(data stored in SCRATCH zone)

SWISSPROT: Q4WDI9_ASPFU

ID   Q4WDI9_ASPFU            Unreviewed;       988 AA.
AC   Q4WDI9;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 2.
DT   11-DEC-2019, entry version 106.
DE   SubName: Full=Leucyl-tRNA synthetase {ECO:0000313|EMBL:EAL85549.2};
DE            EC=6.1.1.4 {ECO:0000313|EMBL:EAL85549.2};
GN   ORFNames=AFUA_6G04910 {ECO:0000313|EMBL:EAL85549.2};
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:EAL85549.2, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL85549.2, 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:RU363039}.
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:EAL85549.2}.
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DR   EMBL; AAHF01000012; EAL85549.2; -; Genomic_DNA.
DR   RefSeq; XP_747587.2; XM_742494.2.
DR   STRING; 746128.CADAFUBP00009075; -.
DR   EnsemblFungi; EAL85549; EAL85549; AFUA_6G04910.
DR   GeneID; 3505135; -.
DR   KEGG; afm:AFUA_6G04910; -.
DR   EuPathDB; FungiDB:Afu6g04910; -.
DR   HOGENOM; HOG000200747; -.
DR   InParanoid; Q4WDI9; -.
DR   KO; K01869; -.
DR   OMA; YANIETQ; -.
DR   OrthoDB; 375759at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
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: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   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 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; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
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; PF08264; Anticodon_1; 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; Q4WDI9.
DR   SWISS-2DPAGE; Q4WDI9.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|RuleBase:RU363039,
KW   ECO:0000313|EMBL:EAL85549.2}; ATP-binding {ECO:0000256|RuleBase:RU363039};
KW   Ligase {ECO:0000256|RuleBase:RU363039, ECO:0000313|EMBL:EAL85549.2};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU363039};
KW   Protein biosynthesis {ECO:0000256|RuleBase:RU363039};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530}.
FT   DOMAIN          82..219
FT                   /note="tRNA-synt_1g"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          269..472
FT                   /note="tRNA-synt_1_2"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          486..650
FT                   /note="tRNA-synt_1"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          794..929
FT                   /note="Anticodon_1"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   988 AA;  110727 MW;  BE90B0E765DB3E1D CRC64;
     MYSISRLRCR PTVFIQGRWR CAVRPVLSNF MRLATTSATS ISRKLDLLAI DRKWQEKWHA
     EGPRSLPDDA NKENRGDRPK SYILSMFPYP SGTLHMGHLR VYTISDVLAR FYRMRGHEVL
     HPMGWDAFGL PAENAAIERG IDPAEWTKQN IAKMKEQLRS ISTSFDWDRE LATCSPEFYE
     HTQRIFLMLY RKGLAYQAEA LVNYDPVDKT VLANEQVDSN GFSWRSGAKV EKLKLKQWFF
     RITDFKEMLL KDLDSLTGAW PERVLTMQRN WLGKSYGAKI KFPVAVDASG DANLHVNVFT
     TRPDTLYGVE YLALSLNHPI VLEAAEKDAA LRKFLDEAAS LPPDSKVGYK LANVTASNPL
     HIIDKESPHI ARRLPIFVAP YVLSDYGEGA VIGVPGHDSR DLAFFKENTN SDSIPVVIEP
     EHLSNPNNDS TGTVTRPNDM KAFTQEGILT SRCWKYQGLH SREAKKQIVT DLKGVGHGDF
     VEQWRLRDWL ISRQRYWGAP IPIIHCESCG PVPVPEDQLP VRLPKIEGDW LKGKKGNPLE
     SSQDWVNTKC PSCSGPAKRD TDTMDTFVDS SWYYLRFPDA HNKEQPFSPS TARQVDIYIG
     GVEHAILHLL YARFIYKFLS QTELFPEIAR SGDGLGPSEP FKTVLTQGMV HGKTYTEPST
     GRFLLPSEVD LSNPNKPLIK GTQVAPNISF EKMSKSKHNG VDPTSCALQY GADATRAHVL
     FSAPVSEVLE WDDTKIVGIE RWFGRLWKLV LDAKQSLASA SFTVSQNDLQ KSPYATSKLP
     SLLQGLGDSD AEGLLHTHQT IVSVTNCIEN NPYGLNTVIS DLTKLTNTLT SSNPTSPQVL
     YLCVSSLVRL LAPVAPALAS ECWEVLNDTL IDQNANTGAR VPDIFDCAWP SPLLTSEQAD
     VLSARGGQIV AVQINGKLRF TVTIPRRLSP TTSADSSDSG AVTDEQDWII SRILETDEGR
     VWLREKNDWE KRRRVVVVKG GKLVNIVF
//

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