(data stored in ACNUC7421 zone)

SWISSPROT: Q4WDN3_ASPFU

ID   Q4WDN3_ASPFU            Unreviewed;       391 AA.
AC   Q4WDN3;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 100.
DE   SubName: Full=Tryptophanyl-tRNA synthetase, putative {ECO:0000313|EMBL:EAL85505.1};
DE            EC=6.1.1.2 {ECO:0000313|EMBL:EAL85505.1};
GN   ORFNames=AFUA_6G05340 {ECO:0000313|EMBL:EAL85505.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL85505.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL85505.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|RuleBase:RU363036}.
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:EAL85505.1}.
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DR   EMBL; AAHF01000012; EAL85505.1; -; Genomic_DNA.
DR   RefSeq; XP_747543.1; XM_742450.1.
DR   STRING; 746128.CADAFUBP00009031; -.
DR   EnsemblFungi; EAL85505; EAL85505; AFUA_6G05340.
DR   GeneID; 3505188; -.
DR   KEGG; afm:AFUA_6G05340; -.
DR   EuPathDB; FungiDB:Afu6g05340; -.
DR   HOGENOM; HOG000059940; -.
DR   InParanoid; Q4WDN3; -.
DR   KO; K01867; -.
DR   OMA; GWGQFKP; -.
DR   OrthoDB; 1298726at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
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   HAMAP; MF_00140_B; Trp_tRNA_synth_B; 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   InterPro; IPR024109; Trp-tRNA-ligase_bac-type.
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; Q4WDN3.
DR   SWISS-2DPAGE; Q4WDN3.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|RuleBase:RU363036,
KW   ECO:0000313|EMBL:EAL85505.1}; ATP-binding {ECO:0000256|RuleBase:RU363036};
KW   Ligase {ECO:0000256|RuleBase:RU363036, ECO:0000313|EMBL:EAL85505.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU363036};
KW   Protein biosynthesis {ECO:0000256|RuleBase:RU363036};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530}.
SQ   SEQUENCE   391 AA;  43809 MW;  EEA46485D65A43A8 CRC64;
     MQRSNCHSSQ VVRILRGARR PRIRAGKPVT SREVFRRWSS SETAKSSSAA NQTIFSGIQP
     TGVPHLGNYL GALREWVRLQ NAAKEGTRLF FSIVDLHALT VPQDASQLRN WRKETFATLI
     AVGLDPNRST IFYQSAVHAH AELFWILCTI ASMGYLSRMT QWKSKLQLPD NANLEDSTAR
     SRLRLGLFSY PVLQAADILV HRATHVPVGD DQRQHLEFSR NTANSFNHVY GPIFPSPEAI
     ISPAKRVMSL KEPTLKMSKS HADRRSRIIL TDSPAEISKK INAALTDSEL TITYDPVRRP
     GVANLIEILS HFDGRTCDEI AMEYRSASLR ALKEHLARTL SNHLEPIREK YLSLVGDQTD
     YLDSIAEQGS EAARANAELT MEQVKVAMGL I
//

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