UniProt: R0JJ15

Database: UniProt
Entry: R0JJ15_ANAPL

LinkDB:  R0JJ15_ANAPL 
Original site:  R0JJ15_ANAPL

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (13)   
   InterPro (9)   
   Pfam (3)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (21)   

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ID   R0JJ15_ANAPL            Unreviewed;      1250 AA.
AC   R0JJ15;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   13-SEP-2023, entry version 39.
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};
DE   Flags: Fragment;
GN   ORFNames=Anapl_11392 {ECO:0000313|EMBL:EOA96986.1};
OS   Anas platyrhynchos (Mallard) (Anas boschas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8839 {ECO:0000313|EMBL:EOA96986.1, ECO:0000313|Proteomes:UP000296049};
RN   [1] {ECO:0000313|Proteomes:UP000296049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23749191; DOI=10.1038/ng.2657;
RA   Huang Y., Li Y., Burt D.W., Chen H., Zhang Y., Qian W., Kim H., Gan S.,
RA   Zhao Y., Li J., Yi K., Feng H., Zhu P., Li B., Liu Q., Fairley S.,
RA   Magor K.E., Du Z., Hu X., Goodman L., Tafer H., Vignal A., Lee T.,
RA   Kim K.W., Sheng Z., An Y., Searle S., Herrero J., Groenen M.A.,
RA   Crooijmans R.P., Faraut T., Cai Q., Webster R.G., Aldridge J.R.,
RA   Warren W.C., Bartschat S., Kehr S., Marz M., Stadler P.F., Smith J.,
RA   Kraus R.H., Zhao Y., Ren L., Fei J., Morisson M., Kaiser P., Griffin D.K.,
RA   Rao M., Pitel F., Wang J., Li N.;
RT   "The duck genome and transcriptome provide insight into an avian influenza
RT   virus reservoir species.";
RL   Nat. Genet. 45:776-783(2013).
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; KB743814; EOA96986.1; -; Genomic_DNA.
DR   AlphaFoldDB; R0JJ15; -.
DR   Proteomes; UP000296049; 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:UP000296049}.
FT   DOMAIN          18..650
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          706..862
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EOA96986.1"
FT   NON_TER         1250
FT                   /evidence="ECO:0000313|EMBL:EOA96986.1"
SQ   SEQUENCE   1250 AA;  143399 MW;  A0AC7BEE89864BE5 CRC64;
     RMVQQVPENI SFPNEEEKIL ELWKKLNCFQ ECLKQSKNRP RFNFYDGPPF ATGLPHYGHI
     LAGTIKDIVT RFAHQSGFHV DRRFGWDCHG LPVEYEIDKT LGIKGPEDVA KMGIAEYNNQ
     CRGIVMRYSK EWEFNVTRLG RWIDFENDYK TLYPEFMESV WWVFKQLYDK GLVYRGVKVM
     PFSTACNTPL SNFESHQNYK DVQDPSVIVS FPLDEDASIS LVAWTTTPWT LPSNLALCVN
     PELQYVKLRG KYNATGKIYI LMESRLIALY KSDTEYEILE RQVHELFHTW FPGITLKGKK
     YKPLFEYFIQ CKDKGAFTVL VDSYVKEEEG TGVVHQAPYF GADDYRVCVD FNIIQKDSVP
     VCPVDASGCF TAEVTDFAGQ YVKDADKNII KLLKEKGRLV HSSSYKHSYP FCWRSDTPLI
     YKAVPSWFVR VEHMVEKLLE NNAQCYWVPD FVREKRFGNW LKDARDWAIS RNRYWGTPIP
     LWVSDDFEEV VCIGSMAELE ELSGVKVTDL HRESIDHLTI PSRCGKGVLH RVPEVFDCWF
     ESGSMPYAQV HYPFENKKEL EDSFPADFIA EGIDQTRGWF YTLLVLSTAL FGRPPFKNVI
     VNGLVLASDG QKMSKRKKNY PDPMAIVNSY GADALRLYLI NSPVVRAENL RFKEEGVRDI
     LKDVFLPWYN AYRFLVQNVQ ILEHKEEGRE FLYNENTVKE SNNIMDKWIL SFTQSLIQFF
     KAEMAAYRLY TVVPRLVKFV DILTNWYVRM NRRRLKGENG TEDCIRALET LFSVLYSMCR
     LMAPYTPFIT ELMYQNLKTL IDPASVQEKN TESIHYLMLP QVREDLIDKK IESAVSCLQS
     VIELGRVIRD RKTIPVKYPL KEVVVIHRDP EALENISSLE KYILEELNVR QVTLSTNKDK
     YGVRLRAEPD HMVLGKRLKG AFKLVMAAIK ELKSEQLEEF QETGTIVVEG HELHEEDLRL
     MYTFDQTAGG SAQFEAHSDA QVLVLLDVTP DQSMVDEGVA REVINRIQKL RKKRNLVPTD
     EITVYYRSYP EGDYLDTVIK EHTDFILATI KAALKPYPVP TSKEVLIQET TQLKGSELEI
     TLVRGGVCQR VGPACAYVNL KVCANGTEQD GVLLLENPKG DNTLNFTGLV DAVSCIFGLK
     NSKLTVFNGK TELINKTDLL TLSGKTLHVT TGSAPALTNS PDALLCQYIN LQLVNAKPQE
     CQKGTMGTLL MENPVGQNGL TYQGLLHETA KVFGLRSRRL KLFLDEAQTQ
//

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