UniProt: A0A078HAR6

Database: UniProt
Entry: A0A078HAR6_BRANA

LinkDB:  A0A078HAR6_BRANA 
Original site:  A0A078HAR6_BRANA

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Ontology (10)   
   GO (10)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (15)   
   InterPro (11)   
   Pfam (3)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (29)   

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ID   A0A078HAR6_BRANA        Unreviewed;      1080 AA.
AC   A0A078HAR6;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   28-JAN-2026, entry version 49.
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   Name=BnaA02g30540D {ECO:0000313|EMBL:CDY33933.1};
GN   ORFNames=DARMORV10_A02P37850.1 {ECO:0000313|EMBL:CAF2144158.1},
GN   GSBRNA2T00055444001 {ECO:0000313|EMBL:CDY33933.1};
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY33933.1, ECO:0000313|Proteomes:UP000028999};
RN   [1] {ECO:0000313|EMBL:CDY33933.1, ECO:0000313|Proteomes:UP000028999}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX   PubMed=25146293; DOI=10.1126/science.1253435;
RA   Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA   Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA   Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA   Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA   Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA   Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA   Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA   Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA   Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA   Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA   Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA   Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA   Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT   "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT   Brassica napus oilseed genome.";
RL   Science 345:950-953(2014).
RN   [2] {ECO:0000313|EMBL:CDY33933.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope - CEA;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:CAF2144158.1}
RP   NUCLEOTIDE SEQUENCE.
RG   Genoscope - CEA;
RA   William W.;
RL   Submitted (JAN-2021) 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; HG994356; CAF2144158.1; -; Genomic_DNA.
DR   EMBL; LK032324; CDY33933.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A078HAR6; -.
DR   STRING; 3708.A0A078HAR6; -.
DR   PaxDb; 3708-A0A078HAR6; -.
DR   Gramene; CDY33933; CDY33933; GSBRNA2T00055444001.
DR   OMA; HRTRNIE; -.
DR   Proteomes; UP000028999; Unassembled WGS sequence.
DR   Proteomes; UP001295469; Chromosome A02.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
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; 1.10.10.830:FF:000003; Isoleucine--tRNA ligase, chloroplastic/mitochondrial; 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:UP000028999};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          122..757
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          803..966
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   DOMAIN          1036..1064
FT                   /note="Zinc finger FPG/IleRS-type"
FT                   /evidence="ECO:0000259|Pfam:PF06827"
FT   REGION          68..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..103
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1080 AA;  121230 MW;  C922A99032D78232 CRC64;
     MSSLFKSFAG NPREAAAMAM VQSSSYRVLS GGSCSNLRRN TPLDSFLAKG RSPVKAFSFM
     FSTQPNNEFG HSSKRRSRGP VMAAKKASEG EKQEDGKYKH TVDLPKTGFG MRANALTREP
     ELQKLWDENQ VFKRVSDSNY GGSFVLHDGP PYANGDLHMG HALNKILKDI INRYKLLQNY
     KVQYVPGWDC HGLPIELKGN NLAVTIKHFS SAAAKFAKAT VKTQMESFKR FGVWADWNNP
     YLTLDPEYEA AQIEVFGQMA LLGYIYRGRK PVHWSPSSRT ALAEAELEYP EGHISRSIYA
     IFKLVGGVKT SLLEEFMPNI CLAVWTTTPW TIPANAAVAV NAKLQYSVVE VQSSSEDESA
     STSNKKKMMG KVLKNQQKLF VIVATDLVPA LEAKWGVKLI ITKTFLGSDL EGFRYTHPVD
     KRDCPVVIGG DYITTESGTG LVHTAPGHGQ EDYATGLKYG LPIVSPVDDG GNFTEEAGQF
     RGLSVLGEGN SAVVSYLDEN MSLVMEESYA HKYPYDWRTK KPTIFRATEQ WFASVEGFRK
     ATMEAINNVK WIPHQAVNRI TAMTSSRSDW CISRQRTWGV PIPVFYHVQT KEPLMNEETV
     DHVKSIISQK GSDAWWYMSV EDLLPEKYRD KAADYEKGTD TMDVWFDSGS SWAGVLGKRE
     GLTFPADVYL EGTDQHRGWF QSSLLTSIAT KGKAPYSSVI THGFVLDEKG MKMSKSLGNV
     VDPLMVIEGG KNSKDAPAYG ADVMRLWVSS VDYTGDVLVG PQILRQMSDI YRKLRGTLRY
     LLGNIHDWRV DNAVPYQDLP IIDQHALFQL ENVVKNIKEC YENYQFFKIF QIIQRFTIVD
     LSNFYFDIAK DRLYTGGTSS FTRRSCQTVL STHLLSILRV IAPIVPHLAE DVWQNLPFEY
     RNEDGCQAKF VFELKWPTLN EQWLSFPAED ILFWERLLEL RTEVNKVLEL ARNGKLIGSS
     LEAKVYLHTP DAGMASKLLK MCEAQNEADT LQRIFITSQV EVLSSVEKEM VSNVQHTGEY
     GEGENKVWIG VSRAEGSKCE RCWNYSGQVG SFSDHPTLCG RCFNVIIANP PQPAVATVIS
//

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