ID A5DSE1_LODEL Unreviewed; 993 AA.
AC A5DSE1;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 101.
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=LELG_00277 {ECO:0000313|EMBL:EDK42099.1};
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK42099.1, ECO:0000313|Proteomes:UP000001996};
RN [1] {ECO:0000313|EMBL:EDK42099.1, ECO:0000313|Proteomes:UP000001996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH981524; EDK42099.1; -; Genomic_DNA.
DR RefSeq; XP_001527757.1; XM_001527707.1.
DR AlphaFoldDB; A5DSE1; -.
DR STRING; 379508.A5DSE1; -.
DR GeneID; 5234780; -.
DR KEGG; lel:LELG_00277; -.
DR VEuPathDB; FungiDB:LELG_00277; -.
DR eggNOG; KOG0433; Eukaryota.
DR HOGENOM; CLU_001493_7_2_1; -.
DR InParanoid; A5DSE1; -.
DR OMA; HCWRCKT; -.
DR OrthoDB; 656at2759; -.
DR Proteomes; UP000001996; 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; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR Gene3D; 1.10.730.20; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR HAMAP; MF_02002; Ile_tRNA_synth_type1; 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; IPR023585; Ile-tRNA-ligase_type1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001996}.
FT DOMAIN 57..702
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 750..905
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 993 AA; 113799 MW; FCC5B2A72B338390 CRC64;
MPGQVYTKAV RRFSKAPRCL EGKPGYSKTL NLPKTAFGPK IPRDKVRDQL IKATSEDLYK
WQESRDSNST NGEFILHDGP PYANGDLHMG HALNKICKDI INRFQLIYNG KKIKYQPGWD
CHGLPIEMKV ENQLSNAQFK DPVETRRACK EWAQAQIENQ KSQFRQLAIM TDFDKPYITM
QHKYEINQLR VFIKLAELGL LSQQLKPVWW GCETQTALAE AELEYNDNHK SVAIYVKFPI
VSEGLKKYIP KKHQEQGKNL HFLIWTSTPW TIPANKAICA NKDVMYTLIT SDKEVLVVAE
NLADTVIELA PDSNFQKTNV QIPGSELVGE QYINPANEDN VKRPVLHGDH VVVTTGTGLV
HTAPAHGRDD YLVAKHNNIS LEESIVNNQG RYVEGKNSGL PPGFAKLASH KVNEVKTNMQ
CVEIMKLHNM IYHMNKSFKH SYPYDWRSLT PVVQRATPQW FVNVEKIKPE ALKALENVEF
SPAGGYSRLK AFVENRSEWC ISRQRCWGVP LPIVYNIQTN EPVLDLEVLE YTVGKIAEFG
TDEWFVKEND IGRWLPDKLD GTKYYKGQDT MDVWFDSGTS WSTLRNDIKE CNDVDAPLAD
IYLEGSDQHR GWFQSSLLNK IIYSGVVRKG VDVFDAKAPF KTVITHGFIT DGKGQKMSKS
KGNIFSPKEA IEGCKKPLTP YLGTDGLRLW VASSNYKQDV SFNPEILNRV SDMGKKYRLT
FKYILGNLYG FKEEQEKEGL ASNYDLSLLD RYVLHTLYTL QQTCFDNYSE YNFSRVVSSI
NAHVNSVLSA LYFDVSKDCL YTDASDSPRR KAIQFVLNET LKCYILALAP IQPLLVQEVW
SQHTGQEDAS PFKQQQGYFK VLQKYENHEL AEQFNTFFNL RDLVNKEIEM LKENKFFKNK
LELELQFYID DKSSSMHGFL KQVETYLEDL FLVSKVSLLN EPIDGDMVPI EIKGEKILLN
ITLSDQHKCP RCWKFIADEE ETLCKKCDSV VNT
//
