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FUMR_ASPFU
ID   FUMR_ASPFU              Reviewed;         622 AA.
AC   Q4WAY8;
DT   07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=C6 finger transcription factor fumR {ECO:0000303|PubMed:24116213};
DE   AltName: Full=Fumagillin gene cluster regulator {ECO:0000303|PubMed:24116213};
GN   Name=fumR {ECO:0000303|PubMed:24116213};
GN   Synonyms=fapR {ECO:0000303|PubMed:24082142}; ORFNames=AFUA_8G00420;
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;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
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.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
RN   [2]
RP   BIOTECHNOLOGY.
RX   PubMed=14913169; DOI=10.1126/science.115.2977.71;
RA   Killough J.H., Magill G.B., Smith R.C.;
RT   "The treatment of amebiasis with fumagillin.";
RL   Science 115:71-72(1952).
RN   [3]
RP   BIOTECHNOLOGY.
RX   PubMed=9177176; DOI=10.1073/pnas.94.12.6099;
RA   Sin N., Meng L., Wang M.Q., Wen J.J., Bornmann W.G., Crews C.M.;
RT   "The anti-angiogenic agent fumagillin covalently binds and inhibits the
RT   methionine aminopeptidase, MetAP-2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:6099-6103(1997).
RN   [4]
RP   BIOTECHNOLOGY.
RX   PubMed=12075057; DOI=10.1056/nejmoa012924;
RG   Agence Nationale de Recherches sur le SIDA 090 Study Group;
RA   Molina J.M., Tourneur M., Sarfati C., Chevret S., de Gouvello A.,
RA   Gobert J.G., Balkan S., Derouin F.;
RT   "Fumagillin treatment of intestinal microsporidiosis.";
RL   N. Engl. J. Med. 346:1963-1969(2002).
RN   [5]
RP   BIOTECHNOLOGY.
RX   PubMed=18209961; DOI=10.1007/s00011-007-7075-5;
RA   Lazarus D.D., Doyle E.G., Bernier S.G., Rogers A.B., Labenski M.T.,
RA   Wakefield J.D., Karp R.M., Clark E.J., Lorusso J., Hoyt J.G.,
RA   Thompson C.D., Hannig G., Westlin W.F.;
RT   "An inhibitor of methionine aminopeptidase type-2, PPI-2458, ameliorates
RT   the pathophysiological disease processes of rheumatoid arthritis.";
RL   Inflamm. Res. 57:18-27(2008).
RN   [6]
RP   IDENTIFICATION, AND INDUCTION.
RX   PubMed=24082142; DOI=10.1073/pnas.1313258110;
RA   Wiemann P., Guo C.J., Palmer J.M., Sekonyela R., Wang C.C., Keller N.P.;
RT   "Prototype of an intertwined secondary-metabolite supercluster.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:17065-17070(2013).
RN   [7]
RP   INDUCTION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=24116213; DOI=10.1371/journal.pone.0077147;
RA   Dhingra S., Lind A.L., Lin H.C., Tang Y., Rokas A., Calvo A.M.;
RT   "The fumagillin gene cluster, an example of hundreds of genes under veA
RT   control in Aspergillus fumigatus.";
RL   PLoS ONE 8:E77147-E77147(2013).
CC   -!- FUNCTION: Transcription factor that regulates the expression of the
CC       gene clusters that mediate the biosynthesis of pseurotin and fumagillin
CC       (PubMed:24116213). {ECO:0000269|PubMed:24116213}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC   -!- INDUCTION: Expression is under the control of the developmental and
CC       secondary metabolism regulators laeA and veA (PubMed:24082142,
CC       PubMed:24116213). {ECO:0000269|PubMed:24082142,
CC       ECO:0000269|PubMed:24116213}.
CC   -!- DISRUPTION PHENOTYPE: Results in silencing of the fumagillin gene
CC       cluster and elimination of fumagillin biosynthesis (PubMed:24116213).
CC       {ECO:0000269|PubMed:24116213}.
CC   -!- BIOTECHNOLOGY: Fumagillin and its derivatives have been intensely
CC       studied for their potential use in the treatment of amebiasis,
CC       microsporidiosis and rheumatoid arthritis (PubMed:14913169,
CC       PubMed:12075057, PubMed:18209961). They have also interesting
CC       antiangiogenic properties by the irreversible inhibition of human type
CC       2 methionine aminopeptidase (METAP2) (PubMed:9177176).
CC       {ECO:0000269|PubMed:12075057, ECO:0000269|PubMed:14913169,
CC       ECO:0000269|PubMed:18209961, ECO:0000269|PubMed:9177176}.
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DR   EMBL; AAHF01000014; EAL85124.1; -; Genomic_DNA.
DR   RefSeq; XP_747162.1; XM_742069.1.
DR   AlphaFoldDB; Q4WAY8; -.
DR   SMR; Q4WAY8; -.
DR   STRING; 746128.CADAFUBP00008393; -.
DR   EnsemblFungi; EAL85124; EAL85124; AFUA_8G00420.
DR   GeneID; 3504498; -.
DR   KEGG; afm:AFUA_8G00420; -.
DR   VEuPathDB; FungiDB:Afu8g00420; -.
DR   eggNOG; ENOG502SKZ7; Eukaryota.
DR   HOGENOM; CLU_034865_0_0_1; -.
DR   InParanoid; Q4WAY8; -.
DR   OMA; SDPGNAM; -.
DR   OrthoDB; 1030413at2759; -.
DR   Proteomes; UP000002530; Chromosome 8.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:1902086; P:fumagillin biosynthetic process; IMP:AspGD.
DR   GO; GO:1902092; P:positive regulation of fumagillin biosynthetic process; IMP:AspGD.
DR   GO; GO:1900851; P:positive regulation of pseurotin A biosynthetic process; IMP:AspGD.
DR   GO; GO:1900790; P:pseurotin A biosynthetic process; IMP:AspGD.
DR   CDD; cd00067; GAL4; 1.
DR   Gene3D; 4.10.240.10; -; 1.
DR   InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR   InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR   Pfam; PF00172; Zn_clus; 1.
DR   SUPFAM; SSF57701; SSF57701; 1.
DR   PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..622
FT                   /note="C6 finger transcription factor fumR"
FT                   /id="PRO_0000437043"
FT   DNA_BIND        94..123
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          127..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          206..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          299..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          556..585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..247
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..317
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   622 AA;  68145 MW;  1B6D17689337EBAF CRC64;
     MDVNRKRMVR MASAQRSEML VRLSGKAKRW TVGGGGEVET HTFHTFCAGQ KSYKSVVRRQ
     RPRIARRDSR PSHPIANRGM NMLVHDLGFS HRACDRCHGQ KLRCRRENNS DTCVRCARAG
     VRCTPRPMRL RSRAQSTKNT QQQQSQSPAN GGSTQQLHVN QEQGPNDTND EHSDHFEYLP
     TSLLDMPTDL NMGMDPSSLQ VDIHPALTAP YGPEGSVHTS QPSGPQAPSH LRTAEQAGQT
     RWSDAPNLDT SDELYDFSLP ATMRSSFPAT YHRHRASLAR NMSPQPAHQQ GRDDMMVDFD
     QAEGNPRGSD GKDSRADSGY GNELSPSDLL RSPYGDAPDS DSELQPRGNS QDQGEQSNSI
     LDTRHQNMTS WIRRLSDTNV QLHQHMQSIP LVGTGKKTRG SGAGTSLSPM ELPVDSTFKL
     SSQYTGLLTS ICARLQACRS CNDSQALAQL ALDQPSQLLV LSSYMCLLAS YDRILQHIEA
     WLKVRLKMGV RGSAMTLDDD ESSSCFPTQL PSLAVGSFEV PKTSSIQSLV LTCIMETNVM
     HMHSLISEIM RPVSHPATGS ASKTAASGPP AAEKRPGNGA ADAGDGLSTV AKVTLQAIEA
     NEDSTLRLVH TVSRLALQRV ML
 
 
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