(data stored in SCRATCH zone)

SWISSPROT: Q4WDH1_ASPFU

ID   Q4WDH1_ASPFU            Unreviewed;       817 AA.
AC   Q4WDH1;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 94.
DE   SubName: Full=Bifunctional purine biosynthetic protein Ade1, putative {ECO:0000313|EMBL:EAL85567.1};
DE            EC=6.3.4.13 {ECO:0000313|EMBL:EAL85567.1};
GN   ORFNames=AFUA_6G04730 {ECO:0000313|EMBL:EAL85567.1};
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:EAL85567.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL85567.1, 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   -!- 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:EAL85567.1}.
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DR   EMBL; AAHF01000012; EAL85567.1; -; Genomic_DNA.
DR   RefSeq; XP_747605.1; XM_742512.1.
DR   SMR; Q4WDH1; -.
DR   STRING; 746128.CADAFUBP00009093; -.
DR   EnsemblFungi; EAL85567; EAL85567; AFUA_6G04730.
DR   GeneID; 3505054; -.
DR   KEGG; afm:AFUA_6G04730; -.
DR   EuPathDB; FungiDB:Afu6g04730; -.
DR   HOGENOM; HOG000030315; -.
DR   InParanoid; Q4WDH1; -.
DR   KO; K11788; -.
DR   OMA; IPRIFSW; -.
DR   OrthoDB; 105366at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IBA:GO_Central.
DR   GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IBA:GO_Central.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:InterPro.
DR   GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR   CDD; cd02196; PurM; 1.
DR   Gene3D; 3.30.1330.10; -; 1.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.90.600.10; -; 1.
DR   Gene3D; 3.90.650.10; -; 1.
DR   HAMAP; MF_00741; AIRS; 1.
DR   HAMAP; MF_00138; GARS; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp.
DR   InterPro; IPR000115; PRibGlycinamide_synth.
DR   InterPro; IPR020560; PRibGlycinamide_synth_C-dom.
DR   InterPro; IPR037123; PRibGlycinamide_synth_C_sf.
DR   InterPro; IPR020562; PRibGlycinamide_synth_N.
DR   InterPro; IPR010918; PurM-like_C_dom.
DR   InterPro; IPR036676; PurM-like_C_sf.
DR   InterPro; IPR016188; PurM-like_N.
DR   InterPro; IPR036921; PurM-like_N_sf.
DR   InterPro; IPR004733; PurM_cligase.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   PANTHER; PTHR10520; PTHR10520; 1.
DR   Pfam; PF00586; AIRS; 1.
DR   Pfam; PF02769; AIRS_C; 1.
DR   Pfam; PF01071; GARS_A; 1.
DR   Pfam; PF02843; GARS_C; 1.
DR   Pfam; PF02844; GARS_N; 1.
DR   SMART; SM01210; GARS_C; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   SUPFAM; SSF55326; SSF55326; 1.
DR   SUPFAM; SSF56042; SSF56042; 1.
DR   TIGRFAMs; TIGR00877; purD; 1.
DR   TIGRFAMs; TIGR00878; purM; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4WDH1.
DR   SWISS-2DPAGE; Q4WDH1.
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Ligase {ECO:0000313|EMBL:EAL85567.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530}.
FT   DOMAIN          116..324
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   817 AA;  86419 MW;  08F230524C838AA7 CRC64;
     MAQEQLRVLV VGNGGREHAY AWKLSQSPLV DVVYVAPGNG GTAQGASSKI TNANVKGDDY
     PALVEFAQKN GVNLVVPGPE APLVDGIQGY FQAVGIRCFG PSKAAARMEG SKTFSKDFMK
     RHNIPTAAYQ NFYEYEPARQ YLDSVNHNVV IKADGLAAGK GVIIPQTKEE AHKALREMML
     DHHFGDAGNE VVIEEYLEGD ELSILTFSDG YTIRSLPPAQ DHKRIFDGDQ GPNTGGMGCY
     APTPISSKEV LEEIDRTIVQ PTIDGMRKDG FPFVGILFTG LMMTKDGPKV LEYNVRGGDP
     ETQTLLPLLS ADTDLAQIMV ACTEHWLDGV DIKIEPKFST TVIAVAGGYP GSYAKGKAIT
     LDPAPEDTLI FHAGTKLFGN ELQTNGGRVI ASTATASTLE EALRKSYAGI SAIHFEDMFY
     RKDIAHRAFR QRDAAASQQQ QSLTYASAGV SIDAGNDLVN KIKSCVARTK RPGTDAVIGG
     FGGLFSLAAA NSAYHPESPT LIGAIDGVGT KLKIAHTVGV HNTVGIDLVA MNVNDLVVQG
     AEPLFFLDCY SCGKLDVETA AAFVAGVADG CVQAGCALIG GETAEMPGLF VDETYDAVGA
     AVGAINTTGK NAKSILPATS AMQAGDVLLA LASSGPHSNG YSLVRKIVER SGLSYDDPAP
     FTMPSSSSES LTLGRALLTP TRIYVKPILK ALSIPPSNSS SGSSAIKGLA HITGGGLVEN
     VPRMLPSTLS AHIDVSAWQL PPVFSWLKKT GNVTAPEMAR AFNCGVGMVI VVEKGSEAAV
     KELFEKEGEV VYQVGELKPR QDGEEGCVLG GLQTWDA
//

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