ABCE_ASPFU
ID ABCE_ASPFU Reviewed; 1274 AA.
AC Q4WA92;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=ABC multidrug transporter E;
GN Name=abcE {ECO:0000303|PubMed:16622700}; ORFNames=AFUA_7G00480;
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 IDENTIFICATION, INDUCTION, AND FUNCTION.
RX PubMed=16622700; DOI=10.1007/s00294-006-0073-2;
RA da Silva Ferreira M.E., Malavazi I., Savoldi M., Brakhage A.A.,
RA Goldman M.H., Kim H.S., Nierman W.C., Goldman G.H.;
RT "Transcriptome analysis of Aspergillus fumigatus exposed to voriconazole.";
RL Curr. Genet. 50:32-44(2006).
CC -!- FUNCTION: Pleiotropic ABC efflux transporter that may be involved in
CC A.fumigatus adaptation to azoles such as vorizonazole.
CC {ECO:0000305|PubMed:16622700}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is induced upon voriconazole treatment.
CC {ECO:0000269|PubMed:16622700}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAHF01000015; EAL84844.1; -; Genomic_DNA.
DR RefSeq; XP_746882.1; XM_741789.1.
DR AlphaFoldDB; Q4WA92; -.
DR SMR; Q4WA92; -.
DR STRING; 330879.Q4WA92; -.
DR EnsemblFungi; EAL84844; EAL84844; AFUA_7G00480.
DR GeneID; 3504327; -.
DR KEGG; afm:AFUA_7G00480; -.
DR eggNOG; KOG0055; Eukaryota.
DR HOGENOM; CLU_000604_17_8_1; -.
DR InParanoid; Q4WA92; -.
DR OMA; FKYSWAL; -.
DR OrthoDB; 186078at2759; -.
DR Proteomes; UP000002530; Chromosome 7.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma 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: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; -; 1.
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; 1.
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; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1274
FT /note="ABC multidrug transporter E"
FT /id="PRO_0000445099"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 697..717
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 737..757
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 818..838
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 840..860
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 924..944
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 120..344
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 377..629
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 697..984
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1023..1269
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 412..419
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1057..1064
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 792
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1044
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1274 AA; 141336 MW; 87C8300D10A592AC CRC64;
MALQQVRPTN KQCRKNKKRA KAKMMESPRR LCRWAIISYE GSPRIACNAT DETAESPFLR
NRERSSCINR GFDISYCVRC AFTPDEHCVW EPCCAIQSVR QQVEVGTSKR TMDIYSPLQF
CFRVTGLRVS AVIRLEYVQA LFSQPISKVD QVSVGTVTNT ITTLSNTIQQ SISDKLAILF
QSLALLLAAF IIAFKYSWAL TLVTSSALLF VVVGCSVTLP FMTKIQQKID KADEKHSSIA
AEVFGSIRTV ISLGAQESLS KRYTTWVEEA RKRGNGLSLI FGIHFALVFF ALYASFSLAF
WFGLKLYREG HIGEINTVIT VFFSVMIVVS VLGNIASPLI IVSKAASAAG SFFELIDSEK
VDSGGLREPD ASAHVDIIFR DVRFTYPTRP DVPVLKGLDI RFQNGKTTAL VGPSGSGKST
IVALIERWYQ LAMSPEDQNQ GSIYVGPHDI NSLDLKWWRS QIGLVQQEPF LFNDTIFNNV
AFGLIGTQWE KEPDSVKKEL IEKACREAFA EEFIQRLPEG YATIVGQNGI KLSGGQRQRL
AIARSIVKEP KILILDEATS AIDVRGEKIV QAALDRVSRN RTTIMIAHRL STIRRADHIV
VMKGGVNVEE GTHEELLQRE GGVYRDLVNA QRLELLAEED SHTGNAVLEL QDEAQSPTMS
VQEKLQDEDN TQDKNRGFIR TIGLVLYEQR ARWPLYVAVL ISTAGAGTAF PLQSWLFAKL
IEVFRFTGQK LVDAANFWAL MFFLLALAVG VLYSTVGFTA NSLSVRISEA CRKEYFQNIL
AKPIPFHDLS ENASGSIVSR LATDPKQVQE LIGLNGAFPL ISTFSMIGCI AIAFSFGWKL
SLVTVFAALP CTFLAAFMRI RYELQFEAMN AAVYAGSSQF AAEAIDAFRT VSSLTMEDAI
LDRYTQLLRE QQKKAFRKAR YATLIFAFSD SVELCAMALT FWYGGQLLAS REYQPTSFFV
IFMAIIQGGQ SAGQFFSFAS NFAQAAASAN RILNSRPQSD ELGAASIEKQ QLVRSGDLTG
ATVEFHDVSF RYASQDVPLF TGLNVSIQSG QFVAFVGPSG CGKTTVISLL ERFYSPSQGT
ITFNGEDIRT LEMTSYRREL SLVAQEPRLF EGSIRENITL GLDQSEFTEE ELIQACKDAE
IHDFITSLPE GYATELGIKA QTSLSGGQRQ RLCIARALLR KPSLLLLDEA TSSLDSQSEK
VVQGAMERLA QKRSLTIVAV AHRLATIQKA DTIYVFGTAH AGQASRIVEQ GTHQELLRAK
GTYWQMVSSP RFLT
