ABCG_ASPFU
ID ABCG_ASPFU Reviewed; 1349 AA.
AC Q4W9C7;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=ABC multidrug transporter G {ECO:0000303|PubMed:32209680};
GN Name=abcG {ECO:0000303|PubMed:32209680}; ORFNames=AFUA_4G01050;
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.
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 seems not to be able to transport
CC azoles, nor rhodamine 6G (R-6G), a known substrate for many ABC
CC transporters. {ECO:0000269|PubMed:32209680}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:32209680};
CC Multi-pass membrane protein {ECO:0000255}.
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; AAHF01000017; EAL84314.2; -; Genomic_DNA.
DR RefSeq; XP_746352.2; XM_741259.2.
DR AlphaFoldDB; Q4W9C7; -.
DR SMR; Q4W9C7; -.
DR STRING; 330879.Q4W9C7; -.
DR EnsemblFungi; EAL84314; EAL84314; AFUA_4G01050.
DR GeneID; 3503854; -.
DR KEGG; afm:AFUA_4G01050; -.
DR VEuPathDB; FungiDB:Afu4g01050; -.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_0_1; -.
DR InParanoid; Q4W9C7; -.
DR OMA; HVWFRWI; -.
DR OrthoDB; 324553at2759; -.
DR Proteomes; UP000002530; Chromosome 4.
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; 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; 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 3: Inferred from homology;
KW ATP-binding; Cell membrane; Glycoprotein; Hydrolase; Membrane;
KW Nucleotide-binding; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1349
FT /note="ABC multidrug transporter G"
FT /id="PRO_0000452660"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 523..543
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 550..570
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 580..600
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 659..679
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1056..1076
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1085..1105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1121..1143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1166..1186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1193..1213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1226..1246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1318..1338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 51..299
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 721..963
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 757..764
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 649
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 994
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1349 AA; 151535 MW; B09E5C45D3AA4E0D CRC64;
MDTPSSGTID LEHGEAGLRK RLTLTFRSVS VHVTAPDAAL GDTLLSVADP RQFLGFLKGS
RPKRTILKDV SGQVKPGEML LVLGRPGSGC TSLLRVLSND RESFDEVIGE TRYGSMDHVA
ARRFRQQIMF NNEDDVHFPT LTVNRTMKFA LRNKVPRERP DGQGSKEFVQ EQRDNILSAL
GIRHTTKTLV GNEFIRGVSG GERKRVSLAE VIAGQSPIQV WDNPTRGLDS KTAVEFARLL
RREADMNQKT MVATMYQAGN GIYNEFDQVL VLADGRVTYY GPRQLAKSYF EDMGFVCPKG
ANVADFLTSV TVLTERIVRP GMEDKVPSTA EEFEARYRQS DIHQKAMEGF DPPEKLTHEV
DELTAAVASE KRKRHLPRSP SVYTTSLWEQ IQACTIRQFQ IMAGDRLSLI IKVVSAILQA
LVCGSLFYNL KDDSSSIFLR PGALFFPVLY FLLESMSETT ASFMGRPILS RQKRFGFYRP
TAFCIANAIT DIPVVLVQVS CFCIILYFMA ALQMDAGRFF TYWIIVIANT LCFMQMFRAV
GALCKRFGNA SKITGLLSTI FFVYGGYLIP YEKMHVWFRW IFYLNPGAYA FEALMANEFV
GKSLQCVQPD YIPYGSGYPG SESPYRGCSI PGSEGDVILG AAYIRAQYNY SWHHIWRSFG
VIIGFWVFFI VLTALGLELL NSQGGSSVLL YKRGSQKTRS EDTTTPVQEA ARASHAKQST
FTWHDLDYHV PYQGQKKQLL DKVFGFVKPG NLVALMGCSG AGKTTLLDVL AQRKDSGEIY
GSILIDGRPQ GISFQRTTGY CEQMDVHEPT ATVREALVFS ALLRQPAHVP REEKLAYVDH
IIDLLELRDI SDALIGVPGA GLSIEQRKRV TLGVELVAKP TLLFLDEPTS GLDGQSAYNI
IRFLRKLVDG GQAVLCTIHQ PSAVLFEAFD SLLLLARGGK MAYFGETGKD SQTVLDYFAR
HGAPCPPDEN PAEHIVEVIQ GNTDKPIDWV QVWNESEEKQ RALAQLQTLN ARGKADADYV
EDTADYATSK WFQFTMVTKR LMVQLWRSPD YVWNKVILHV FAALFSGFTF WKIGDGAFDL
QLRLFAIFNF IFVAPGCINQ MQPFFLHNRD IFEAREKKSK IYHWLAFIGA QTVSEIPYLI
LCATLYFACW YFTAGFPTTA SISGHMYLQM IFYEFLYTSI GQGIAAYAPN EYFAAVMNPV
LIGAGLVSFC GVVVPFSQMQ PFWRDWLYYL DPFTYLVGGL LGEVLWDVEV RCDPSELVRF
RAPLGQTCGE YMAAFLAEKP GYLVDGNATA CEFCQYSTGA DYARTFNLKE RYYSWRDTGI
TALFCVSSYA MVFLMMKLRS KKTKSARSE
