UniProt: A0A7I8KWH0

Database: UniProt
Entry: A0A7I8KWH0_SPIIN

LinkDB:  A0A7I8KWH0_SPIIN 
Original site:  A0A7I8KWH0_SPIIN

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Ontology (10)   
   GO (10)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (15)   
   InterPro (11)   
   Pfam (3)   
   PROSITE (1)   
All databases (27)   

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ID   A0A7I8KWH0_SPIIN        Unreviewed;      1059 AA.
AC   A0A7I8KWH0;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   28-JAN-2026, entry version 18.
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};
GN   ORFNames=SI8410_09012053 {ECO:0000313|EMBL:CAA7401375.1};
OS   Spirodela intermedia (Intermediate duckweed).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Araceae; Lemnoideae; Spirodela.
OX   NCBI_TaxID=51605 {ECO:0000313|EMBL:CAA7401375.1, ECO:0000313|Proteomes:UP000663760};
RN   [1] {ECO:0000313|EMBL:CAA7401375.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Scholz U., Mascher M., Fiebig A.;
RL   Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
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; LR746272; CAA7401375.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7I8KWH0; -.
DR   OrthoDB; 10264412at2759; -.
DR   Proteomes; UP000663760; Chromosome 9.
DR   GO; GO:0005739; C:mitochondrion; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0032543; P:mitochondrial translation; IEA:TreeGrafter.
DR   GO; GO:0009791; P:post-embryonic development; IEA:UniProtKB-ARBA.
DR   GO; GO:0048608; P:reproductive structure development; IEA:UniProtKB-ARBA.
DR   CDD; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR   CDD; cd00818; IleRS_core; 1.
DR   FunFam; 1.10.730.20:FF:000001; Isoleucine--tRNA ligase; 1.
DR   FunFam; 3.90.740.10:FF:000013; Isoleucine--tRNA ligase, chloroplastic/mitochondrial; 1.
DR   FunFam; 3.40.50.620:FF:000111; Mitochondrial isoleucyl-tRNA synthetase; 1.
DR   Gene3D; 1.10.730.20; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 1.10.10.830; Ile-tRNA synthetase CP2 domain-like; 1.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR   HAMAP; MF_02002; Ile_tRNA_synth_type1; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR033708; Anticodon_Ile_BEm.
DR   InterPro; IPR002301; Ile-tRNA-ligase.
DR   InterPro; IPR023585; Ile-tRNA-ligase_type1.
DR   InterPro; IPR050081; Ile-tRNA_ligase.
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   InterPro; IPR010663; Znf_FPG/IleRS.
DR   NCBIfam; TIGR00392; ileS; 1.
DR   PANTHER; PTHR42765:SF1; ISOLEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42765; SOLEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF06827; zf-FPG_IleRS; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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:UP000663760};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          96..739
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          785..948
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   DOMAIN          1018..1045
FT                   /note="Zinc finger FPG/IleRS-type"
FT                   /evidence="ECO:0000259|Pfam:PF06827"
FT   REGION          37..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1059 AA;  118788 MW;  E1B8A38F79E6BF6D CRC64;
     MDAPSLLRLA RYPVSNAAVV VTSFRLSLFH GRQLSTGVGE GFPGSSSKRR ARGPVMAAKK
     ASDGEKQNEG KYKHTLNLPK TAFGMRANSS VREPEIQKLW EENQVMKRVV ERNNAGTFIL
     HDGPPYANGS LHMGHALNKI LKDIINRYKL LQNYKVHYVP GWDCHGLPIE LKVLQSMDQD
     ARKELTPIKL RKKAAKFARD TVATQMKSFK RYGIWADWNN PYLTLAPEYE AAQIEVFGQM
     ALQGYIYRGR KPVHWSPSSR TALAEAELEY PEGHTSKSIY VILKLVNSPP DSSALLTEFF
     PHLFLAIWTT TPWTIPANAA VAVNAQLTYA IVEVQSVEKE SISQESRLKV GNVLKGGNQK
     LFLVVASELV PTLQSKWGVK LVVKKTFLGS ALENSRYIHP IDERECPVVI GGDYITTESG
     TGLVHTAPGH GQEDYVTGLK YGLPILSPVD DLGKFTEEAG GFSGLDVLGD GNAAVVKFLD
     EKLSIILEEP YKHKYPYDWR TKKPTIFRAT EQWFASVEGF RKLALDAINE VTWIPQQAQN
     RITAMTSSRS DWCISRQRTW GVPIPVFYHV TTKKPLINEE TINHVKSVVS EKGADAWWYM
     TKEDLLPDKY RHQASEYEKG TDTMDVWFDS GSSWAAVLGK REELHFPADL YLEGTDQHRG
     WFQSSLLTSV AVKGKAPYSS VITHGFVLDE KGMKMSKSVG NVVDPENVIS GGKNQKDEPG
     YGADVLRLWV SSVDYSGDVL IGPQVLRQMS DIYRKLRGTL RYLLSNLHDW TPEYAVSYDD
     LPKIDKFALF QLENVVNAIK ESYETYQFYK IFQIMQRFAI VDLSNFYFDV AKDRLYVGGT
     AGFTRRSCQT VLAAHLLKIT RVIAPILPHL AEDAWQNLPF EHTTVGGSAT RFVFESKWPD
     SNDQWLAVPV EDIDFWRKIL ELRSEVNKVL ETARVGKLIG SSLEARVHLY TEDAAMASRL
     RELCEAKNDA DALTRIFITS QVEILSSLAG SDEIPCTGEL VGEGQRIWIG VSRAVGTKCE
     RCWNYSPKVG SFVGHPTLCE RCYDVIEGPL PVGAMAEVS
//

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