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Database: UniProt
Entry: A0A0A0HU76_PARBD
LinkDB: A0A0A0HU76_PARBD
Original site: A0A0A0HU76_PARBD 
ID   A0A0A0HU76_PARBD        Unreviewed;      1488 AA.
AC   A0A0A0HU76;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=ABC transporter domain-containing protein {ECO:0000259|PROSITE:PS50893};
GN   ORFNames=PADG_12014 {ECO:0000313|EMBL:KGM91873.1};
OS   Paracoccidioides brasiliensis (strain Pb18).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502780 {ECO:0000313|EMBL:KGM91873.1, ECO:0000313|Proteomes:UP000001628};
RN   [1] {ECO:0000313|EMBL:KGM91873.1, ECO:0000313|Proteomes:UP000001628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pb18 {ECO:0000313|EMBL:KGM91873.1,
RC   ECO:0000313|Proteomes:UP000001628};
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-miconazole(in) + ATP + H2O = (R)-miconazole(out) + ADP +
CC         H(+) + phosphate; Xref=Rhea:RHEA:61928, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:82894, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00000258};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61929;
CC         Evidence={ECO:0000256|ARBA:ARBA00000258};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-miconazole(in) + ATP + H2O = (S)-miconazole(out) + ADP +
CC         H(+) + phosphate; Xref=Rhea:RHEA:61932, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:82897, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00001626};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61933;
CC         Evidence={ECO:0000256|ARBA:ARBA00001626};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + voriconazole(in) = ADP + H(+) + phosphate +
CC         voriconazole(out); Xref=Rhea:RHEA:61912, ChEBI:CHEBI:10023,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00000665};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61913;
CC         Evidence={ECO:0000256|ARBA:ARBA00000665};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + fluconazole(in) + H2O = ADP + fluconazole(out) + H(+) +
CC         phosphate; Xref=Rhea:RHEA:61916, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:46081, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00001886};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61917;
CC         Evidence={ECO:0000256|ARBA:ARBA00001886};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC       PDR (TC 3.A.1.205) subfamily. {ECO:0000256|ARBA:ARBA00006012}.
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DR   EMBL; KN275963; KGM91873.1; -; Genomic_DNA.
DR   RefSeq; XP_010761603.1; XM_010763301.1.
DR   STRING; 502780.A0A0A0HU76; -.
DR   GeneID; 22587911; -.
DR   KEGG; pbn:PADG_12014; -.
DR   VEuPathDB; FungiDB:PADG_12014; -.
DR   eggNOG; KOG0065; Eukaryota.
DR   HOGENOM; CLU_000604_35_0_1; -.
DR   InParanoid; A0A0A0HU76; -.
DR   OMA; IMPRFVT; -.
DR   OrthoDB; 5473955at2759; -.
DR   Proteomes; UP000001628; Unassembled WGS sequence.
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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd03233; ABCG_PDR_domain1; 1.
DR   CDD; cd03232; ABCG_PDR_domain2; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013525; ABC2_TM.
DR   InterPro; IPR029481; ABC_trans_N.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
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   PANTHER; PTHR19241:SF668; ABC MULTIDRUG TRANSPORTER (EUROFUNG); 1.
DR   PANTHER; PTHR19241; ATP-BINDING CASSETTE TRANSPORTER; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001628};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        522..539
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        546..565
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        585..618
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        630..650
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        656..676
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        725..746
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1150..1170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1182..1201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1221..1254
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1266..1288
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1420..1438
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          155..406
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          812..1055
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          777..805
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1488 AA;  166583 MW;  98B42F9265F0B70C CRC64;
     MAGDSPHSSG HEDPEYLPDE KDHDYNDDED ESRHGDSSSN EDTRFNLIRS LTRDPNTELS
     RIASVFSHAD EHSTATDSLA RIDTLAGLQL GDAVLNPSSP QFDFYKWARM LMKLMEEDGL
     KRRRTGITFR NLSVYGSGPA LQLQSTVSTP IMALFRFQET FGVGRRTQKR ILNNFNGALR
     EGEMLVVLGR PGSGCSTFLK TICGETHGLE LEREASVQYN GIPQTTFKKE FRGEAVYSAE
     DEKHFPHLTV GQTLEFAAAC RTPSARVMGM ARKEFSHHIA RVVMAIFGLS HTANTKVGDD
     YVRGVSGGER KRVSIAELGL SGAPVICWDN STRGLDSATA LEFTRALRVA SDVMGATQAV
     AIYQASQAIY DLFDKAVVLY DGRQIYYGPA NSAKKYFEDM GWYCPPRQTT GDFLTSITNP
     MERRVREGFE SKVPRTAHEF ETYWRNSLQF KDVLAEIEQC EHEHPVGGPA LGELREAHNQ
     AQAKHVRPKS PYTITIPMQV KLCTTRAYQR LWNDKASTIS RVMAQLIMSL IIGSLYFNTP
     QVTSSFFSKG SVLFFAILLN ALLSISEINT KDSQRPIVSK HVSYALYYSC VEAFAGIVSD
     IPIKLITSTV FNIIIYFLGD LRRQADHFFI FFLFTFITML TMSAIFRTLA AATKTISQAL
     AFAGVMVLAI VIYTGFHNSA VIYIVPPYGE GMNFQCPIAG AVPGERSVSG DAWVESQYGY
     KYSHIWRNLG FIFAFQVFFY VLYLTATQLN TASASTAEFL VFRRGNVPKY MLKQNDEEND
     KAAPPAAAAA AGANSKNEED KTNVLPPQTD VFTWRNVTYD ITIKGEDRRI LDHVSGWVRP
     GTLTALMGVS GAGKTTLLDV LAQRISFGVV TGDMFVNGKP LDLSFQRKTG YCQQQDLHLE
     TSTVREALRF SAMLRQPQSV SKQEKYEFVE DVIKMLNMED FAEAVVGSPG EGLNVEQRKL
     LTIGVELAAK PQLLLFLDEP TSGLDSQSAW AIVTFLRKLA DHGQAVLSTI HQPSAVLFQE
     FDRLLLLAKG GKTVYFGEIG KNSETMLNYF AAHGAERCRP DENPAEYMLN VVGAGPSGKS
     TQDWAAVWNN SQEAKQVQDE LDRIHAEKAE KHDPTADQQA VTQEFAMPMT SQIYYVTFRV
     FQQYWRTPTY IWGKFLLGFM SAVFIGFSFY KQNSSSSGLQ NTLFAIFMLT TIFTSLVQQI
     MPRFVTQRSL FEVRERPSRT YGWKAFLLAN IIVEIPYQIL LGIVVWASLY FPVFGKNQTS
     EQQGTFLIYS VQFMIFASTF AHMVIAGLPD AETAGHIATT LFSLSLTFNG VMQPPRALPG
     FWIFMWRVSP LTYTVGGLAA TGLHNRIVNC AENEFAIFNP PSGATCGQYL AEFFAAGAQG
     QLEDPNATQG CRYCSLRNAD QFLARSEVFW SQRWRNFGLG WAYIGFNVFA AVALYYMLRV
     RTSTGKTRKR ASLVKHYVRW VGGWVRALFT TRIEKTPEEK IHVNDRIL
//
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