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FSQA_ASPFU
ID   FSQA_ASPFU              Reviewed;         525 AA.
AC   Q4WD42;
DT   15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=C6 finger transcription factor fsqA {ECO:0000303|PubMed:27065235};
DE   AltName: Full=Fumipyrrole biosynthesis protein R {ECO:0000303|PubMed:25582336};
DE   AltName: Full=Fumisoquins biosynthesis protein A {ECO:0000303|PubMed:27065235};
GN   Name=fsqA {ECO:0000303|PubMed:27065235};
GN   Synonyms=fmpR {ECO:0000303|PubMed:25582336}; ORFNames=AFUA_6G03430;
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   INDUCTION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=25582336; DOI=10.1111/mmi.12926;
RA   Macheleidt J., Scherlach K., Neuwirth T., Schmidt-Heck W., Strassburger M.,
RA   Spraker J., Baccile J.A., Schroeder F.C., Keller N.P., Hertweck C.,
RA   Heinekamp T., Brakhage A.A.;
RT   "Transcriptome analysis of cyclic AMP-dependent protein kinase A-regulated
RT   genes reveals the production of the novel natural compound fumipyrrole by
RT   Aspergillus fumigatus.";
RL   Mol. Microbiol. 96:148-162(2015).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=27065235; DOI=10.1038/nchembio.2061;
RA   Baccile J.A., Spraker J.E., Le H.H., Brandenburger E., Gomez C., Bok J.W.,
RA   Macheleidt J., Brakhage A.A., Hoffmeister D., Keller N.P., Schroeder F.C.;
RT   "Plant-like biosynthesis of isoquinoline alkaloids in Aspergillus
RT   fumigatus.";
RL   Nat. Chem. Biol. 12:419-424(2016).
CC   -!- FUNCTION: Transcription factor that regulates the expression of the
CC       gene cluster that mediates the biosynthesis of the isoquinoline
CC       alkaloids fumisoquin A, fumisoquin B and fumisoquin C; as well as small
CC       amounts of fumipyrrole as a shunt metabolite (PubMed:25582336,
CC       PubMed:27065235). The products of the cluster lead to a brown
CC       coloration and are important for growth and conidiation
CC       (PubMed:25582336). {ECO:0000269|PubMed:25582336,
CC       ECO:0000269|PubMed:27065235}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC   -!- INDUCTION: Expression is induced by the cAMP-dependent protein kinase A
CC       signaling pathway (PubMed:25582336). {ECO:0000269|PubMed:25582336}.
CC   -!- DISRUPTION PHENOTYPE: Leads to reduced growth and sporulation, but does
CC       not affect virulence in infected mice (PubMed:25582336). Impairs the
CC       production of isoquinolines (PubMed:27065235).
CC       {ECO:0000269|PubMed:25582336, ECO:0000269|PubMed:27065235}.
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DR   EMBL; AAHF01000012; EAL85696.1; -; Genomic_DNA.
DR   RefSeq; XP_747734.1; XM_742641.1.
DR   AlphaFoldDB; Q4WD42; -.
DR   STRING; 746128.CADAFUBP00009220; -.
DR   EnsemblFungi; EAL85696; EAL85696; AFUA_6G03430.
DR   GeneID; 3505181; -.
DR   KEGG; afm:AFUA_6G03430; -.
DR   VEuPathDB; FungiDB:Afu6g03430; -.
DR   eggNOG; ENOG502SYRD; Eukaryota.
DR   HOGENOM; CLU_605645_0_0_1; -.
DR   InParanoid; Q4WD42; -.
DR   OMA; YILQAYE; -.
DR   OrthoDB; 1576792at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
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:0008152; P:metabolic process; IEA:UniProt.
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   SUPFAM; SSF57701; SSF57701; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..525
FT                   /note="C6 finger transcription factor fsqA"
FT                   /id="PRO_0000438868"
FT   DNA_BIND        12..53
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          80..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          327..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..346
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   525 AA;  58058 MW;  B13101FE73A0C7F0 CRC64;
     MMDDKHGRYG ACDRCRGQKL RCVGAGKPIP NSSSRLLRNE IPCDRCRRAK VECYSVRPAP
     RRAASNVKEQ MIATQAASER SSSLAYHTSG PVVSPPNSLV TAASKPHPNS LSFNHPRSDA
     VAAPGGLQTR RQSRDTDSLG DMPSMPHEWM AYLHDHKMDD RQGLGMETPP LIESDLNLSR
     DPAMDSMHEH NMMMELIHQD HQEEWNSGPP ELEAYPDPIV PPNPAPLKAR KLTSPDCDDY
     PYGHTRRSSH TPTQPPEPAG RSCIQELAQF NEMLLRDKCS LEDTSARRGY KDSWLSIGRT
     LHHCQQFFSI LKRIKYSRPD SQLSADRARS QWSSLPEGTS LADGAPTDSP QARRSLARGA
     TPCSSSLARS SSTSSAASTS YLGLSTLLSI LFCYTYILQA YEDILTSILH AVTRPTPTIP
     PTLSGLRIDG FQLDGHHTLQ LECLLHVSYN LLEKIENILF GSAGPEELSN PVKYGILGDK
     LSAGLIDALF EHNETNGLLH CQGKREVAAK RLIREIQAAL KQLDL
 
 
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