ID   A0A093URI5_TALMA        Unreviewed;       921 AA.
AC   A0A093URI5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
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=GQ26_0440570 {ECO:0000313|EMBL:KFX42490.1};
OS   Talaromyces marneffei PM1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX42490.1, ECO:0000313|Proteomes:UP000029285};
RN   [1] {ECO:0000313|Proteomes:UP000029285}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PM1 {ECO:0000313|Proteomes:UP000029285};
RX   PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA   Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA   Lin X.;
RT   "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT   of Dimorphic Transition in Penicillium marneffei.";
RL   PLoS Genet. 10:e1004662-e1004662(2014).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFX42490.1}.
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DR   EMBL; JPOX01000044; KFX42490.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093URI5; -.
DR   HOGENOM; CLU_001493_7_2_1; -.
DR   Proteomes; UP000029285; 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   CDD; cd00818; IleRS_core; 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   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; 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   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          35..631
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          677..734
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   921 AA;  104430 MW;  C231D0F47A263218 CRC64;
     MTRSWTSTLK LPRSTFPARA PVADQTKYLR RCSDELYAWQ RENRPASDTF VLHDGPPYAN
     GELHVGHALN KILKDIINRT QLSRGKRIHY APGWDCHGLP IELKALQAQQ KDGNDFSKGL
     GSAATIRKAA RKLAEKTVKE QMRGFQGWGV MADWEGHYKT LDKKFEMSQL GIFREMVEKG
     LIYRRFKPVY WSPSTGTALA EAELEYNENH ISTTAFVRFP LVKVPEQIRS NPLVDTDSLS
     AVIWTTTPWT LPANAAIAIS ESLNYLIVKS SNHGQLLIAE SRLTYFQDML KEDLQVLGIR
     AFAPVNDEGR FTDEAMPHKP SFLSGKSVLD EGNTLVLQYV ESTNQLLNQH KYEHKYPYDW
     RSKKPIIIRA TEQWFADVAN IRESALASLE DVTFVPATGK QRLKNFVQNR TEWCISRQRA
     WGVPIPALYD KTTGQAVLTK ETVSHIMNVI DERGIDAWWT DSPEDPAWIP HHLQQENSPG
     YRRGTDTMDV WFDSGTSWTQ VEDKSLGKER PADIYLEGTD QHRGWFQSSL LTYVSHQVAS
     GTVESSTIKA PFKHLITHGF TLDQDARKMS KSIGNVIQPD AIMNGTLLPP LKQKKSKSAK
     EQKASGPVYD ALGPDALRLW VASSDYTRDV VIGQQVLQTV NTSLHKFRVT FKLLLGALGD
     FDPKVNMRQY EDLHKIDRQA LMQLTRLVDT CRNAFDNFEF YKAVNALNRW ANLEFSAFYM
     ETLKDRLYTE AENRGVGSYH ALLVEESWEH TPELVKAQLE HPLQRIARTT PTEWVDETIS
     IDFIDLMAAN TAVKVIQESA RSKKQMGSSL QSFVHFELPD NASHDIFQRY LSELPDLFVV
     SSVSLGVRGS NSLPSGIASA EWTYAEEFEL PNSGKKATVH VYAPNQAKCP RCWRYVAPEP
     VVEEAPLCKR CDDVIRTLDG N
//