FSQE_ASPFU
ID FSQE_ASPFU Reviewed; 1285 AA.
AC Q4WD46;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=ABC-type transporter fsqE {ECO:0000303|PubMed:27065235};
DE AltName: Full=Fumipyrrole biosynthesis protein D {ECO:0000303|PubMed:25582336};
DE AltName: Full=Fumisoquins biosynthesis protein E {ECO:0000303|PubMed:27065235};
GN Name=fsqE {ECO:0000303|PubMed:27065235};
GN Synonyms=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;
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 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).
RN [3]
RP FUNCTION.
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: ABC-type transporter; part of the gene cluster that mediates
CC the biosynthesis of the isoquinoline alkaloids fumisoquin A, fumisoquin
CC B and fumisoquin C; as well as small amounts of fumipyrrole as a shunt
CC metabolite (PubMed:25582336, PubMed:27065235). The products of the
CC cluster lead to a brown coloration and are important for growth and
CC conidiation (PubMed:25582336). FsqE possibly plays a role of self-
CC protection (Probable). {ECO:0000269|PubMed:25582336,
CC ECO:0000269|PubMed:27065235, ECO:0000305|PubMed:27065235}.
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 fumisoquins
CC biosynthesis specific transcription factor fsqA (PubMed:25582336).
CC {ECO:0000269|PubMed:25582336, ECO:0000269|PubMed:27065235}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
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DR EMBL; AAHF01000012; EAL85692.1; -; Genomic_DNA.
DR RefSeq; XP_747730.1; XM_742637.1.
DR AlphaFoldDB; Q4WD46; -.
DR SMR; Q4WD46; -.
DR STRING; 746128.CADAFUBP00009216; -.
DR EnsemblFungi; EAL85692; EAL85692; AFUA_6G03470.
DR GeneID; 3505177; -.
DR KEGG; afm:AFUA_6G03470; -.
DR VEuPathDB; FungiDB:Afu6g03470; -.
DR eggNOG; KOG0055; Eukaryota.
DR HOGENOM; CLU_000604_17_2_1; -.
DR InParanoid; Q4WD46; -.
DR OMA; FIIACSY; -.
DR OrthoDB; 186078at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 2.
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;
KW ATP-binding; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1285
FT /note="ABC-type transporter fsqE"
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 REGION 627..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 413..420
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1078..1085
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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
