UniProt: A0A2R5G099

Database: UniProt
Entry: A0A2R5G099_9STRA

LinkDB:  A0A2R5G099_9STRA 
Original site:  A0A2R5G099_9STRA

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (13)   
   InterPro (9)   
   Pfam (3)   
   PROSITE (1)   
All databases (21)   

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ID   A0A2R5G099_9STRA        Unreviewed;      1167 AA.
AC   A0A2R5G099;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   08-OCT-2025, entry version 25.
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=FCC1311_001642 {ECO:0000313|EMBL:GBG23945.1};
OS   Hondaea fermentalgiana.
OC   Eukaryota; Sar; Stramenopiles; Bigyra; Labyrinthulomycetes;
OC   Thraustochytrida; Thraustochytriidae; Hondaea.
OX   NCBI_TaxID=2315210 {ECO:0000313|EMBL:GBG23945.1, ECO:0000313|Proteomes:UP000241890};
RN   [1] {ECO:0000313|EMBL:GBG23945.1, ECO:0000313|Proteomes:UP000241890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Sedici K., Godart F., Aiese Cigliano R., Sanseverino W., Barakat M.,
RA   Ortet P., Marechal E., Cagnac O., Amato A.;
RT   "Sequencing, de novo assembly and annotation of complete genome of a new
RT   Thraustochytrid species, strain FCC1311.";
RL   Submitted (DEC-2017) 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: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:GBG23945.1}.
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DR   EMBL; BEYU01000001; GBG23945.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R5G099; -.
DR   FunCoup; A0A2R5G099; 426.
DR   InParanoid; A0A2R5G099; -.
DR   OrthoDB; 1706657at2759; -.
DR   Proteomes; UP000241890; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; 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; 1.10.730.10:FF:000004; Isoleucyl-tRNA synthetase, cytoplasmic; 1.
DR   FunFam; 3.40.50.620:FF:000023; 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   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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; 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   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   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363035};
KW   Reference proteome {ECO:0000313|Proteomes:UP000241890}.
FT   DOMAIN          35..662
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          722..864
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1167 AA;  133024 MW;  546E7EE2A1D77375 CRC64;
     MATTTKDEEG AGESGSASFE HVSDRFSFPT MEREVLEFWE ESDAFQKSMQ MAIEEGRPEY
     TFYDGPPFAT GMPHYGHILA GTIKDIVTRY ASLTGYHVSR RFGWDCHGLP VEYEIDKKLG
     ITGSDDVAKM GIAKYNAECR SIVTRYCSEW ERIVKRMGRW IDFQNDYKTM EPWYMESVWW
     VFKTIFEKDL VYKGFRVMPY STGCTTPLSN FEATSNYKDV SDPAVVVAFP LKEDPEVAFV
     AWTTTPWTLP SNMALCVNPE FTYVQIKDLA TGKQYILAKD RLSQLYPKML KQKAKYKGGE
     WEIVKEFLGK DLEGKEYEPL FPYFADWEKA FRVLVDGYVT DDSGTGIVHN APGFGEDDYR
     VCMEQGVIVA GGDLPCPVDA DGRFTKEITD FVGRYVKEAD NDICAAVKAA GRLVNKNSIM
     HSYPFCWRSD TPLIYRAVPS WFVRLDPIKE NLLQNNLETY WVPATVKEKR FHNWLVQARD
     WNISRNRYWG TPLPIWMSDD EEEIVVIGSI EELQELSGRE VTDLHRESID DITIPSKQGK
     GVLRRIPEVF DCWFESGSMP YAQLHYPFEN KERFEKGFPA DFIAEGLDQT RGWFYTLMVL
     STALFSRPAM KNLIVNGLVL AEDGKKMSKR LKNYPDPMNV VESYGADALR LYLINSPVVR
     AEPLRFSEEG VLQNVKEIFN PWYNAYRFLT QNVARAERDN SGWTFDRSIA FETARGSQNI
     MDRWIQASLN GLIKFVRQEM EAYRLYTVVP RLVDFIDNLT NMYVRLNRSR LKGGMADSNE
     DDTKIGLYCL YTVLLSLSKL MAPFTPFFAE FLYRRLARPD DERKASVHYL SIPEVDESLI
     DEKMVMRMRH LREIITAGRL ARGNELPLKR PLRELIIANK DQETLDDILT LKEYIEIELN
     VRKVSVTTDE QQFCKLSAKA NGAVLGVILG KKFGPINKAV QKLSHEELAA FQESGKMTVE
     DVELTTDQVF LNRVVVADES KYKAKVTPSN VVVVLDTFFD KSLLYGQVAR EVTSRVQKLR
     KAAGVKLEDV LDVYYGVEGD ADAVQIVHES IQAESEYVTS VIRQRLHPVS VCPSYAPVLA
     TNTDEVNDTQ FTVILCNPCP IVAKPDALAK SLGVDAAVAQ SLTSCIASMD YEWLKKEASS
     SLELTLDGKL YKLEAGTHYF LSVDQVP
//

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