665};
DE Flags: Fragment;
GN Name=Iars {ECO:0000313|EMBL:NWV16785.1};
GN ORFNames=ORISOL_R02368 {ECO:0000313|EMBL:NWV16785.1};
OS Origma solitaria.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Meliphagoidea; Acanthizidae; Origma.
OX NCBI_TaxID=720586 {ECO:0000313|EMBL:NWV16785.1, ECO:0000313|Proteomes:UP000571324};
RN [1] {ECO:0000313|EMBL:NWV16785.1, ECO:0000313|Proteomes:UP000571324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-029-52 {ECO:0000313|EMBL:NWV16785.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the specific attachment of an amino acid to its
CC cognate tRNA in a 2 step reaction: the amino acid (AA) is first
CC activated by ATP to form AA-AMP and then transferred to the acceptor
CC end of the tRNA. {ECO:0000256|ARBA:ARBA00003170}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tRNA(Ile) + L-isoleucine + ATP = L-isoleucyl-tRNA(Ile) + AMP +
CC diphosphate; Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666, Rhea:RHEA-
CC COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58045,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78528, ChEBI:CHEBI:456215; EC=6.1.1.5;
CC Evidence={ECO:0000256|ARBA:ARBA00048359};
CC -!- SUBUNIT: Part of a multisubunit complex that groups tRNA ligases for
CC Arg (RARS1), Asp (DARS1), Gln (QARS1), Ile (IARS1), Leu (LARS1), Lys
CC (KARS1), Met (MARS1) the bifunctional ligase for Glu and Pro (EPRS1)
CC and the auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18.
CC {ECO:0000256|ARBA:ARBA00063494}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
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:NWV16785.1}.
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DR EMBL; VZRL01000363; NWV16785.1; -; Genomic_DNA.
DR OrthoDB; 1706657at2759; -.
DR Proteomes; UP000571324; Unassembled WGS sequence.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IEA:UniProtKB-ARBA.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA deacylase 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 FunFam; 3.40.50.620:FF:000414; Isoleucine--tRNA ligase, cytoplasmic-like; 1.
DR FunFam; 1.10.730.10:FF:000004; Isoleucyl-tRNA synthetase, cytoplasmic; 1.
DR FunFam; 3.40.50.620:FF:000050; Isoleucyl-tRNA synthetase,cytoplasmic; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 1.
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; IPR057033; Ubiquitin_IARS1.
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 Pfam; PF23567; Ubiquitin_IARS1; 2.
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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363035};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363035};
KW Reference proteome {ECO:0000313|Proteomes:UP000571324}.
FT DOMAIN 20..661
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 717..873
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 1100..1182
FT /note="Isoleucine--tRNA ligase cytoplasmic ubiquitin-like"
FT /evidence="ECO:0000259|Pfam:PF23567"
FT DOMAIN 1192..1282
FT /note="Isoleucine--tRNA ligase cytoplasmic ubiquitin-like"
FT /evidence="ECO:0000259|Pfam:PF23567"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NWV16785.1"
FT NON_TER 1285
FT /evidence="ECO:0000313|EMBL:NWV16785.1"
SQ SEQUENCE 1285 AA; 147173 MW; CFFF4750120F0134 CRC64;
WQRMVQQVPE NINFPNEEEK ILKLWKNLNC FKECLKQSKN RPRFNFYDGP PFATGLPHYG
HILAGTIKDI VTRFAHQSGF HVDRRFGWDC HGLPVEYEID KTLGIKGPED VAKMGIEAYN
KQCRGIVMRY AKEWELSVTR LGRWIDFEND YKTLYPEFME SVWWVFKQLY DKGLVYRGVK
VMPFSTACNT PLSNFESHQN YKDVQDPSVT VSFPLEEDPS VSLVAWTTTP WTLPSNLALC
VNPELQYVKL RGKYKATGKI YILMESRLVA LYKSDSEYQI LDRQVQKLLH LLTFSIFLDQ
KFPGIALKGK KYKPLFDYFI QCKEKGAFTV VVDGYVKEEE GTGVVHQAPY FGADDYRVCM
DFNIIQKDSV PVCPVDASGC FTAEVADFAG QYVKDADKHI IRWLKEKGRL IHSTTFQHSY
PFCWRSDTPL IYKAVPSWFV RVEHMVDKLL ENNAQCYWVP DFVREKRFGN WLKDARDWAI
SRNRYWGTPI PLWVSEDLEE VVCVGSIAEL EELSGVKVTD LHRESIDQLS IPSRSGKGSL
RRVPEVFDCW FESGSMPYAQ VHYPFENRRE LEDAFPADFI AEGIDQTRGW FYTLLVLSTA
LFGKPPFKNV IVNGLVLASD GQKMSKRKKN YPDPMHIVDN YGADALRLYL INSPVVRAEN
LRFKEEGVRD ILKDVFLPWY NAYRFLVQNV HILQHKDEGR EFLYNENTVK ESNNIMDKWI
LSFTQSLIQF FKAEMAAYRL YTVVPRLVKF VDVLTNWYVR MNRRRLKGEN GTEDCIMALE
TLFSVLFSMC RLMAPYTPFI TELMYQNLKT LIDPASVQEK NTESIHYLML PQVREDLIDK
KIESAVSCLQ SVIELGRVIR DRKTIPVKYP LKEVVVIHQD PEALENIRSL EKYVLEELNV
RALTLTADKG RYGVRLRAEP EHTVLGRRLK GAFKPVMAAI KELSSEQLER FQETGTIVVE
GHELHGEDLR LMYQMTEGSA QFEAHSDAQV LVLLDVTPDQ SMVDEGVARE VINRIQKLRK
KRNLVPTDEI MVYYRSLPQG DYLDTVIQEH AEFIFATIKA DLKPYPVPTS KEVLIQETTQ
LKGSELEITL VRGGVCQSVG PACAYVNLKV CVNGTEQDGV LLLENPKGDN TLNFTGLVDA
VSCIFGLKNS KLTVFNGNTE LLNQTDLLGL SGKTLHVTAG SAPALPSSPS ALLCQYINLQ
LMNAKPQECQ KGTVGTLLME NPVGQNGLTY KGLLHETAKV FGLRSRRLKL FLDEALTHEI
TKDVSMKNLN MKTLYVHVIP TTAEC
//
