ID A1C9U8_ASPCL Unreviewed; 1355 AA.
AC A1C9U8;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=ABC multidrug transporter Mdr1 {ECO:0000313|EMBL:EAW12516.1};
GN ORFNames=ACLA_009390 {ECO:0000313|EMBL:EAW12516.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW12516.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW12516.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Multidrug resistance exporter (TC 3.A.1.201) subfamily.
CC {ECO:0000256|ARBA:ARBA00007577}.
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DR EMBL; DS027049; EAW12516.1; -; Genomic_DNA.
DR RefSeq; XP_001273942.1; XM_001273941.1.
DR STRING; 344612.A1C9U8; -.
DR EnsemblFungi; EAW12516; EAW12516; ACLA_009390.
DR GeneID; 4706897; -.
DR KEGG; act:ACLA_009390; -.
DR VEuPathDB; FungiDB:ACLA_009390; -.
DR eggNOG; KOG0055; Eukaryota.
DR HOGENOM; CLU_000604_17_2_1; -.
DR OMA; RSDANFW; -.
DR OrthoDB; 1067095at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd18577; ABC_6TM_Pgp_ABCB1_D1_like; 1.
DR CDD; cd18578; ABC_6TM_Pgp_ABCB1_D2_like; 1.
DR CDD; cd03249; ABC_MTABC3_MDL1_MDL2; 2.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR PANTHER; PTHR24221:SF503; LP14331P; 1.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 114..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 265..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 344..367
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 784..807
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 827..855
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 906..926
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 932..952
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1014..1034
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1046..1070
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 118..408
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 443..688
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 786..1075
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1110..1348
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1355 AA; 148065 MW; F147C0058D46E9A8 CRC64;
MVSPENDISS QEKHAADSRV ASLEKGRSTS LSSNPENEKP QDQNSVSGST VTPSAGKKND
PSPALAGQKV DLGDDALFAH LPEHERAILK KQLDAPDIKV SFGILYRYAS RMDIFIILVS
TICAIIAGAA LPLFTILFGS LASAFQNITL GTISYSDFYH QLTKNVLYFV YLGIAEFVTV
YVSTVGFIYT GEHLTQKIRE HYLEAILRQN MAYFDKLGAG EVTTRITADT NLIQDAISEK
VGLTLTALAT FVTAFIVAYV KYWKLALICT STIVALVLVM GGGSRFIVKY SKKSLESYGA
GGTVAEEVIS SIRNATAFGT QDKLAKQYET HLAEAEKWGI KQQIIMGMMI GGMFGIMYSN
YGLGFWMGSR FLVDGEVGVG QILTVLMAIL IGSFSLGNVA PNGQAFTNGV AAAAKIYSTI
DRLSPLDPYS DEGEKLENFE GNIEFRNIKH IYPSRPEVTV MEDVSLLMPA GKTTALVGPS
GSGKSTVVGL VERFYLPVGG KVLLDGRDIQ TLNLRWLRQQ ISLVSQEPVL FGSTIYKNIR
HGLIGTRFET ESEDKIRELI ENAAKMANAH EFIMALPEGY ETNVGQRGFL LSGGQKQRIA
IARAIVSDPK ILLLDEATSA LDTKSEGVVQ AALDRAAEGR TTIVIAHRLS TIKTAHNIVA
MVGGKIAEQG THDELVDRKG TYFSLVEAQR INEEKEAEAL DGDANMNADD FAQEEVARIK
TAASSSSSLD DEDKHVRLEM KRTGTQKSVS SAVLSKRAPE TTRKYSLWTL LKFITSFNRP
ETGYMLIGLV FSVLAGGGQP TQAVLYAKAI STLSLPETMF QKLRHDANFW SLMFFVVGIA
QFISLAINGS AFAVCSERLI RRARSQAFRS ILRQDISFFD REENSTGALT SFLSTETKHL
SGVSGVTLGT ILMTSTTLGA AMIIALSIGW KLALVCISVV PILLACGFLR FYMLARFQQR
SKTAYEGSAS YACEATSAIR TVASLTREED VWAVYHGQLQ NQGKKSLISI LKSSLLYASS
QALVFFCVAL GFWYGGTLLG KHEYSIFRFF VCFSEILFGA QSAGTVFSFA PDMGKAKNAA
AEFKKLFDRR PTIDIWSEEG EKLDSVDGEI EFRDVHFRYP TRPEQPVLRG LNLSVKPGQY
IALVGPSGCG KSTTIALLER FYDTLAGGVF VDGKDITKLN VNSYRSFLAL VSQEPTLYQG
SIKENILLGV DKDDVPEEAL IKVCKDANIY DFIMSLPEGF DTVVGSKGGM LSGGQKQRVA
IARALLRDPK VLLLDEATSA LDSESEKVVQ AALDAAARGR TTIAVAHRLS TIQKADIIYV
FDQGKIVESG THQELIRNKG RYFELVNMQS LGKTQ
//
