ID A0A6C1E1D0_SACPS Unreviewed; 1002 AA. AC A0A6C1E1D0; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 02-OCT-2024, entry version 16. 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=ISM1_1 {ECO:0000313|EMBL:QID82935.1}; GN ORFNames=GRS66_005369 {ECO:0000313|EMBL:QID82935.1}; OS Saccharomyces pastorianus (Lager yeast) (Saccharomyces cerevisiae x OS Saccharomyces eubayanus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=27292 {ECO:0000313|EMBL:QID82935.1, ECO:0000313|Proteomes:UP000501346}; RN [1] {ECO:0000313|EMBL:QID82935.1, ECO:0000313|Proteomes:UP000501346} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 1483 {ECO:0000313|EMBL:QID82935.1, RC ECO:0000313|Proteomes:UP000501346}; RX PubMed=31791228; RA Salazar A.N., Gorter de Vries A.R., van den Broek M., Brouwers N., RA de la Torre Cortes P., Kuijpers N.G.A., Daran J.G., Abeel T.; RT "Chromosome level assembly and comparative genome analysis confirm lager- RT brewing yeasts originated from a single hybridization."; RL BMC Genomics 20:0-916(2019). CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP048997; QID82935.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6C1E1D0; -. DR Proteomes; UP000501346; Chromosome scxvi. 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; cd07960; Anticodon_Ia_Ile_BEm; 1. DR CDD; cd00818; IleRS_core; 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 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; 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 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 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}. FT DOMAIN 83..712 FT /note="Aminoacyl-tRNA synthetase class Ia" FT /evidence="ECO:0000259|Pfam:PF00133" FT DOMAIN 758..879 FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase FT anticodon-binding" FT /evidence="ECO:0000259|Pfam:PF08264" SQ SEQUENCE 1002 AA; 115765 MW; 2B38899D1D094F7A CRC64; MKRSRLVPQH IFSIISKRYL AKHAYQKTLN LPKTKFPNRS NLEITLRELI PKSSQLVYKE QLCDFFEEFS KLNTTDEKLE FIKEKLFILH DGPPYANGEL HLGHALNKIL KDIINRYQLS QGKYIFYKPG WDCHGLPIEI KALKDLSAQQ IESISPLKIR SMALKHAQKA IKRQRETFQH FAILTDWETP YLTMDKDYEI NQLNIFKEMY ERGLIKRQNK PVYWGTETRT ALAEGELEYN ESHKSIAAYV KFPLEKKSQM DLCKKLGITN NLPIYCLIWT STPWTLLSNR AICFNQDFSY SLLRLNSELI LVETGSIDKL GLTTNSFETI KQFQGTHLNG LYYQNLLVDD KVGRPLLHGA HVTSGTGTGL VHTAPGHGQD DYLIGIQNGL EIYSPVDHQG RYQLNELPQS VRSIVRDEGD LTKGRQVLDA ETAKIILCKL SDLNLLYKSH EYTHSYPYDW RSKKPVIIRA TPQWFADLHD VKNLALESIS RVKFCPKRGY SRLSSFIKSR NEWCISRQRS WGIPILSFYK KSEPDSVLMN SEILAHAIEK IKQKGINAWF DDKDNDMKEW LPEKYHDVAH EYCRSQDTMD VWFDSGSSWR VIKDFYEKSL KLSKLPSPLY QVCLEGSDQH RGWFQSSLLT KVASSNVPVA PYEEVITHGF TLDENGLKMS KSVGNTISPE AIIRGDENLG LPALGVDGLR YLIAQSNFTT DIVAGPTVMK HVGEALKKVR LTFRYLLSNL QKSQDFNLLP IEQLRRVDQY TLYKINELLQ TTREHYQKYN FSKVLITLQY HLNNELSAFY FDISKDILYS NQISSLARRQ VQTTLVHILN AYRAILAPIL PVMVQEVWKY IPEGWLQGQE HIDINPMRGK WPFLDSNTEI VTSFENFELK ILKQFQEEFK RLSLEEGVTK TTHSHVTIFT KHHLPFSSDE LCDILQSSAV DILQMDDNNN SLPTIELGSG INVQILVERS KRHNCPRCWK ANSAEEDKLC DRCKEAVDHL MS //