ABCH_ASPFU
ID ABCH_ASPFU Reviewed; 1424 AA.
AC Q4WFQ4;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=ABC multidrug transporter H {ECO:0000303|PubMed:32209680};
GN Name=abcH {ECO:0000303|PubMed:32209680}; ORFNames=AFUA_3G01400;
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, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION,
RP AND INDUCTION.
RX PubMed=32209680; DOI=10.1128/mbio.00338-20;
RA Esquivel B.D., Rybak J.M., Barker K.S., Fortwendel J.R., Rogers P.D.,
RA White T.C.;
RT "Characterization of the efflux capability and substrate specificity of
RT Aspergillus fumigatus PDR5-like ABC transporters expressed in Saccharomyces
RT cerevisiae.";
RL MBio 11:0-0(2020).
CC -!- FUNCTION: ABC efflux transporter that is able to transport rhodamine 6G
CC (R-6G), a known substrate for many ABC transporters, but seems not to
CC transport azoles. {ECO:0000269|PubMed:32209680}.
CC -!- ACTIVITY REGULATION: The efflux inhibitor FK506 impairs the transport
CC activity. {ECO:0000269|PubMed:32209680}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:32209680};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression is induced in triazole-resistant isolates.
CC {ECO:0000269|PubMed:32209680}.
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; AAHF01000010; EAL86423.2; -; Genomic_DNA.
DR RefSeq; XP_748461.2; XM_743368.2.
DR AlphaFoldDB; Q4WFQ4; -.
DR SMR; Q4WFQ4; -.
DR STRING; 330879.Q4WFQ4; -.
DR EnsemblFungi; EAL86423; EAL86423; AFUA_3G01400.
DR GeneID; 3506093; -.
DR KEGG; afm:AFUA_3G01400; -.
DR VEuPathDB; FungiDB:Afu3g01400; -.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_0_1; -.
DR InParanoid; Q4WFQ4; -.
DR OMA; PWFGWIY; -.
DR OrthoDB; 1022017at2759; -.
DR Proteomes; UP000002530; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
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; PF19055; ABC2_membrane_7; 1.
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; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Hydrolase; Membrane;
KW Nucleotide-binding; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1424
FT /note="ABC multidrug transporter H"
FT /id="PRO_0000452661"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 520..540
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 544..564
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 569..589
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 605..625
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 629..649
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 710..730
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1131..1151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1161..1181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1200..1220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1240..1260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1268..1288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1300..1320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1395..1415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 96..351
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 794..1037
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 830..837
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 790
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 798
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1424 AA; 159328 MW; 41DCBFEC45888F53 CRC64;
MEDQGHLPSE PRALFDRRDD TDSTNTALDE TDLSRTPLQD TSHTPHAEDW SLMPDLKKQH
DRNVASGFRR RELGVTWKNL SVDVVSADAA INENVLSQFN IPQHIRESRN KAPLRTILHE
SHGCVKPGEM LLVLGRPGSG CTTLLRMLSN HRLGYKAIRG DVRFGSLTPE EASKYRGQIV
MNTEEELFFP TLTVAQTLDF ATRLKVPFNL PDGVTSPEAF RQETREFLLK SMGISHTSDT
KVGNEYVRGV SGGERKRVSI IECLATRGSV FCWDNSTRGL DASTALEWAK AVRAMTDVFG
LSSIVTLYQA GNGIYDLFDK VLVLDEGKQI YYGPMSQARP FMEEQGFVCR EGSNVADFLT
GVTVPTERKI RPGYENRFPR NADELLAAYE KSPIRAQMAI EYDYPDTEST RERTEEFKLG
VLDEKAKRLS KNSPFTVDFL QQVKACIIRQ YQIIWTDKAT FAIKQISTVI QALVAGSLFY
NAPDNSGGLF IKSGALFFSL LYNSLLAMSE VTDSFSGRPV LIKHKYFAFF HPAAFCIAQI
AADIPVLLFQ ISMFAVVVYF MVGLTTSAGA FFSYWIIIFV ATMVMTALFR AIGALFSTFD
GASKVSGFLI SALIMYCGYL EPYHAMHPWF IWIYWINPLA YAFDALLSIE FHNKIIPCVG
NNLVPFGPGY DDTTFQSCAG VGGAVRGMTY VTGDQYLASL TYSYSHVWRN FGILWAWWAL
FVAVTIIATS RWKSAAEAGN SLLIPRETVA KHHAVVRKDE EAQLNEKAGH KGTGTDSEAQ
SNVDQHLVRN TSVFTWKNLT YTVKTPSGDR VLLDNVYGWV KPGMLGALMG SSGAGKTTLL
DVLAQRKTDG TIRGSIMVDG RPLPVSFQRS AGYCEQLDVH EPFATVREAL EFSALLRQPR
HIPREEKLKY VDVIIDLLEL HDLEHTLIGR VGAGLSVEQR KRVTIGVELV SKPSILIFLD
EPTSGLDGQS AFNTVRFLRK LADVGQAVLV TIHQPSAQLF AEFDTLLLLA KGGKMVYFGD
IGDNAQTVKD YFARYGAPCP ANVNPAEHMI DVVSGHLSQG RDWNQVWLES PEHSSASREL
DSIISEAASK PPGTVDDGYE FAMPLWEQTK IVTQRMSTSL YRNCDYIMNK IALHIGSALF
NGFSFWMIGD SVADMQLKLF TIFNFIFVAP GVINQLQPLF IERRDIYDAR EKKSKMYSWV
AFVTALIVSE FPYLCVCAVL YFVCWYYTVG FPSDSDKAGA IFFIMLCYEF LYTGIGQFIA
AYAPNATFAA LTNPLILGTL VSFCGVLVPY AQIQAFWRYW IYWLNPFNYL MGSMLVFSVF
DTDVKCKEGE FAVFDTPNGT TCADYLSTYL QGVGSRANLV NPEATSGCRV CQYRYGSDYL
YTINLKDYYY GWRDTAIVCI FVLSSYALVY ALMKLRTKAS KKAE
