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Database: UniProt
Entry: B6K4I4_SCHJY
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ID   B6K4I4_SCHJY            Unreviewed;      1063 AA.
AC   B6K4I4;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   24-JAN-2024, entry version 69.
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=irs1 {ECO:0000313|JaponicusDB:SJAG_03545};
GN   ORFNames=SJAG_03545 {ECO:0000313|EMBL:EEB08391.1};
OS   Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=402676 {ECO:0000313|EMBL:EEB08391.1, ECO:0000313|Proteomes:UP000001744};
RN   [1] {ECO:0000313|EMBL:EEB08391.1, ECO:0000313|Proteomes:UP000001744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=yFS275 / FY16936 {ECO:0000313|Proteomes:UP000001744};
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
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};
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DR   EMBL; KE651167; EEB08391.1; -; Genomic_DNA.
DR   RefSeq; XP_002174684.1; XM_002174648.2.
DR   AlphaFoldDB; B6K4I4; -.
DR   STRING; 402676.B6K4I4; -.
DR   EnsemblFungi; EEB08391; EEB08391; SJAG_03545.
DR   GeneID; 7048804; -.
DR   JaponicusDB; SJAG_03545; irs1.
DR   VEuPathDB; FungiDB:SJAG_03545; -.
DR   eggNOG; KOG0434; Eukaryota.
DR   HOGENOM; CLU_001493_1_1_1; -.
DR   OMA; EIIVIHK; -.
DR   OrthoDB; 656at2759; -.
DR   Proteomes; UP000001744; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
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; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IBA:GO_Central.
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; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EEB08391.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001744}.
FT   DOMAIN          11..634
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          689..844
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   1063 AA;  122453 MW;  20604752881FEEFB CRC64;
     MSFRVPEEEE KILQFWRDID AFNTQLELSK DRRPFTFYDG PPFATGLPHH GHLLASTIKD
     IVTRFACLKG YSVTRRFGWD THGLPVEHEI DKKLGITGRD DVMALGIDKY NAECRKIVMT
     YAGEWRQTIE RLGRWIDFDN DYKTLYPTFM ESVWWVFKEL FKKNKVYRGY RVMPYSTACT
     TPLSNFEAQQ NYKEVQDPAV VIAFTLKSDP SVKALAWTTT PWTLPSNIAL AVHPDLEYVK
     ILDKETGNKY ILMESCLGTL YKNPKKAPIE ILERFPGAKL NGERYEPLFP YFKEQFAERA
     FKIYTASYVE AGSGTGIVHQ APAFGEEDYE AAWNAGIIDA DHQAPCPVDD NGHFTAEVTD
     FAGMYVKDAD KDVIRHLKGT GNLIKQSTIF HSYPFCWRSD TPLLYRAVPS WFVKVKEITD
     KMVDNVMKTH WVPSNIRDKR FANWLKNARD WNISRNRYWG TPIPLWVSED YEEVVCIGSI
     AELEELSGVK NITDLHRDSI DDITIPSKQG KGVLRRVSEV FDCWFESGSM PYASRHYPFE
     NQKEFEQGFP ADFISEGIDQ TRGWFYTLTV LGTHLFNTAP FKNVIVSGLV MAEDGKKMSK
     RLKNYPEPGL IIERYGSDAL RLYLINSPVV RAEVLKFKED GVKEVVARVL IPWWNSYKFF
     EAQASLYKKV TGKDFKFDEN APASANVMDR WIIARCQSLI EFVDHEMSVY RLYTVVPQLL
     GLIEEMTNWY IRFNRRRLKG EDGEAETVAA LTALFEVLYT LVRTMAPFTP FITENIYQHL
     KAYLNIDEND VSKRSVHFLS FPTVRPELVD NIVLRRVSRL QNVIELGRYI REQNNISLKV
     PLKTMVVVAT DNEFMDDVKA LEKYILEELN VREVIFSADE EKYGVVYSVQ ADWPVLGKKL
     RKDMAKVKKA LPSVTSEQVK AFQIQKEMVL DGIKLVEGDL QIHRSVQSTD EFLKSNTDRH
     VVVLLDTRMY PELESEGLAR EVINRVQRLR KKSQLQVTDD IRMTYSMTND SIGLADAIKA
     NQGLFEKVLR RNLEADDGET SGVIANEEQE VQGATFMLKL LKL
//
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