ID F2SB08_TRIT1 Unreviewed; 1012 AA.
AC F2SB08;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=TESG_08670 {ECO:0000313|EMBL:EGE00758.1};
OS Trichophyton tonsurans (strain CBS 112818) (Scalp ringworm fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=647933;
RN [1] {ECO:0000313|EMBL:EGE00758.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112818 {ECO:0000313|EMBL:EGE00758.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Henn M., Martinez D., Young S.K., Zeng Q., Gargeya S., Haas B.,
RA Alvarado L., Berlin A., Chapman S., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Howarth C.,
RA Larson L., Mehta T., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., White T.C.,
RA Abdel-Rahman S., Graser Y., Gurr S.J., Kohler G., Martinez-Rossi N.,
RA Oliver B.C., Rossi A., Shelest E., Summerbell R., Lander E., Nusbaum C.,
RA Birren B.;
RT "Annotation of Trichophyton tonsurans strain CBS 112818.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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; GG698551; EGE00758.1; -; Genomic_DNA.
DR AlphaFoldDB; F2SB08; -.
DR HOGENOM; CLU_001493_7_2_1; -.
DR OrthoDB; 656at2759; -.
DR Proteomes; UP000009172; 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; 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 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}.
FT DOMAIN 41..695
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 741..894
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1012 AA; 113747 MW; 5B1721E8436750B7 CRC64;
MPELSRSLAR SWSSTLKLPK STFPPRIALA DQSKYLKRCS DDLYSWQQRN RPATATFTLH
DGPPYANGDL HIGHALNKIL KDIICRVQLA KGKRVHYVPG WDCHGLPIEL KALQGQKELG
DLRLAGRDGA AQIRSAARQL AEKTVSQQME GFRNWAIMGD WDNAYTTMNK DFERRQLAVF
LEMVEKGLIY RRYKPVYWSP SSSTALAEAE LEYKEDHIST AALVKFVLDN LPSQVLEHPL
LAGNDISAVI WTTTPWTLPA NAALAVNPDF EYTIVDSTRH GKLLVAQSRL QYLQELLEDD
FTVVIPAIMG SELLNSTYRS HFKGPESEKQ RVIAADFVTA DAGSGIVHCA PGHGMEDYEV
CLALGIPAYA PVDGEGRFTQ SAMPTKPDLL TGKAVLGDGN HAVIKYLSEK GILIHKHAYK
HKYPYDWRSK LPVIIRATEQ WFADVGDIRG EAIQALQSVQ FIPPTGKSRL ETFVRNRSEW
CISRQRAWGV PIPALYHRTT GEAILTKESV SHIIKMIEER GIDAWWTDDE FDQAWLPASL
RDSSSPQYKR GTDTMDVWFD SGTSWAQLKD DSHENPPADV YLEGSDQHRG WFQSSLLTYI
SHQLAEGGKS SFKAPFKTLI THGFTLDQYG RKMSKSIGNT IQPDEIMGGT LLPPLKPKKI
KGKGPKPNPD IPVYDALGPD ALRLWAAGSD YTKDVIIGQQ VLKAVNISLH KFRVTFKLLL
GALQDFDPRN EVPYESLHAI DKISLVQLHN LVKTSQEAVD KMEFFKAVTA MNKWANLEFS
AFYIEAIKDR LYADSESGIS RRAAQTTLFH IYTHIQSLLG PIVPLLVEET WEHTPGSIKG
FLKHPFQRTF KSPDSKWKND ILEHEYSAMV AANSAIKAMQ ETARSKKQMG SSLQSFVHLV
LPEGFEISEQ LQSELPDFFV VSSVTIGSEC DSVLDDITQA EWSYNSEFKL PNDQIGKAWV
YTPTQAKCPR CWRYAVQPTE TGPKDEEELC HRCEEVVHEI DQQSDTGTST PN
//
