ID A0A1B7NX17_9EURO Unreviewed; 1249 AA.
AC A0A1B7NX17;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=ABC transporter domain-containing protein {ECO:0000259|PROSITE:PS50893};
GN ORFNames=ACJ72_04341 {ECO:0000313|EMBL:OAX81322.1};
OS Emergomyces africanus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX NCBI_TaxID=1955775 {ECO:0000313|EMBL:OAX81322.1, ECO:0000313|Proteomes:UP000091918};
RN [1] {ECO:0000313|EMBL:OAX81322.1, ECO:0000313|Proteomes:UP000091918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 136260 {ECO:0000313|EMBL:OAX81322.1,
RC ECO:0000313|Proteomes:UP000091918};
RA Cuomo C.A., Schwartz I.S., Kenyon C., de Hoog G.S., Govender N.P.,
RA Botha A., Moreno L., de Vries M., Munoz J.F., Stielow J.B.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAX81322.1}.
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DR EMBL; LGUA01000498; OAX81322.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B7NX17; -.
DR STRING; 1658172.A0A1B7NX17; -.
DR OrthoDB; 5473955at2759; -.
DR Proteomes; UP000091918; Unassembled WGS sequence.
DR GO; GO:0016020; C: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; 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; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR034003; ABCG_PDR_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010929; PDR_CDR_ABC.
DR PANTHER; PTHR19241; ATP-BINDING CASSETTE TRANSPORTER; 1.
DR PANTHER; PTHR19241:SF625; ATP-DEPENDENT PERMEASE PDR10-RELATED; 1.
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; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000091918};
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 290..313
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 325..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 401..424
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 430..452
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 538..559
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 942..963
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 975..996
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1016..1042
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1062..1085
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1091..1110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1122..1143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1216..1235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 620..862
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 584..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1249 AA; 139781 MW; 31D9BC18A7B906F1 CRC64;
MHNQFRGEAT YTAETDVHFP QLTVGQTLEF AARARAPANR IPGVTREQYA IHMRDVVMAS
FGLTHTMNTN VGNDFIRGVS GGERKRVSIA EACLSQAPLQ CWDNSTRGLD SANALEFCRT
LRLSTDYMGA TICVAIYQAS QSAYDYFDKV TVLYEGRQIY FGRTDEAKKF FVDMGFECPE
RQTTADFLTS LTSPVEHVIR AGFEGKTPRT PDEFEAAWKN SAAYAKLLQD IDEYETRYPI
GGPSVDKFIE SRKAQQSKSQ RVKSPYTLSV SQQIGLCVHR GFQRLRRDMS LTLSALIGNF
FMSLILGSVF YNLNETTESF YRRGALLFFA VLMSAFASAL EILTLYAQRA IVEKHSRYAL
YHPFAEAISS MLCDLPYKFL NSITFNLPIY FLSNLRREPR VYFVFWLFTL VTTLAMSMIF
RTIAATSRTL AQALAPAAVL ILGLVIYTGF AIPTRNMLGW ARWMNYVDPV AYAFEALMVN
EFHDRQFDCA GFIPSGGEYE NYPLENKVCG TVGSIAGSRR VDGDLYLRLS YQYEYSHIWR
NLGIIFGFIF FFMFTYLFAT EYISESKSKG EVLLFRKGHQ PKKAKNSDIE ASPPPSSGEK
SSGSSSQGVS ASIQKQTAVF QWRDVCYDIK IKKEDRRILD HVDGWVKPGT CTALMGVSGA
GKTTLLDVLA TRVTMGVVSG EMLVDGQPRD ESFQRKTGYI MQQDLHAAST TVREALNFSA
MLRQPASVPR AEKLAYVDEV IKLLEMEDYA DAVVGVPGEG LNVEQRKRLT IGVELAAKPQ
LLLFLDEPTS GLDSQTSWSI LNLLDTLTKH GQAILCTIHQ PSAMLFQRFD RLLFLASGGK
TVYFGDVGDR SSILSSYFEK NGASPCPPDA NPAEWMLEVI GAAPGSKSDI DWPESTLAEK
AQVQPADRNP EDYREFAAPF GVQVWECLVR VFSQYWRSPT YIYSKTALCA LSGLFIGFSF
FNAQSSLQGL QNQMFAVFML MTIFGNLAQQ IMPNFVAARA LYEARERPSK SYSWKAFMIA
NIFVELPWNS LMAVIIFACW YYPIGLYNNA IPNDQVAERG ALMFLLILSF LLFTSTFSHL
AIAGIEVAET GANIANLLFM LCLIFCGVLA SKDALPGFWI FLYRLSPFTY LVSAMLSTGL
AGADIVCESV EFLRFNPVAN QTCEQYLAPF RESYPPRGYL QNPLATTDCG FCAMEKTDSF
LAGIGSYYSD AWRNFGLMWV YIVFNIAGAV LIYWLTRVPK GARAKGPTA
//
