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
//