(data stored in ACNUC7421 zone)

SWISSPROT: Q75C28_ASHGO

ID   Q75C28_ASHGO            Unreviewed;       389 AA.
AC   Q75C28;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 113.
DE   SubName: Full=ACR089Cp {ECO:0000313|EMBL:AAS51315.1};
GN   ORFNames=AGOS_ACR089C {ECO:0000313|EMBL:AAS51315.1};
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:AAS51315.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51315.1, 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:RU363036}.
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DR   EMBL; AE016816; AAS51315.1; -; Genomic_DNA.
DR   RefSeq; NP_983491.1; NM_208844.1.
DR   STRING; 33169.AAS51315; -.
DR   EnsemblFungi; AAS51315; AAS51315; AGOS_ACR089C.
DR   GeneID; 4619618; -.
DR   KEGG; ago:AGOS_ACR089C; -.
DR   HOGENOM; HOG000059940; -.
DR   InParanoid; Q75C28; -.
DR   KO; K01867; -.
DR   OMA; LGHYFGT; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004830; F:tryptophan-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0070183; P:mitochondrial tryptophanyl-tRNA aminoacylation; IBA:GO_Central.
DR   GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd00806; TrpRS_core; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002305; aa-tRNA-synth_Ic.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002306; Trp-tRNA-ligase.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   PRINTS; PR01039; TRNASYNTHTRP.
DR   TIGRFAMs; TIGR00233; trpS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q75C28.
DR   SWISS-2DPAGE; Q75C28.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|RuleBase:RU363036};
KW   ATP-binding {ECO:0000256|RuleBase:RU363036};
KW   Ligase {ECO:0000256|RuleBase:RU363036};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU363036};
KW   Protein biosynthesis {ECO:0000256|RuleBase:RU363036};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
SQ   SEQUENCE   389 AA;  43063 MW;  7681D208524E928D CRC64;
     MVRYKDLSNL ISSSGITMQI KCGSGLRQFV RKASTIQNID YANRSLKLPD GAVVFSLIQP
     TGKFHLGNYL GAVRVWTELS EDAPAGGKCI FGTADLHAIT IPKPDGNAFR QMRHEAIASL
     LAVGIDPTKS ILFHQSQVPE HAELCWYLST LTSMGALNRM TQWKTKANIK DTSSEKVGAV
     KLGLFTYPVL QAADVLLYKS THIPVGEDQV QQLELTRQLA QAFNSTYKTR YFREPTTLLT
     PTRKVLSLQN PLKKMSKSDA NQNSCICVTD EPDAIRRKIR SAVTDSIGHE FKYDPEGRPG
     VSNLINIVAG IQKKTIAAVE ADIAGFKDHA TFKNYVTDIL VAELRGPREE FARYMNDKSY
     IYEVERNGAE RAGAIAAKTL AEVRAIMGY
//

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