ID B8M0U7_TALSN Unreviewed; 1079 AA.
AC B8M0U7;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 13-SEP-2023, entry version 77.
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=TSTA_087130 {ECO:0000313|EMBL:EED21480.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED21480.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; EQ962653; EED21480.1; -; Genomic_DNA.
DR RefSeq; XP_002478443.1; XM_002478398.1.
DR AlphaFoldDB; B8M0U7; -.
DR STRING; 441959.B8M0U7; -.
DR GeneID; 8100845; -.
DR VEuPathDB; FungiDB:TSTA_087130; -.
DR eggNOG; KOG0434; Eukaryota.
DR HOGENOM; CLU_001493_1_0_1; -.
DR InParanoid; B8M0U7; -.
DR OMA; EIIVIHK; -.
DR OrthoDB; 656at2759; -.
DR PhylomeDB; B8M0U7; -.
DR Proteomes; UP000001745; 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 Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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:UP000001745}.
FT DOMAIN 12..634
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 691..846
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1079 AA; 124746 MW; E326D411AEBFD173 CRC64;
MSIDFPAEEE TVLKRWREID AFRRQVELSR GRKPYTFYDG PPFATGLPHY GHLLASTIKD
IIPRYFSMTG HYCERRFGWD THGVPIEHEI DKKLGMSGSE AVEKLGIAKY NEECRAIVMR
YASEWRQTIE RLGRWIDFDN PYRTLDATFM ESVWWIFKQL ADKDMVYRGY RVMPYSTALN
TPLSNFEASQ NYKDVTDPAV VVSFPLVDDP NVCLLAWTTT PWTLPSNVGL CVHPDFEYVK
VLDEASGKHY ILMESLLRTL YKDPKKAKFK IVDRFKGSAM KGWRYEPLFD YFIDDFKDCG
FRVCNDTYVT SDAGTGIVHQ APAFGEDDYR VAVEHGVISD KVLPPNPVDE TGNFTFEVRD
FVGQHVKAAD RVIIKHLKGT GRLIVDGQIT HSYPFCWRSD TPLIYRAVPA WFVKVGPVIP
TMLKGIEDSH WVPSFVKEKR FANWIQNARD WNIARNRYWG TPIPLWVSDD FKEVVAIGSV
SELKELSGYE GELTDLHRDK IDHITIPSKQ GKGQLRRVPE VFDCWFESGS MPYASVHYPF
ERKDTFQDAF PAQFIAEGLD QTRGWFYTLS VLGCHLFGKL PYQNVIVNGI VLAEDGKKMS
KRLKNYPDPT LIMDRYGSDA LRLYLINSPV VRAEPLRFKE AGVKEIISKV LLPLWNSYKF
FEGQVALLKK IENIDYCFDP KAEVTNTNVM DRWILASCQS LLKFVNQEMS AYRLYTVVPR
LLELIDNTTN WYIRFNRRRL KGENGVDDTQ HALNTLFEVL YTLVRGLAPF IPFITDTIYL
RLLPHIPESL RGEDDRSVHF QPYPQVREEL FDEVIERRVA RMQRVIELGR VSRERRTLAL
RQPLKTLVVI HQDQQYLDDV KSLESYIVEE LNVRDLILSL DEEKYNVQYS VSADWPTLGK
KLKKDAQKVK KFLPSLTSDD VKKFVAEKRI VVDGIELAEE DLVVKRGIKE DETSQNMETN
SDSDVLTILD VNIYPELADE GLGREIISRV QRLRKKAGLQ TTDDVKMEYK VLSDPDNVGL
DRVFKTQSAA FEKVLRRPID HHVITHVAGE IPKEEEPGLI MEEEQEVQKA TFLLRLLKL
//
