ID A0AA88TGB2_9TELE Unreviewed; 1266 AA.
AC A0AA88TGB2;
DT 27-MAR-2024, integrated into UniProtKB/TrEMBL.
DT 27-MAR-2024, sequence version 1.
DT 28-JAN-2026, entry version 9.
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};
GN ORFNames=Q8A67_021695 {ECO:0000313|EMBL:KAK2874542.1};
OS Cirrhinus molitorella (mud carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Cirrhinus.
OX NCBI_TaxID=172907 {ECO:0000313|EMBL:KAK2874542.1, ECO:0000313|Proteomes:UP001187343};
RN [1] {ECO:0000313|EMBL:KAK2874542.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Prfri {ECO:0000313|EMBL:KAK2874542.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAK2874542.1};
RA Liu H.;
RT "Chromosome-level Genome Assembly of mud carp (Cirrhinus molitorella).";
RL Submitted (AUG-2023) 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:KAK2874542.1}.
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DR EMBL; JAUYZG010000021; KAK2874542.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AA88TGB2; -.
DR Proteomes; UP001187343; 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; 3.90.740.10:FF:000044; Isoleucine--tRNA ligase; 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:UP001187343}.
FT DOMAIN 18..638
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 693..849
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 1083..1165
FT /note="Isoleucine--tRNA ligase cytoplasmic ubiquitin-like"
FT /evidence="ECO:0000259|Pfam:PF23567"
FT DOMAIN 1174..1263
FT /note="Isoleucine--tRNA ligase cytoplasmic ubiquitin-like"
FT /evidence="ECO:0000259|Pfam:PF23567"
SQ SEQUENCE 1266 AA; 144757 MW; 79F248FE8AEA1A30 CRC64;
MVEAVPESIN FPTEEERILK FWLEKDCFQE CLKQSKNRPR FTFYDGPPFA TGLPHYGHIL
AGTIKDIVTR FAHQNGFHVD RRFGWDCHGL PVEYEIDKSL NIKGPEDVAK MGIAEYNKQC
RSIVMRYANE WETSVRRMGR WIDFRNDYKT LYPWFMETVW WVFKQLYDTG LVYRGVKVMP
FSTACNTPLS NFEAHQNYKD VQDPSVIVTF PLLEDETVSF IAWTTTPWTL PSNLALCVNP
DFIYVKVKDN SSQKVYIMME ARLVALFKSD SEYTILDKFP GKTLEGKKYK PLFEYFIKCR
ETGAFSVVMD NYVRDDDGTG VVHQAPYFGA DDFRVCAEYN IIQKDSTPIC PVDSSGIFTA
EVTHFAGQYV KDADKNIIKW LKENGRLVNS GSFKHSYPFC WRSDTPLIYK AVPSWFVRVE
HMVEKLLDNN SKCYWVPEFV KEKRFGNWLR DARDWAISRN RYWGTPIPLW VSDDYEEVVC
VGSMAELEEL TGVKVSDLHR ESIDGLTIPS RCGKGQLKRV SEVFDCWFES GSMPYAQVHY
PFENRREFED AFPADFIAEG IDQTRGWFYT LLVLSTALFG KPPFKNVIVN GLVLASDGQK
MSKRKKNYPD PSLIVQSYGA DALRLYLINS PVVRAENLRF KEEGVRDVLK DVFLPWYNAY
RFLVQNVQRL QKEEAIEFLY NERTASVSDN IMDKWIQSFT QSLIQFFRDE MGAYRLYTVV
PKLVKFVDML TNWYVRTNRR RLKGESGTED CMRALETLFS VLFSMCRLMA PFTPFITELM
YQNLRHLIDP ASVEEKDTGS IHYLMLPHVR ESLIDKRIES AVTQMQSVIE LGRVIRDRKT
LPVKYPLKEV VVIHQDPEAL RDIQSLQKYI LEELNVRQLT LSTDKDKYGI RLRAEPDHMV
LGKRLKGAFK SVTSSIKELK SEELENFQRT GSIVVDGHEL HEDDLRLMYT FDQTSGTPSQ
YEAHSDAQVL VLLDVTPDQS MVDEGVAREV INRIQKLRKK GHLVPSDEIT VYYSSQPAGE
YLDKVIQAHT DFIFATTKAP LKPYPVGNNA SVIVQEKTQL KGSDLELTIV RGAAVSRAPL
TTAACAYVNL RVTLKDKQQE GVVLLENPKG DNILDVERLK TVCCSVFGLN GAPVTIFNGK
TALKAQTDLM SLSGKTLTVT SGSSPADVSS SDSLLCPYVN LQLMNSSPAE CQTGDVATLL
LMNPEGKNAL QFPDLLHETA KVFGLRGRKL MLYMNEDLTE ELEASSLQTL NTKTLYVKVL
PTTAEA
//
