(data stored in ACNUC7421 zone)

SWISSPROT: FMPD_ASPFU

ID   FMPD_ASPFU              Reviewed;        1285 AA.
AC   Q4WD46;
DT   15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 109.
DE   RecName: Full=ABC transporter fmpD {ECO:0000303|PubMed:25582336};
DE   AltName: Full=Fumipyrrole biosynthesis protein D {ECO:0000303|PubMed:25582336};
GN   Name=fmpD {ECO:0000303|PubMed:25582336}; ORFNames=AFUA_6G03470;
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: ABC transporter; 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is positively regulated by the fumipyrrole
CC       biosynthesis specific transcription factor fmpR (PubMed:25582336).
CC       {ECO:0000269|PubMed:25582336}.
DR   EMBL; AAHF01000012; EAL85692.1; -; Genomic_DNA.
DR   RefSeq; XP_747730.1; XM_742637.1.
DR   SMR; Q4WD46; -.
DR   STRING; 746128.CADAFUBP00009216; -.
DR   EnsemblFungi; EAL85692; EAL85692; AFUA_6G03470.
DR   GeneID; 3505177; -.
DR   KEGG; afm:AFUA_6G03470; -.
DR   EuPathDB; FungiDB:Afu6g03470; -.
DR   InParanoid; Q4WD46; -.
DR   KO; K05658; -.
DR   OMA; GVFQAKM; -.
DR   OrthoDB; 186078at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   Proteomes; UP000002530; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   Gene3D; 1.20.1560.10; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00664; ABC_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF90123; SSF90123; 2.
DR   PROSITE; PS50929; ABC_TM1F; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   2: Evidence at transcript level;
DR   PRODOM; Q4WD46.
DR   SWISS-2DPAGE; Q4WD46.
KW   ATP-binding; Glycoprotein; Membrane; Nucleotide-binding;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1285
FT                   /note="ABC transporter fmpD"
FT                   /id="PRO_0000438872"
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        203..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        281..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        312..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        707..727
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        753..773
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        831..851
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        855..875
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        931..951
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        968..988
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          54..343
FT                   /note="ABC transmembrane type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          380..622
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          713..996
FT                   /note="ABC transmembrane type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          1043..1281
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   NP_BIND         413..420
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   NP_BIND         1078..1085
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CARBOHYD        467
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1037
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1138
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   1285 AA;  139635 MW;  8F5B46138F8B610B CRC64;
     MTPPQMVSQL DDARLDERQR AILDRQLHGL GGETKQRKNV FAYATVSDRI VLSVSSICAV
     LAGALNPLVP VIYGLLVSVY DGFAAGTVSA SELRSKTATF SLYYVYLSIG LFAFTYVATV
     GFYYTGERMA RALRTTYLAA ILRQNMAFFD LLGPGEITSR IMSDMGTVQE AVTSKLAVML
     TAIATFCAAF VVAFIMYWKT ALIISPFFVI MIVTETLGGA YMVRHHKRAM ELYSQAAGIA
     EEAIAAIKHV TAFGIQTLLS QRYLSVLEQA AKADRKAENM VAGMIAWMNA MPNLIYALAF
     WAGSIYLTRG QMSVAEVSAT TLAVTIGSFA IIRIAPSAQA LLSGIAITGE ILKSIARRSP
     QDPLVKEGDE PSTVVGDIVL DRVGLIYPSR DDVDILQDVS LRCAAMKKTA IVGSSGSGKS
     SILGLVERFY EPTSGTVLLD GRDIQSLNLR WLRRQIALVD QMPVLFNATI LENILYGCSD
     MVSQWSESEQ LDRVVQASKK ANAHDFISAL PDGYHTHVGE KGLQLSGGQR QRVAIARALI
     RDPKILLLDE ATSALDSKSE AMVQEALDAA AEHRTTIIVA HRLSTIQNAD HIIVLDHGKV
     VEEGTHHALV AQNGAYAALV QKQQIGDTHD HKAPDGARLS IEDDDDEDSR YGGNTEYVDE
     KDIRTEEVAL SSAAHDEGTQ RDSLKLSALQ TIAFIARLSK RDWKVLLFGL ANAILAGLTI
     PVQSVFFAKI LTVIGFPPPQ YPQLRSEVDF WSGLYVMLTG TTFLFWMGVE IALSYATQKL
     ARRVREVCFR SILVQDMAFF DVPGNSPSAL SSVLSKSTND LAGLGGPVMG GILTFLSTIL
     AGIVLALAIG WKLALVCTAT IPIVVACGWL RLQVLSTFDS KVRQSGIESA AYAGELVRTV
     RTVASLGLEE HALARYEGIL AKQAAKSLRS ILLASALYAA SASVVYLCAA LAFWYGGTLI
     ASHEYSTFQV YICFVSLISG SQIAGSIFTY APDASKAMHA SREIQDIMNL KPSINKVAPT
     GPPPAHEGTE KNQPQQNLSA CRVEFEHVSF TYPSRPTRRA LDNLHITVEP GQTLALVGQS
     GSGKSTCVSL LERFYDPDQG RILIDGQDIK LRDVDEYRRD ISLVSQETII FSGTIRDNIT
     VGLAGQEVSD DEILEACKQA NILEFVQSLP DGLSTLVGTG GSMLSGGQKQ RIAIARAFLR
     KPKILLLDEA TSALDSQSEA IVQEAMDAIR KDRTTIMVAH RLSTVQNADV ICVLQDGKLL
     EIGTHEQLLG KRGKYWEMVS MQSLH
//

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