(data stored in ACNUC7421 zone)

SWISSPROT: Q757H0_ASHGO

ID   Q757H0_ASHGO            Unreviewed;       873 AA.
AC   Q757H0;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 129.
DE   SubName: Full=AER043Cp {ECO:0000313|EMBL:AAS52727.1};
GN   ORFNames=AGOS_AER043C {ECO:0000313|EMBL:AAS52727.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS52727.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS52727.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|RuleBase:RU363039}.
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DR   EMBL; AE016818; AAS52727.1; -; Genomic_DNA.
DR   RefSeq; NP_984903.1; NM_210257.1.
DR   STRING; 33169.AAS52727; -.
DR   EnsemblFungi; AAS52727; AAS52727; AGOS_AER043C.
DR   GeneID; 4621105; -.
DR   KEGG; ago:AGOS_AER043C; -.
DR   HOGENOM; HOG000200747; -.
DR   InParanoid; Q757H0; -.
DR   KO; K01869; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004823; F:leucine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0097157; F:pre-mRNA intronic binding; IEA:EnsemblFungi.
DR   GO; GO:0000372; P:Group I intron splicing; IEA:EnsemblFungi.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
DR   GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR   Gene3D; 3.40.50.620; -; 1.
DR   Gene3D; 3.90.740.10; -; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR002302; Leu-tRNA-ligase.
DR   InterPro; IPR025709; Leu_tRNA-synth_edit.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
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; PTHR43740; PTHR43740; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR00985; TRNASYNTHLEU.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00396; leuS_bact; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q757H0.
DR   SWISS-2DPAGE; Q757H0.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|RuleBase:RU363039};
KW   ATP-binding {ECO:0000256|RuleBase:RU363039};
KW   Ligase {ECO:0000256|RuleBase:RU363039};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU363039};
KW   Protein biosynthesis {ECO:0000256|RuleBase:RU363039};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
FT   DOMAIN          50..187
FT                   /note="tRNA-synt_1g"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          236..413
FT                   /note="tRNA-synt_1_2"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          428..586
FT                   /note="tRNA-synt_1"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
SQ   SEQUENCE   873 AA;  97967 MW;  44B655300A7012AD CRC64;
     MRGFPGAWCK RSLNTASDAV DLVKVGQKWK SKVLSGVPQP AAEGTRPHMY VLSMFPYPSG
     MLHIGHLRVY TISDALNRFY RMKGYEVVHP MGWDAFGLPA ENAALERGIA PADWTRQNIA
     RMKQQKGDML AHFEWGREVT TCDPEYYRFT QELFLELWHH GMAYKKEAEI NWDPVDKTVL
     ANEQVDAQGR SWRSGALVEK RKLNQWFLRI TRFAHELSHD LDGLDGWPAK VKAMQKHWIG
     EVEGTEVRLC TGDGEAIVAF TPRIEAVFGL QYVAISTEHA LTKKMAERLP ELCEFLQRPL
     VLSESDLSGF QLPGTYVQHP FAKDHGHRIP VFVSPYVPAD GAGAVLGTPA HDEFDHKFWR
     ANKPAEPVIS SFEASGECDD ECHIQTKGIL NAKAGNLKGI SSQDAKQVLA DKLVATGDGR
     QTTQYRLRDW LISRQRYWGA PIPIIYCDSC GTVPVPKQDL PVMLPNIAGL SKKGNTLEHI
     PEFVNTSCPS CGGPAKRETD TMDTFMDSSW YFFRYLDSHN QKEPFGYDKA TRSMPVDMYI
     GGVEHSILHL LYARFISKFL ASIGKWDGSA CNGEPFKRLV TQGMVHGKTF IDPENGSFLK
     PEELDMSNPA DPIICRTGQK PRVSYEKMSK SKYNGADPAQ CISKHGPDAI RAHILFQAPI
     SDVVNWDETK IVGIERWLAR IIKLAHTLAA DSQLKHGPVA KLTNMHEIAL FNEVQKLLGS
     ITDSFSRTLS LNTVISDYMK LTNLLDQALK NKDINPAWLL THFKKLVSVI HPTVPAVSEE
     AADIIKGHLQ LLTWDHYVWP TVDAQQKDNS VGYRVFVDGK MRFIYPAPSA FINDKNGVLK
     ALLAHPDGGK YLAGRQVKNL ILKKNIISLV LQK
//

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