(data stored in SCRATCH zone)

SWISSPROT: FMPB_ASPFU

ID   FMPB_ASPFU              Reviewed;         366 AA.
AC   Q4WD44;
DT   15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 65.
DE   RecName: Full=N-methyltransferase fmpB {ECO:0000305};
DE            EC=2.1.1.- {ECO:0000305};
DE   AltName: Full=Fumipyrrole biosynthesis protein B {ECO:0000303|PubMed:25582336};
DE   Flags: Precursor;
GN   Name=fmpB {ECO:0000303|PubMed:25582336}; ORFNames=AFUA_6G03450;
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;
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   FUNCTION, AND INDUCTION.
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).
CC   -!- FUNCTION: Methyltransferase; part of the gene cluster that mediates the
CC       biosynthesis of fumipyrrole, a brown pigment that is involved in growth
CC       and conidiation (PubMed:25582336). {ECO:0000269|PubMed:25582336}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:25582336}.
CC   -!- INDUCTION: Expression is positively regulated by the fumipyrrole
CC       biosynthesis specific transcription factor fmpR (PubMed:25582336).
CC       {ECO:0000269|PubMed:25582336}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
DR   EMBL; AAHF01000012; EAL85694.1; -; Genomic_DNA.
DR   RefSeq; XP_747732.1; XM_742639.1.
DR   SMR; Q4WD44; -.
DR   STRING; 746128.CADAFUBP00009218; -.
DR   EnsemblFungi; EAL85694; EAL85694; AFUA_6G03450.
DR   GeneID; 3505179; -.
DR   KEGG; afm:AFUA_6G03450; -.
DR   EuPathDB; FungiDB:Afu6g03450; -.
DR   HOGENOM; HOG000217011; -.
DR   InParanoid; Q4WD44; -.
DR   OMA; KYLWDET; -.
DR   OrthoDB; 762504at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   Proteomes; UP000002530; Unassembled WGS sequence.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   InterPro; IPR019257; MeTrfase_dom.
DR   InterPro; IPR017804; MeTrfase_EgtD-like.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR017805; SAM_MeTrfase_EasF-type_put.
DR   Pfam; PF10017; Methyltransf_33; 1.
DR   PIRSF; PIRSF018005; UCP018005; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR03439; methyl_EasF; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; Q4WD44.
DR   SWISS-2DPAGE; Q4WD44.
KW   Glycoprotein; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Signal; Transferase.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..366
FT                   /note="N-methyltransferase fmpB"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000438870"
FT   CARBOHYD        270
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   366 AA;  40933 MW;  3B3A6F8007143AF5 CRC64;
     MSSNVQDIRG WPPPFANAAY QPDASSRRAR YGGLQVHNLR QATTANSLVP SIIQGLRAED
     RELPSLLLWD DQGLSLFNAI LDSPEYYLAN KEWALLHNEV HNIVASISSG DRLVELGAGN
     MKKTALILHT LQSQRKYIHY IACDVDRVAL QRGLRNLQAI FPASTSSIKI QGLVATYEDC
     AAWLQRNPGS GHTSLMWLGN SLANFPPPEA SEYIRSFLST GASLILALDG CQDHEQIARA
     YEGPSNQKFV LNGLRHANDV LGTDAFDVRN WSFLGRWNPE LWMHESFYAA KRDLTLKIGR
     ETFVFRKGET IRSIRSGKWP KPKVVDICRE AGGDVVDWWM NPDESYGKST TLMGYLARVL
     IDSVSD
//

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