ID   ABCA_ASPFM              Reviewed;        1452 AA.
AC   Q8X170;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=ABC multidrug transporter A {ECO:0000303|PubMed:12172968};
GN   Name=abcA {ECO:0000303|PubMed:12172968};
OS   Neosartorya fumigata (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=746128;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, AND FUNCTION.
RC   STRAIN=ATCC46645;
RX   PubMed=12172968; DOI=10.1007/s00294-002-0313-z;
RA   Langfelder K., Gattung S., Brakhage A.A.;
RT   "A novel method used to delete a new Aspergillus fumigatus ABC transporter-
RT   encoding gene.";
RL   Curr. Genet. 41:268-274(2002).
CC   -!- FUNCTION: ABC transporter that seems not to be involved in the efflux
CC       of toxic substances, at least not the classical compounds such as
CC       itraconazole, amphotericin B, voriconazole, posaconazole, ravuconazole,
CC       or echinocandins. {ECO:0000269|PubMed:12172968}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Does not lead to growth defects or changes in
CC       developmental patterns and does not affect sensitivity to itraconazole,
CC       amphotericin B, voriconazole, posaconazole, ravuconazole, or
CC       echinocandins. {ECO:0000269|PubMed:12172968}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC       PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
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DR   EMBL; AJ417501; CAD10327.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8X170; -.
DR   SMR; Q8X170; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IEA:InterPro.
DR   CDD; cd03233; ABCG_PDR_domain1; 1.
DR   CDD; cd03232; ABCG_PDR_domain2; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013525; ABC_2_trans.
DR   InterPro; IPR029481; ABC_trans_N.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR034001; ABCG_PDR_1.
DR   InterPro; IPR034003; ABCG_PDR_2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010929; PDR_CDR_ABC.
DR   Pfam; PF01061; ABC2_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF14510; ABC_trans_N; 1.
DR   Pfam; PF06422; PDR_CDR; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Glycoprotein; Membrane; Nucleotide-binding; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1452
FT                   /note="ABC multidrug transporter A"
FT                   /id="PRO_0000445095"
FT   TRANSMEM        474..494
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        508..528
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        554..574
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        583..603
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        616..636
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        725..745
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1153..1173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1183..1203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1223..1243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1271..1291
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1297..1317
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1418..1438
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          110..363
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          802..1044
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         838..845
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CARBOHYD        2
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        10
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        228
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        287
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        311
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1350
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1365
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1391
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   1452 AA;  163156 MW;  4680775E75A730BA CRC64;
     MNESHEAGKN SSTNVEEREE EVLRLARQFT EQSSYSTAGQ TPFAAEAGSA LDPNGERFNA
     RAWCKAMLQM HIGDKEAHPL RTLGVAFSNL NVHGFGSDTD YQKSVGNVWL KTLSLARIAF
     GQKQRKVDIL QNLEGLVEAG EMLVVLGPPG SGCSTFLKTI AGETYGFHVD KNSNINFQGI
     AKQMAHEFRG EAIYTAEVDV HFPKLTVGDT LYFAARARTP RHIPGGVNAT QYAGHMRDVI
     MAMFGISHTK NTIVGNDFIR GVSGGERKRV SIAEACLSNA PLQCWDNSTR GLDSANAIEF
     CKTLRMQADI NGTTACVSLY QAPQAAYDYF DKVLVLYEGR EIYFGPTSMA KHYFLQMGFV
     CPDRQTDADF LTSMTSHLER VVQPGYEDRV PRTPDEFAAR WKASPQRAQL MQHIKSYNAK
     FALDGEYLDK FKQSRRAQQA KAQRVSSPYT LSYVQQVKLC LWRGYQRLKA DPSVTISSLF
     GNTIISLVIA SIFYNLKADT STFFQRGALL FFAVLMNALG CGLEMLTLYA QRGIIEKHSR
     YALYHPSAEA FSSMIMDLPY KILNAITSNI VLYFMTNLRR APGAFFFFVF TSFILTLTMS
     MFFRSMASLS RSLVQVLPFS AVLLLGLSMY TGFAIPTGYM LGWARWIAYI NPISYGFESL
     MINEFHNRDF PCMDYVPSGP GYTDVGLNNR VCSTVRSVPG QAFVNGNAYI ESAYSYTASH
     KWRNIGVIFA YMFLLGAVYL VATDFITEKK PKGEILVFPR GHKALKKGKS DEDLEGGGGR
     SATVEKIGSD GLAMIERQTA IFQWKDVCFD IKIGKENCRI LDHVDGWVKP GILTALMGVS
     GAGKTTLLDV LATRTTMGII SGEMLVDGQP RDESFQRKTG YAQQQDLHLS TATVREALEF
     SALLRQSAHV PRQEKIDYVT EVIKLLDMTE YADAVIGVPG EGLNVEQRKR LTIGVELAAR
     PQLLLFLDEP TSGLDSQTSW AILDLLDKLK KNGQAILCTI HQPSAMLFQR FDRLLFLQAG
     GRTVYFGEIG QNSQILIDYF VRNGAPPCPP DANPAEWMLD VIGAAPGSHT SINWFETWRR
     SPEYARVQEH LAELKHERRH QTNLFRTTSG QKREDKDSYR EFAAPFWAQL YQVQVRVFQQ
     IWRSPTYINS KTALCVLSAL FVGFSLFHTP NTIQGLQNQM FGIFMLLTLF GQLIQQIMPH
     FVAQRALYEV RDRPAKTYSW KAFLIANIVV ELPWNSLMSV LMFLCWYYPI GLYRNAEPTD
     AVHLRGTQMW LMIWTFLLFS STFAHFMIAA FDAAENAGNL GNLLFLLCLL FCGVLATPDQ
     LPRFWIFMYR VSPFTYLVSG MLSVGISNTN VTCADNEYLR FDPVNGTCGE YMGSYMSNLG
     GYLADEMATA NCSFCPIKET NVFLGRVSSS YSDIWRNFGL MWVFIVFNIF AACSLYWWVR
     VPRDKKPVAK AE