(data stored in ACNUC7421 zone)

SWISSPROT: Q4WDL1_ASPFU

ID   Q4WDL1_ASPFU            Unreviewed;       412 AA.
AC   Q4WDL1;
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=Glycogen synthase kinase (Skp1), putative {ECO:0000313|EMBL:EAL85527.1};
DE            EC=2.7.1.- {ECO:0000313|EMBL:EAL85527.1};
GN   ORFNames=AFUA_6G05120 {ECO:0000313|EMBL:EAL85527.1};
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:EAL85527.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL85527.1, 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 protein kinase superfamily.
CC       {ECO:0000256|RuleBase:RU000304}.
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:EAL85527.1}.
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DR   EMBL; AAHF01000012; EAL85527.1; -; Genomic_DNA.
DR   RefSeq; XP_747565.1; XM_742472.1.
DR   STRING; 746128.CADAFUBP00009053; -.
DR   EnsemblFungi; EAL85527; EAL85527; AFUA_6G05120.
DR   GeneID; 3505041; -.
DR   KEGG; afm:AFUA_6G05120; -.
DR   EuPathDB; FungiDB:Afu6g05120; -.
DR   HOGENOM; HOG000233017; -.
DR   InParanoid; Q4WDL1; -.
DR   KO; K03083; -.
DR   OMA; MQYTQCK; -.
DR   OrthoDB; 990896at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IBA:GO_Central.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR   GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   CDD; cd14137; STKc_GSK3; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR039192; STKc_GSK3.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4WDL1.
DR   SWISS-2DPAGE; Q4WDL1.
KW   ATP-binding {ECO:0000256|RuleBase:RU000304};
KW   Kinase {ECO:0000313|EMBL:EAL85527.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304};
KW   Transferase {ECO:0000313|EMBL:EAL85527.1}.
FT   DOMAIN          53..336
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   412 AA;  47080 MW;  4BC55AAB0A111134 CRC64;
     MSQNRPGVFS NLRMGENITQ EPVELTALLS DHTEVVREKV QDGLTGETKE ISYSQCKIVG
     NGSFGVVFQT KMMPSGEDAA IKRVLQDKRF KNRELQIMRI VRHPNIVELK AFYYSNGERK
     DEVYLNLVLE YVPETVYRAS RYFNKLKTTM PMLEVKLYIY QLFRSLAYIH SQGICHRDIK
     PQNLLLDPST GILKLCDFGS AKILVENEPN VSYICSRYYR APELIFGATN YTTKIDVWST
     GCVMAELMLG QPLFPGESGI DQLVEIIKVL GTPTREQIRT MNPNYMEHKF PQIKPHPFNK
     VFRRAPHEAI DLISALLEYT PTQRLSAIEA MCHPFFDELR DPNTRLPDSR HPGGAARDLP
     NLFDFSRHEL SIAPALNSRL VPPHARAALE ARGLDIDNFT PLTKEEMMAR LD
//

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