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
//