ID B8M4A6_TALSN Unreviewed; 1414 AA.
AC B8M4A6;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 13-SEP-2023, entry version 82.
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_024270 {ECO:0000313|EMBL:EED19101.1};
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:EED19101.1, 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; EQ962654; EED19101.1; -; Genomic_DNA.
DR RefSeq; XP_002479535.1; XM_002479490.1.
DR STRING; 441959.B8M4A6; -.
DR GeneID; 8109609; -.
DR VEuPathDB; FungiDB:TSTA_024270; -.
DR eggNOG; KOG0433; Eukaryota.
DR eggNOG; KOG1198; Eukaryota.
DR HOGENOM; CLU_001493_7_2_1; -.
DR InParanoid; B8M4A6; -.
DR OMA; YHDHKST; -.
DR OrthoDB; 656at2759; -.
DR PhylomeDB; B8M4A6; -.
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:0016491; F:oxidoreductase activity; IEA:InterPro.
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 CDD; cd08276; MDR7; 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; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR033708; Anticodon_Ile_BEm.
DR InterPro; IPR011032; GroES-like_sf.
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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
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; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00984; TRNASYNTHILE.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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 23..355
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 1414 AA; 157047 MW; 84911636CB5C4098 CRC64;
MSSTYQAWHV YRNASTQSEK SLDILDNLVL EEIEKPVPGP GQVLVRIHAA ALNFRDLLIT
AFSPKYPVPT TLGLSPCSDG AGAIEAVGPD NKIWNVGDEV IFRVSNSWDS GDVSNFKGNG
IGSGDIHGTL SQYLVMDESW LVRKPTHLTW EHAASIAGAG GTAIQALFHN GISNGLDLSG
KTVLTQGTGG SSIFCAQFAV AAGARVIGTT SSESKAELLK SLGVHEVVNY KIHPAWADEV
LKLTEGRGVD LVIDVGGSAT FEQSLKAARF GGTVAAVGFL TEPQPSDPGL IHTIIFGAKT
LRGQMAASLV MYHEMVELME KHKIEPVVGQ VFEWSAAKEA FKALMKQSVP GKIVIKVCQC
GRSGTYGAMG FPIGQPSSMT RSWTSTLKLP RSSFPARVSV ADQAKYLRKC SDELYAWQRE
NRPANETFVL HDGPPYANGE LHVGHSLNKI LKDIINRTQL SRGKRIHYVP GWDCHGLPIE
LKALQAQQKN VIDFTQGPGS AATIRKAARK LAEKTVKEQM RVFRGFGIMA DWEGHWKTLD
KGFEMKQLGI FREMVEKGLI YRRFKPVYWS PSTGTALAEA ELEYNDNHIS TAALVRFPLA
KLPEQIRDKP LVDVTSLSAV IWTTTPWTLP ANAAIAVHES LNYLIVQSSN HGQLLIAESR
LGYFQDMLKE ELQVLVPSIQ GSELCQKTTY RPLFPRDGVE EQPIIAADFV TADSGSGLVH
CAPGHGMDDY EVCLAQGIQA FAPVTDEGCF TDEAMPRDPS FLSGKSVLDE GNTLVLQYVE
SMSQLLCQHK YEHKYPYDWR SKRPIIIRAT EQWFADVANI RESALASLED VTFVPASGKQ
RLKNFVQNRT EWCISRQRAW GVPIPALYDK VTGQAVLTKE TVSHIMNVID ERGIDAWWTD
SPEDPAWIPP FLQQDGSSDY RRGTDTMDVW FDSGTSWTQV ENESLEKDRP ADIYLEGTDQ
HRGWFQSSLL TYVAHQVASG KSDASTIKSP FKHLITHGFT LDQDARKMSK SIGNIIQPDA
IMNGTLLPPL KQKKSKGTKE QKVSGPVYDA LGPDALRLWV ASSDYTRDVV IGQQVLQTIN
TSLHKYRVTF KLLLGALGDF DPSVNLRQYE DLHKIDRLAL MQLTRLVDTC RNAFDSFEFY
KAVNALNRWA NHEFSAFYME TLKDRLYTEA EDGASRRAAQ TTLFHIYTYL QELLAPITPL
LVEESWEHTS ERVKAQLKHP LQRISRAAPA EWVDETTSHD FVDLMAANAA VKIIQESARS
KKQMGSSLQS FVYFELRDES LGTFQRYISE LPDLFVVSSV SLGVKGSDLP GEIASAKWSY
TQEFELPNSK QKATVHVYAP TQAKCPRCWR YAAPEAVAEE PPLCERYQCT IRGADKMKIR
GNPSPYHIGA SPDQSNDVCI PTSERVQIAR IGLF
//