ID A0A087Y1H2_POEFO Unreviewed; 1268 AA.
AC A0A087Y1H2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 24-JAN-2024, entry version 44.
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};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000011875.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000011875.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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; AYCK01000361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007549323.1; XM_007549261.2.
DR AlphaFoldDB; A0A087Y1H2; -.
DR STRING; 48698.ENSPFOP00000011875; -.
DR Ensembl; ENSPFOT00000011892.2; ENSPFOP00000011875.2; ENSPFOG00000011883.2.
DR GeneID; 103136144; -.
DR KEGG; pfor:103136144; -.
DR CTD; 3376; -.
DR eggNOG; KOG0434; Eukaryota.
DR GeneTree; ENSGT00550000074921; -.
DR OMA; EIIVIHK; -.
DR OrthoDB; 656at2759; -.
DR Proteomes; UP000028760; 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:UP000028760}.
FT DOMAIN 17..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"
SQ SEQUENCE 1268 AA; 145395 MW; 986589E6538C6694 CRC64;
MVEPVPESIN FPSEEEKILQ FWQERDCFQE CLKQSKNRPR YTFYDGPPFA TGLPHYGHIL
AGTIKDIVTR FAHQSGFHVD RRFGWDCHGL PVEYEIDKTL GIKGPEDVAK MGIAEYNKQC
RNIVMRYSNE WEATVRRMGR WIDFKNDYKT LYPWFMETVW WVFKQLYDKG LVYRGVKVMP
FSTACNTPLS NFESHQNYKD VQDPSVIVSF PLVESENVSL IAWTTTPWTL PSNLALCVNP
EFLYVQVKEN TTERTYIMME ARLGALFKSE GEYTILNKFP GKDLKGKKYK PLFHYFSKCA
EKGAFQVVTD NYVKEEEGTG VVHQAPYFGA DDYRVCTEYN IIQRDQTPIC PVDASGCFTS
EVTDFAGQYV KDADKNIIKL LKEKGRLVNA STFKHNYPFC WRSDTPLIYK AVPSWFVRVE
HMVDKLLDCN GKCYWVPEFV REKRFGNWLR DARDWAISRN RYWGTPIPLW VSDDFEEVVC
VGSMAELEEV TGVKVTDLHR ENIDSLTIPS RCGKGVLRRI TEVFDCWFES GSMPYAQVHY
PFENRKEFED TFPADFIAEG IDQTRGWFYT LLVLSTALFG KPPFKNVIVN GLVLASDGQK
MSKRKKNYPD PGVIVQNYGA DALRLYLINS PVVRAENLRF KEEGVRDVLK DVFLPWYNAY
RFLVQNVQRL QKEEEIQFLY NENTVKQSDN IMDKWIQSFT QSLIQFFKAE MDAYRLYTVV
PRLVKFVDML TNWYVRTNRR RLKGESGTED CLWALETLFS VLFSMCRLMA PFTPFITEMM
YQNLRHLIDP ASVEEKDSNS IHYLMLPQVR DNLIDKRIES AVSQMQSVIE LGRVIRDRKT
LPVKYPLKEV VVIHQDPEAL KDIQSLEKYI LEELNVRQLT LSTEKDKYGI RLRAEPDHMV
LGKRLKGAFK AVTASIKELT SEQLEAFQKT GSIVVDGHEL HEEDLRLMYT FDQTSDSAAQ
YEAHSDAQVL VLLDVTPDQS MVDEGVAREV INRIQKLRKK AHLVPSDDIL VYYRCQPEGE
YLGSVIEAHT DFILATTKAP LLPFPVPKTA SVIIEEKTQL KGSDLEFTIV KGSSLSQTKP
NGPVCAYINL RVKVDNKEQE GVVLLENPRG DNRLDLDKLR KVCSSIFGIN NTQLRFFSDQ
SELTSSADLQ AYSGKTLLVT SGPSPPGAVP TADTLLCPYV NLLLWNAVPA ECQAGDAGTL
LLVNPVGRNE LDHSGLLSEA AKLFGLRGRR IKLYLDHHLT SELPAESSVK SLHTKTLFVR
VFPTTAEA
//