ABCB_ASPFU
ID ABCB_ASPFU Reviewed; 1458 AA.
AC Q4WT65;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=ABC multidrug transporter B;
GN Name=abcB {ECO:0000303|PubMed:16622700}; ORFNames=AFUA_1G10390;
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. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
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DR EMBL; AAHF01000004; EAL90367.2; -; Genomic_DNA.
DR RefSeq; XP_752405.2; XM_747312.2.
DR AlphaFoldDB; Q4WT65; -.
DR SMR; Q4WT65; -.
DR STRING; 330879.Q4WT65; -.
DR EnsemblFungi; EAL90367; EAL90367; AFUA_1G10390.
DR GeneID; 3510660; -.
DR KEGG; afm:AFUA_1G10390; -.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_5_1; -.
DR InParanoid; Q4WT65; -.
DR OMA; YAAISFP; -.
DR OrthoDB; 138195at2759; -.
DR Proteomes; UP000002530; Chromosome 1.
DR GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015440; F:ABC-type peptide transporter activity; IBA:GO_Central.
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 CDD; cd18579; ABC_6TM_ABCC_D1; 1.
DR CDD; cd18580; ABC_6TM_ABCC_D2; 1.
DR Gene3D; 1.20.1560.10; -; 2.
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; IPR044746; ABCC_6TM_D1.
DR InterPro; IPR044726; ABCC_6TM_D2.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00664; ABC_membrane; 1.
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..1458
FT /note="ABC multidrug transporter B"
FT /id="PRO_0000445097"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..295
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 541..561
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 940..960
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 978..998
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1016..1036
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1040..1060
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1125..1145
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1156..1176
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 283..561
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 626..853
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 933..1182
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1219..1449
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 660..667
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1252..1259
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 702
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 804
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 879
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1458 AA; 160873 MW; 6CC0BEE7877779BA CRC64;
MTGSSPPLSC QQVDNTLHIP ALSCRGGFDF SLLFEELILG ILPLGIVLII APFRLYHLFW
RQAKVVASWL LWAKITAWLA LGIVQLVLAV YWARPAATRT QASIAANAII TVGFFILCLL
SCAEHLRSTT PSFLLNIYLL FTLLFDIAKT RTLWLRSSGQ TDETIAILTS VTVGIKFLLL
ILEAVEKRHI LRKGQSGYPP EATAGIFNRS FFLWLNPLFR SGFSKILDVE DLFDLDKHLS
SRRLYSTLET LWDKVPKKNP NTLLFISLKA FKWPLLSAVP PRACLAALNF CQPLLLHRSL
AFATEPVNNH TNSIGYGLIG AYILVYIGMG VTMGQYQHMT YRTITMVRGG VVSMIYNKAS
RLGIKDADPA ASLTLMSADI ERIVQGWQTI HDIWGNAAEI ALAIYLLERE LGVACVVPVG
VALVALIGCL ITLSFVVARQ AVWLEAIERR ISSTASMLSS MKGIKMLGLK SAIMKSLHGL
RLEELEISKK FRRLLVWNMA LGWTTRIFAP IFALGAFYGI MHSRGKDSAF DMSTAYTSLS
LFALLADPLL SLVMALMTFV GSIGSFSRIQ EFLEKDDHVD CRLKPLHASY ESFEPKAMVL
VDDSDATETA SDRSIHRGKS VYHDALTVKN ATFAWNVEKE PVLKGLTISI ARGSFTMIVG
PSGCGKSTLL KAILGEVPCV NGEIRLSSDS IAFCDQIPWH MNATIRESIV AMSSFDKEWY
ASVVHACGLV QDFEQLPRGD ETVIGSKGIA LSGGQSQRIA LARAVYARKD IVILDDAFSG
LDAATEDYVF HSLVGIHGLL RKINSTIIVA SSSAKRLPYA DQIVVLDKMG YASEQGSLKA
LNAAGGYVSS FGLGSPEWKS EIDKPSVTDL AQPKILRPNR TEAIKEDPRR QSGDLSIYLY
YIRSIGWLPT RLVLTDMTGI WVKWWAISNE EDPNGRTGYY LGIYAMLGAV GMLSLIIGCW
EMVINMVPKS GESFHRKLLA TVLNAPMSFF AATDSGSILN RFSQDLQLID MELPVAAINT
FATLILCLAQ MILMGIASRY AAISFPLVIL AVYSIQKVYL RTSRQLRFLD LEAKAPLYSH
FSDCLNGLVT LRAFGWQPAL EDKNFQLLDY SQRPFYLLYA IQRWLTLTLD MVVAAIAVIL
IVLVVTLRGT ISAGDVGVAL LNVILFSQSI KLLVTFWTNL ETHIGSIVRI RSFTETVSSE
NLPTEKDDVP PNWPWGGDIE FKSVSAEYRP SEPVLGDVSL TIKSGEKVGI CGRTGSGKTS
LIMSLFRMVE LSSGSIHIDG VDITKIPRQE IRSRINGVSQ SPLLIKGSIR RNMDPNGSYA
EKAIIEAIKS VGLYTKIQEK GGLDTDISEV FLSQGQQQLF CLARAILRPG KVLVLDEATS
NVDAKTDEIM QRVIREKFCT HTILAVAHKL ETILDYDKVV VLDAGRVVES GDPCTLLSTE
GSYFSRLYAS SMALAEEQ
